text:
Summary: Cadherin-like
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Cadherin Edit Wikipedia article
Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other.[1] Cadherins are a class of type-1 transmembrane proteins. They are dependent on calcium (Ca2+) ions to function, hence their name. Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with a large number of adaptor and signaling proteins, collectively referred to as the cadherin adhesome.
The cadherin superfamily includes cadherins, protocadherins, desmogleins, and desmocollins, and more.[2][3] In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. There are multiple classes of cadherin molecule, each designated with a prefix (in general, noting the type of tissue with which it is associated). It has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development.[4] For example, cells containing N-cadherin tend to cluster with other N-cadherin-expressing cells. However, it has been noted that the mixing speed in the cell culture experiments can have an effect on the extent of homotypic specificity.[5] In addition, several groups have observed heterotypic binding affinity (i.e., binding of different types of cadherin together) in various assays.[6][7] One current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes.[8]
Structure and function
Cadherins are synthesized as polypeptides and undergo many post-translational modifications to become the proteins which mediate cell-cell adhesion and recognition.[9] These polypeptides are approximately 720–750 amino acids long. Each cadherin has a small cytoplasmic component, a transmembrane component, and the remaining bulk of the protein is extra-cellular (outside the cell). The transmembrane component consists of single chain glycoprotein repeats.[10] Because cadherins are Ca2+ dependent, they have five tandem extracellular domain repeats that act as the binding site for Ca2+ ions.[11] Their extracellular domain interacts in two separate trans dimer conformations: strand-swap dimers (S-dimers) and X-dimers.[11] To date, over 100 types of cadherins in humans have been identified and sequenced.[12]
The functionality of cadherins relies upon the formation of two identical subunits, known as homodimers.[10] The homodimeric cadherins create cell-cell adhesion with cadherins present in the membranes of other cells through changing conformation from cis-dimers to trans-dimers.[10] Once the cell-cell adhesion between cadherins present in the cell membranes of two different cells has formed, adherens junctions can then be made when protein complexes, usually composed of α-, β-, and γ-catenins, bind to the actin cytoskeleton portion of the cadherin.[10]
Cadherins behave as both receptors and ligands for other molecules. During development, their behavior assists in properly positioning cells: they are responsible for the separation of the different tissue layers, and for cellular migration.[13] In the very early stages of development, E-cadherin (epithelial cadherin) is most greatly expressed. Many cadherins are specified for specific functions in the cell, and they are differentially expressed in a developing embryo. For example, during neurulation, when the neural plate is forming in the embryo, the tissues residing near the cranial neural folds have decreased N-cadherin expression.[14] Conversely, the expression of the N-cadherins remains unchanged in the other regions of the neural tube that is located on the anterior-posterior axis of the vertebrate.[14] The expression of the different types of cadherins in the cell are varying dependent upon the specific differentiation and specification of the organism during development.
Cadherins play a vital role in the migration of cells through the epithelial-mesenchymal transition (EMT), which requires cadherins to forms adherents junctions with neighboring cells. In neural crest cells, which are transient cells that arise in the developing organism during gastrulation and function in the patterning of the vertebrate body plan, the cadherins are necessary to allow migration of cells to form tissues or organs.[14] In addition, cadherins responsible in the EMT event in early development have also been shown to be critical in the reprogramming of specified adult cells into a pluripotent state, forming induced pluripotent stem cells (iPSCs).[1]
After development, cadherins play a role in maintaining cell and tissue structure, and in cellular movement.[12] Regulation of cadherin expression can occur through promoter methylation among other epigenetic mechanisms.[15]
Tumour metastasis
The E-cadherin–catenin complex plays a key role in cellular adhesion; loss of this function has been associated with greater tumour metastasis.[16]
|Cadherin domain
There are said to be over 100 different types of cadherins found in vertebrates, which can be classified into four groups: classical, desmosomal, protocadherins, and unconventional.[18][19] This large amount of diversity is accomplished by having multiple cadherin encoding genes combined with alternative RNA splicing mechanisms. Invertebrates contain fewer than 20 types of cadherins.[19]
Different members of the cadherin family are found in different locations.
- CDH1 – E-cadherin (epithelial): E-cadherins are found in epithelial tissue
- CDH2 – N-cadherin (neural): N-cadherins are found in neurons
- CDH12 – cadherin 12, type 2 (N-cadherin 2)
- CDH3 – P-cadherin (placental): P-cadherins are found in the placenta.
- Desmoglein (DSG1, DSG2, DSG3, DSG4)
- Desmocollin (DSC1, DSC2, DSC3)
- CDH9 – cadherin 9, type 2 (T1-cadherin)
- CDH10 – cadherin 10, type 2 (T2-cadherin)
- CDH4 – R-cadherin (retinal)
- CDH5 – VE-cadherin (vascular endothelial)
- CDH6 – K-cadherin (kidney)
- CDH7 – cadherin 7, type 2
- CDH8 – cadherin 8, type 2
- CDH11 – OB-cadherin (osteoblast)
- CDH13 – T-cadherin – H-cadherin (heart)
- CDH15 – M-cadherin (myotubule)
- CDH16 – KSP-cadherin
- CDH17 – LI cadherin (liver-intestine)
- CDH18 – cadherin 18, type 2
- CDH19 – cadherin 19, type 2
- CDH20 – cadherin 20, type 2
- CDH23 – cadherin 23 (neurosensory epithelium)
See also
- ^ a b Alimperti, Stella; Andreadis, Stelios T. "CDH2 and CDH11 act as regulators of stem cell fate decisions". Stem Cell Research. 14 (3): 270–282. doi:10.1016/j.scr.2015.02.002.
- ^ Hulpiau P, van Roy F (February 2009). "Molecular evolution of the cadherin superfamily". Int. J. Biochem. Cell Biol. 41 (2): 349–69. doi:10.1016/j.biocel.2008.09.027. PMID 18848899.
- ^ Angst B, Marcozzi C, Magee A (February 2001). "The cadherin superfamily: diversity in form and function". J Cell Sci. 114 (Pt 4): 629–41. PMID 11171368.
- ^ Bello, S.M.; Millo, H.; Rajebhosale, M.; Price, S.R. (2012). "Catenin-dependent cadherin function drives divisional segregation of spinal chord motor neurons". Journal of Neuroscience. 32 (2): 490–505. doi:10.1523/jneurosci.4382-11.2012.
- ^ Duguay, D.; A. Foty R., RA; S. Steinberg M., MS (2003). "Cadherin-mediated cell adhesion and tissue segregation: qualitative and quantitative determinants". Dev. Biol. 253 (2): 309–323. doi:10.1016/S0012-1606(02)00016-7. PMID 12645933.
