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How To Write Horror Fiction
Horror fiction can creating haunting tales that can stick with a person for life. Whether it's invading aliens that are turning people into plants or a serial killer who is hunting down specific people in a community, knowing how to write horror fiction correctly can help you avoid the many clichés that this genre tends to have.
People like to be frightened. What is different about this genre, however, is that the horror people like to experience is inside their heads. You'll still find slasher stories and gory novels with descriptions that will make you want to vomit, but good horror today asks one question: "What would you do?" Answer that and you'll be ready to start following these additional tips.
#1. Outline your scenario of events before you start writing.
This is one of the most important aspects of the horror genre. Because you might be moving back and forth throughout the narrative, it is important to make sure that you get your time lines right. If they're off by just a fraction, it is going to make your fiction seem awkward and distant. This is very much like the A-B-C story elements that are taught in elementary school today.
#2. Expand your outline to include narration events.
This is where you can begin to fill in the details of each scenario that you plan to include within your story. You'll see where each event will take place within the novel, allowing you to be able to add some fullness to the experience. Start adding in some of the details that will enhance the fright a reader is going to experience. Take notes here about any changing perspectives, stresses, or outside factors that could further enhance the reader's experience. The goal is to develop a climax that will be both scary and satisfying.
#3. Write a fast first rough draft.
When writing horror fiction, it is important for the writer to not be overly critical of their first draft. You want to get the ideas out without over-thinking them very much. Even though you've creative scenarios and outlines, you might find that some circumstances call for change. It's okay to make these changes. You are not bound by any previous outline or design you've created. Write down your ideas, let them flow, and then come back and change them if necessary.
#4. Use the second draft to pay attention to the fine details.
Once you've gotten the general ideas down in a first draft of your horror fiction, you're ready to begin fleshing the story out. Focus particularly on the narrative tone that you're using. Does it seem realistic? Is it too harsh in places, taking readers away from the events that are taking place? Have you put in transitions that make sense for your characters so they can adapt to changing circumstances?
You'll also need to focus on the rhythm of what you've written and your syntax. If you take a reader out of the rhythm of a story, it won't seem frightening. It will feel to them that you're trying to hard. Make it as natural as possible, be willing to include moments of grace, but be convincing about the reality of the situation.
#5. You're not done drafting yet.
Your third draft is the neat copy that you'll be presenting as part of a novel pitch. This is the place where you can make the final revisions necessary to perfect your story. Many writers try to pound out the third draft as their first draft – this doesn't work when writing horror fiction. You must address these scenarios in a series of steps in order for the authenticity of the story to be developed. At some level, the horror must be believable if the reader is going to keep reading it.
#6. Don't be afraid of your imagination.
Anything can become the foundation of a horror story. There might be a natural phenomenon that mysteriously develops in space. The military might be developing a special weapon that leaks out of a top-secret facility. Zombies are always a popular bad guy in horror, though finding something unique in that sub-genre might be a little difficult. Use your imagination, push your boundaries, and don't feel like you have to follow a certain direction. There is no one way to write a good horror story.
Knowing how to write horror fiction means taking a personal approach to your story, using your imagination, and coming up with new impressions that will leave a frightening effect when read by your audience. Weave a plot through your story, come up with a conclusion that is satisfying for your events [not necessarily for your readers], and you'll have a tight story that people will want to read.


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This is the blog of Dr. Curt Bonk, Professor at Indiana University and President of CourseShare (there are NO Guest Blogs and NO advertisements permitted).
At 5:22 PM, Dan said…
I can't believe you don't have any comments on this yet! :)I see this as the precursor to a larger movement. With large networks of learners, it's not necessary to have these rigid start and stop times (though I do see a benefit for timed courses...I'd never finish otherwise). With a large network, you will always have people either in the same course at the same time or people willing to interact and work with those in the course. You see this dynamic in all successful online communities.The biggest problem with this model at Rio Salado is the absence of an available network. We are not at a point yet in which this can be done well by a small organization. Possibly larger organizations, such as Open University could pull this off. More likely, you will need to have large partnerships with many universities to pull this off.Without these extensive learning networks, these unbounded courses are little more than the classic self-study courses with huge dropout rates. This is noted by many in the article's comments section in relation to University of Phoenix's programs. Without some sort of grouping, it will be difficult (if not impossible) for instructors to keep up engagement with the students. This will likely result in over-dependence on interaction with the content and not people working with the content.I'm not saying that it can't be pulled off, but, at the same time, I can't imagine how it could be done well.Sorry, I didn't directly address many of your questions, but I'll leave that to others :)Enjoying following your blog Curt. Keep it up.Dan
At 10:50 PM, Curt Bonk said…
Thanks for being the first to respond here Dan and really give me good stuff to ponder. I uderstand what you mean by having an online support community and that only larger organizations or consortia of them will be able to pull this off effectively. Are you teaching at Rio Salado? I see you said "we are not at the point yet." I hope to visit you in Korea sometime in 2008.
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subset: commoncrawl


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Mother presents me daily with a myriad of lessons. However, the most common – and most painful – is the
daily hourly lesson of just how extremely selfish I truly am. Motherhood confronts every natural comfort, desire and longing. It stands in direct contrast to what comes easily to me – serving myself.
However, every now and then by grace alone, I am able to get beyond myself and tread on holy ground. Join me at a The Better Mom as I share the story of one of those times that happened a few years ago.
If you've just joined us here from The Better Mom, I want to say thank you so much for stopping by! I hope you will make yourself at home, look around awhile, and maybe even introduce yourself.


