{'fraction_non_alphanumeric': 0.01707317073170732, 'fraction_numerical': 0.0, 'mean_word_length': 5.729508196721311, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Brain site‐specific determination of protein solubility in Alzheimer's disease

Neurodegenerative disease such as Alzheimer's disease (AD) is characterized by the presence in nervous tissue of aggregates of protein with decreased solubility. Recently, we described our use of proteomic methods to discover novel proteins with decreased solubility in temporal cortex of patients with AD compared to controls. We have developed a technique of graded tissue extraction to more precisely compare the solubilities of proteins in brain tissue derived from patients with AD, prodromal dementia, and nondemented controls. Application of this method to a variety of brain tissue sites demonstrates site‐ and disease‐specific correlations between the solubilities of proteins known to be important in AD and novel protein species.