- ^ Niessen, Carien M.; Gumbiner, Barry M. (2002). "Cadherin-mediated cell sorting not determined by binding or adhesion specificity". The Journal of Cell Biology. 156 (2): 389–399. doi:10.1083/jcb.200108040. PMC 2199232 . PMID 11790800.
- ^ Volk, T.; Cohen, O.; Geiger, B. (1987). "Formation of heterotypic adherens-type junctions between L-CAM containing liver cells and A-CAM containing lens cells". Cell. 50 (6): 987–994. doi:10.1016/0092-8674(87)90525-3. PMID 3621349.
- ^ Bayas, Marco V.; Leung, Andrew; Evans, Evan; Leckband, Deborah (2005). "Lifetime Measurements Reveal Kinetic Differences between Homophilic Cadherin Bonds". Biophysical Journal. 90 (4): 1385–95. doi:10.1529/biophysj.105.069583. PMC 1367289 . PMID 16326909.
- ^ Harris, T. J.; Tepass, U (2010). "Adherens junctions: From molecules to morphogenesis". Nature Reviews Molecular Cell Biology. 11 (7): 502–14. doi:10.1038/nrm2927. PMID 20571587.
- ^ a b c d Marie, Pierre J.; Haÿ, Eric; Modrowski, Dominique; Revollo, Leila; Mbalaviele, Gabriel; Civitelli, Roberto (2014-01-01). "Cadherin-Mediated Cell–Cell Adhesion and Signaling in the Skeleton". Calcified Tissue International. 94 (1): 46–54. doi:10.1007/s00223-013-9733-7. ISSN 0171-967X. PMC 4272239 .
- ^ a b Priest, Andrew Vae; Shafraz, Omer; Sivasankar, Sanjeevi. "Biophysical basis of cadherin mediated cell-cell adhesion". Experimental Cell Research. 358 (1): 10–13. doi:10.1016/j.yexcr.2017.03.015.
- ^ a b Tepass, U; Truong, K; Godt, D; Ikura, M; Peifer, M (2000). "Cadherins in embryonic and neural morphogenesis". Nature Reviews Molecular Cell Biology. 1 (2): 91–100. doi:10.1038/35040042. PMID 11253370.
- ^ Gumbiner, B. M. (2005). "Regulation of cadherin-mediated adhesion in morphogenesis". Nature Reviews Molecular Cell Biology. 6 (8): 622–34. doi:10.1038/nrm1699. PMID 16025097.
- ^ a b c Taneyhill, Lisa A.; Schiffmacher, Andrew T. (2017-06-01). "Should I stay or should I go? Cadherin function and regulation in the neural crest". genesis. 55 (6): n/a–n/a. doi:10.1002/dvg.23028. ISSN 1526-968X.
- ^ Reinhold, WC; Reimers, MA; Maunakea, AK; Kim, S; Lababidi, S; Scherf, U; Shankavaram, UT; Ziegler, MS; Stewart, C; Kouros-Mehr, Hosein; Cui, H; Dolginow, D; Scudiero, DA; Pommier, YG; Munroe, DJ; Feinberg, AP; Weinstein, JN (Feb 2007). "Detailed DNA methylation profiles of the E-cadherin promoter in the NCI-60 cancer cells". Molecular cancer therapeutics. 6 (2): 391–403. doi:10.1158/1535-7163.MCT-06-0609. PMID 17272646.
- ^ Beavon, IR (August 2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation". European Journal of Cancer. 36 (13 Spec No): 1607–20. doi:10.1016/S0959-8049(00)00158-1. PMID 10959047.
- ^ PDB: 3Q2V; Harrison, O.J.; Jin, X.; Hong, S.; Bahna, F.; Ahlsen, G.; Brasch, J.; Wu, Y.; Vendome, J.; Felsovalyi, K.; Hampton, C.M.; Troyanovsky, R.B.; Ben-Shaul, A.; Frank, J.; Troyanovsky, S.M.; Shapiro, L.; Honig, B. (2011). "The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins". Structure. 19 (2): 244–56. doi:10.1016/j.str.2010.11.016. PMC 3070544 . PMID 21300292.; rendered with PyMOL
- ^ Stefan Offermanns; Walter Rosenthal (2008). Encyclopedia of Molecular Pharmacology. Springer. pp. 306–. ISBN 978-3-540-38916-3. Retrieved 14 December 2010.
- ^ a b Lodish, Harvey; Berk, Arnold; Kaiser, Chris; Krieger, Monte; Bretscher, Anthony; Ploegh, Hidde; Amon, Angelika (2013). Molecular Cell Biology (Seventh ed.). New York: Worth Publ. p. 934. ISBN 978-1-4292-3413-9.
Further reading
- Beavon IR (2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation". Eur. J. Cancer. 36 (13 Spec No): 1607–20. doi:10.1016/S0959-8049(00)00158-1. PMID 10959047.
- Berx G, Becker KF, Höfler H, van Roy F (1998). "Mutations of the human E-cadherin (CDH1) gene". Hum. Mutat. 12 (4): 226–37. doi:10.1002/(SICI)1098-1004(1998)12:4<226::AID-HUMU2>3.0.CO;2-D. PMID 9744472.
- Bryant DM, Stow JL (2005). "The ins and outs of E-cadherin trafficking". Trends Cell Biol. 14 (8): 427–34. doi:10.1016/j.tcb.2004.07.007. PMID 15308209.
- Chun YS, Lindor NM, Smyrk TC, et al. (2001). "Germline E-cadherin gene mutations: is prophylactic total gastrectomy indicated?". Cancer. 92 (1): 181–7. doi:10.1002/1097-0142(20010701)92:1<181::AID-CNCR1307>3.0.CO;2-J. PMID 11443625.
- Georgolios A, Batistatou A, Manolopoulos L, Charalabopoulos K (2006). "Role and expression patterns of E-cadherin in head and neck squamous cell carcinoma (HNSCC)". J. Exp. Clin. Cancer Res. 25 (1): 5–14. PMID 16761612.
- Hazan RB, Qiao R, Keren R, et al. (2004). "Cadherin switch in tumor progression". Ann. N. Y. Acad. Sci. 1014 (1): 155–63. doi:10.1196/annals.1294.016. PMID 15153430.
- Moran CJ, Joyce M, McAnena OJ (2005). "CDH1 associated gastric cancer: a report of a family and review of the literature". Eur J Surg Oncol. 31 (3): 259–64. doi:10.1016/j.ejso.2004.12.010. PMID 15780560.
- Reynolds AB, Carnahan RH (2005). "Regulation of cadherin stability and turnover by p120ctn: implications in disease and cancer". Semin. Cell Dev. Biol. 15 (6): 657–63. doi:10.1016/j.semcdb.2004.09.003. PMID 15561585.
- Wang HD, Ren J, Zhang L (2004). "CDH1 germline mutation in hereditary gastric carcinoma". World J. Gastroenterol. 10 (21): 3088–93. PMID 15457549.