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Amino acid metabolism
Amino acids are categorized into two types - non-essential amino acids (can be synthesized by the body) and essential amino acids which cannot, and have to be provided from the diet. The non-essential amino acids are glycine, alanine, serine, asparagine, aspartic acid, glutamine, glutamic acid, proline, cysteine, tyrosine and arginine. The essential amino acids include valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, threonine, lysine and histidine.
The amino acids arginine, methionine and phenylalanine are considered essential because their rate of synthesis is insufficient to meet the growth needs of the body. Most of synthesized arginine is cleaved to form urea. Methionine is required in large amounts to produce cysteine if the latter amino acid is not adequately supplied in the diet. Similarly, phenylalanine is needed in large amounts to form tyrosine if the latter is not adequately supplied in the diet.
The amino acid pool comes from protein degradation in the gastro-intestinal tract, intracellular protein degradation and de novo synthesis and is used in protein synthesis and metabolism. Each amino acid type has its own metabolic fate and specific functions. Not only does this metabolic process generate energy, but it also generates key intermediates for the biosynthesis of certain non-essential amino acids, glucose and fat.
Synthesis of non-essential amino acids
Essential amino acids - valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, threonine, lysine and histidine - cannot be synthesized by the human body and thus have to be provided from the diet. While the amino acids arginine, methionine and phenyalanine can be synthesized by mammalian cells they are considered dietary essentials as their rate of synthesis is insufficient to meet the growth needs of the body. Methionine and phenylalanine are required in large amounts for the synthesis of cysteine and tyrosine respectively[1][2][3].
Figure 1. Pathways involved in the synthesis of non-essential amino acids glycine, alanine, serine cysteine, aspartic acid, asparagine, glutamic acid, glutamine, proline and ornithine[3]. Click for enlarged view. Enzyme abreviations: ADH18-A1: aldehyde dehydrogenase 18 family, member A1; PYCR1: pyrroline-5-carboxylate reductase 1; OAT: ornithine aminotransferase. The glycolytic intermediates 3-phosphoglycerate and pyruvate are used in the synthesis of serine, glycine, cysteine and alanine. The tricarboxylic acid cycle intermediates oxaloacetate and α-ketoglutarate are involved in the synthesis of aspartic acid, glutamic acid, asparagine, glutamine, ornithine and proline. See text for details. The synthesis of non-essential amino acids glycine, alanine, serine, asparagine, aspartic acid, glutamine, glutamic acid, proline, cysteine, tyrosine is summarised in Figure 1. Glycolysis provides two intermediates for amino acid synthesis: 3-phosphoglycerate and pyruvate[3].
Serine, Glycine and Cysteine synthesis – The NADH-linked dehydrogenase (3-phosphoglycerate dehydrogenase) converts the glycolytic intermediate 3-phosphoglycerate into the keto acid, 3-phosphohydroxypyruvate (Figure 1). Transamination of 3-phosphohydroxypyruvate by phosphoserine aminotransferase 1, utilizing glutamate as a donor, produces 3-phosphoserine, which is converted to serine by phosphoserine phosphatase [3].
Glycine is synthesised from serine in a one-step reversible reaction (catalyzed by serine hydroxymethyltransferase), that involves the transfer of the hydroxymethyl group from serine to the cofactor tetrahydrofolate, producing glycine and N5,N10-methylene- tetrahydrofolate[3].
Serine is also involved in the synthesis of cysteine (Figure 1). The sulfur for cysteine synthesis comes from the essential amino acid methionine. A condensation of ATP and methionine, catalyzed by methionine adenosyltransferase, yields S-adenosylmethionine, a precursor for several methyl transfer reactions in the body. The result of methyl transfer is the conversion of S-adenosylmethionine to S-adenosylhomocysteine which is then cleaved by adenosylhomocysteinase to yield homocysteine and adenosine. In a reaction catalyzed by the enzyme cystathionine β-synthase, the homocysteine condenses with serine to produce cystathionine, which is subsequently cleaved by cystathionine γ-lyase to produce cysteine and α-ketobutyrate[3].
Synthesis of alanine. The other glycolytic product involved in amino acid synthesis is pyruvate which on transamination by alanine transaminase (also called serum glutamate-pyruvate transaminase, SGPT), again using glutamate as nitrogen donor, generates alanine and the TCA cycle intermediate α-ketoglutarate[3](Figure 1).
Synthesis of aspartic acid and glutamic acid. The tricarboxylic acid cycle intermediates oxaloacetate and α-ketoglutarate are the ketoacids involved in the synthesis of the amino acids aspartate and glutamate by transamination[3] (Figure 1). The enzyme involved is aspartate aminotransferase (formerly called serum glutamic oxaloacetic transaminase (SGOT)). Glutamate alternatively can be synthesized by the reductive amination of α-ketoglutarate by glutamate dehydrogenase in a nitrogen-incorporating reaction and by other aminotransferase (transamination) reactions, with the amino nitrogen being donated by a number of different amino acids[3]. Examples in Figure 1 are alanine aminotransferase and ornithine aminotransferase. Thus, glutamate is a general collector of amino nitrogen[3]. Glutamate can also be formed by the deamination of glutamine by the enzyme glutaminase [3] (Figure 1).
As mentioned above aspartate is formed in a transamination reaction catalyzed by aspartate transaminase, where oxaloacetate is the amino acceptor and glutamate is the amino donor. Aspartate can also be formed by deamination of asparagine catalyzed by asparaginase [3] (Figure 1).
Synthesis of asparagine and glutamine. As shown in Figure 1, asparagine and glutamine can be synthesised from their respective α-amino acids (aspartate and glutamate) by the enzymes asparagine synthetase and glutamine synthetase [3].
Glutamine is produced from glutamate by the direct incorporation of ammonia, another nitrogen incorporating reaction[3]. Asparagine, however, is formed by a different reaction, catalyzed by an amidotransferase[3]. In contrast to aminotransferase (transamination) reactions (which are readily reversible), transamidation reactions are dependent on ATP and considered irreversible. As a consequence, the degradation of asparagine and glutamine take place by a hydrolytic pathway rather than by a reversal of the synthetic pathway by which they were formed[3]. As discussed in the previous subsection, asparagine can be degraded to aspartate by the enzyme asparaginase with the release of ammonia[3] (Figure 1).
Proline and ornithine biosynthesis. Glutamate is also the precursor of both proline and ornithine with Δ1-pyrroline-5-carboxylate serving as a branch point intermediate leading to one or the other of these two products[3] (Figure 1). While ornithine is not one of the 20 amino acids used in protein synthesis, it plays a significant role as the acceptor of carbamoyl phosphate (generated from ammonia, CO2 and ATP) in the urea cycle[4], the cycle used by humans and animals to quickly detoxify ammonia formed as a result of amino acid catabolism (see below). The production of ornithine from glutamate is important when dietary arginine, the other principal source of ornithine, is limited. The synthesis of ornithine from glutamate occurs only in the intestines[3].
Tyrosine synthesis. Tyrosine is produced in cells by hydroxylating the essential amino acid phenylalanine. The enzyme involved is the mixed-function oxygenase phenylalanine hydroxylase [3]. Half of the daily requirement for phenylalanine is for the production of tyrosine; if the diet is rich in tyrosine itself, the requirements for phenylalanine can be reduced by about 50%[3].
Amino acid catabolism
The catabolism of amino acids accounts for 10 to 15% of the human body's energy production[5]. The liver is the major site of nitrogen metabolism in the body with the potentially toxic nitrogen of amino acids eliminated via transaminations, deamination, and urea formation[3].
The urea cycle
The urea cycle (Figure 2) mediates the removal of ammonia as urea in the amount of 10 to 20 g per day in the healthy adult. This cycle was the first metabolic cycle discovered (Hans Krebs and Kurt Henseleit, 1932), five years before the discovery of the tricarboxylic acid cycle. In mammals, the urea cycle takes place primarily in the liver, and to a lesser extent in the kidney[4].
The initial two steps of the urea cycle occur in the mitochondria. The first by carbamyl phosphate synthetase, mediates the formation of carbamyl phosphate from NH3−, HCO3− and ATP. The second step is the condensation of ornithine with carbamyl phosphate by the enzyme ornithine transcarbamylase to form citrulline. The activity of this enzyme is directly related to dietary protein[4].
Figure 2. The urea cycle which serves to excrete excess nitrogen as urea in most vertebrates. Click for enlarged view. The first two steps occur in the mitochondria, the remainder in the cytosol. See text for details. Based on Hauke, 2002[1]. Citrulline is released to the cytosol, where it condenses with aspartate to form argininosuccinate via the enzyme argininosuccinate synthetase. Argininosuccinate is cleaved in the cytosol by argininosuccinate lyase, to yield fumarate, which is oxidized in the TCA cycle, and arginine, which is rapidly cleaved to urea and ornithine via the hepatic enzyme arginase. Both argininosuccinate lyase and arginase are induced by starvation, dibutyryl cAMP and corticosteroids[4].
Glucogenic and ketogenic amino acids
Depending on their metabolic fates, amino acids are referred to as 'glucogenic', 'ketogenic' or 'glucogenic and ketogenic'[5].Glucogenic amino acids are broken down into one of the following metabolites: pyruvate, α-ketoglutarate, succinyl CoA, fumarate or oxaloacetate which can be oxidized into CO2 and H2O to generate ATP via the tricarboxylic acid cycle (TCA cycle) and oxidative phosphorylation[5]. Alternatively the carbon skeletons from these metabolites can be used to synthesise glucose by the process of gluconeogenesis hence the term glucogenic amino acids.
In contrast ketogenic amino acids are broken down into acetyl-CoA and or the ketone body acetoacetate, neither of which can bring about net glucose production in humans. A third group of amino acids are catabolised to both glucogenic and ketogenic intermediates. Thirteen amino acids: glycine, alanine, serine, aspartic acid, asparagine, glutamic acid, glutamine, proline, valine, methionine, cysteine, histidine and arginine, are purely 'glucogenic'; five amino acids: tryptophan, phenylalanine, tyrosine, isoleucine and threonine are both 'glucogenic and ketogenic'; while the remaining two amino acids - lysine and leucine - are purely 'ketogenic'[5].
Catabolism of the glucogenic amino acids
Glucogenic amino acids catabolised to pyruvate: alanine, serine, glycine and cysteine
Alanine catabolism. Alanine is second only to glutamine in prominence as a circulating amino acid. In this capacity it serves a unique role in the transfer of nitrogen from peripheral tissues to the liver[3]. Alanine is transferred to the circulation by many tissues, but mainly by muscle, in which alanine is formed from pyruvate (by transamination) at a rate proportional to intracellular pyruvate levels generated by the catabolism of glycogen (glycogenolysis) and glucose (glycolysis)[3][5].
Figure 3. The glucose-alanine cycle[3]. The glucose-alanine cycle is used primarily as a mechanism for skeletal muscle to eliminate nitrogen while replenishing its energy supply. Glucose oxidation produces pyruvate which can undergo transamination to alanine. Additionally, during periods of fasting, skeletal muscle protein is degraded for the energy value of the amino acid carbons and alanine is a major amino acid in protein. The alanine then enters the blood stream and is transported to the liver. Within the liver alanine is converted back to pyruvate which is then a source of carbon atoms for gluconeogenesis. The newly formed glucose can then enter the blood for delivery back to the muscle. The amino group transported from the muscle to the liver in the form of alanine is converted to urea in the urea cycle and excreted[3].As summarised in Figure 3, the liver accumulates alanine from the blood, uses alanine transaminase to reverse the transamination that occurs in muscle regenerating pyruvate for further oxidation by the tricarboxylic acid cycle or conversion to glucose (gluconeogenesis), and proportionately increases the elimination of unwanted nitrogen (ammonia) via the urea cycle (Figure 3). When alanine transfer from muscle to liver is coupled with glucose transport from liver back to muscle, the process is known as the glucose-alanine cycle (Figure 3). The key feature of the cycle is that through a single molecule, alanine, peripheral tissues export pyruvate and ammonia to the liver, where the carbon skeleton is recycled and most nitrogen eliminated[3].
Serine catabolism – Serine catabolism involves its conversion to pyruvate and ammonia by the enzyme serine dehydratase which catalyses the β-elimination of the hydroxyl group of serine to form an amino acrylate intermediate which tautomerizes into the imine which is then hydrolyzed to produce ammonia and pyruvate[5]. Serine is glucogenic as it can be metabolized back to the glycolytic intermediate, 3-phosphoglycerate, by a pathway that is essentially a reversal of serine biosynthesis (Figure 1). However, the enzymes are different[3].
Glycine catabolism - The main glycine catabolic pathway leads to the production of CO2, ammonia, one equivalent of N5,N10-methylene tetrahydrofolate and NADH + H+. The oxidative decarboxylation is catalysed by the mitochondrial enzyme, glycine dehydrogenase (decarboxylating) which is also called the glycine cleavage complex (GCC)[3]. Glycine is classified as a glucogenic amino acid since, as shown in Figure 1, it can be converted to serine (by serine hydroxymethyltransferase) which can be converted back to the glycolytic intermediate, 3-phosphoglycerate as mentioned in the previous paragraph[3][5].
Cysteine catabolism - The major cysteine catabolic pathway in humans occurs via the action of cysteine dioxygenase type 1 (CDO1). CDO1 oxidizes the sulfhydryl group of cysteine to sulfinate, producing the intermediate cysteine sulfinate[3]. Catabolism of cysteine sulfinate proceeds through transamination (catalyzed by cytosolic aspartate transaminase) to β-sulfinylpyruvate (3-sulfinylpyruvate) which then undergoes desulfuration yielding pyruvate and bisulfite, (HSO3–) which is in equilibrium with sulfite (SO32–) at pH 7.2[3]. The enzyme sulfite oxidase then catalyzes the conversion of sulfite to sulfate.
The enzyme cysteine desulfurase is another important enzyme associated with cysteine catabolism as it removes the sulfur from cysteine yielding alanine. The sulfur remains associated with cysteine desulfurase and is subsequently transferred to numerous enzymes that possess iron-sulfur clusters for their activity. Other than protein, the most important metabolic products derived from cysteine are glutathione (GSH), the bile salt modifying compound, taurine, and as a source of the sulfur for coenzyme-A synthesis[3].
Glucogenic amino acids catabolised to oxaloacetate or α-ketoglutarate: aspartic acid, asparagine, glutamic acid, glutamine, histidine, proline, ornithine and arginine
Aspartic and glutamic acid catabolism. The acidic amino acids aspartic acid and glutamic acid are important in collecting amino nitrogen (ammonia) via the enzymes asparagine synthetase and glutamine synthetase [3] (see Figure 1). They are also important in eliminating ammonia via the urea cycle (see Figure 2). The catabolic path of the carbon skeletons involves simple 1-step aminotransferase reactions that directly produce net quantities of a TCA cycle intermediate, oxaloacetate or α-ketoglutarate[3]. The glutamate dehydrogenase reaction operating in the direction of α-ketoglutarate production provides a second avenue leading from glutamate to gluconeogenesis[3] (Figure 1).
Asparagine catabolism begins with the enzyme asparaginase which converts asparagine into ammonia and aspartate. Aspartate can serve as an amino donor in transamination reactions yielding oxaloacetate, which follows the gluconeogenic pathway to glucose[3] (Figure 1).
Glutamine catabolism involves the enzyme glutaminase, an important kidney tubule enzyme, that converts glutamine (from liver and from other tissues) to glutamate and NH4+, with the NH4+ being excreted in the urine[3]. Glutaminase activity is present in many other tissues as well, although its activity is not nearly as prominent as in the kidney. The glutamate produced from glutamine is converted to α-ketoglutarate via the action of glutamate dehydrogenase, making glutamine a glucogenic amino acid[3].
Histidine catabolism proceeds via a 4-step pathway to glutamate which begins with release of the α-amino group catalyzed by histidine ammonia-lyase (also called histidase), introducing a double bond into the molecule. As a result, the deaminated product, urocanate, is not the usual α-keto acid associated with loss of α-amino nitrogens. The end product of histidine catabolism is glutamate, making histidine one of the glucogenic amino acids[3]. The process of histidine catabolism represents, not only a catabolic reaction pathway, but a major folic acid derivative biosynthesis pathway. In the course of the catabolism, a portion of the carbon skeleton of histidine is transferred to tetrahydrofolate (THF) forming the folate derivative, N5-formimino-THF.
Ornithine and proline catabolism is essentially a reversal of their synthesis from glutamate (see Figure 1). Proline is oxidized back to Δ1-pyrroline-5-carboxylate via the action of proline dehydrogenase. Ornithine can be deaminated to Δ1-pyrroline-5-carboxylate via a reversal of the ornithine aminotransferase reaction. The resulting Δ1-pyrroline-5-carboxylate is oxidized to glutamate via the action of aldehyde dehydrogenase 4 family, member A1, (also called delta-1-pyrroline-5-carboxylate dehydrogenase)[3].
Arginine catabolism involves several pathways, with the major catabolic pathway being its cleavage by the enzyme arginase [3][4][5] to form ornithine and urea in the urea cycle (Figure 2). The enzyme ornithine δ-aminotransferase transfers the δ-aminogroup of ornithine to α-ketoglutarate to form glutamate and glutamate γ-semialdehyde, the latter being converted to a second molecule of glutamate by the enzyme glutamate-5-semialdehyde dehydrogenase [3][5] (Figure 1). The glutamate can be converted to α-ketoglutarate for further metabolism as described above.
In some tissues arginine serves as the precursor for nitric oxide (NO) production via the action of nitric oxide synthase [3]. The citrulline byproduct of the NOS reaction can feed back into arginine synthesis via the hepatic urea cycle enzymes argininosuccinate synthetase (ASS1) and argininosuccinate lyase (ASL). Arginine also serves as the precursor for creatine synthesis and, therefore, arginine can be excreted in the urine as the creatine byproduct, creatinine. The cycling of citrulline back to arginine involves the urea cycle enzymes, argininosuccinate synthetase and argininosuccinate lyase [3] (Figure 2).
Glucogenic amino acids catabolised to succinyl CoA: methionine, valine and in humans, threonine
Methionine catabolism involves nine steps[5]. The first step is catalyzed by methionine adenosyl transferase which tranfers the adenosyl group of ATP to the sulfur of methionine to form S-adenosylmethionine (SAM). SAM methylase transfers the activated methyl group to an acceptor to form S-adenosylhomocysteine which is hydrolyzed by adenosylhomocysteinase to form homocysteine. Cystathionine β-synthase catalyzes the condensation of a serine residue with homocysteine to form cystathionine. Cystathioniine γ-lyase cleaves cystathionine into cysteine and α-ketobutyrate, the latter being converted into propionyl CoA by α-ketobutyrate dehydrogenase [5].
The propionyl-CoA is converted, via a mitochondrially-localized three reaction ATP-dependent pathway, to succinyl-CoA which can then enter the TCA cycle for further oxidation. The enzymes required for this conversion are propionyl-CoA carboxylase, methylmalonyl-CoA epimerase, and methylmalonyl-CoA mutase, respectively. This propionyl-CoA conversion pathway to succinyl CoA is also required for the metabolism of the amino acids valine, isoleucine, and threonine and the odd-chain fatty acids[3].
Valine catabolism. The catabolism of valine[6] is similar to that of the other branched chain amino acids, isoleucine (a 'glucogenic and ketogenic' amino acid) and leucine (a 'ketogenic' amino acid) [3][5] as shown in Figure 4.
Figure 4. The catabolism of branched-chain amino acids valine, isoleucine and leucine[5,6]. Click for enlarged view. The first two steps involve the same enzymes for all three amino acids, after that the pathways diverge and use different enzymes. See text for details. While most amino acid catabolism occurs in the liver, that of branched-chain amino acids such as isoleucine, leucine and valine is not, due to the absence in liver of the first enzyme in their catabolic pathways - branched chain amino acid transferase (BCAT) [5]. Valine, isoleucine and leucine are catabolized mainly in muscle, adipose tissue, kidney and brain[5]. Branched-chain amino acid (BCAA) catabolism yields both NADH and FADH2 which can be utilized for ATP generation which is a primary reason for their high rates of catabolism in skeletal muscle[3].
The catabolism of all three of these amino acids uses the same enzymes in the first two steps[3][5][6]. The first step in each case is a transamination using one of two branched-chain aminotransferase, (BCATc or BCATm) with α-ketoglutarate as amine acceptor (Figure 4). The resulting α-ketoacids are then oxidatively decarboxylated via the action of the enzyme complex, branched-chain ketoacid dehydrogenase (BCKD). The BCKD reaction generates the CoA derivatives of the decarboxylated ketoacids while also generating the reduced electron carrier, NADH. After these first two reactions the catabolic pathways for the three amino acids diverge (Figure 4). The third reaction of valine amino acid catabolism involves a dehydrogenation step catalysed by isobutyryl-CoA dehydrogenase (IBD) [6] to form mathylacrylyl CoA and the reduced electron carrier FADH2. As shown in Figure 4 the catabolism of valine involves four additional enzymic reactions carried out by the enzymes methacrylyl CoA hydratase, hydroxyisobutyryl CoA hydrolase and methylmalonate semialdehyde dehydrogenase, that culminate in the production of propionyl CoA[6]. The propionyl CoA can be then converted to succinyl-CoA via a mitochondrially-localized three reaction ATP-dependent pathway involving propionyl-CoA carboxylase, methylmalonyl-CoA epimerase, and methylmalonyl-CoA mutase. Succinyl CoA can enter the TCA cycle for further oxidation or after conversion to oxaloacetate, be metabolised to glucose via gluconeogenesis[3][5].
Threonine catabolism. While there are three catabolic pathways for threonine in mammals only one appears important in humans[3]. This pathway involves glycine-independent serine/threonine dehydratase yielding α-ketobutyrate which is further catabolized to propionyl-CoA. Serine/threonine dehydratase is expressed at high levels only in the liver[3]. The resulting propionyl-CoA is converted to succinyl-CoA for further oxidation or conversion to glucose as discussed above.
A second threonine catabolism pathway in mammals involves the enzymes threonine dehydrogenase and α-amino-β-ketobutyrate lyase resulting in the conversion of threonine to acetyl CoA (a ketogenic product) and glycine (a glucogenic product that can be converted to serine and then back to the glycolytic intermediate 3-phosphoglycerate by a pathway that is essentially a reversal of the serine biosynthesis pathway (Figure 1)). However the enzymes are different[3]. This pathway, that yields both ketogenic and glucogenic products, does not appear to be functional in humans because the human gene for threonine dehydrogenase contains three inactivating mutations and is non-functional[3]. Thus in humans threonine can be considered purely glucogenic.
Catabolism of the 'glucogenic and ketogenic' amino acids: threonine, isoleucine, phenylalanine, tyrosine and tryptophan.
Threonine catabolism. There are alternate catabolic pathways for threonine in mammals that lead to the production of either propionyl CoA (glucogenic) or acetyl CoA (ketogenic), and glycine (glucogenic) as end products. However, as discussed in the preceding section, only one, the glucogenic propionyl CoA pathway, appears to be important in humans[3][5].
Isoleucine catabolism is similar to that of the other branched-chain amino acids (BCAA) valine (glucogenic) and leucine (ketogenic) and occurs predominantly in skeletal muscle. BCAA catabolism yields both NADH and FADH2 which can be utilized for ATP generation which is a primary reason for their high rates of catabolism in skeletal muscle[3]. As summarized in Figure 5, the first step in the catabolism of isoleucine is a transamination using a pyridoxal phosphate-dependent BCAA aminotransferase (termed a branched-chain aminotransferase, BCAT), with α-ketoglutarate as amine acceptor. The resulting α-keto-β-methylvalerate is then oxidatively decarboxylated via the action of the enzyme complex, branched-chain ketoacid dehydrogenase (BCKD). The BCKD reaction generates α-methylbutyryl CoA and NADH. The third reaction of branched-chain amino acid catabolism involves a dehydrogenation step carried out by the enzyme short/branched-chain acyl-CoA dehydrogenase (SBCAD) yielding tiglyl CoA and FADH2. The final three reactions in isoleucine catabolism involve the three enzymes involved in the terminal steps of fatty acid oxidation - enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-ketoacyl-CoA thiolase which convert tiglyl CoA to acetyl CoA (ketogenic) and propionyl CoA (glucogenic). The former can gives rise to ketone bodies while the latter can be converted to succinyl CoA for further oxidation or conversion to glucose as discussed above in the section on valine catabolism[3][5][6]. The second last reaction, by 3-hydroxyacyl-CoA dehydrogenase, generates NADH + H+ for ATP synthesis via oxidative phosphorylation.
Figure 5. Catabolic pathway for phenylalanine and tyrosine catabolism[5]. Click to enlarge. See text for details. Source: ref [5].Phenylalanine and tyrosine catabolism. The degradation of aromatic amino acids requires molecular oxygen to break down the aromatic rings[5]. As shown in Figure 5 the degradation of phenylalanine begins with a monooxygenase, phenylalanine hydroxylase which adds a hydroxyl group to phenylalanine to form tyrosine[5]. From there the remaining five catabolic pathways for phenylalanine and tyrosine are the same. Tyrosine aminotransferase deaminates tyrosine to form p-hydroxyphenylpyruvate which is converted into homogentisate by the enzyme p-hydroxyphenylpyruvate dioxygenase [5]. The final three steps in the catabolism of tyrosine and phenylalanine are carried out by the enzymes homogentisate 1,2-dioxygenase, maleylacetoacetate isomerase and fumarylacetoacetate hydrolase resulting in the production of fumarate (glucogenic) and acetoacetate (ketogenic)[5].
Tryptophan catabolism. The catabolism of tryptophan in humans is complex[7] with one major pathway resulting in the formation of acetoacetyl CoA, the precursor of ketone bodies - acetoacetate, 3-hydroxybutyrate and acetone[3][5]. As shown in Figure 6, tryptophan catabolism includes the generation of the glucogenic amino acid alanine, which allows tryptophan to be classified as a 'glucogenic and ketogenic' amino acid[3]. The tryptophan catabolic pathway starts with either tryptophan 2,3-dioxygenase, or indoleamine 2,3-dioxygenase 1 which open the indole ring to form N-formyl-kynurenine[3][5]. N -formyl-kynurenine is then converted to kynurenine by the enzyme, arylformamidase (also called kynurenine formamidase ) [3][5].
Figure 6. Simplified pathway of tryptophan catabolism[5]. Click for enlarged view. See text for details. Source: ref [5].As shown in Figure 6, kynurenine then undergoes a series of catabolic reactions resulting in complete oxidation to acetoacetyl-CoA[3][5]. The first is catalyzed by kynurenine hydroxylase (also called kynurenine 3-monooxygenase) forming 3-hydroxykynurenine. The next step in the pathway is catalyzed by kynureninase and produces 3-hydroxyanthranilic acid and the amino acid alanine hence the classification of tryptophan as a 'glucogenic and ketogenic' amino acid. The next step in the pathway is the conversion of 3-hydroxyanthranilic acid to 2-amino-3-carboxymuconate-6-semialdehyde (ACMS) and quinolinic acid by the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. ACMS can be metabolized via the action of the enzyme ACMS decarboxylase followed by 10 other enzymes to acetoacetyl-CoA, the end product of complete tryptophan catabolism[3][5].
Aside from its role as an amino acid in protein biosynthesis, tryptophan also serves as a precursor for the synthesis of the neurotransmitters serotonin and melatonin and kynurenine also serves as an important intermediate in the pathway for the synthesis of the nicotinamide adenine dinucleotide co-factors, NAD+ and NADP+[3].
Catabolism of the ketogenic amino acids lysine and leucine.
Lysine catabolism. Lysine and leucine are the only two amino acids that are purely ketogenic[5]. The primary pathway of lysine catabolism in the liver is one that begins with the formation of the adduct between lysine and α-ketoglutarate called saccharopine. The formation of saccharopine and its hydrolysis to α-aminoadipic-6-semialdehyde is catalyzed by the bifunctional enzyme α-aminoadipic semialdehyde synthase. This reaction results in the amino nitrogen remaining with the α-carbon of α-ketoglutarate, producing glutamate and α-aminoadipic-6-semialdehyde. Because this transamination reaction is not reversible, lysine is an essential amino acid [3][5]. The ultimate end-product of lysine catabolism is acetoacetyl CoA[3] which can be further converted in the liver to the Ketone bodies acetoacetate, 3-hydroxybutyrate and acetone.
Leucine catabolism As summarised in Figure 4, leucine catabolism, like that of the other branched-chain amino acids valine and isoleucine, begins with transamination by a branched amino acid aminotransferase to form α-ketoisocaproate which is then oxidatively decarboxylated to form isovaleryl CoA by the branched chain α-ketoacid dehydrogenase complex [3][5]. In the next step isovaleryl CoA is dehydrogenated to form 3-methylcrotonyl CoA. The enzyme that catalyzes this dehydrogenation is isovaleryl CoA dehydrogenase. 3-Methylcrotonyl CoA is then carboxylated by a biotin containing enzyme called methylcrotonyl CoA carboxylase. This two-step reaction involves the ATP-dependent carboxylation of the biotin cofactor with bicarbonate serving as the source of CO2 and the transfer of the carboxyl group to 3-methylcrotonyl CoA to form 3-methylglutaconyl CoA. 3-methylglutaconyl CoA is then hydrated by 3-methylglutaconyl CoA hydratase to form 3-hydroxy-3-methylglutaryl CoA which can be cleaved into acetyl CoA and acetoacetate by the enzyme 3-hydroxy-3-methylglutaryl CoA lyase [3][5] (Figure 4).
^ Haucke V, Protein Turnover & Amino Acid Catabolism, In: Berg JM et al,, Biochemistry, 5th ed., Chapter 23; 2002, WH Freeman, New York.
^ Protein Degradation https://www.rpi.edu/dept/bcbp/molbiochem/MBWeb/mb2/part1/protease.htm
^ Amino acid synthesis and metabolism - http://themedicalbiochemistrypage.org/amino-acid-metabolism.php
^ Urea cycle - http://www.ncbi.nlm.nih.gov/books/NBK27982/
^ Miles B, Amino acid degradation - https://www.google.com.au/?gws_rd=ssl#q=Miles+Amino+acid+catabolism
^ Taniguchi K et al., The valine catabolic pathway in human liver: effect of cirrhosis on enzyme activities. Hepatology 1996; 24:1395-1398.
^ Tryptophan metabolic pathways - http://www.genome.jp/kegg/pathway/map/map00380.html


