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The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria

Molecular microbiology, 2012-01, Vol.83 (2), p.275-288

2012

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The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin

PloS one, 2013, Vol.8 (1), p.e54766-e54766

2013

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Molecular basis of α 1 -antitrypsin deficiency revealed by the structure of a domain-swapped trimer

EMBO reports, 2011-10, Vol.12 (10), p.1011-1017

2011

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DNA Accelerates the Inhibition of Human Cathepsin V by Serpins

The Journal of biological chemistry, 2007-12, Vol.282 (51), p.36980-36986

2007

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Aeropin from the Extremophile Pyrobaculum aerophilum Bypasses the Serpin Misfolding Trap

The Journal of biological chemistry, 2007-09, Vol.282 (37), p.26802-26809

2007

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Common Fold Mediates Vertebrate Defense and Bacterial Attack

Science (American Association for the Advancement of Science), 2007-09, Vol.317 (5844), p.1548-1551

2007

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Mechanisms of Ataxin-3 Misfolding and Fibril Formation: Kinetic Analysis of a Disease-associated Polyglutamine Protein

Journal of molecular biology, 2007-04, Vol.368 (2), p.595-605

2007

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Kinetic Instability of the Serpin Z α1-Antitrypsin Promotes Aggregation

Journal of molecular biology, 2010-02, Vol.396 (2), p.375-383

2010

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Conformational change in the chromatin remodelling protein MENT

PloS one, 2009-03, Vol.4 (3), p.e4727

2009

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Serpin Acceleration of Amyloid Fibril Formation: A Role for Accessory Proteins

Journal of molecular biology, 2007-02, Vol.366 (2), p.666-676

2007

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The N terminus of the serpin, tengpin, functions to trap the metastable native state

EMBO reports, 2007-07, Vol.8 (7), p.658-663

2007

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Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer

EMBO reports, 2011-10, Vol.12 (10), p.1011-1017

2011

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Preventing serpin aggregation: The molecular mechanism of citrate action upon antitrypsin unfolding

Protein science, 2008-12, Vol.17 (12), p.2127-2133

2008

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Production of Recombinant Serpins in Escherichia coli

Methods in Enzymology, 2011, Vol.501, p.13-28

2011

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

The FEBS journal, 2007-07, Vol.274 (14), p.3622-3632

2007

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

Biochemical and biophysical research communications, 2004-11, Vol.324 (2), p.729-735

2004

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The Roles of Helix I and Strand 5A in the Folding, Function and Misfolding of [alpha].sub.1-Antitrypsin

PloS one, 2013-01, Vol.8 (1), p.e54766

2013

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Molecular basis of [alpha]1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer

EMBO reports, 2011-10, Vol.12 (10), p.1011

2011

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Blind Man’s Bluff – Elaboration of Fragment Hits in the Absence of Structure for the Development of Antitrypsin Deficiency Inhibitors

Australian journal of chemistry, 2013, Vol.66 (12), p.1525

2013

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Kinetic Instability of the Serpin Z α 1-Antitrypsin Promotes Aggregation

Journal of molecular biology, 2010, Vol.396 (2), p.375-383

2010

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Expression, purification and characterization of recombinant Z α1-Antitrypsin—The most common cause of α1-Antitrypsin deficiency

Protein expression and purification, 2009-12, Vol.68 (2), p.226-232

2009

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Conformational Change and Intermediates in the Unfolding of α1-Antichymotrypsin

The Journal of biological chemistry, 2000-09, Vol.275 (37), p.28513-28518

2000

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Expression, purification and characterization of recombinant Z α 1-Antitrypsin—The most common cause of α 1-Antitrypsin deficiency

Protein expression and purification, 2009, Vol.68 (2), p.226-232

2009

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Kinetic instability of the serpin Z alpha1-antitrypsin promotes aggregation

Journal of molecular biology, 2010-02, Vol.396 (2), p.375-383

2010

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Conformational Change and Intermediates in the Unfolding of Î±1-Antichymotrypsin

The Journal of biological chemistry, 2000-09, Vol.275 (37), p.28513

2000

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The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria

The roles of helix I and strand 5A in the folding, function and misfolding of α1-antitrypsin

Molecular basis of α 1 -antitrypsin deficiency revealed by the structure of a domain-swapped trimer

DNA Accelerates the Inhibition of Human Cathepsin V by Serpins

Aeropin from the Extremophile Pyrobaculum aerophilum Bypasses the Serpin Misfolding Trap

Common Fold Mediates Vertebrate Defense and Bacterial Attack

Mechanisms of Ataxin-3 Misfolding and Fibril Formation: Kinetic Analysis of a Disease-associated Polyglutamine Protein

Kinetic Instability of the Serpin Z α1-Antitrypsin Promotes Aggregation

Conformational change in the chromatin remodelling protein MENT

Serpin Acceleration of Amyloid Fibril Formation: A Role for Accessory Proteins

The N terminus of the serpin, tengpin, functions to trap the metastable native state

Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer

Preventing serpin aggregation: The molecular mechanism of citrate action upon antitrypsin unfolding

Production of Recombinant Serpins in Escherichia coli

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

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

The Roles of Helix I and Strand 5A in the Folding, Function and Misfolding of [alpha].sub.1-Antitrypsin

Molecular basis of [alpha]1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer

Blind Man’s Bluff – Elaboration of Fragment Hits in the Absence of Structure for the Development of Antitrypsin Deficiency Inhibitors

Kinetic Instability of the Serpin Z α 1-Antitrypsin Promotes Aggregation

Expression, purification and characterization of recombinant Z α1-Antitrypsin—The most common cause of α1-Antitrypsin deficiency

Conformational Change and Intermediates in the Unfolding of α1-Antichymotrypsin

Expression, purification and characterization of recombinant Z α 1-Antitrypsin—The most common cause of α 1-Antitrypsin deficiency

Kinetic instability of the serpin Z alpha1-antitrypsin promotes aggregation

Conformational Change and Intermediates in the Unfolding of Î±1-Antichymotrypsin

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