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Structure of a serpin-protease complex shows inhibition by deformation

Nature (London), 2000-10, Vol.407 (6806), p.923-926

2000

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Conformational disease

The Lancet (British edition), 1997-07, Vol.350 (9071), p.134-138

1997

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Contents of partitions and the combinatorics of permutation factorizations in genus 0

Transactions of the American Mathematical Society, 2018-07, Vol.370 (7), p.5051-5080

2018

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Serpinopathies and the conformational dementias

Nature reviews. Genetics, 2002-10, Vol.3 (10), p.759-768

2002

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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

The Journal of biological chemistry, 2001-09, Vol.276 (36), p.33293-33296

2001

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The Anticoagulant Activation of Antithrombin by Heparin

Proceedings of the National Academy of Sciences - PNAS, 1997-12, Vol.94 (26), p.14683-14688

1997

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Mutations in the shutter region of antithrombin result in formation of disulfide‐linked dimers and severe venous thrombosis

Journal of thrombosis and haemostasis, 2004-06, Vol.2 (6), p.931-939

2004

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Conformational changes and disease — serpins, prions and Alzheimer's

Current opinion in structural biology, 1998-12, Vol.8 (6), p.799-809

1998

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Latent antithrombin and its detection, formation and turnover in the circulation

Journal of thrombosis and haemostasis, 2004-12, Vol.2 (12), p.2170-2177

2004

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Prevalence of antithrombin deficiency in the healthy population

British journal of haematology, 1994-05, Vol.87 (1), p.106-112

1994

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Implications of the three-dimensional structure of α1-antitrypsin for structure and function of serpins

Biochemistry (Easton), 1989, Vol.28 (23), p.8951-8966

1989

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The mechanism of Z α1-antitrypsin accumulation in the liver

Nature (London), 1992-06, Vol.357 (6379), p.605-607

1992

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The conformational basis of thrombosis

Thrombosis and haemostasis, 2001-07, Vol.86 (1), p.14-22

2001

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Formation of the Antithrombin Heterodimer In Vivo and the Onset of Thrombosis

Blood, 1999-11, Vol.94 (10), p.3388-3396

1999

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The Serpin Inhibitory Mechanism Is Critically Dependent on the Length of the Reactive Center Loop

The Journal of biological chemistry, 2001-07, Vol.276 (29), p.27541-27547

2001

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

Nature structural & molecular biology, 1995-02, Vol.2 (2), p.96-113

1995

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How Small Peptides Block and Reverse Serpin Polymerisation

Journal of molecular biology, 2004-09, Vol.342 (3), p.931-941

2004

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Association between conformational mutations in neuroserpin and onset and severity of dementia

The Lancet (British edition), 2002-06, Vol.359 (9325), p.2242-2247

2002

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Antithrombins Wibble and Wobble (T85M/K) : Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation

Blood, 1998-10, Vol.92 (8), p.2696-2706

1998

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Crystal structure of uncleaved ovalbumin at 1.95 Å resolution

Journal of molecular biology, 1991-10, Vol.221 (3), p.941-959

1991

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Serpin Polymerization Is Prevented by a Hydrogen Bond Network That Is Centered on His-334 and Stabilized by Glycerol

The Journal of biological chemistry, 2003-04, Vol.278 (17), p.15116-15122

2003

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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

Proceedings of the National Academy of Sciences - PNAS, 2000-01, Vol.97 (1), p.67-72

2000

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Effects of mutations in the hinge region of serpins

Biochemistry (Easton), 1993-08, Vol.32 (30), p.7650-7657

1993

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Mobile reactive centre of serpins and the control of thrombosis

Nature (London), 1991-10, Vol.353 (6344), p.576-578

1991

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Crystal structure of ovalbumin as a model for the reactive centre of serpins

Nature (London), 1990-09, Vol.347 (6288), p.99-102

1990

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Structure of a serpin-protease complex shows inhibition by deformation

Conformational disease

Contents of partitions and the combinatorics of permutation factorizations in genus 0

Serpinopathies and the conformational dementias

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

The Anticoagulant Activation of Antithrombin by Heparin

Mutations in the shutter region of antithrombin result in formation of disulfide‐linked dimers and severe venous thrombosis

Conformational changes and disease — serpins, prions and Alzheimer's

Latent antithrombin and its detection, formation and turnover in the circulation

Prevalence of antithrombin deficiency in the healthy population

Implications of the three-dimensional structure of α1-antitrypsin for structure and function of serpins

The mechanism of Z α1-antitrypsin accumulation in the liver

The conformational basis of thrombosis

Formation of the Antithrombin Heterodimer In Vivo and the Onset of Thrombosis

The Serpin Inhibitory Mechanism Is Critically Dependent on the Length of the Reactive Center Loop

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

How Small Peptides Block and Reverse Serpin Polymerisation

Association between conformational mutations in neuroserpin and onset and severity of dementia

Antithrombins Wibble and Wobble (T85M/K) : Archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation

Crystal structure of uncleaved ovalbumin at 1.95 Å resolution

Serpin Polymerization Is Prevented by a Hydrogen Bond Network That Is Centered on His-334 and Stabilized by Glycerol

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

Effects of mutations in the hinge region of serpins

Mobile reactive centre of serpins and the control of thrombosis

Crystal structure of ovalbumin as a model for the reactive centre of serpins

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