C. Roumestand

发表

Scorpion-toxin mimics of CD4 in complex with human immunodeficiency virus gp120 crystal structures, molecular mimicry, and neutralization breadth.

François Stricher, Wayne A Hendrickson, Peter D Kwong, 2005, Structure.

The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes

Brian Henderson, Claire Bagnéris, Philippe Barthe, 2005, Nature Structural &Molecular Biology.

Scorpion toxins as natural scaffolds for protein engineering.

C. Roumestand, C. Vita, A. Ménez, 1995, Proceedings of the National Academy of Sciences of the United States of America.

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

P. Barthe, C. Roumestand, K. de Guillen, 2021, Biology.

Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein.

J C Gluckman, C. Roumestand, C. Vita, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Inhibition of Akt Kinase Activity by a Peptide Spanning the βA Strand of the Proto-oncogene TCL1*

C. Roumestand, M. Noguchi, M. Hiromura, 2004, Journal of Biological Chemistry.

Structural basis for functional diversity of animal toxins

Flavio Toma, Christian Roumestand, C. Roumestand, 1992 .

Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins.

C. Roumestand, A. Ménez, B. Gilquin, 1995, Biochemistry.

Volumetric properties underlying ligand binding in a monomeric hemoglobin: a high-pressure NMR study.

C. Roumestand, C. Royer, J. Lecomte, 2013, Biochimica et biophysica acta.

The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking.

S. Arold, F. Löhr, C. Roumestand, 2008, Journal of molecular biology.

Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes

D. Missé, F. Stricher, Loïc Martin, 2003, Nature Biotechnology.

Low-cost equilibrium unfolding of heme proteins using 2 μl samples.

B. Vallone, C. Roumestand, C. Royer, 2013, Analytical biochemistry.

A Tumor-Imaging Method Targeting Cancer-Associated Fibroblasts

D. Jäger, U. Haberkorn, J. Debus, 2018, The Journal of Nuclear Medicine.

The concept of effective correlation times for describing backbone motions in proteins. Part II. Tentative interpretation of the residue-specific correlation time in terms of overall rotation-diffusion

C. Roumestand, D. Canet, P. Mutzenhardt, 2005 .

Pseudo-3D NMR of proteins with selective excitation by DANTE-Z. One-dimensional TOCSY-NOESY experiment

C. Roumestand, F. Toma, D. Canet, 1990 .

Do cardiotoxins possess a functional site? Structural and chemical modification studies reveal the functional site of the cardiotoxin from Naja nigricollis.

L. Mouawad, C. Roumestand, A. Ménez, 1990, Biochimie.

Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: Comparison with X-ray data

M. Stern, A. Padilla, C. Roumestand, 2000, Journal of biomolecular NMR.

Paracrine behaviors arbitrate parasite-like interactions between 1 tumor subclones 2 3

M. Hochberg, C. Roumestand, P. Lassus, 2021 .

Analysis of the C12A-p8MTCP1 protein internal motions using fast spectral density mapping at multiple magnetic fields

P. Barthe, C. Roumestand, J. Roche, 2008 .

Full paper / Memoire Analysis of the C12A-p8 MTCP1 protein internal motions using fast spectral density mapping at multiple magnetic fields

P. Barthe, C. Roumestand, J. Roche, 2007 .

Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans

C. Roumestand, J. Armengaud, F. Confalonieri, 2015, Proteomics.

Isolation and structure elucidation of a highly haemolytic saponin from the Merck saponin extract using high-field gradient-enhanced NMR techniques.

C. Delay, C. Roumestand, A. Aumelas, 1997, Carbohydrate research.

Exploring Protein Conformational Landscapes Using High-Pressure NMR.

C. Roumestand, C. Royer, J. Roche, 2019, Methods in enzymology.

Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase.

E. Margeat, A. Padilla, P. Barthe, 2011, Structure.

Structure of the Mycobacterium tuberculosis OmpATb protein: A model of an oligomeric channel in the mycobacterial cell wall

C. Roumestand, V. Molle, G. Molle, 2011, Proteins.

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 Magnaporthe oryzae

T. Kroj, A. Padilla, P. Barthe, 2022, International journal of molecular sciences.

The TCL1A Oncoprotein Interacts Directly with the NF-κB Inhibitor IκB

M. Stern, S. Arold, S. Benichou, 2009, PloS one.

Protein–Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure

C. Roumestand, D. Matulis, V. Petrauskas, 2021, The journal of physical chemistry. B.

Unravelling the Adaptation Mechanisms to High Pressure in Proteins

F. Hoh, C. Roumestand, P. Oger, 2022, International journal of molecular sciences.

Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry, and NMR.

