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dc.creatorUversky, VN
dc.creatorOldfield, CJ
dc.creatorMidic, U
dc.creatorXie, H
dc.creatorXue, B
dc.creatorVucetic, S
dc.creatorIakoucheva, LM
dc.creatorObradovic, Z
dc.creatorKeith, AK
dc.date.accessioned2021-02-01T00:28:45Z
dc.date.available2021-02-01T00:28:45Z
dc.date.issued2009-07-07
dc.identifier.issn1471-2164
dc.identifier.issn1471-2164
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5554
dc.identifier.other19594884 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5572
dc.description.abstractBackground: Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) lack stable tertiary and/or secondary structure yet fulfills key biological functions. The recent recognition of IDPs and IDRs is leading to an entire field aimed at their systematic structural characterization and at determination of their mechanisms of action. Bioinformatics studies showed that IDPs and IDRs are highly abundant in different proteomes and carry out mostly regulatory functions related to molecular recognition and signal transduction. These activities complement the functions of structured proteins. IDPs and IDRs were shown to participate in both one-to-many and many-to-one signaling. Alternative splicing and posttranslational modifications are frequently used to tune the IDP functionality. Several individual IDPs were shown to be associated with human diseases, such as cancer, cardiovascular disease, amyloidoses, diabetes, neurodegenerative diseases, and others. This raises questions regarding the involvement of IDPs and IDRs in various diseases. Results: IDPs and IDRs were shown to be highly abundant in proteins associated with various human maladies. As the number of IDPs related to various diseases was found to be very large, the concepts of the disease-related unfoldome and unfoldomics were introduced. Novel bioinformatics tools were proposed to populate and characterize the disease-associated unfoldome. Structural characterization of the members of the disease-related unfoldome requires specialized experimental approaches. IDPs possess a number of unique structural and functional features that determine their broad involvement into the pathogenesis of various diseases. Conclusion: Proteins associated with various human diseases are enriched in intrinsic disorder. These disease-associated IDPs and IDRs are real, abundant, diversified, vital, and dynamic. These proteins and regions comprise the disease-related unfoldome, which covers a significant part of the human proteome. Profound association between intrinsic disorder and various human diseases is determined by a set of unique structural and functional characteristics of IDPs and IDRs. Unfoldomics of human diseases utilizes unrivaled bioinformatics and experimental techniques, paves the road for better understanding of human diseases, their pathogenesis and molecular mechanisms, and helps develop new strategies for the analysis of disease-related proteins. © 2009 Uversky et al; licensee BioMed Central Ltd.
dc.format.extentS7-S7
dc.language.isoen
dc.relation.haspartBMC Genomics
dc.relation.isreferencedbySpringer Science and Business Media LLC
dc.rightsCC BY
dc.subjectAlternative Splicing
dc.subjectComputational Biology
dc.subjectHumans
dc.subjectProtein Folding
dc.subjectProtein Processing, Post-Translational
dc.subjectProtein Structure, Secondary
dc.subjectProtein Structure, Tertiary
dc.subjectProteins
dc.subjectStructure-Activity Relationship
dc.titleUnfoldomics of human diseases: Linking protein intrinsic disorder with diseases
dc.typeArticle
dc.type.genreConference Proceeding
dc.relation.doi10.1186/1471-2164-10-S1-S7
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.date.updated2021-02-01T00:28:40Z
refterms.dateFOA2021-02-01T00:28:46Z


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