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Friday, September 20, 2013
Space 1889: Soldier's Companion First Impressions
I acquired Soldier's Companion (in dead tree) a few years ago, around the same time I acquired some French Foreign Legion and Lizard Men in 15mm. I really wanted the book more for source material / campaign background ideas than for gaming and so, while i read them, it was never with the intent of actually playing the rules, either wargame or as RPG.
But, as part of the Save a Dead Tree project, I decided to spend some time with them and actually use them.
Last night, I had a chance to break out a half-warband of lizard warriors and a squad of Prussian infantry (aka my imagi-nation of Riesling) to try out the basics of the rules.
[As an aside, it was great seeing these figures again. It has been quite some time since I brought them out last and it was a bit like going home. Victorian Sci-Fi / Darkest Africa type games were some of the first I really invested time in. For a long time, the lizard folk were my largest force]
Wow. It sucks to be irregular infantry armed only with melee weapons.
Initiative is 1d6 for each side, highest score of result + modifiers goes first. As it turns out, regular vs. irregular get a +1 bonus right off the bat.
Only the winner of initiative does any moving - the loser can defensive fire or participate in any melee it's dragged into, but can't instigate any of its own.
In my first quick setup, the lizard folk were in the open, possibly a charge distance away - they never moved and were shot to pieces. Even with the long range penalty, they dropped like flies. Morale didn't even allow them to flee.
Speaking of morale, it's not entirely clear to me whether or not casualties count on successive morale checks or only in the turn in which they occur. As written, it sounds to me like the latter, which led to the unusual situation of 2 lizard warriors passing morale checks when a comrade was dropped.
For the second setup, I took Mr. Chadwick's advice on playing irregular's from his Designer Notes chapter, and had the lizard folk ambush the Riesling soldiers. By starting hidden, they could automatically steal the initiative.
If I am reading the rules correctly, defensive fire occurs before melee and so charging troops can be shot up at any point along their charge path. The result is that the lizard folk were stopped halfway to their objective, having failed their morale check.
Although it looked like it'd be a repeat of the first test there on out, luck was on the lizard warriors' side and they won the initiative several times - but troops that are "checked" (failed their morale) can't act in the remainder of the turn in which they are checked, or in the entire turn after, so much of those wins were negated.
I think it was in my Intro. to Philosophy class that we talked about two runners, who having run halfway to the finish line, run half of the remaining distance to reach it, and then half of that again, and so on, but never reach the end (because you can split numbers in half infinitely) - obviously physical objects can travel distances, so something is up.
Anyway, that's how the lizard warriors advanced, never quite making it close enough to contact the European troops. And in the end, they were slaughtered.
I want to try some bow armed irregulars next, because at least they can attack from a distance.
My goal is to play the Martian Messiah scenario from the rule book, reskinned for Helvetica and then go from there for perhaps a mini-campaign.
6 comments:
That's Xeno's Paradox. :)ReplyDelete
Sounds like fun.Replies
That's it! I could not for the life of me remember the name!
On the face of it, the usual result when irregulars take on European Colonials. Fun, for the guys with superior fire power; for the irregulars, not so much.ReplyDelete
But, think Zulu wars. What if the lizards attack in several impis, from different directions? Johnny Colonial's fire is split and he then runs the real risk of being over run!Replies
Hi Kobold,Delete
Thanks for the comment!
For the scenario I ran most recently (Helvetican Messiah), the lizard warband split, and that might have been effective were it not for an oddity in the rules (or my application of them) which resulted in my imperial force getting a better position than when they were ambushed into melee.
I think for a larger force this would have worked well.
I agree with Kobold. At 1:1 the scalies are going to drop like flies. Try 3:1 instead. I ran a game at Cangames in Ottawa this year and also ran into some initiative issues. See http://irregularwarbandfast.blogspot.ca/2013/06/cangames-day-iiii-day-iii.html for a suggestion from Oerjan in the comments.ReplyDelete
Another question would be did you give the lizards any field craft? That can help quite a bit.Replies
Hi Pat G,Delete
In this little sample, I didn't put the lizard anywhere that Fieldcraft would have helped. When they did ambush from suitable cover, I failed to flank the Riesling force and they were thus able to shoot at the attackers. In the actual full game I just ran though, the Fieldcraft helped quite a bit in keeping the lizard warriors alive.
Ordinarily if I'm playing natives vs colonial troops, I shoot for 3:1, but when I was doing these little tests, I already knew the scenario called for around 2 to one. In retrospect, I should have gone with my gut and upped it to 3:1.
Thank you for the link. A great looking game by the way! I like the initiative suggestions. Although I wanted to play more or less rules as written the first time, this might be something to consider as a tweak to make the rules salvageable for future use.