- Wijnhoven BP, Dinjens WN, Pignatelli M (2000). "E-cadherin-catenin cell-cell adhesion complex and human cancer". The British journal of surgery. 87 (8): 992–1005. doi:10.1046/j.1365-2168.2000.01513.x. PMID 10931041.
- Wilson PD (2001). "Polycystin: new aspects of structure, function, and regulation". J. Am. Soc. Nephrol. 12 (4): 834–45. PMID 11274246.
- Renaud-Young M, Gallin WJ (2002). "In the first extracellular domain of E-cadherin, heterophilic interactions, but not the conserved His-Ala-Val motif, are required for adhesion". Journal of Biological Chemistry. 277 (42): 39609–39616. doi:10.1074/jbc.M201256200. PMID 12154084.
External links
- Proteopedia Cadherin - view cadherin structure in interactive 3D
- Cadherin domain in PROSITE
- The cadherin family
- Alberts, Bruce. Molecular Biology of the Cell
- The Cadherin Resource
- InterPro: IPR002126
- [1]
- "Cadherin adhesome at a glance". J Cell Sci 126, 373-378
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Cadherin-like Provide feedback
This cadherin domain is usually the most N-terminal copy of the domain.
Literature references
Elledge HM, Kazmierczak P, Clark P, Joseph JS, Kolatkar A, Kuhn P, Muller U;, Proc Natl Acad Sci U S A. 2010;107:10708-10712.: Structure of the N terminus of cadherin 23 reveals a new adhesion mechanism for a subset of cadherin superfamily members. PUBMED:20498078 EPMC:20498078
Trivedi M, Laurence JS, Williams TD, Middaugh CR, Siahaan TJ;, Int J Pharm. 2012;431:16-25.: Improving the stability of the EC1 domain of E-cadherin by thiol alkylation of the cysteine residue. PUBMED:22531851 EPMC:22531851
Internal database links
|Similarity to PfamA using HHSearch:
This tab holds annotation information from the InterPro database.
InterPro entry IPR013164
Cadherins are a family of adhesion molecules that mediate Ca2+-dependent cell-cell adhesion in all solid tissues of the organism which modulate a wide variety of processes including cell polarisation and migration [PUBMED:2197976, PUBMED:14570569]. Cadherin-mediated cell-cell junctions are formed as a result of interaction between extracellular domains of identical cadherins, which are located on the membranes of the neighbouring cells. The stability of these adhesive junctions is ensured by binding of the intracellular cadherin domain with the actin cytoskeleton. There are a number of different isoforms distributed in a tissue-specific manner in a wide variety of organisms. Cells containing different cadherins tend to segregate in vitro, while those that contain the same cadherins tend to preferentially aggregate together. This observation is linked to the finding that cadherin expression causes morphological changes involving the positional segregation of cells into layers, suggesting they may play an important role in the sorting of different cell types during morphogenesis, histogenesis and regeneration. They may also be involved in the regulation of tight and gap junctions, and in the control of intercellular spacing. Cadherins are evolutionary related to the desmogleins which are component of intercellular desmosome junctions involved in the interaction of plaque proteins.
Structurally, cadherins comprise a number of domains: classically, these include a signal sequence; a propeptide of around 130 residues; a single transmembrane domain and five tandemly repeated extracellular cadherin domains, 4 of which are cadherin repeats, and the fifth contains 4 conserved cysteines and a N-terminal cytoplasmic domain [PUBMED:11736639]. However, proteins are designated as members of the broadly defined cadherin family if they have one or more cadherin repeats. A cadherin repeat is an independently folding sequence of approximately 110 amino acids that contains motifs with the conserved sequences DRE, DXNDNAPXF, and DXD. Crystal structures have revealed that multiple cadherin domains form Ca2+-dependent rod-like structures with a conserved Ca2+-binding pocket at the domain-domain interface. Cadherins depend on calcium for their function: calcium ions bind to specific residues in each cadherin repeat to ensure its proper folding, to confer rigidity upon the extracellular domain and is essential for cadherin adhesive function and for protection against protease digestion.
This entry represents a cadherin domain that is usually found at the N terminus of cadherin proteins.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan E-set (CL0159), which has the following description:
This clan includes a diverse range of domains that have an Ig-like fold and appear to be distantly related to each other. The clan includes: PKD domains, cadherins and several families of bacterial Ig-like domains as well as viral tail fibre proteins. it also includes several Fibronectin type III domain-containing families.
The clan contains the following 218 members:A2M A2M_BRD A2M_recep Adeno_GP19K AlcCBM31 Alpha-amylase_N Alpha_adaptinC2 Alpha_E2_glycop Arch_flagellin Arylsulfotran_N ASF1_hist_chap ATG19_autophagy BACON Big_1 Big_10 Big_11 Big_2 Big_3 Big_3_2 Big_3_3 Big_3_5 Big_4 Big_5 Big_6 Big_7 Big_8 Big_9 Bile_Hydr_Trans BiPBP_C bMG1 bMG10 bMG3 bMG5 bMG6 BslA BsuPI Cadherin Cadherin-like Cadherin_2 Cadherin_3 Cadherin_4 Cadherin_5 Cadherin_pro CagX Calx-beta Candida_ALS_N CARDB CBM39 CBM_X2 CD45 CelD_N Ceramidse_alk_C CHB_HEX_C CHB_HEX_C_1 ChitinaseA_N ChiW_Ig_like CHU_C Coatamer_beta_C COP-gamma_platf CopC Cyc-maltodext_N Cytomega_US3 DsbC DUF11 DUF1410 DUF1425 DUF1929 DUF2271 DUF3244 DUF3327 DUF3416 DUF3458 DUF3501 DUF3823_C DUF3859 DUF3872 DUF4165 DUF4179 DUF4426 DUF4448 DUF4469 DUF4625 DUF4879 DUF4981 DUF4982 DUF5001 DUF5008 DUF5011 DUF5065 DUF5115 DUF525 DUF5643 DUF916 EB_dh ECD EpoR_lig-bind ERAP1_C EstA_Ig_like Filamin FixG_C Flavi_glycop_C FlgD_ig fn3 Fn3-like fn3_2 fn3_4 fn3_5 fn3_6 FN3_7 Fn3_assoc fn3_PAP GBS_Bsp-like Glucodextran_B Glyco_hydro2_C5 Glyco_hydro_2 Glyco_hydro_61 Gmad2 GMP_PDE_delta GPI-anchored Hanta_G1 He_PIG He_PIG_assoc HECW_N HemeBinding_Shp Hemocyanin_C Herpes_BLLF1 HYR IFNGR1 Ig_GlcNase Ig_mannosidase IL12p40_C Il13Ra_Ig IL17R_fnIII_D1 IL17R_fnIII_D2 IL2RB_N1 IL3Ra_N IL4Ra_N IL6Ra-bind Inhibitor_I42 Inhibitor_I71 Integrin_alpha2 Interfer-bind Invasin_D3 IRK_C IrmA Iron_transport LEA_2 Lep_receptor_Ig LIFR_N Lipase_bact_N LPMO_10 LRR_adjacent LTD Mannosidase_ig MG1 MG2 MG3 MG4 Mo-co_dimer N_BRCA1_IG Na_K-ATPase NEAT Neocarzinostat Neurexophilin NPCBM_assoc PapD_C PBP-Tp47_c Peptidase_C25_C Phlebovirus_G2 PhoD_N PKD PKD_2 PKD_3 Pollen_allerg_1 Pox_vIL-18BP Pur_ac_phosph_N Qn_am_d_aII Qn_am_d_aIII RabGGT_insert Reeler REJ RET_CLD1 RET_CLD3 RET_CLD4 RGI_lyase RHD_dimer Rho_GDI Rib SCAB-Ig SKICH SLAM SoxZ SprB SusE SVA SWM_repeat T2SS-T3SS_pil_N Tafi-CsgC TarS_C1 TcA_RBD TcfC TIG TIG_2 TIG_plexin Tissue_fac Top6b_C Transglut_C Transglut_N TRAP_beta Tuberculin UL16 Velvet WIF Wzt_C Y_Y_Y YBD ZirS_C Zona_pellucida
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
