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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

Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation.

M L Schmitz, +5 more
- 14 Oct 1994 - 
TL;DR: A model suggesting that primarily unstructured acidic activation domains can adopt a secondary structure upon contacting their target molecules by an "induced fit" mechanism is proposed.
Journal ArticleDOI

Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB.

Ishwar Radhakrishnan, +3 more
- 03 Jul 1998 - 
TL;DR: Heteronuclear NMR spectroscopic analyses reveal that the KID domain is largely unstructured except for residues that comprise the αA helix in the pKID‐KIX complex, which populate helical conformations to a significant extent.
Journal ArticleDOI

Predicting Disordered Regions from Amino Acid Sequence: Common Themes Despite Differing Structural Characterization.

Ethan C. Garner, +4 more
- 01 Jan 1998 - 
TL;DR: The results from the two predictors suggest that disordered regions comprise a sequence-dependant category distinct from that of ordered protein structure.
Journal ArticleDOI

Role of Secondary Structure in Discrimination between Constitutive and Inducible Activators

David Parker, +9 more
- 01 Aug 1999 - 
TL;DR: The results indicate that the constitutive and inducible activation properties of c-Myb and CREB reflect secondary structural characteristics of their corresponding activating regions that influence the thermodynamics of formation of a complex with CBP.
Journal ArticleDOI

How representative are the known structures of the proteins in a complete genome? A comprehensive structural census

Mark Gerstein
- 01 Nov 1998 - 
TL;DR: The proteins encoded by the genomes are significantly different from those in the structure databank, and their sequence lengths, which follow an extreme value distribution, are longer than the PDB proteins and much shorter than the biophysical proteins.
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 -