Journal ArticleDOI
Natively unfolded proteins.
TLDR
New algorithms have been developed to identify disordered regions of proteins and have demonstrated their presence in cancer-associated proteins and proteins regulated by phosphorylation.About:
This article is published in Current Opinion in Structural Biology.The article was published on 2005-02-01. It has received 687 citations till now. The article focuses on the topics: Intrinsically disordered proteins & Nuclear pore.read more
Citations
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Classification of intrinsically disordered regions and proteins.
Robin van der Lee,Robin van der Lee,Marija Buljan,Benjamin Lang,Robert J. Weatheritt,Gary W. Daughdrill,A. Keith Dunker,Monika Fuxreiter,Julian Gough,Joerg Gsponer,David T. Jones,Philip M. Kim,Richard W. Kriwacki,Christopher J. Oldfield,Rohit V. Pappu,Peter Tompa,Peter Tompa,Vladimir N. Uversky,Vladimir N. Uversky,Peter E. Wright,M. Madan Babu +20 more
TL;DR: Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes and is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood.
Journal ArticleDOI
Protein structure homology modeling using SWISS-MODEL workspace
Lorenza Bordoli,Florian Kiefer,Florian Kiefer,Konstantin Arnold,Konstantin Arnold,Pascal Benkert,Pascal Benkert,James N. D. Battey,James N. D. Battey,Torsten Schwede,Torsten Schwede +10 more
TL;DR: Homology modeling aims to build three-dimensional protein structure models using experimentally determined structures of related family members as templates to generate reliable structural models and is routinely used in many biological applications.
Journal ArticleDOI
Understanding protein non-folding.
TL;DR: This review describes the family of intrinsically disordered proteins, members of which fail to form rigid 3-D structures under physiological conditions, either along their entire lengths or only in localized regions.
Journal ArticleDOI
Flexible nets. The roles of intrinsic disorder in protein interaction networks.
A. Keith Dunker,Marc S. Cortese,Pedro Romero,Pedro Romero,Lilia M. Iakoucheva,Vladimir N. Uversky,Vladimir N. Uversky +6 more
TL;DR: This review examines the roles of intrinsic disorder in protein network architecture and shows that there are three general ways that intrinsic disorder can contribute: First, intrinsic Disorder can serve as the structural basis for hub protein promiscuity; secondly, intrinsically disordered proteins can bind to structured hub proteins; and thirdly, intrinsic disorderCan provide flexible linkers between functional domains with the linkers enabling mechanisms that facilitate binding diversity.
Journal ArticleDOI
Structure and Mechanism of the Hsp90 Molecular Chaperone Machinery
TL;DR: Present knowledge of Hsp90 structure and function gleaned from crystallographic studies of individual domains and recent progress in obtaining a structure for the ATP-bound conformation of the intact dimeric chaperone are discussed.
References
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Journal ArticleDOI
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E. Wright,H. Jane Dyson +1 more
TL;DR: Many proteins that lack intrinsic globular structure under physiological conditions have now been recognized, and it appears likely that their rapid turnover, aided by their unstructured nature in the unbound state, provides a level of control that allows rapid and accurate responses of the cell to changing environmental conditions.
Journal ArticleDOI
Why are "natively unfolded" proteins unstructured under physiologic conditions?
TL;DR: Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, has been applied to two sets of proteins and shows that “natively unfolded” proteins are specifically localized within a unique region of charge‐hydrophobia phase space.
Journal ArticleDOI
Intrinsically unstructured proteins.
TL;DR: In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where proteins can be comprehensively classified on the basis of structure and function.
Journal ArticleDOI
Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.
TL;DR: An automatic method for recognizing natively disordered regions from amino acid sequence is described and benchmarked against predictors that were assessed at the latest critical assessment of techniques for protein structure prediction (CASP) experiment and represents a statistically significant improvement on the methods evaluated on the same targets at CASP.
Journal ArticleDOI
Natively unfolded proteins: a point where biology waits for physics.
TL;DR: Results of this analysis showed that intrinsically unstructured proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity, and the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globule, premolten globules, and random coils) is discussed.
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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
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