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Monday, July 13, 2015
Alternative Stitching
That being said, my daughter sent me a photo and asked if I would crochet a Cabbage Patch wig for the newest baby. What??? Crochet??? I dug out the old rusty hooks and got busy. It's nice to have a baby doll for a model.
While Googling for a pattern, I came across a cute little Minion beanie on You Tube – also in crochet! Since I was on a crochet roll I figured I'd give it a try as well. It was a huge hit with the grandchildren. Now I have requests for a few more. Guess I may be doing a bit more crochet in the days ahead.
I'll be linking this up with Beth's Monday Makings.
24 comments:
- Sandie @ crazy'boutquilts said...
Love the minion hat and model! Very cute!
- July 13, 2015 at 1:52 PM
- Jeanna said...
Oh. my. goodness! Mary, the minion is just too cute. You do amazing crochet. I'm sure all of the grands are going to want one.
- July 13, 2015 at 3:21 PM
- quiltmania said...
Lol! They are adorable. Really worth dusting off your crochet hook for.
- July 13, 2015 at 4:37 PM
- creativity amongst chaos said...
Oh my goodness... how adorable! I too love crochet, and I don't make near enough time for it. What a couple of treasures...the minion - well I have a little guy that would love that! So glad you brought out the hook, it reminds me how much fun it can be....and I will have to make some more cats..lol. Have a wonderful week Mary! ~Cori
- July 13, 2015 at 4:45 PM
- Maria said...
No I don't do crochet but your wee hats are sew cute... The Minon Hat looks great on the little fella. Love to see the new babe with the cabbage patch hat on too...
- July 13, 2015 at 5:03 PM
- beth s said...
Oh those hats are TOO fun! You'll be busy for sure. ;)
- July 13, 2015 at 5:15 PM
- Kate said...
The Minion beanie is just too cute! You'll be the favorite grandmother after making all of those.
- July 13, 2015 at 5:36 PM
- Nat Palaskas said...
So cute! Don't you wish you could photocopy them each time you get a request? Hugs Nat
- July 13, 2015 at 10:19 PM
- OPQuilt said...
That Minion hat is the greatest! (or, as my granddaughter would say: It's the bomb!) You have more skills than anyone I know--always able to pick up any needlework that needs doing. The Cabbage patch wig is very cute, too. Love the bows!
- July 14, 2015 at 8:43 AM
- Michele said...
Very cute and I'm betting we'll be seeing more and more Minions things on the web in the coming weeks and months.
- July 15, 2015 at 4:32 AM
- barcord said...
The minion hat is so funny. However, I just love the cabbage patch wig. My question is, why does a very small baby need a cabbage patch wig. I would love to see that picture.lol.
- July 15, 2015 at 6:56 AM
- My Sister Made Me Do It.... said...
Is there no limit to what you can do?? LOL......Like you, I have put my crochet hooks away....but not forever....it is fun to do something different every once in awhile! Today is Mom's 93rd birthday! Off to bake her a cake!
- July 15, 2015 at 8:00 AM
- Soma Acharya said...
LOL!! The hats are so cute!! Yes, I daresay that you will be doing a LOT more crocheting in the future :)
- July 15, 2015 at 1:02 PM
- Rhonda said...
You did an excellent job. You'll be getting requests for quite some time!!
- July 16, 2015 at 1:19 AM
- Susan said...
They are both so cute! Nice job!
- July 16, 2015 at 5:14 AM
- Teresa in Music City said...
OMG - I remember making cabbage patch dolls! I made several for my daughter and then a few for her friends. I never made clothes for them though - they wanted the ones they saw in the stores :) That's one adorable set of curls you crocheted my friend!!! And my little grandson is nuts about the minions right now, but I'm afraid he would be on to something else by the time I got one of those caps crocheted :)
- July 16, 2015 at 7:16 AM
- Mdm Samm said...
Ohhh Mary, I love this post filled with you and your lovely entourage minions at their best
- July 17, 2015 at 8:17 AM
- Lara B. said...
You are on a roll Mary! The cabbage patch wig is so funny! And the minion hats are sure to be a big hit with everyone!
- July 17, 2015 at 3:27 PM
- Karen Walker said...
How funny!
- July 22, 2015 at 6:51 AM
- Live a Colorful Life said...
The minion beanie is awesome! I know of a couple little ones of my own who would love this one.
- July 22, 2015 at 3:56 PM
- Raewyn said...
Gorgeous beanies! Those are the sorts of things my kids keep requesting I make for the yet-to-be-born-grandbabies!!
- July 23, 2015 at 9:59 PM
- Michele said...
Looks like everyone had a blast!! You can't go wrong with Minions! Those hats are adorable!!!! I just saw a Minion Flash Drive in Walgreens. Unfortunately my teen son wasn't interested in it.
- July 26, 2015 at 11:00 AM
- Carol said...
Those are just the cutest crocheted hats! My grandson would love that minion one!
- August 1, 2015 at 5:56 AM
- ✾Jamie Lee Cooley✾ said...
Cute minion hat! My daughter Esther says she wants one too:)
- August 27, 2015 at 3:16 PM