C. Roumestand, D. Matulis, V. Sirotkin, 2016, The journal of physical chemistry. B.

Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 37 kDa surface antigen protein Bd37 from Babesia divergens

M. Strub, F. Löhr, C. Roumestand, 2005, Journal of biomolecular NMR.

Extending the excitation sculpting concept for selective excitation.

C. Roumestand, D. Canet, 2000, Journal of magnetic resonance.

Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH

B. García-Moreno E., C. Roumestand, C. Royer, 2011, Proteins.

1H, 15N and 13C Backbone resonance assignments of a conformational mutant of the adhesion protein ∆-Bd37 from Babesia divergens

P. Barthe, C. Roumestand, B. Murciano, 2012, Biomolecular NMR Assignments.

Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure

C. Roumestand, C. Royer, N. Sibille, 2013, Journal of Biomolecular NMR.

Peptide inhibitors of E. collagenolyticum bacterial collagenase--effect of N-methylation. Consequences on biological activity and conformational properties.

C. Roumestand, B. Gilquin, V. Dive, 2009, International journal of peptide and protein research.

Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola.

P. Barthe, C. Roumestand, F. de Lamotte, 2007, Journal of molecular biology.

Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins.

C. Roumestand, A. Ménez, B. Gilquin, 1991, Science.

Gradient‐Enhanced Band‐Filtering Experiments

C. Roumestand, D. Canet, P. Mutzenhardt, 1996 .

The use of sample rotation for minimizing convection effects in self-diffusion NMR measurements.

C. Roumestand, M. Delsuc, T. Parella, 2001, Journal of magnetic resonance.

A practical approach to the implementation of selectivity in homonuclear multidimensional NMR with frequency selective‐filtering techniques. Application to the chemical structure elucidation of complex oligosaccharides †

C. Roumestand, D. Canet, J. Gavín, 1999 .

A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic.

F. Stricher, P. Barthe, C. Roumestand, 2005, The Biochemical journal.

A Practical Approach to the Implementation of Selectivity in Homonuclear Multidimensional NMR with Frequency Selective‐Filtering Techniques. Application to the Chemical Structure Elucidation of Complex Oligosaccharides

C. Roumestand, D. Canet, J. Gavín, 1999 .

Synthesis and solution structure of the antimicrobial peptide protegrin-1.

C. Roumestand, L. Chiche, G. Grassy, 1996, European journal of biochemistry.

The Use of Band Filtering in Multidimensional NMR. Evaluation of Two "User-Friendly" Techniques

C. Roumestand, J. Mispelter, D. Canet, 1995 .

Analytical expressions for the DANTE pulse sequence

C. Roumestand, D. Canet, J. Brondeau, 1995 .

Suppression of Unwanted Sideband Excitations in the DANTE-Z Experiment

C. Roumestand, D. Canet, 1995 .

DANTE-Z, an alternative to low-power soft pulses. Improvement of the selection scheme and applications to multidimensional NMR studies of proteins

C. Roumestand, F. Toma, D. Canet, 1994 .

An NMR study of the interaction of cardiotoxin gamma from Naja nigricollis with perdeuterated dodecylphosphocholine micelles.

C. Roumestand, A. Ménez, S. Pinkasfeld, 1995, European journal of biochemistry.

Monitoring Unfolding of Titin I27 single- and bi-Domain with High-Pressure NMR Spectroscopy

F. Rico, C. Roumestand, K. Deguillen, 2018, bioRxiv.

Proto‐oncogene TCL1: more than just a coactivator for Akt

C. Roumestand, M. Noguchi, F. Suizu, 2007, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Identification of Akt Association and Oligomerization Domains of the Akt Kinase Coactivator TCL1

M. Stern, F. Hoh, J. Laine, 2002, Molecular and Cellular Biology.

Structural and Functional Characterization of Bc28.1, Major Erythrocyte-binding Protein from Babesia canis Merozoite Surface*

C. Roumestand, B. Murciano, Yinshan Yang, 2012, The Journal of Biological Chemistry.

Side reaction during the deprotection of (S-acetamidomethyl)cysteine in a peptide with a high serine and threonine content.

