(Q57980256)

1

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Timothy R. Dafforn

2

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Peter G. W. Gettins

3

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David A Lomas

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

2 August 2000

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number of pages

6

1 reference

based on heuristic

inferred from page(s)

published in

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volume

275

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issue

43

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page(s)

33663-33668

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cites work

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Inhibitory conformation of the reactive loop of alpha 1-antitrypsin

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

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Mapping the serpin-proteinase complex using single cysteine variants of alpha1-proteinase inhibitor Pittsburgh

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Structural basis for serpin inhibitor activity

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

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

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alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.

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

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

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Plasminogen-activator inhibitor type 2 (PAI-2) is a spontaneously polymerising SERPIN. Biochemical characterisation of the recombinant intracellular and extracellular forms

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

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A Kinetic Mechanism for the Polymerization of α1-Antitrypsin

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17 The use of singlet-singlet energy transfer to study macromolecular assemblies

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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.

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Detection of actin assembly by fluorescence energy transfer

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Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease

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Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins

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The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer

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

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Distortion of the active site of chymotrypsin complexed with a serpin

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Risk of cirrhosis and primary liver cancer in alpha 1-antitrypsin deficiency

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