text:
Adopt a child and save a child
People with everything doesn't value it and the one who doesn't have, they struggle to get it. Value what you have and what you are capable of.
A couple who want's a baby in their life but couldn't have due to any health issue can adopt one. Even though if a couple is physically capable of reproducing should also adopt a child or if a person is financially good should take the responsibility of an orphan kid's education. If everyone will start thinking in this manner there is no more a need of orphanage in our country. Every child is special in it's own way.


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Stuffed Animals Details
** Stuffed Greyhound
** Dark Brindle Body with White Chest and Paws
** Made by Douglas Toys
** 13 inch
Greyhounds aren't just a nationwide bus system you know, though the bus line did take as their mascot and logo, this very dog. Having ridden on a Greyhound bus before, we can tell you with no uncertainty that they should maybe have taken the turtle as their logo. We were nine hours late this one time. But we digress.
Douglas Toy brings the wiry grace, speed and agility of the greyhound to life in their Classics collection with this 13-inch long greyhound.
Greys are sighthounds, which was important in their old profession, as companions to hunters. They tracked prey by sight and sped along swiftly to chase it down and keep it cornered until the dogs' slow human masters could come up behind. A greyhound at their peak can reach up to 39 miles per hour/63 kilometers per hour. Few dogs can boast that ability. Deep chests, slim builds and flexible spines keep them supple and swift. But in addition to being a four-legged version of The Flash, these canines make sweet and loving companions and family pets.
Douglas' captures the charm and docile nature like few other toy makers could. Just look at that soft coat, that slim profile. This stuffed Greyhound begs to run and play with you, but is just as comfortable sitting at home, snuggled up on the couch. Unlike some breeds, he doesn't have boundless energy. His strength comes in his speed, not his endurance. But that doesn't mean he won't love you forever if you give him snuggles and a treat now and again.


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The Globe has positions for editors and reporters. All must currently be enrolled in academic classes at the Germantown campus.
Reporters primarily write the articles that appear in the newspaper and may not work on every edition. They may cover a particular beat such as Student Senate or athletics, or they may be assigned a topic by the editors. They will be asked to attend occasional editorial meetings and a training session at the beginning of the semester. Depending on the number of articles they write during the semester, they will receive a small stipend for their participation. No experience is necessary to be a reporter, but individuals must have strong writing skills, be reliable in meeting commitments, and be comfortable working on their own in getting information for their assigned articles.
Editors have a more time-consuming job and perform a variety of tasks: the editor-in-chief has overall responsibility for the paper. A news editor works with reporters on assigning articles, ensuring they are delivered on time, and edits copy received. A layout editor does the actual layout of the paper and must have some software and graphics ability. Editors may also write articles for The Globe. They must be available to attend bi-weekly editorial meetings in addition to their academic classes. Editors must also have strong writing skills and be reliable in meeting deadlines and working independently. Preference is given to individuals with experience working on a newspaper although training can be given to those without experience. It is preferred that individuals in editorial positions do not work outside of the college. Presuming they fulfill the requirements of their position, they will receive a significant stipend at the end of the semester.
To apply for a position on The Globe, click below to fill out and submit online application:
© 2019 Montgomery College. All Rights Reserved.
©2019, Montgomery College


text: Joey Hess wrote: > > This is your third and final reminder. I count 542 packages remaining, > down only 9 from last month. I assume most of the people below do not > read debian-devel, so I've taken the librerty of BCCing you all. :-P > > Debian Apache Maintainers <email@example.com> > apache2 apache2 will be fixed when 2.0.55 is released upstream and I upload it to sid (which is due to happen any day now). I didn't see the point in an upload just to fix this issue. ... Adam


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"I am going to kill you," her assailant screamed at her as he relentlessly pummeled and punched and kicked her.
Beryl Esterhuizen was attacked in her home at about 10:30 on Thursday morning (21/07)
THE determination to survive and the grace of God is what saved a 72-year-old woman from Odendaalsrus from certain death.
"I am going to kill you," her assailant screamed at her as he relentlessly pummeled and punched and kicked her.
The woman was attacked in her home at about 10:30 on Thursday morning (21/07).
Beryl Esterhuizen was overpowered in the spare bedroom of her home by a man with murderous intent. Esterhuizen says she heard one of her dogs barking.
"I was in the spare bathroom. As I came into the bedroom, he overpowered me."
Esterhuizen says the man was big and he had a stubbly beard and a moustache.
"It was like a circle on his face.
"I fought back with every ounce of fight I had in me. I am sure I broke two of his fingers. I was bending them and I heard something snap. I offered him money if he would let me live.
"I must have said about five times, if you let me go, I will give you money. But he was adamant he wanted me dead."
Esterhuizen says he eventually had her down on the floor.
"That's when I grabbed his knackers and squeezed very hard. He put his foot on the side of my face and ground it hard into my flesh. I did not let go and he backed off. He threw the spare bed on top of me before leaving the room. I just lay there quietly as if I was dead, just in case he came back. The next thing I heard my neighbour, Isabel (Janse van Rensburg). She was standing over me asking me why I was lying under the bed."
Estehuizen says her neighbour had heard her shouting.
"She thought I had fallen and came to my rescue. She did not realise that I was actually being attacked."
Her neighbour notified friends of Esterhuizen' s ordeal. She tried to phone the police. Among others, Bunny and Brian House rushed from Riebeeckstad (15 minutes away) to be with her.
"It was only when we eventually threatened the police with Vista that they came to the scene. That must have been one and a half hours later," says Bunny House.
Esterhuizen was admitted to hospital, but released on the same day. She had sustained a concussion and severe abrasions and lacerations.
Capt. Stephen Thakeng of the Welkom police has confirmed the incident. He says that the police did not take as long to get to Esterhuizen as was alleged.
"The vehicle that attends to complaints was at the culpable homicide case, where a pedestrian was hit and died.
"The station commander, Col. Disebo Cezula, immediately took her private vehicle to the scene.
"So it is very clear that we did not take one and a half hour to attend to the complaint," says Thakeng.
According to Thakeng, the man was wearing a balaclava when he overpowered Esterhuizen in the kitchen.
Esterhuizen is recuperating at home. She is being supported by her grandson Keith Shannon and his wife, Leandri.
"Gran is a fighter. She has always taught us to be strong," says Keith.


