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

doi:10.1006/JMBI.1999.3110

Journal ArticleDOI

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

Peter E. Wright, +1 more

- 22 Oct 1999 -

Journal of Molecular Biology

- 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.

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

Daniel J. Klionsky, +2522 more

- 21 Jan 2016 -

Autophagy

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.

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

Anne-Claude Gavin, +37 more

- 10 Jan 2002 -

Nature

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.

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Intrinsically unstructured proteins and their functions.

H. Jane Dyson, +1 more

- 01 Mar 2005 -

Nature Reviews Molecular Cell Biology

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.

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Journal ArticleDOI

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

Vladimir N. Uversky, +3 more

- 15 Nov 2000 -

Proteins

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.

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Intrinsically unstructured proteins.

Peter Tompa

- 01 Oct 2002 -

Trends in Biochemical Sciences

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.

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References

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Transcriptional control: Versatile molecular glue

Ralf Janknecht, +1 more

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Current Biology

TL;DR: CBP and p300 are versatile coactivators that physically connect many DNA-binding factors to the basal transcription machinery.

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Himangshu S. Bose, +3 more

- 22 Jun 1999 -

Proceedings of the National Academy of S...

TL;DR: As the mitochondrial proton pump results in an electrochemical gradient, and as StAR must unfold during mitochondrial entry, StAR probably undergoes a similar conformational shift to an extended structure while interacting with the mitochondrial outer membrane, allowing this apparent molten globule form to act as an on/off switch for cholesterol entry into the mitochondria.

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Journal ArticleDOI

Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface.

V. E. Bychkova, +5 more

- 14 May 1996 -

Biochemistry

TL;DR: The conditions at which the alcohol-induced molten globule exists could be similar to those existing near negatively charged membrane surfaces and might explain how the molten globules state can be achieved under physiological conditions.

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Journal ArticleDOI

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David H. Bechhofer

- 01 Sep 1990 -

Molecular Microbiology

TL;DR: The ermC gene confers resistance to MLS antibiotics in a Bacillus subtilis host by constituting a ribosomal RNA methylase and is inducible by the addition of subinhibitory concentrations of erythromycin.

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The patterns of binding of RAR, RXR and TR homo- and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains.

Sylvie Mader, +5 more

- 15 Dec 1993 -

The EMBO Journal

TL;DR: Heterodimerization of retinoid X receptor (RXR) with either retinoic acid receptors (RAR) or thyroid hormone receptor (TR) alters the binding site repertoires of RAR, RXR and TR homodimers, and evidence is provided supporting the view that the cooperative binding of the RXR/RAR and RXr/TR DBDs to directly repeated elements is anisotropic.

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