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- alignment generated by searching the metagenomics sequence database using the family HMM
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
|Representative proteomes
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
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HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
|Seed source:
|Pfam-B_179 (release 17.0)
|Previous IDs:
|Sequence Ontology:
|Finn RD
|Number in seed:
|Number in full:
|Average length of the domain:
|82.20 aa
|Average identity of full alignment:
|35 %
|Average coverage of the sequence by the domain:
|9.42 %
HMM information
|HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Model details:
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
- superkingdom
- kingdom
- phylum
- class
- order
- family
- genus
- species
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
Anomalies in the taxonomy tree
There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
Tree controlsHide
Download tree
- Save a text representation
Selected sequences
- (Uncheck all)
- graphically
- as an alignment
- sequence accessions
- sequences in FASTA format
The tree shows the occurrence of this domain across different species. More...
Species trees
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
Interactive tree
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cadherin_2 domain has been found. There are 44 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
Loading structure mapping...


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Stratovarius was founded in 1984 by three guys from Helsinki, Finland; drummer and vocalist Tuomo Lassila, bass player John Viherv� and guitarist Staffan Str�hlman. Before Stratovarius the same line up performed under name Black Water.
The music of early Stratovarius was very different from what it is today. Back then it was heavily influenced by Black Sabbath and Ozzy Osbourne. Guitar player Staffan brought in some classical elements. Bass player John left the band by the end of 1984 and was replaced by Jyrki Lentonen, who previously played with Timo Tolkki in a band called Road Block.
1985 Staffan did not want to play in Stratovarius anymore and he left one week before the band was supposed to play one gig in Aalborg, Denmark. Tuomo Lassila phoned to Timo Tolkki and asked him to join the band. Timo learned all the songs from cassette tape and after a few rehearsals the band travelled to Denmark. At that time Tuomo was still singing and playing the drums at the same time. It soon became evident that the band needed a singer because Tuomo's vocal range. However, good singers are few and far between and so Timo Tolkki took over the vocal duties. At this point the music was starting to sound more like it is today: very melodic and classically influenced. Timo Tolkki brought along his influences; Blackmore, Rainbow and Baroque music. The band rehearsed and gigged extensively in Helsinki and made its first demo tape under this line up in 1987. It contained songs "Future Shock", "Fright Night" and "Night Screamer".
The demos were sent to various record companies in Finland and CBS Finland wanted to sign the band after seeing a show at Tavastia Club, Helsinki. At this point the band had a new keyboard player Antti Ikonen. The band recorded its first single "Future Shock/Witch Hunt" in 1988. This was followed by another single "Black Night/Night Screamer" in the beginning of 1989 and finally the debut album "Fright Night" saw daylight in May 1989.
The band gigged extensively during the summer and autumn 1989 and played a huge outdoor gig Giants Of Rock in H�meenlinna with Anthrax and many other metal acts. After all this bass player Jyrki Lentonen left the band. New material was written and demoed early 1990 but CBS lost interest of releasing more Stratovarius material. The band did not give up but rehearsed a lot and made new songs and finally went to record the follow-up to "Fright Night". All this time the band did not have a record contract and it had to finance the recordings by itself. Timo played all the bass parts and even though there is a photo of a new bassist Jari Behm in "Twilight Time" actually play on the album. Soon Jari was asked to leave the band because his style of playing did not fit to the band's music at all.
The second album called "Stratovarius II" was released in Finland early 1992. At this point it was pretty clear that the market for Stratovarius was outside Finland. Many tapes were sent all over the world and Shark Records wanted to sign the band after hearing the song "Hands of Time". Finally "Stratovarius II" was released with a new cover and a new name "Twilight Time" in October 1992 all over the Europe. Soon import copies started to spread to the Japanese market and "Twilight Time" was five months in Top 10 of import disks in Japan. Evetually it became the best selling import album in Japan in 1993. The band also got a big record contract with JVC Victor Entertainment inJapan which released "Twilight Time" in July 1993. Timo Tolkki flew to Japan for the first time in the same month to do promotion and saw that the bands popularity was skyrocketing with enthusiastic fans. The spare time between searching for the record deal was spent on writing new material and the band recorded new songs during the whole year 1993. Also a new bass player Jari Kainulainen joined the band as 70% of the new material was already recorded. At this time Tuomo Lassila had a severe stress injury in his both hands and was not able to play drums for 8 weeks. The record had to be completed with Kingston Wall drummer Sami Kuoppam�ki, who played on 4 tracks.
Finally the third album "Dreamspace" was released worldwide in February and March 1994. It was highly praised among the critics and took the bands popularity to a different level. It contained such all time Stratovarius classics as "Dreamspace", "4th Reich" and "Chasing Shadows" to name a few. In June the band headed to Japan for the first tour and played concerts in Tokyo, Osaka and Nagoya seeing Japanese fans face to face for the 1st time. In Finland they played just one gig before heading for Japan in the now defunct, legendary Shadow Club in Helsinki. This was also JK's very first live appearance with Stratovarius.
New material was written from the spring to summer 1994 and band hit the studio once again with very good vibes from Japan Tour. Timo Tolkki fulfilled his long time dream by recording the solo album "Classical Variations and Themes". It contained songs like "Fire Dance Suite", which was originally written for "Stratovarius" back in 1986, "Lord Of The Rings" and many other classically influenced tracks. The album was released in October 1994. Stratovarius spent the whole summer of 1994 in studio finishing its fourth album.