C. Roumestand, A. Ménez, C. Deprun, 2009, International journal of peptide and protein research.

Cavities determine the pressure unfolding of proteins

Jose A. Caro, Julien Roche, Catherine A. Royer, 2012, Proceedings of the National Academy of Sciences.

Paracrine Behaviors Arbitrate Parasite-Like Interactions Between Tumor Subclones

M. Hochberg, C. Roumestand, P. Lassus, 2020, bioRxiv.

Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP studied by NMR relaxation

J. Lefèvre, T. Malliavin, M. Stern, 1999, Journal of biomolecular NMR.

On the Convergent Evolution of Animal Toxins

C. Roumestand, C. Vita, A. Ménez, 1997, The Journal of Biological Chemistry.

Mapping of two "neutralizing" epitopes of a snake curaremimetic toxin by proton nuclear magnetic resonance spectroscopy.

C. Roumestand, S. Zinn-Justin, A. Ménez, 1993, Biochemistry.

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

V. J. Planelles-Herrero, P. Barthe, C. Roumestand, 2021, International journal of molecular sciences.

Unraveling protein dynamics through fast spectral density mapping

P. Barthe, C. Roumestand, D. Canet, 2007, Journal of biomolecular NMR.

The concept of effective correlation times for describing backbone motions in proteins. Part I. A residue-per-residue self-consistent analysis of multifield 15N relaxation parameters

C. Roumestand, D. Canet, P. Mutzenhardt, 2005 .

Solution Structure and Backbone Dynamics of the Pleckstrin Homology Domain of the Human Protein Kinase B (PKB/Akt). Interaction with Inositol Phosphates

M. Stern, P. Barthe, C. Roumestand, 2004, Journal of biomolecular NMR.

Helix motion in protein C12A‐p8MTCP1: Comparison of molecular dynamics simulations and multifield NMR relaxation data

Laurent Chiche, Philippe Barthe, Christian Roumestand, 2002, J. Comput. Chem..

Equivalence between Euler angle conventions for the description of tensorial interactions in liquid NMR: application to different software programs

P. Barthe, C. Roumestand, P. Dosset, 2013, Journal of Biomolecular NMR.

Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity‐creating mutations

A. Garcia, B. García-Moreno E., C. Roumestand, 2013, Proteins.

Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism.

L. Kremer, P. Barthe, C. Roumestand, 2009, Structure.

Structural Studies of the Complex Between Akt-in and the Akt2-PH Domain Suggest that the Peptide Acts as an Allosteric Inhibitor of the Akt Kinase

P. Barthe, C. Roumestand, M. Noguchi, 2009 .

The Mycobacterium tuberculosis Ser/Thr Kinase Substrate Rv2175c Is a DNA-binding Protein Regulated by Phosphorylation*

L. Kremer, P. Barthe, C. Roumestand, 2009, The Journal of Biological Chemistry.

Refined three‐dimensional solution structure of a snake cardiotoxin: Analysis of the side‐chain organization suggests the existence of a possible phospholipid binding site

C. Roumestand, S. Zinn-Justin, A. Ménez, 1993, Biopolymers.

Solution structure of human p8MTCP1, a cysteine-rich protein encoded by the MTCP1 oncogene, reveals a new alpha-helical assembly motif.

J. Soulier, M. Stern, H. van Tilbeurgh, 1997, Journal of molecular biology.

Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation

C. Roumestand, L. Chiche, G. Grassy, 1996, FEBS letters.

Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins.

C. Roumestand, A. Ménez, B. Gilquin, 1991, European journal of biochemistry.

Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112

A. Witney, S. Waddell, P. Barthe, 2019, Molecular microbiology.

Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the global transcriptional regulator Lsr2

A. Witney, S. Waddell, P. Barthe, 2019, bioRxiv.

The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation.

Philippe Barthe, Christian Roumestand, Martin Cohen-Gonsaud, 2010, Structure.

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

P. Barthe, C. Roumestand, Cécile Dubois, 2020, Molecules.

Monitoring protein folding through high pressure NMR spectroscopy.

C. Roumestand, C. Royer, Julien Roche, 2017, Progress in nuclear magnetic resonance spectroscopy.

Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1.

C. Roumestand, C. Royer, H. Yamada, 2002, Journal of molecular biology.

Solution structure of a green mamba toxin that activates muscarinic acetylcholine receptors, as studied by nuclear magnetic resonance and molecular modeling.