text:
Brooklyn, New York
Secret Mausoleum Club: The First Gathering
The most secret gatherings in New York City have been under lock-and-key for centuries, until now.
The start of summer comes with the thrill of a roller coaster ride – it smells like sea and sunscreen, sounds like a hot grill, and feels like a carnival. Our debut gathering of the Secret Mausoleum Club pays homage to the start of summer and the visionaries of amusements found within Green-Wood Cemetery's walls.
A peaceful hush falls over Green-Wood's grounds each night as the gates close. It is in that near-darkness when the members of the Secret Mausoleum Club congregate; as centuries-old monuments stand guard over those laid to permanently rest within. Following the success of the annual Into The Veil festival, Atlas Obscura and Green-Wood Cemetery are collaborating this year to present The Secret Mausoleum Club, opening Green-Wood's historic gates and selected mausoleums for an extraordinary series of intimate after-hours immersive experiences.
Each exclusive evening has been specially curated to celebrate legends, legacies, and lore, and each meeting will feature a unique mausoleum with programming inspired by the surroundings. Clues shared before each event will help guests decipher the night's theme. Take in an inspiring performance and a historic persona or two – an evening of surprising discoveries awaits.
- Your ticket includes an open wine, beer, and special cocktail bar from local favorite Sea Witch Tavern. A special after-party will commence at Sea Witch in the hours following the event with Secret Mausoleum Club drink specials.
- This event is strictly 21+; I.D. required. Cocktail attire and carnival-themed accessorization is encouraged, as is sensible footware. Keep in mind that the cemetery can get quite chilly at night.
This event meets at the Fort Hamilton Entrance, and not the main gate of the cemetery. The entrance is located at Fort Hamilton Parkway and Micieli Place.
Email email@example.com.
Stay connected! Subscribe to Atlas Obscura's New York Obscura Society newsletter and like our Facebook page for a first glimpse at upcoming events.
Advance Tickets Only. All Sales Final. No Refunds or Exchanges.


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If you do have an account with 32 Red Casino, you may with to consider closing it to have your voice heard. Only then will they perhaps see the error of their ways.


text:
Rep. Hunter Warns Against Opening The Military To "Transgenders" And "Hermaphrodites"
During his State of the Union address, President Obama announced his intention to overturn the military's "Don't Ask, Don't Tell" (DADT) policy in 2010. "This year, I will work with Congress and our military to finally repeal the law that denies gay Americans the right to serve the country they love because of who they are," he declared. "It's the right thing to do."
Predictably, conservatives are opposing the push to repeal the discriminatory policy. Despite the fact that top military brass, including Joint Chiefs of Staff Chairman Adm. Mike Mullen, firmly agree with Obama, congressional Republicans are fear mongering about the effects of allowing gay men and women to serve openly.
On NPR yesterday, Rep. Duncan Hunter (R-CA) was asked why he believes DADT should remain in place. Hunter, a former marine, said that it would hurt the "special bond" between soldiers "if you open up the military to transgenders, to hermaphrodites, to gays and lesbians."
HOST: You are not in favor of a repeal of "Don't Ask, Don't Tell." Why not?
HUNTER: Well, because I think that it's bad for the cohesiveness and the unity of the military units, especially that are in close combat -- that are in close quarters in country right now. It's not the time to do it. It's -- the military is not civilian life, and I think the folks that have been in the military that have been in these very close situations with each other -- there has to be a special bond there, and I think that that bond is broken if you open up to the military to transgenders, to hermaphrodites, to gays and lesbians.
Of course, being a "hermaphrodite" has absolutely nothing to do sexual orientation. As Autumn Sandeen writes, "repealing Don't Ask, Don't Tell is not going to result in transsexuals -- or other transgender people -- the ability to serve openly in the U.S. military. And, perhaps this may be news to Rep. Hunter, but intersex conditions are not a sexual preference; I'm pretty damn sure too that intersex people are already allowed to serve in the military."


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Because of India's close historical partnership with Wonderful Britain, you can also locate English brands of some goods not accessible in typical groceries. For a lot more bargains, never forget to verify out our Plus Size Clothes Sale section and Clearance Plus Size Clothing section! The Plus Size Active Wear lens highlights some of the ideal on-line vendors for plus size active wear. Love yoga and hiking – 1 of the ideal activewear brands I've identified that fits my 3x/4x physique is Zella, at Nordstroms.
Thai ladies do have the benefit of getting in a position to stay petite and lithe for the duration of their lifetime, so practically any style of clothing looks very good on them. There are thousands of women's clothing on eBay and sizes for each physique kind, including Misses, Petites, Plus and Juniors. It does provide international shipping, although there are some restrictions (primarily based on brands).
They are iconic and the most recognized and respected brands of UK. FCUK established in 1972 and manufactures fashionable males and women clothing. I have sold used women's clothing on eBay belonging to my girl friend but I did not get much for them. Forever 21 is a very-acclaimed retailer of trendy and higher-quality clothing that's been regarded as amongst the best in the style planet. Elie Tahari – the nature and position in life determined the philosophy of designer brands. This French style residence was founded by Coco Chanel (CC logo) in 1925 and has been the epitome of haute couture and luxury brands ever considering that.
Charlotte Russe , a San Francisco, California-based, specialty clothes retail store operator, is popularly recognized for its economical yet chic array of retro and contemporary clothes products, footwear and accessories which the avid fashionistas would adore digging their hands into. Charlotte Russe focuses mostly on dresses and other clothing products and also gives a little collection of accessories (mainly jewelry) and swimwear.


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I'm sure that if you frequent a lot of Cricut themed sites, you have probably run across Everyday Cricut. I was so inspired by their Saturday Designer's Post. If you haven't seen Monique Griffith's blog MonkeyDoodle Cricut - you should check it out. Her projects are beautiful - she has a great sense of color and utilizes every space in her layouts. Since I'm so new to scrapbooking (about one month into it at this point), I'm not really sure whether or not I have found my "style" yet, so I made a compromise with myself - one week of super girly themed projects - but I had to try some new techniques. (Roughly translated...I can't glitter EVERYTHING!)
"Scrap-lifting" did not come without a few consequences - I cut my finger open using my x-acto knife while trying to cut the cupcake out to accent the top of the journaling space, I had no idea how hard making little stitch lines would be and the layout took me a whopping 2 hours to complete. Whew! Trying out new things takes a lot of time!
Materials Used:
- 12 x 12 base - brown cardstock from DCWV Cardstock Stack
- 12 x 12 frame cut at 10" from Gypsy Wanderings - DCWV Sweet Stack
- Flower Mat cut at 8.32 from Storybook - welded along with the 12 x 12 frame - DCWV Sweet Stack
- Accent Strip cut at +++ x 12 - DCWV Sweet Stack
- Photo Mats cut at 4 1/2 x 6 1/2 & 4 1/4 x 6 1/4 from George and Basic Shapes
- Journaling Mats cut at 3 1/4", 3 3/4", and 4" from George and Basic Shapes - attached with pop dots
- "If the Crown Fits" sentiment cut at 2" from Once Upon a Princess - attached with pop dots
- Ice Cream Cone cut at 1" from Once Upon a Princess - attached with pop dots (please note that I think there was at some point a stem for the cherry, but it got lost somehow, so I drew the stem)
- Cupcake cut at 1 1/2" from Once Upon a Princess - attached with pop dots
- Balloons cut at 2 1/4" from Once Upon a Princess - attached with pop dots (please note that the balloons' strings tore twice when I cut them, so I decided to give up and draw in their strings)
- "2" in crown cut at 2 3/4" from Once Upon a Princess (font) - attached with pop dots
- Tsukineko Pigment Ink - Cosmic Copper
- Sakura Gelly Roll Pen - White
- Turquoise jewels - K & Co


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If you're looking for ways to improve your backyard this summer, then you should consider installing a fire pit. Having a fire pit allows you to spend more time with friends and family out in your yard even after the sun has gone down - and there's nothing quite like roasting a few hot dogs or marshmallows over an open flame come summer time. If you do decide to install a fire pit, you may want to invest in a few fire pit accessories.
There are plenty of different options when it comes to choosing what kind of seating you want. A few outdoor chairs can suffice, as can a bench or two. However, if you want to create a focal point in your yard around your fire pit, then consider building a stone bench that circles around the fire pit.
Outdoor Pillows
Sitting around a fire pit should be a cozy experience, so make sure that you and your guests are comfortable by having a few outdoor pillows for your benches or chairs.
A Small Table
A small table can be very useful for holding all of your drinks, food, dishes and utensils so that you don't have to place them on the ground or have them take up space on your bench. There are many high-quality outdoor tables that are the perfect size for use near a fire pit, but you can also buy a more affordable fold out table that can easily put away as well.
When buying a table, look for something that's not too tall. You're going to be low near the flames, so something large like a kitchen table isn't going to be very practical. Something the size of a small coffee table will probably be more appropriate.
A Safety Screen
If you know how to use your fire pit, then you shouldn't really have any problems as far as the open flames go. However, having a safety screen to place over the fire is still a good precaution to take, especially if you have children or pets around. This will help prevent sparks or errant flames from causing injuries.
A Fire Pit Grill Grate
Although there's certainly some charm to sticking a hot dog or a marshmallow on a stick and holding it over a flame, cooking over your fire pit will be a lot easier and safer if you use a grill grate. This will allow you to cook multiple sausages, burgers, steaks or any other type of food at once without having to worry about it falling into the fire. Just make sure that when you pick up a grill grate that it's large enough in diameter to cover the entire fire pit so that it won't fall in.
Mosquito Repellent
Mosquitoes can be a real nuisance during the summers. They can be especially problematic when you're trying to enjoy your fire pit. This is because mosquitoes are not only attracted to light, but also to carbon dioxide.
Odds are, you won't want to have to cover yourself in mosquito repellent from head to toe every time you want to go sit by your fire pit. Fortunately, there are other methods of dealing with those pesky mosquitoes. One of the most effective methods is to put up citronella tiki torches around your fire pit area. Citronella is a natural mosquito repellent and the torches themselves will add to the ambiance of your fire pit area to boot.
Fire Roasting Sticks
You could just use any old stick in your yard to cook up your hot dog or marshmallow, but that's not very sanitary. Instead, pick up a set of fire roasting sticks that are manufactured specifically for the purpose of roasting small food items over an open flame.
A Popcorn Popper
While not a necessity, a popcorn popper is certainly a fun accessory to have for your fire pit during the summers, especially if you have a love for popcorn. Popcorn poppers consist of a long handle and a box or container that you can fill with popcorn. You can then just hold it over the flames like you would a marshmallow on a stick until the popcorn has popped.
A Bucket of Sand
A bucket full of sand isn't much of an investment, but you should have one nearby whenever you use your fire pit. This way, if the fire grows out of control or something nearby catches on fire, you can easily put it out with the sand.
Installing a fire pit is a fantastic way to get more enjoyment out of your yard during the summer months. If you plan on adding a fire pit, consider picking up some of these accessories as well.