At this stage Timo Tolkki decided that his singing days were over and that the band should find a proper singer to take the band's sound even further. As advertisements were put to local music papers, somebody remembered a guy from Lappaj�rvi, Finland, who had approached the band one and half years earlier. So Timo Kotipelto got a phone call from Timo Tolkki and an audition was arranged. The band jammed some songs and as the new guy opened his mouth for the first time, everybody knew that he was the new singer.
Timo's sound can be heard all over the bands fourth release "Fourth Dimension". The title of the album says it all and the sound and the songs on this album were something totally different than before but still the musical style remained as true Stratovarius metal. "Fourth Dimension" was released worldwide in March 1995 and it doubled the sales of "Dreamspace"
The band toured heavily playing shows in all over Germany, Switzerland, The Netherlands, Finland, Greece and Japan. After all these tours Tuomo Lassila and Antti Ikonen, the long time members were asked to leave the band. There were many reasons for this line up change, the most important were personal chemistry and musical differences. The guys just could not play the material that was developing in Timo Tolkki's mind.
After the success of "Fourth Dimension" Timo Tolkki and Timo Kotipelto wanted to take the bands music even further. New drummer J�rg Michael and new keyboard player Jens Johansson entered the band.
The mixing of bands fifth album "Episode" took place at Finnvox Studios in Helsinki. This album was once again a huge step forward for the band. With the fresh attitude and sound of Johansson and Michael the result was dramatic, melodic and symphonic metal album. Also for the first time a choir of 40 singers and a string orchestra of 20 players were used. The album contains some Stratovarius classics as "Father Time", "Eternity" and "Will the Sun Rise?".
Stratovarius' next album "Visions" was released in the April of 1997 and it hit the Finnish charts position #5 in an instant. It spent a total of 24 weeks on the Finnish Top 40. "Visions" also launched an extensive tour, during which Stratovarius entertained not only Finns but also their fans in Japan, Europe and South America. "Visions" exceeded the gold disc plateau of 20.000 sold copies in Finland and the gold disc was celebrated at Tavastia Club in Helsinki June 10th 1998 with a little party and a special gig with a couple of unusual song choices.
During Visions tour Stratovarius recorded their first live album, double CD "Visions of Europe", which was released late March 1998. It contains over 100 minutes of material. Also this album has been a huge success both critically and commercially.
April 1998 Stratovarius started rehearsing their new studio material for the forthcoming album, their seventh full length studio release "Destiny" The album was recorded at Finnvox studios during the spring and summer of 1998 and the release date was October 5th 1998. The first single from the album is entitled SOS was released August 17th and it hit the chart position #3 on Finnish single charts faster than the speed of light. Strangely enough, Destiny debuted the Finnish charts on position #1 the Thursday BEFORE it was officially released. The future will show us if we will see another Stratovarius gold disc party within one year.
The coming of the year 1999 saw Stratovarius again surpassing the gold disc plateau with "Destiny" and this was but sign of more fine things to come. This year has already seen Stratovarius clinch the merits as the best Finnish metal band in the annual readers' poll of the Finnish metal Magazine"SFP". Also the video for SOS was voted the best domestic metal video in Finland in 1998 in the same poll. Soundi magazine's readers' poll confirmed that Stratovarius is now in the big league in Finland, Timo Tolkki took a landslide victory in the "best musician" category for the second time in a row, Stratovarius was elected th 2nd best band, Timo Kotipelto was voted the 3rd in the "best singer" category, Destiny was elected the 2nd best album and SOS the 2nd best song. Also both Timos vere voted in the "Wondeful Person" category and Jens was voted in foreign musicians category. Stratovarius also got laurels from Finnish record industry, they got an "Emma" trophy for being an outstanding export band.
The closing half of 1999 sees Stratovarius building up their new studio album, which will be released by Nuclear Blast Records February 28th 2000.
The expectations towards Infinite were extremely high and those expectations were met. Infinite was yet again very successful album and it certified gold in Finland. It was 3rd album in a row to do that for Stratovarius.
At the end of 2000 Stratovarius returned form their most succesful and longest Tour ever, promoting the Infinite Album they ever did performing in front of more than 300.000 people. Right afte that they decided to do a break for an unknow amount of time. Some musicians inside the band took the chance to work on their solo albums like Timo Tolkki and Timo Kotipelto. A b-side rare material, bonus track - mix called "Intermission" inlcuding 4 new songs was released in 2001 to close the gap until the new album would be released followed by a very selective choice of festival appearance in summer 2001.
After a long break of one year the band hit the studio again in summer 2002 to work on their fouthcoming album called "Elements Pt. 1".
Believing in the opinions of the musicians the album will represent the most symphonic and epic material the band ever has recorded.
The release date is planned for January 27, 2003 followed by another world tour starting on March 19th in Finland.
And the story WILL continue...as soon as the webmaster finds the time
STRATOVARIUS History
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A Unique Approach to Research
Only a multidisciplinary approach, such as that found in the Research Division at Joslin Diabetes Center, can fully explore the most promising pathways to prevent, treat, and cure type 1 and type 2 diabetes and their complications.
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Our investigators, who engage in both basic and clinical research across the sections into which the Research Division is organized, are advancing science at an unusually fast pace due to Joslin's unique environment. For example, Joslin's Diabetes Research and Endocrinology Research Center (DRC) provides the infrastructure necessary to support research efforts across all the disciplines and encourage the development of young scientists. The DRC offers researchers specialized technical assistance as well as a network of colleagues from across the medical and scientific community.
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In addition, Joslin's Clinical Research Center (CRC) supports a large number of clinical studies which translates many of the discoveries from the bench to the clinical arena. This center facilitates the moving of anti-inflammatory drugs such as salicylate from the basic lab to NIH-funded, multi-center trial as a treatment for type 2 diabetes. The CRC has also translated the discovery of brown fat existence in adults and its induction by other proteins which can be novel treatments for obesity in type 2 diabetes.
These types of collaborations offer an incredibly rich setting in which to work, and provide a significant asset to our researchers. Our affiliations with Brigham and Women's Hospital, Beth Israel Deaconess Medical Center, Boston Children's Hospital, and Harvard Medical School enable Joslin researchers to work with investigators with complementary interests and expertise through such programs as the Harvard Stem Cell Institute, the Clinical Islet Transplantation Program at Harvard Medical School and the Juvenile Diabetes Research Foundation Center on Immunological Tolerance in Type 1 Diabetes.
To extend the reach of our work, Joslin investigators not only partner with their colleagues down the hall and in the Harvard community, but work with scientists across the globe. We are committed to conquering diabetes in all of its forms and will continue to lead the scientific community on new pathways of discovery in diabetes.
