List of works - Véronique Receveur-Bréchot

Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state.

scientific article published on 3 June 2016

Assessing protein disorder and induced folding

scientific article

Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase

scientific article published on 28 February 2018

Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking aminopeptidase from Pyrococcus horikoshii

scientific article

How random are intrinsically disordered proteins? A small angle scattering perspective

scientific article published on February 2012

How random is a highly denatured protein?

scientific article published in December 1994

Orchestration of algal metabolism by protein disorder

scientific article published on 10 August 2019

Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A.

scientific article published on 23 May 2017

Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism

scientific article

Small-angle X-ray scattering and crystallography: a winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes

scientific article published on 01 January 2012

Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system.

scientific article

The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner

scientific article published in February 2004

The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

scientific article published on 5 March 2003

The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

scientific article published on August 2005

The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium

scientific article

The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.

scientific article

List of works by Véronique Receveur-Bréchot

Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state.

Assessing protein disorder and induced folding

Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase

Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking aminopeptidase from Pyrococcus horikoshii

How random are intrinsically disordered proteins? A small angle scattering perspective

How random is a highly denatured protein?

Orchestration of algal metabolism by protein disorder

Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A.

Redox cofactors insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism

Small-angle X-ray scattering and crystallography: a winning combination for exploring the multimodular organization of cellulolytic macromolecular complexes

Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system.

The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner

The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein

The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded

The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium

The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners.