Philippe Barthe

University of Montpellier

France

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Articles (12)

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2025

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2024

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2024

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2023

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2023

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2022

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2022

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2022

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2021

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2021

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2021

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2020

Collaborators (10)

Pierre Gladieux

University of Montpellier

FRANCE

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Christian ROUMESTAND

Professor (PU-CLEX2)

University of Montpellier

FRANCE

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Rita Puglisi

King’s College London

UNITED KINGDOM

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ANDRE PADILLA

CNRS Délégation Languedoc-Roussillon

FRANCE

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Gress Kadaré

Associate Professor

Sorbonne Université

FRANCE

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Martin Cohen-Gonsaud

University of Montpellier

FRANCE

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Assia Mouhand

Assistant professor (Biochemistry/Structural biology)

University of Montpellier

FRANCE

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Stephane Delbecq

Prof

University of Montpellier

FRANCE

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Virginie Ropars

Researcher

CEA Saclay

FRANCE

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Karine de Guillen

FRANCE

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Philippe Barthe

Research Interests

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Articles (12)

Understanding the Relationship between Pressure and Temperature Unfolding of Proteins

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited

1H, 13C and 15N backbone and side-chain resonance assignments of the human oncogenic protein NCYM

Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal α-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae

A Mycobacterium tuberculosis Effector Targets Mitochondrion, Controls Energy Metabolism, and Limits Cytochrome <i>c</i> Exit

Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors from <i>Magnaporthe oryzae</i>

1H, 13C, 15 N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae

PYK2 senses calcium through a disordered dimerization and calmodulin-binding element

Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR

Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1

The study of the determinants controlling Arpp19 phosphatase-inhibitory activity reveals an Arpp19/PP2A-B55 feedback loop

Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways

Collaborators (10)

Pierre Gladieux

Christian ROUMESTAND

Rita Puglisi

ANDRE PADILLA

Gress Kadaré

Martin Cohen-Gonsaud

Assia Mouhand

Stephane Delbecq

Virginie Ropars

Karine de Guillen

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