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942- Engineering Design
The students will be introduced to Engineering Design Concepts of BioEngineering, Civil Engineering, Mechanical and Transporation. Students will learn Employability Preparation, 2D Drawing, Orthographic Projection, Dimensioning and Tolerancing, CT & MRI Segmentation, Scale Model Building and 3D Drawing and Design. Engineering and state-of-arts field-trips though-out the school year. Students will be using drawing boards, AutoCad, SolidWorks and MIMIC software.
Mr. Wilson
x 70383


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April 24–25, 2010 / Jubilate
John 16:16-22
"Come and See the Awesome Works of Our God"
In the Name of the Father and of the + Son and of the Holy Spirit. Amen. "Come and see the awesome works of God," invites the Psalmist. They are the cause of joyful shouts, singing, and praise.
He has turned the sea to dry ground. This defines all the works of the Lord. For first of all, He is the God who delivered us out of slavery, the God who provides the promise, the crushing of our enemy's skull, before the consequence and curse. The Lord has intervened on our behalf. He has thrown horse and rider into the sea. He has marked us with the blood of His Lamb so that the angel of death passes over us. He has turned the sea to dry ground.
But that is not all. There are other works of God toward men. He has also brought us into the net. He has laid affliction on our backs. We go through fire and through water. This is also the Lord's doing toward us. He breaks us. He exposes us. He accuses and even kills us.
Because we are sinners. We are selfish, resentful, hateful, petty, and proud. We are surrounded by beautiful wives, without a care in the world, and cast our eyes with lust and greed upon the one who belongs to Uriah. We are surrounded by delicious and interesting food in the plush vitality of paradise, without any hunger or need, and we look upon the single tree, the unworthy and seductive fruit, and though it means the loss of all we love, the torture of animals, plants, and even the earth, the sorrow and death of our children, the partial-loss of God's image and the perversion of marital intimacy and companionship, even though it means our own death, we look with lust and greed upon the forbidden fruit and we take it.
We do not need to sin. We can overcome it. We are not simply weak victims. The devil does not make us do it. Rather, we are evil. We choose it. We crush our consciences. Do not make excuses. Do not pretend to be ignorant. Like Adam and David you have chosen sin without need or any extenuating circumstance. You have rebelled against God and dared Him to notice or act against you. You have been stupid with lust and pride, taken huge risks, without care for what would happen to you or those you love if you were caught. Repent.
This is the net the Lord has brought you to. This is the affliction He lays upon your back. Repent, but do not despair. Rather, as the Psalmist says, "rejoice." See the effects of the Law on your life, your illnesses, your divorce, your child support payments, indebtedness, funerals, loneliness, and so forth, and praise God for all of them. For He loves you too much to leave you on your own. He breaks you, exposes you, and even kills you. But this He does, as He does all things, in perfect mercy. He does not do this for His benefit or from some perverse enjoyment, but He does this for your benefit, out of your need, lest you fall away, that He might bring you life again.
Even as He has led you into the Law's net, so also, He has brought you to rich fulfillment, out of slavery, out of death. He keeps your soul among the living. He does not allow your feet to be moved. He hears your prayers. He is merciful. He is good. This is the foundation of all our praise, the reason we are bold to pray at all, the strength of our faith and the essence of our hope. Yes, we are sinners, unworthy of God's grace in Jesus Christ, but He is steadfast in His love. We do not praise God because we are good but because He is good. He does not love us because we deserve it, but because He has made a Promise. He is not stopped by our sin. He loves us and forgives us and counts us as His own perfect, undefiled, immaculate Bride.
Our Lord prophesies on the night in which He was betrayed that we will have sorrow. Our hour has not yet come. We must yet endure the chaos of a broken world. We must wait until the last saint, the elect of God, is sealed in the waters of Holy Baptism and creation's anticipatory groaning is brought to an end. But our sorrows will turn to joy, in a little while, in our resurrections like unto His Resurrection, at some near, but imprecise point in the future, we will see Jesus. Our hearts will rejoice. No one will take our joy from us and all our sorrow will cease. For the Lord Jesus Christ did not abandon His disciples in laying down His life. He was taken from them for a little while, and they had terrible sorrows until the third day and the revelation of His victory over death and the fulfillment of all the Scriptures, but He did not abandon them. Rather He served them. He went away for their good, to provide what they most needed: reconciliation with the Father, righteousness won through Hell's worst punishment.
There is a sense in which even your sorrows, in Christ, are a cause for joy, for hope. Not simply because the Lord works all things together for good, which He does, but because your sorrows show your dissatisfaction with this world, that you do not belong here. Nothing here can ever satisfy you because everything here, no matter how good it is, is always broken, always tainted with sin. You are sorrowful because you long to be with your Shepherd, to be free, not only of the sins of others, but also of your own sin and temptation. Your sorrows demonstrate that you belong to Jesus, that this is not your home. They also show that the Word of the Lord is true. He said you would have sorrows and you do. Your sorrows also show how the Lord provides. For the Lord Jesus only eats with and receives sinners. It is only the sick who need the Physician. It is only the sorrowful who need the comfort of the Holy Spirit. You need Jesus and Jesus provides. And finally, your sorrows bring you into the way of the cross, into the way of Jesus. Faith sees these things and confesses against them, like standing in the cemetery and saying, "O grave, where is thy victory?" In the midst of evil, in the midst of sorrow, faith says, "The Lord is good and works all things together for good."
The Law shines light upon our errors - our ever-seeking after pleasures of the flesh, control of our lives, or security in this world, and because we belong to Jesus, because we are baptized, we do not reject the light and slink back into the darkness. But we confess. We repent. We wait for the mercy of the Lord to make Himself known.
Come see what the Law has done to us, the work of the Lord toward us. Come and see our disease, and rejoice. For when can liars ever be trusted? When they say, 'I am a liar.' This is how it is with our confession. It pleases God because it is true. We say, "I am a liar. I am a sinner. I am man of unclean lips." And the angels in heaven say, "Amen," and rejoice. Not only because we have told the truth, but also because the holy angels rejoice over every sinner who repents.
The Lord shines that light, His holy Law, in mercy. He shines it that we would return to the way of righteousness, that we would repent. Thus do we pray that the Lord would grant to all of us, who are admitted into the fellowship of Christ's religion by grace, who have received the forgiveness of all our sins and are declared holy by Christ, the power to avoid those things that are contrary to our faith and follow such things that are good, which is to say, the things that the Law of the Lord has shown us are good.
Yes, we are sinners. We have sorrows. Our lives are broken. It is our fault, our own, most grievous fault. But so too do we have hope. The Lord turned the sea to dry ground, death to life, sorrow to joy. Jesus lives. Death is dead. Hell has no power over us or claim upon us. Jesus lives and there is no one left to accuse us. Your works, your life, your faith are pleasing to God. You are the cause of angelic rejoicing. In a little while, your sorrows will end. The Lord will complete the good work He has begun in you. You will rise from the dead, free of the old man and all temptation. You will be like the Lord. You will be as you were always meant to be, as Jesus has already declared you to be: righteous, holy, innocent, without shame, beloved of the Lord.
Rejoice. Jesus lives. Your sins are forgiven. In + Jesus' Name. Amen.


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Mod News: Early Bird
Welcome to another Mod News, folks. I don't like to start with an excuse, but for the next couple of weeks I'll be compiling these just a little bit early, as I'm away in the latter halves of the weeks in question. If I've missed anything really huge that's happened in the last 24 hours or so, try not to kill me: I'll lob it in with next week's update. Onwards for the past seven days in mod-related happenings, then…
Gorgeous fantasy multiplayer mod Kingdoms Collide, for Half-Life 2, has a release date for its final version. It'll arrive in – ooh – just a few days, on January 16th. The last version was well-received but many felt it had a few balancing issues. Let's hope they're fixed for v1.0. In the meantime, there's a video of the co-op survival mode beyond that link.
Also for Half-Life 2 is the fan-made sequel to Opposing Force. It's known, imaginatively, as Opposing Force 2, and it's looking absolutely beautiful. I mean, just take a look at the new screenshots. The team have also set up a livestream to show off the mod in action, though I haven't seen it at a time when it's switched on yet. Have you?
Darting back in time to Half-Life 1 mod news – and yes, we'll get off the Half-Lives soon enough – there's a Cry of Fear update. This is the hyper-impressive horror mod that's been in development forever. But it appears to be so close to being finished now, one of its developers saying they're basically putting the finishing touches on the completed maps. And ironsights! Aren't they always splendid? I still can't believe they've managed to get this engine looking so good: it doesn't quite compete with the modern beasts, but it isn't anywhere near as far behind as you'd expect.
People do still like modding for the older games. Deus Ex, too, has been getting some love this week. This mod, Nihilum, is still some way away from release (its developer estimates January 2012), but being a Deus Ex mod it's still something I'm keeping an eye on. A bit of information, and some teasery music, is about all there is to go on at the moment.
And finally, last week I mentioned Far Cry 2010 (and got all confused about who owns the Far cry license). This week, there's a lovely video showing off all the swanky visual updates to the game. It looks predictably wonderful. And look! There's also a demo. We're being spoilt.
Just spotted the one notable release this week (no doubt more have slipped beneath my beady eyes), but it's one that made me immediately delighted: Spelunky with multiplayer! Co-op, specifically, with the second player taking on the roll of the damsel in distress. Spelunky, despite being a mere 8mb freebie, is probably my favourite game of the last few years. No, seriously. Here's Quinns being right about it.
Only the one new release, but plenty of updates. First up is Titan Quest mod Underlord. Popular in various countries, it's been patched to include support for several different European languages. But not Spanish. Sorry if you're Spanish! Grab it from ModDB.
Then there's Command & Conquer: Tiberian Sun mod Twisted Insurrection, which has found its way to a second public beta. The mod, which concerns a second terrifying Tiberian war, now features a whole bunch of new artwork, new maps, altered missions and various new or tweaked features to tighten everything up.
Elsewhere, super-popular Crysis mod MechWarrior: Living Legends has received an update. It's now at public versin 0.4.0, which sounds a lot smaller than you'd expect for a mod that's been on the scene for ages. The biggest change, perhaps, is that it's now supported by both Crysis and Crysis Wars. There's also a new game mode, as well as new units, new weapons and stuff.
Finally, there's Mushroomia, which sounds interesting. It's a total conversion for Grand Theft Auto: San Andreas, set in a brand new world (albeit one with a pretty small map). It's hard to work out what exactly it's all about (and my copy of San Andreas is on the PS2, so I shan't be able to check it out), but one of the screenshots on its ModDB page does appear to show you driving around a pumpkin world in something resembling a mine cart. Clearly, it's the best thing to have ever been created by anyone.
If you're a mod-maker, this could be interesting to you: a 20-brush challenge. Basically, create a workable multiplayer map using 20 solid objects or less. It appears to have been spearheaded by Radiator dude Robert Yang, making him the most prolific man in all of the world, ever.
'Til next week.


