Inhibiting polymerization: new therapeutic strategies for Z alpha1-antitrypsin-related emphysema. (Q47963712)

7 February 2018

title

Inhibiting polymerization: new therapeutic strategies for Z alpha1-antitrypsin-related emphysema. (English)

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7 February 2018

author

Tim Dafforn

2

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author name string

Helen Parfrey

1

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7 February 2018

Didier Belorgey

3

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David A Lomas

4

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Ravi Mahadeva

5

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publication date

11 March 2004

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American Journal of Respiratory Cell and Molecular Biology

published in

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volume

31

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issue

2

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page(s)

133-139

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The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature

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Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function

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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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Structure of a serpin-protease complex shows inhibition by deformation

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

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Familial dementia caused by polymerization of mutant neuroserpin

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Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)

21 January 2018

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Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease

21 January 2018

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Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy

21 January 2018

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6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis

21 January 2018

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Mutations which impede loop/sheet polymerization enhance the secretion of human alpha 1-antitrypsin deficiency variants.

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Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A.

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Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin

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Probing serpin reactive-loop conformations by proteolytic cleavage

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Inhibition of human pancreatic proteinases by mucus proteinase inhibitor, eglin c and aprotinin

21 January 2018

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Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide

21 January 2018

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The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions

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Biological implications of a 3 A structure of dimeric antithrombin

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Polymerization of plasminogen activator inhibitor-1.

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

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A Kinetic Mechanism for the Polymerization of α1-Antitrypsin

21 January 2018

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Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins

21 January 2018

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Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin

21 January 2018

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Theoretical and practical aspects of proteinase inhibition kinetics

21 January 2018

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21 January 2018

Identifiers

DOI

10.1165/RCMB.2003-0276OC

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7 February 2018

PubMed ID

15016619

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7 February 2018