Function and structure of inherently disordered proteins - Wikidata - awgldk - TriplyDB

Function and structure of inherently disordered proteins

Function and structure of inherently disordered proteins

http://www.wikidata.org/entity/Q22061740

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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins Protein-mediated enamel mineralization SAHG, a comprehensive database of predicted structures of all human proteins Recommendations of the wwPDB NMR Validation Task Force SPINE-D: accurate prediction of short and long disordered regions by a single neural-network based method ProRepeat: an integrated repository for studying amino acid tandem repeats in proteins Separate roles of structured and unstructured regions of Y-family DNA polymerases Intrinsically disordered proteins in a physics-based world Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry Intrinsically disordered proteins are potential drug targets Prostate-associated gene 4 (PAGE4), an intrinsically disordered cancer/testis antigen, is a novel therapeutic target for prostate cancer Drug Development in Alzheimer's Disease: The Contribution of PET and SPECT An Overview of Predictors for Intrinsically Disordered Proteins over 2010-2014 A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins Mechanisms of amyloid formation revealed by solution NMR Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes Protein Folding and Mechanisms of Proteostasis Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Macromolecule-assisted de novo protein folding What macromolecular crowding can do to a protein Small-molecule inhibitors of the Myc oncoprotein A nonsynonymous mutation in the transcriptional regulator lbh is associated with cichlid craniofacial adaptation and neural crest cell development.Structure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated Glycan Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF Ordering a Dynamic Protein Via a Small-Molecule Stabilizer Intrinsically Disordered Side of the Zika Virus Proteome Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: Identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1 Order and disorder in large multi-site docking proteins of the Gab family--implications for signalling complex formation and inhibitor design strategies Structural polymorphism of 441-residue tau at single residue resolution Markov models of amino acid substitution to study proteins with intrinsically disordered regions The impact of small molecule binding on the energy landscape of the intrinsically disordered protein C-myc Melanoma-associated cancer-testis antigen 16 (CT16) regulates the expression of apoptotic and antiapoptotic genes and promotes cell survival Prokaryotic ubiquitin-like protein pup is intrinsically disordered NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin

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P2860

Function and structure of inherently disordered proteins

http://www.wikidata.org/entity/Q22061740

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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Function and structure of inherently disordered proteins

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J.SBI.2008.10.002

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Current Opinion in Structural Biology

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Function and structure of inherently disordered proteins

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A Keith Dunker

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scholarly article

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1121029

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10.1016/J.SBI.2008.10.002

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Joel L. Sussman

Vladimir Uversky

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2008-12-01T00:00:00Z

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23415435

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protein structure

structural biology