Extraordinary Teamwork
But perhaps it is the collaborations that occur within the walls of Joslin that most often give rise to the important questions that stimulate thinking and drive progress toward cure and prevention of diabetes. Here at Joslin, independent thinking and creativity are valued and supported because we recognize these are the ingredients that lead to greater understanding and discovery.
Researchers have the opportunity to exchange ideas and challenge one another in a setting that nurtures teamwork and allows for the unpredictability of research.
The scientific process requires a multidisciplinary team approach like the one found at Joslin Diabetes Center. Where else could you gather the experts necessary to understand why some people who have lived with type 1 diabetes for 50 years do not have complications? Joslin's 50-Year Medalist Study is an example of the unique relationship between clinical researchers at Joslin and their colleagues who specialize in clinical epidemiology, genetics, biochemistry, and cell biology. The discovery that many of the 50-Year Medalists still have insulin-producing islet cells now requires an even broader course of action.
Certainly tackling the complexity of diabetes complications, such as cardiovascular, kidney, and eye disease, warrants a comprehensive and creative approach. Where else could you find a database of biological and psychological data from patients with diabetes, stretching back decades? Joslin Clinic records have been invaluable in studying how complications develop and progress over time. Genetics researchers at Joslin are studying what changes in the genes make people with diabetes susceptible to these complications. Other investigators focus on the impact of insulin on blood vessels. And still others specialize in the molecular mechanisms that lead to long-term complications.
Or consider the mystery of islet failure in type 1 and type 2 diabetes. At Joslin, groups of investigators who specialize in different disciplines collaborate. For example, we have researchers from the Integrative Physiology and Metabolism Section who focus on insulin action and islet survival; scientists from the Islet Cell and Regenerative Biology Section who study islet growth and action along with the regeneration of cells and experts from the Immunobiology Section who study autoimmune responses.
Moving Forward As Never Before
To extend the reach of our work, Joslin investigators not only partner with their colleagues down the hall and in the Harvard community, but work with scientists across the globe. We are committed to conquering diabetes in all of its forms and will continue to lead the scientific community on new pathways of discovery in diabetes.


text:
Taylor Hubbard, the 2010 Miss Kentucky Teen USA, knows the thrill of winning a beauty pageant. Sadly, she also knows what it's like to have her All-American looks scarred.
The high school senior, only minutes after switching from her prom gown into a leisure outfit last May, was attacked by a 5-year-old Siberian husky. Rushed to the hospital, Hubbard endured five-and-a-half hours of surgery and ended up with 200 stitches on her face.
She knew it was bad. "They wouldn't let me see my face," she said, "but I could feel out the bottom of my chin with my tongue. I knew how bad it was."
The healing process has continued over the summer months and additional surgeries will be required.
Hubbard recently received some good news. Others have stepped forward to help out with her specialized medical care needs.
The Miss Universe Organization, owned by Donald Trump, will be paying for all travel expenses, including hotel stays and flight costs to New York, and Dr. Paul Nassif, the doctor from Real Housewives of Beverly Hills, will be performing her surgeries pro-bono.
"I'm so excited. Words cannot even describe that they would care so much about a girl from southeastern Kentucky, go out of their way for me," she said.
Hubbard's life has been one dominated by emotional highs and lows.
She lost her mother, Denna, to cancer just two weeks after she returned home as the winner of the Teen USA competition at age 14.
"For every negative thing in my life, I've grown from it," Hubbard said. "I had a lot of inspiration and guidance. I could never have done anything I've done on my own and not any of it at all without my faith."
A short time after being attacked by a friend's dog, she was off on a mission trip to Puerto Rico. On the trip, Hubbard met an Alabama girl who had previously been in a car accident. She went through the windshield.
"She had had the same surgeries I was going to have," Hubbard said. "She talked to me about the procedures."
This did much to calm her fears.
Her next surgery will take place in Lexington, Ky., in about two months. Its primary goal will be to smooth the scars and advance the healing, Hubbard said.
From there, she will travel to New York for revision and removal with Dr. Nassif, who will follow up with a microdermabrasion surgery, also there. Hubbard then will be sent back to Lexington for a second laser surgery.
Surprisingly, Hubbard said her life is no different today than it was before she was bitten.
"They (scars) don't bother me. I could go through my life with them," she said. "I never placed an emphasis on outward appearances.
"I hope people don't first notice what's on the outside. I want to be noticed by my actions."
Details for this story were provided by Carrie Dillard, a reporter for the Sentinel-Echo in London, Ky.


text:
Cocktail Party Invitations
Other than the usual cleaning and laundry I do on days off, I did sneak in enough time to whip up these invites. One of my good groups of girlfriends and I get together every month or two at someone's house. The number who attend varies, but consistently there's at least 6 of us. We take turns hosting so usually host once or twice a year, and next month I get to play hostess with the mostess. We drink champagne, eat delish food, and gab all night. My friend Meghan's hubby dubbed us the Champagne Mafia a couple of years ago and it has stuck ever since.
Anyways, the point of this post is that I LOVE actual invites. I do not judge if you invite me somewhere via facebook or evite, but I personally love the look and feel of an actual paper invite. For me, especially, they are super easy to whip up, and since I'm a lover of all things old fashioned, I appreciate the nod to the past in which things were amiably formal.
And, gosh, I'm starting to get embarrassed by my constant mention of the dollar store, but I got this set of 10 invites (paper, backing and envelope) for just $2 making these 20 cents a piece. Best of all, this set by Peter Pauper Press sells on their website for $10. Shabang! Oh Dollorama, how I heart you <3


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As a part of the physical exam for
eating disorders, a doctor may order
certain tests to see whether your body is generally healthy. These may include
blood or urine tests to check:
A doctor may also test whether you have difficulty
digesting certain foods, such as milk and dairy products.
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August 25, 2011
Healthwise Staff
Medical Review:
Adam Husney, MD, MD - Family Medicine & W. Stewart Agras, MD - Psychiatry
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Women's Totem Valley Curated Crew Socks
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Inspired by the mountains. Made for everywhere. Our Women's Totem Valley Curated Crew socks were designed to help you express your wild side with Curateded patterns and premium Merino wool comfort that won't quit.
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The mountain village of Abisko is located at the foot of Mt. Nuolja in Swedish Lappland. This is where the finish line is for Fjällräven Classic and it is also the northern-most point of the classic trekking trail Kungsleden, the Kings Trail. Surrounded by the national park and beautiful mountains, Abisko is perfect as a point of departure for day hikes. It was with these kinds of adventures in mind that we developed the Abisko product family.
Wide-brimmed sun hat in fast-drying, cool G-1000 Lite. Adjustable chin strap and press ...
