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Cited by 270

The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.

Native State Proline Isomerization: An Intrinsic Molecular Switch

Andreotti, Amy H.·2003·Biochemistry
DOI 10.1021/bi0350710
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Abstract

Exquisite control of biological function is achieved via tight regulation of the catalytic and binding activities of cellular proteins. The mechanistic details of protein regulation vary from targeted chemical modification of amino acid side chains (1) to the quite drastic global unfolding of an entire polypeptide chain (2). Peptidyl prolyl cis/trans isomerization is emerging as a potentially general mechanism for the control of protein function (3). While most structures of native, folded proteins reveal peptidyl-prolyl imide bonds that adopt either the cis or trans conformation, there are a growing number of folded proteins that exhibit conformational heterogeneity about one or more peptidyl-prolyl bonds. Unlike covalent modification or global unfolding, proline isomerization is an intrinsic conformational exchange process that has the potential to direct ligand recognition and to control protein activity within the confines of the native state.

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Metadata

Authors
Andreotti, A. H.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2003-07-24
Volume
42
Issue
32
Pages
9515-9524
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi0350710
OpenAlex
W2057451487
Cited by
270
References
17
FWCI
4.29
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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