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Journal ArticleDOI

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.

Peter E. Wright, +1 more
- 22 Oct 1999 - 
- Vol. 293, Iss: 2, pp 321-331
TLDR
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.
About: 
This article is published in Journal of Molecular Biology.The article was published on 1999-10-22. It has received 2804 citations till now. The article focuses on the topics: Protein structure function & Intrinsically disordered proteins.

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Citations
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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Functional organization of the yeast proteome by systematic analysis of protein complexes

Anne-Claude Gavin, +37 more
- 10 Jan 2002 - 
TL;DR: The analysis provides an outline of the eukaryotic proteome as a network of protein complexes at a level of organization beyond binary interactions, which contains fundamental biological information and offers the context for a more reasoned and informed approach to drug discovery.
Journal ArticleDOI

Intrinsically unstructured proteins and their functions.

H. Jane Dyson, +1 more
- 01 Mar 2005 - 
TL;DR: Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
Journal ArticleDOI

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Vladimir N. Uversky, +3 more
- 15 Nov 2000 - 
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.

Peter Tompa
- 01 Oct 2002 - 
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.
References
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Journal ArticleDOI

Folding intermediates of SNARE complex assembly.

Klaus M. Fiebig, +3 more
- 01 Feb 1999 - 
TL;DR: NMR spectroscopy data suggest a directed assembly process beginning distal to the membrane surfaces and proceeding toward them, bringing membranes into close proximity and possibly leading to membrane fusion.
Journal ArticleDOI

Induced α Helix in the VP16 Activation Domain upon Binding to a Human TAF

Motonari Uesugi, +8 more
- 29 Aug 1997 - 
TL;DR: Identification of the two hydrophobic residues that make nonpolar contacts suggests a general recognition motif of acidic activation domains for hTAFII31, a human TFIID TATA box – binding protein-associated factor.
Journal ArticleDOI

The 'molten globule' state is involved in the translocation of proteins across membranes?

V. E. Bychkova, +2 more
- 10 Oct 1988 - 
TL;DR: It is proposed that a compact state having secondary but not rigid tertiary structure and called the ‘molten globule' state may be suitable candidates for protein translocation across biological membranes.
Journal ArticleDOI

Design of DNA-binding peptides based on the leucine zipper motif

Karyn T. O'Neil, +2 more
- 17 Aug 1990 - 
TL;DR: A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of a "leucine zipper" sequence that associates into noncovalent, parallel, alpha-helical dimers and a covalently connected basic region necessary for binding DNA.
Proceedings Article

Thousands of proteins likely to have long disordered regions.

Pedro Romero, +6 more
TL;DR: The results support proposals that consideration of structure-activity relationships in proteins need to be broadened to include unfolded or disordered protein.
Related Papers (5)

Intrinsically unstructured proteins and their functions.

H. Jane Dyson, +1 more
- 01 Mar 2005 - 

Intrinsically unstructured proteins.

Peter Tompa
- 01 Oct 2002 - 

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Vladimir N. Uversky, +3 more
- 15 Nov 2000 - 

Intrinsically Disordered Proteins

Vladimir N. Uversky, +2 more

Intrinsic Disorder and Protein Function

A. Keith Dunker, +4 more
- 01 May 2002 -