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Since 1960, nature's been in our DNA
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|December 6th, 2011, 03:15 PM
Join Date: May 2008
Location: Cyprus
Posts: 92
Mills on para-Mamluks
Hi Pierre,
About the para-Mamluk on FIG 50
I found an article by John Mills on Hali 93 (July 1997) presenting the painting: Mark Enthroned with Saints (detail) by Giovanni Martini da Udine, 1501, Duomo di Udine.
and a related rug
Title of the article:
THE CHIHIL SUTUN PARA-MAMLUK PRAYER RUG An unusual and enigmatic woolen prayer rug is among the precious relics preserved in the Chihil Sutun kiosk in Esfahan, built in the mid 17th century by Shah Abbas II. This article considers the relationship of the Chihil Sutun prayer rug to the well-known East Mediterranean (so-called Damascus) compartment or chess board carpets and the design-related para-Mamluk rugs.
Trying to synthesize at the maximum the article: while compartment rugs share design elements with the Cairo-made Mamluks, they differ in structure. Their wool is Z-spun, like the Anatolians but unlike the Cairenes, which are S-spun. Their knots, however, are asymmetric, like the Mamluks and unlike the Anatolians.
Thats why many attribute them to the environs of Damascus or Aleppo.
The structure of the para-Mamluk is less defined, meaning that they could use both types of knots (even on the same rug).
The prayer rug in question is symmetrically knotted. Its unique Kufik border is unknown (according to Mills) in its exact rendition on surviving rugs but illustrated on other paintings of the same period.
In short, The evidence from the paintings ant the Chihil Sutun prayer rug itself suggests that it is a 15th century artefact woven within the Mamluk cultural sphere, in an area susceptible to direct and relatively recent Timurid influence. This seems to point once again to the northern part of the Mamluk domain, either Damascus or further north in Aleppo or the Adana Plain.
I hope this is of some interest
Best regards,
|December 7th, 2011, 10:01 AM
Join Date: Oct 2009
Posts: 87
Hi Filiberto,
Thank you for having discovered the author of the painting and this superb extant rug !
As stated by Mills, the beautiful border of the Chihil Sutun rug caught the eyes of several other renaissance painters. For example A. Mantegna in a famous fresco (1471-1474) of the Ducal Palace in Mantova. FIG 1 & 2 . below), T. DAndria (1487. Duomo di Savona) or A. Previtali (1508. Annunciation. Vittorio Veneto).
Does Mills write anything about the red dye used in the Chihil Sutun rug? Does he perhaps mention lac (Kerria lacca)? This red insect dye has a typical shade, rather easy to differentiate from madder- or cochineal reds and is claimed to be a very rare occurrence in rugs, except on ( Cairene ) «Mamluk» carpets and sometimes on Safavid Persian pieces. Its presence (or not) could give a minor clue about the provenance of the rug.
By the way, while «Para-Mamluk» rugs were frequently used as studio props during the 14th and until well into the 15th century, I am a trifle puzzled by the conspicuous absence of so-called «Mamluk» rugs in paintings before 1540 M. da Brescia was perhaps the first to feature Mamluk rugs in "Daughters of the House of Martinengo" ca. 1543-1547 ).
Did the Ottoman not hang the last Mamluk ruler ca. 1515 or 1517? Do we have other proofs (C14 tests on extant rugs for example) that these «Mamluk» rugs were indeed woven during the Mamluk empire? Or should we rather call them «Cairene Ottoman rugs» or perhaps «Posthumous Mamluk rugs» ? Perhaps the explanation is that their traditional low-contrast patterns and subdued shades which did not appeal to most Italian painters nor to their patrons?
Best regards
|December 7th, 2011, 05:34 PM
Join Date: May 2008
Location: Cyprus
Posts: 92
Hi Pierre,
No, Mills doesn't mention anything specific about the kind of dyes. Actually, he doesn't mention having met personally the rug in question, which I doubt.
About your perplexity on "the conspicuous absence of so-called «Mamluk» rugs in paintings before 1540", I went to read "in diagonal" Michael Franses' article (second part) on the Museum of Islamic Art in Doha. It's available in pdf format on HALI's website here:
but I think you should have it already.
Franses's phrase:
"Carpets in the 'Mamluk-style' (I use this term because most surviving examples were probably made after the Ottomans overthrew the Mamluk Sultanate in 1517)"
should clarify your doubts, as well as the following:
Recently published research by Marco Spallanzani informs us that "…in 1545 Iacopo Capponi went to Alexandria with instructions to buy various things for Duke Cosimo I de Medici, including an unspecified number of rugs to be made to order",which were shipped to Livorno in 1547.
By the way, note 70 of the same article lists "fifteen European paintings… that depict identifiable Mamluk-style carpets from Cairo" which you may want to check if some of them are missing from your database.
|December 9th, 2011, 03:23 PM
Join Date: Oct 2009
Posts: 87
Hi Filiberto,
So, Frances already had stated that «Mamluk rug» is a misnomer? But how comes? Fantasy names are such a rare occurence in Rugdom.
Quote: fifteen European paintings that depict identifiable Mamluk-style carpets from Cairo
I agree. Indeed, several «Mamluk» rugs are probably missing in our painting data base. However, I do claim extenuating circumstances: the lack of contrast of these rugs does not make their identification easy on pictures.
In Da Brescias «Daughters of House of Martinengo, 1543-1546», one can note an interesting point:
Many (most?) extant «Mamluk» rugs show a dominant «lac» red shade. See for example FIG 1 (15th century, Thyssen Bornmisza collection) and FIG 2.
But in the six Martinengo rugs a reddish-brown shade dominates (FIG 3). Perhaps these rugs were made on order, (the 6 rugs are very similar) and Sig. Martinengo influenced the choice of the shade. Or Da Brescias red pigment was poor.
FIG 3. M. da Brescia. 1543-1546. Daughters of the House of Martinengo. Brescia.
|December 9th, 2011, 06:58 PM
Join Date: May 2008
Location: Cyprus
Posts: 92
Hi Pierre,
Using colors of an old painting as yardstick is not a good idea.
I don't want to bore our few readers, but colors change with age, varnish oxides. As such the painting may be in need of cleaning and so on (and while cleaning, good restorer should leave a nice patina in any case).
As far I can see, Moretto da Brescia's murals (that - it seems - combined different techniques: fresco, tempera, and oils) show on the "sky" part traces of a yellowish varnish that, if present also on the rugs section could alter the perception of the original red. But that section looks like a "fresco" technique, so no varnish…
Then, there is the old, classical problem… Is the photo itself good? This one seems too yellow.
It took a while, but I found better photos at the Web Gallery of Art.
This, for example:
(link: http://www.wga.hu/html_m/m/moretto/fresco1.html)
The shade of red here is much more compatible – with the aforementioned caveats – with the photos of those Mamluk rugs, I think. Do you agree?
If so, you owe to Mr. Moretto da Brescia an apology four questioning his pigments.