C. Roumestand, S. Zinn-Justin, A. Ménez, 1995, Biochemistry.

Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications.

C. Roumestand, A. Ménez, B. Gilquin, 1992, Biochemistry.

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

T. Kroj, A. Padilla, P. Barthe, 2022, Biomolecular NMR Assignments.

Solid-phase synthesis: Structural and functional characterisation of charybdotoxin and of two truncated analogues

C. Roumestand, C. Vita, A. Ménez, 1993 .

New data on the 3D structure of natural charybdotoxin show that scorpion toxins and insect defensins share a common structural motif

C. Roumestand, A. Ménez, B. Gilquin, 1992 .

Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations.

A. Garcia, C. Roumestand, C. Royer, 2012, Biochemistry.

Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution

P. Barthe, C. Roumestand, Y. Kuroda, 2019, Biomolecules.

Capture in the metabolic arena: co-selection of gamma and deltaretrovirus envelope glycoproteins and their receptors

M. Sitbon, C. Roumestand, N. Manel, 2009, Retrovirology.

Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy.

A. Garcia, C. Roumestand, C. Royer, 2013, Journal of the American Chemical Society.

Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure

C. Roumestand, C. Royer, N. Sibille, 2014, Journal of biomolecular NMR.

Proton NMR studies of the structural and dynamical effect of chemical modification of a single aromatic side-chain in a snake cardiotoxin. Relation to the structure of the putative binding site and the cytolytic activity of the toxin.

L. Mouawad, C. Roumestand, A. Ménez, 1994, Journal of molecular biology.

High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.

D. Barrick, A. Garcia, C. Roumestand, 2016, Biophysical journal.

Assessing the Contribution of Cavity Density to Protein Partial Molar Expansivity by High-Pressure NMR

A. Garcia, C. Roumestand, C. Royer, 2013 .

Synthesis and NMR solution structure of an α‐helical hairpin stapled with two disulfide bridges

P. Barthe, C. Roumestand, C. Vita, 2000, Protein science : a publication of the Protein Society.

Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study.

C. Roumestand, S. Zinn-Justin, A. Ménez, 1992, Biochemistry.

Engineering Novel Bioactive Mini-Proteins on Natural Scaffolds

C. Roumestand, C. Vita, O. Combes, 2000 .

Protein dynamics studies on a wheat type 2 lipid transfer protein

C. Roumestand, J. Pons, M. Gautier, 2001 .

Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.

C. Roumestand, C. Royer, Julien Roche, 2015, Sub-cellular biochemistry.

Towards the total synthesis of trichormamide A, a cyclic undecapeptide

C. Roumestand, B. Legrand, N. Inguimbert, 2018, Tetrahedron Letters.

Structural Basis for the Co-activation of Protein Kinase B by T-cell Leukemia-1 (TCL1) Family Proto-oncoproteins*

M. Stern, S. Arold, P. Barthe, 2004, Journal of Biological Chemistry.

Refined three‐dimensional solution structure of a snake cardiotoxin: Analysis of the side‐chain organization suggests the existence of a possible phospholipid binding site

C. Roumestand, S. Zinn-Justin, A. Ménez, 1993, Biopolymers.

Oligomerization of protegrin‐1 in the presence of DPC micelles. A proton high‐resolution NMR study

C. Roumestand, G. Grassy, A. Aumelas, 1998, FEBS letters.

Solution structure of the recombinant human oncoprotein p13MTCP1

M. Stern, M. Strub, F. Hoh, 1998, Journal of biomolecular NMR.

Structure refinement of flexible proteins using dipolar couplings: Application to the protein p8MTCP1

P. Barthe, C. Roumestand, M. Delsuc, 2002, Journal of biomolecular NMR.

1H, 15N and 13C Backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide

B. Vallone, C. Roumestand, F. Allemand, 2014, Biomolecular NMR Assignments.

A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic.

F. Stricher, P. Barthe, C. Roumestand, 2005, The Biochemical journal.

Investigation of the function of PknB using omics tools

A. Witney, P. Barthe, C. Roumestand, 2019 .

Monitoring protein folding through high pressure NMR spectroscopy.

C. Roumestand, C. Royer, Julien Roche, 2017, Progress in nuclear magnetic resonance spectroscopy.

The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited.

T. Kroj, C. Roumestand, P. Gladieux, 2024, PLoS pathogens.