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pExtra Guard cylinder is perfect in many situations:
- Public and private offices
- Building complexes
- Private homes
pExtra Guard break secure lock has been developed specifically to meet the TS007 3-Star standard for lock cylinders and has undergone rigorous testing prior to its full approval to the new standard. Many customers refer to anti snap, snap resistant cylinders which is an inaccurate term as the cylinder has been designed to snap but in a secure/ safe manner to ensure even after snapping the cylinder can't be manipulated or overcome even with tools.
To provide a counter measure to, amongst others, the increasing threat of snapping locks, the cylinder itself features several layers of protection. In particular, the cylinder features a sacrificial break slot, which ensures that in the event of the cylinder being snapped, the secure core of the lock is retained within the door preventing forced override of the cylinder.
pExtra Guard protects your door from all common types of attack:
pExtra Guard cylinder is perfect in many situations:
To effectively protect your door, the Door & Hardware Federation in the UK (DHF) advises that the lock cylinder and door handles on external entrance doors should meet the highest standard, and protect against all the latest forms of attack. The DHF advises home and business owners that their lock cylinders should be upgraded to the TS007 Kitemark standard.
Secured by Design (the Association of Chief Police Officer's crime prevention initiative) has worked with the DHF and the Glass & Glazing Federation (GGF) to develop the TS007 standard.
Source: www.dhfonline.org.uk


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Dear Editor,
Any chance you can stop the ink and space for Barbara J Carlson's column? She raises her head from the sand long enough to shout accusations and babble … never any solutions … before plunging it back under the sand again.
She now holds John Kerry and Hillary Clinton responsible for advising George Bush on the Iraq war and WMDs? She refers to Egypt, Libya, and now Syria as being the left's problem … not a word about Iraq and Afghanistan except that it must be the fault of Kerry and Clinton?
Does Carlson think we are all a bunch of turnips reading her stuff?
Is it possible for the Star to stop her ink and space? If not, can you at least stop throwing this stuff on my porch?
John I Prestwood


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0 views
The Blacklist Season 6
Dr. Hans Koehler is an episode of The Blacklist starring James Spader, Megan Boone, and Diego Klattenhoff. Red gives the Task Force a Blacklister case, who creates new identities for criminals. Liz and her sister secretly...
Genres: Crime, Drama, Mystery, Thriller
Actor: James Spader, Megan Boone, Diego Klattenhoff, Amir Arison
Director: Bill Roe
Production: Davis Entertainment, Universal Television, Sony Pictures Television
Country: USA


text: Reiserfs, XFS, JFS, xia, msdos, umsdos, vfat, ntfs, proc, nfs, iso9660, hpfs, sysv, smb, ncpfs DESCRIPTION When, as is customary, the proc filesystem is mounted on /proc, you can find in the file /proc/filesystems which filesystems your kernel currently supports. If you need a currently unsupported one, insert the corresponding module or recompile the kernel. In order to use a filesystem, you have to mount it; see mount(8). Below a short description of a few of the available filesystems. minix is the filesystem used in the Minix operating system, the first to run under Linux. It has a number of shortcomings: a 64MB partition size limit, short filenames, a single timestamp, etc. It remains useful for floppies and RAM disks. ext is an elaborate extension of the minix filesystem. It has been completely superseded by the second version of the extended filesystem (ext2) and has been removed from the kernel (in 2.1.21). ext2 is the high performance disk filesystem used by Linux for fixed disks as well as removable media. The second extended filesystem was designed as an extension of the extended filesystem (ext). ext2 offers the best performance (in terms of speed and CPU usage) of the filesystems supported under Linux. ext3 is a journaling version of the ext2 filesystem. It is easy to switch back and forth between ext2 and ext3. ext4 is a set of upgrades to ext3 including substantial performance and reliability enhancements, plus large increases in volume, file, and directory size limits. Reiserfs is a journaling filesystem, designed by Hans Reiser, that was integrated into Linux in kernel 2.4.1. XFS is a journaling filesystem, developed by SGI, that was integrated into Linux in kernel 2.4.20. JFS is a journaling filesystem, developed by IBM, that was integrated into Linux in kernel 2.4.24. xiafs was designed and implemented to be a stable, safe filesystem by extending the Minix filesystem code. It provides the basic most requested features without undue complexity. The xia filesystem is no longer actively developed or maintained. It was removed from the kernel in 2.1.21. msdos is the filesystem used by DOS, Windows, and some OS/2 ntfs replaces Microsoft Window's FAT filesystems (VFAT, FAT32). It has reliability, performance, and space-utilization enhancements plus features like ACLs, journaling, encryption, and so on. proc is a pseudo filesystem which is used as an interface to kernel data structures rather than reading and interpreting /dev/kmem. In particular, its files do not take disk space. See proc(5). iso9660 is a CD-ROM filesystem type conforming to the ISO 9660 standard. High Sierra Linux supports High Sierra, the precursor to the ISO 9660 standard for CD-ROM filesystems. It is automatically recognized within the iso9660 filesystem support under Linux. Rock Ridge Linux also supports the System Use Sharing Protocol records specified by the Rock Ridge Interchange Protocol. They are used to further describe the files in the iso9660 filesystem to a UNIX host, and provide information such as long filenames, UID/GID, POSIX permissions, and devices. It is automatically recognized within the iso9660 filesystem support under Linux. hpfs is the High Performance Filesystem, used in OS/2. This filesystem is read-only under Linux due to the lack of available documentation. sysv is an implementation of the SystemV/Coherent filesystem for Linux. It implements all of Xenix FS, SystemV/386 FS, and Coherent FS. nfs is the network filesystem used to access disks located on remote computers. smb is a network filesystem that supports the SMB protocol, used by Windows for Workgroups, Windows NT, and Lan Manager. To use smb fs, you need a special mount program, which can be found in the ksmbfs package, found at <ftp://sunsite.unc.edu /pub/Linux/system/Filesystems/smbfs>. ncpfs is a network filesystem that supports the NCP protocol, used by Novell NetWare. To use ncpfs, you need special programs, which can be found at <ftp://linux01.gwdg.de/pub/ncpfs>.


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"Provide energy
Boost strength
Bolster endurance
Level blood sugar
Induce weight loss
Aid intestinal regularity
Chia slows the impact of sugars on the system, if eaten together. Chia gel creates a physical barrierbetween carbohydrates and the digestive enzymes that break them down, which slows the conversion of carbs into sugar. That means the energy from the food is released steadily, resulting in more endurance. This is clearly of great benefit to diabetics in particular. It also means that I can combine chia with super-sweet tastes like apple juice and not get super-spiked ;)
Due to the exceptional water-absorption quality of chia, it can help you prolong hydration and retainelectrolytes, especially during exertion." -source
Eddie Coyle, Ph.D. at the University of Texas in Austin, has shown that consuming carbohydrate during exercise at 70 percent of maximal effort can delay fatigue by 30 to 60 minutes. For the best results, try to take in 40 to 80 grams of carbohydrate (160 to 320 carbohydrate calories) every hour of cycling." -source
-Eat foods with good protein such as spinach, nuts, hemp seeds, and beans.
-Also, healthy fats and protein like quinoa and avocado. Rice is also good.
"Did you know that fruit has protein? It does! Many fruits contain between 4-8% protein and as a significant part of your diet, they provide a significant amount of complete protein. That's right, fruit is a complete protein with all 8 essential amino acids! On an average day, I'll get anywhere from 18-22 grams of protein from fruit, which provides almost half of my daily protein requirements.
Non-sweet fruit like tomatoes, zucchini and cucumbers also have protein.
Leafy green vegetables are a good source of protein. Two cups of kale has 4 grams while dandelion will have 3 grams. A head of leaf lettuce will provide about 5 grams. Basically, two large bunches of dark leafy greens each day will supply anywhere from 14-20 grams of protein. I eat most of my greens in green smoothies or shredded up in salads.
Spirulina is about 68% protein and also helps detoxify the body. It's packed with vitamins and contains EFA's (essential fatty acids).
Chlorella is about 60% protein and is known for it's rapid tissue repair properties. It's a great food if you're very physically active or have higher protein requirements. Use it in your shakes to help speed up recovery times." -source


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Q. When did ALA first adopt the Library Bill of Rights?
A. The first Library Bill of Rights was approved by the ALA Council at its meeting on June 19, 1939, during the Annual Conference in San Francisco. It was modeled on a similar statement written by Forrest Spaulding, librarian at the Des Moines Public Library. A news item in the ALA Bulletin (precursor to American Libraries) in the December 1939 issue states, "Forrest Spaulding of Des Moines has been appointed by the Executive Board as chairman of a special committee on censorship, following the recent banning by a number of libraries of John Steinbeck's Grapes of Wrath. The committee is to report on existing censorship and to formulate a statement of policy for the board's consideration."
In her chapter (historical overview) in the 7th edition of the Intellectual Freedom Manual, Judith F. Krug reviewed the history of ALA's development of its strong advocacy of intellectual freedom in some depth. She describes the "wavering" position of ALA during the 1920s and 1930s, noting that there was concern voiced about censorship in 1924, 1929, and in 1934 … but not against the Hitler regime, when it ordered books burned in 1933.
Although the original document focused on unbiased book selection, a balanced collection, and open meeting rooms, it reflected the climate of the times. The preamble to the first document started, "Today indications in many parts of the world point to growing intolerance, suppression of free speech, and censorship affecting the rights of minorities and individuals..." The Library Bill of Rights has evolved over the years, with several revisions and amendments, as well as interpretations, which may be found on the ALA website.'