The loss of tryptophan 194 in antichymotrypsin lowers the kinetic barrier to misfolding (Q58023315)

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1 January 2020

title

The loss of tryptophan 194 in antichymotrypsin lowers the kinetic barrier to misfolding (English)

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1 January 2020

3

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4

Stephen P Bottomley

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1 January 2020

author name string

Mary C Pearce

series ordinal

1

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1 January 2020

Lisa D Cabrita

series ordinal

2

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language of work or name

English

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publication date

3 July 2007

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1 January 2020

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1 January 2020

volume

274

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issue

14

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page(s)

3622-3632

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How do proteins avoid becoming too stable? Biophysical studies into metastable proteins

1 January 2020

cites work

1 reference

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Structure of a serpin-protease complex shows inhibition by deformation

21 January 2018

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Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.

21 January 2018

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Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition

21 January 2018

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Promiscuous beta-strand interactions and the conformational diseases.

21 January 2018

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Biological implications of a 3 A structure of dimeric antithrombin

21 January 2018

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Cleaved antitrypsin polymers at atomic resolution

21 January 2018

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Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A Linkage

21 January 2018

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What do dysfunctional serpins tell us about molecular mobility and disease?

21 January 2018

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Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.

21 January 2018

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Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function.

21 January 2018

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Mutation of the Highly Conserved Tryptophan in the Serpin Breach Region Alters the Inhibitory Mechanism of Plasminogen Activator Inhibitor-1

21 January 2018

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Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding.

21 January 2018

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Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state

21 January 2018

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Conformational changes in serpins: I. the native and cleaved conformations of α 1 -antitrypsin 1 1Edited by J. M. Thornton

21 January 2018

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Identification of residual structure within denatured antichymotrypsin: implications for serpin folding and misfolding

21 January 2018

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Nucleation of alpha 1-antichymotrypsin polymerization

21 January 2018

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The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity

21 January 2018

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The mechanism of alpha 1-antitrypsin polymerization probed by fluorescence spectroscopy.

21 January 2018

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Acid Denaturation of alpha1-antitrypsin: characterization of a novel mechanism of serpin polymerization.

21 January 2018

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The mechanism of Z alpha 1-antitrypsin accumulation in the liver

21 January 2018

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The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins

21 January 2018

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The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion

21 January 2018

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Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation.

21 January 2018

1 reference

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Loop-sheet polymerization: the structural basis of Z alpha 1-antitrypsin accumulation in the liver

21 January 2018

1 reference

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Physical characterization of serpin conformations

21 January 2018

1 reference

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10.1111/J.1742-4658.2007.05897.X

21 January 2018

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17608807%20AND%20SRC:MED&resulttype=core&format=json

1 January 2020

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