P.S. - I do apologize for posting a picture too wide, but I did it for the sake of proper visibility of the colors
|December 9th, 2011, 08:50 PM
Join Date: Oct 2009
Posts: 87
Yes Filiberto,
The combination of a better picture and your expertise of painting restoration is persuasive enough.
I hope Mr. Da Brescia will accept my apologies.
|March 15th, 2012, 07:36 PM
Join Date: May 2008
Location: Fairport, NY
Posts: 38
I'm curious about your statement concerning the rarity of lac-dyed rugs. Is that specific for these 16th c rugs or do you mean all rugs. If the latter, how do you account for the descriptions of lac in many Turkmen pieces? ("many" is relative, of course, but there a quite a few truly antique Turkmens with this description.
|March 15th, 2012, 10:02 PM
Join Date: Oct 2009
Posts: 87
Hi Marvin,
Well, lac has been found in some persian- (see for example H. Boehmer, Kekboya, page 202) and Mamluk rugs. But I haven't met, so far, any analytical work proving its presence in Turkmen rugs. Do you? It would be interesting.
A few mentions of lac dyes in Turkmen carpets have been made in collector- or dealer books or articles, but I can't remember any mention of analytical tests. I have seen a rather... creative theory about Salor tribesmen being involved in lac trade, but have serious doubts, especially when the description of the lac shade conflicts with reality.
Of course, the possibility that some lac had found its way to this region cannot be completely excluded.
By the way, the dyes of a rather large number of anatolian rugs of the museum of Budapest have been analyzed too, and unless I err, lac has not been identified in any.
I can offer no explanation for the limited use of this beautiful (but rather dull) dye, which is not difficult to apply on wool or silk and has excellent fastness.
Best regards
|March 16th, 2012, 02:34 PM
Join Date: May 2008
Location: Fairport, NY
Posts: 38
Thanks, Pierre, for that comment about the lack of evidence for lac in Turkmen pieces. I had always believed that dealer/collector comments about its presence was suspect. Just another myth to add to the many in the rug literature. Too bad there is no report of the analysis of these lac-red areas in Turkmen pieces.
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The "90210" actress AnnaLynne McCord has been named the face of Marc Ecko Handbags for the label's spring/summer 2011 ad campaign that will be launched online and in-print. Photographed by celebrity and fashion photographer Tony Duran, at Siren Studios in Hollywood, the ad has a provocative and sexy touch, with AnnaLynne McCord wearing nothing but Marc Ecko handbags. Speaking about the brand's new face, Ecko seems more than thrilled about the choice made saying that "AnnaLynne is a proper bombshell. She makes my heart skip a beat. S... Read More


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ROSES ARE RED brand introduces a luxury collection of timeless silk dresses, kimonos and lingerie for women who choose high production quality, pure fabrics and elegant lifestyle.
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The Changing States of Solids, Liquids, and Gases
When a substance goes from one state of matter — solid, liquid, or gas — to another state of matter, the process is a change of state. Some rather interesting things occur during this process.
Melting point as a chemistry concept
If you measure the temperature of a chunk of ice, you may find it to be –5° Celsius or so. If you take temperature readings while heating the ice in a pot on your stove, you find that the temperature of the ice begins to rise as the heat from the stove causes the ice particles to begin vibrating faster and faster.
After a while, some of the particles move so fast that they break free of the crystal lattice (which keeps a solid solid), and the lattice eventually breaks apart. The solid begins to go from a solid state to a liquid state — a process called melting. The temperature at which melting occurs is the melting point (mp) of the substance. The melting point for ice is 32° Fahrenheit, or 0° Celsius.
If you watch the temperature of ice as it melts, you see that the temperature remains steady at 0°C until all the ice has melted. During changes of state (phase changes), the temperature remains constant even though the liquid contains more energy than the ice (because the particles in liquids move faster than the particles in solids).
Boiling point of water
If you heat a pot of cool water, the temperature of the water rises and the particles move faster and faster as they absorb the heat. The temperature rises until the water reaches the next change of state — boiling. As the particles move faster and faster, they begin to break the attractive forces between each other and move freely as steam — a gas.
The process by which a substance moves from the liquid state to the gaseous state is called boiling. The temperature at which a liquid begins to boil is called the boiling point (bp). The bp is dependent on atmospheric pressure, but for water at sea level, it's 212°F, or 100°C. The temperature of the boiling water will remain constant until all the water has been converted to steam.
You can summarize the process of water changing from a solid to a liquid to a gas in this way:
Because the basic particle in ice, water, and steam is the water molecule, the same process can also be shown as:
Here the (s) stands for solid, the (l) stands for liquid, and the (g) stands for gas. Unlike water, most chemical substances don't have different names for the solid, liquid, and gas forms.
Freezing point of a substance
If you cool a gaseous substance, you can watch the phase changes that occur. The phase changes are:
Condensation — going from a gas to a liquid
Freezing — going from a liquid to a solid
The gas particles have a high amount of energy, but as they're cooled, that energy is reduced. The attractive forces now have a chance to draw the particles closer together, forming a liquid. This process is called condensation. The particles are now in clumps, but as more energy is removed by cooling, the particles start to align themselves, and a solid is formed. This is known as freezing. The temperature at which this occurs is called the freezing point (fp) of the substance.
You can represent water changing states from a gas to a solid like this:
Most substances go through the logical progression from solid to liquid to gas as they're heated — or vice versa as they're cooled. But a few substances go directly from the solid to the gaseous state without ever becoming a liquid. Scientists call this process sublimation. Dry ice — solid carbon dioxide — is the classic example of sublimation. You can see dry ice particles becoming smaller as the solid begins to turn into a gas, but no liquid is formed during this phase change.
The process of sublimation is represented as:
In addition to dry ice, mothballs and certain solid air fresheners also go through the process of sublimation. The reverse of sublimation is deposition — going directly from a gaseous state to a solid state.


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Studs Terkel noted that people around the world respond to someone who's just told them they're from the Windy City with "Oh, I know Chicago! Bang! Bang!"
Al Capone is truly the man who made Chicago infamous, but soon people the world over may think of a new sound when they hear about Chicago -- the love song of its most famous gangster.
Capone never sang to the feds, but his stint in Alcatraz turned him into a songwriter.
It turns out he penned a traditional Italian love song he called "Madonna Mia," but it has never been performed.
Rich Larson, from the Capone Fan Club (that's right -- there's a Capone fan club) was instrumental in putting a band together to record the music. He called the song a "tearjerker."
The song is soon to be released on CD. An inscribed copy of the music is now up for a cool $65,000, the Associated Press noted.
"Madonna Mia," by the way, is also a poem by Oscar Wilde, who spent some time in jail himself, although for entirely different reasons. Not sure if Capone was trying to tell us something there.


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