Christian Roumestand
Structure, dynamique et fonction des biomolécules par RMN
04 67 41 77 04
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Liste des publications
2024
2023
Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-Terminal alpha-Helical Extension in the 3D Structure of MAX60 Drastically Changes the Folding Pathway Described for Other MAX-Effectors from Magnaporthe oryzae
Lahfa M, Mouhand A, deGuillen K, Barthe P, Kroj T, Padilla A, Roumestand C, Molecules, 2023
1H, 13C and 15N backbone and side-chain resonance assignments of BmSA1, the surface antigen of Babesia microti
Mouhand A, Pissarra J, Delbecq S, Roumestand C, Barthe P, Biomol NMR Assign, 2023
2022
Unravelling the Adaptation Mechanisms to High Pressure in Proteins
Calio A, Dubois C, Fontanay S, Koza MM, Hoh F, Roumestand C, Oger P, Peters J, Int J Mol Sci, 2022
1H, 13C, 15N backbone and side-chain NMR assignments for three MAX effectors from Magnaporthe oryzae
Lahfa M, Padilla A, deGuillen K, Pissarra J, Raji M, Cesari S, Kroj T, Gladieux P, Roumestand C, Barthe P, Biomol NMR Assign, 2022
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
Dubois C, Lahfa M, Pissarra J, deGuillen K, Barthe P, Kroj T, Roumestand C, Padilla A, Int J Mol Sci, 2022
2021
Paracrine Behaviors Arbitrate Parasite-Like Interactions Between Tumor Subclones
Noble RJ, Walther V, Roumestand C, Hochberg ME, Hibner U, Lassus P, Front Ecol Evol, 2021
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
Van Deuren V, Yang YS, deGuillen K, Dubois C, Royer CA, Roumestand C, Barthe P, Biology (Basel), 2021
Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure
Skvarnavicius G, Toleikis Z, Michailoviene V, Roumestand C, Matulis D, Petrauskas V, J Phys Chem B, 2021
Pressure and Chemical Unfolding of an alpha-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1
Dubois C, Planelles-Herrero VJ, Tillatte-Tripodi C, Delbecq S, Mammri L, Sirkia EM, Ropars V, Roumestand C, Barthe P, Int J Mol Sci, 2021
2020
2019
Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112
Alqaseer K, Turapov O, Barthe P, Jagatia H, De Visch A, Roumestand C, Wegrzyn M, Bartek IL, Voskuil MI, O'Hare HM, Ajuh P, Bottrill AR, Witney AA, Cohen-Gonsaud M, Waddell SJ, Mukamolova GV, Mol Microbiol, 2019
Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution
Saotome T, Doret M, Kulkarni M, Yang YS, Barthe P, Kuroda Y, Roumestand C, Biomolecules, 2019
Exploring Protein Conformational Landscapes Using High-Pressure NMR
Roche J, Royer CA, Roumestand C, Meth Enzymol, 2019
2018
Towards the total synthesis of trichormamide A, a cyclic undecapeptide
Gaillard S, Das S, Djibo M, Raviglione D, Roumestand C, Legrand B, Inguimbert N, Tetrahedron Letters, 2018
A Tumor-Imaging Method Targeting Cancer-Associated Fibroblasts
Loktev A, Lindner T, Mier W, Debus J, Altmann A, Jager D, Giesel F, Kratochwil C, Barthe P, Roumestand C, Haberkorn U, J Nucl Med, 2018
Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy
Herrada I, Barthe P, Vanheusden M, DeGuillen K, Mammri L, Delbecq S, Rico F, Roumestand C, Biophys J, 2018
2017
2016
High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape
Fossat MJ, Dao TP, Jenkins K, Dellarole M, Yang Y, McCallum SA, Garcia AE, Barrick D, Roumestand C, Royer CA, Biophys J, 2016
Volume of Hsp90 Protein-Ligand Binding Determined by Fluorescent Pressure Shift Assay, Densitometry, and NMR
Toleikis Z, Sirotkin VA, Skvarnavicius G, Smirnoviene J, Roumestand C, Matulis D, Petrauskas V, J Phys Chem B, 2016
2015
Evolutionarily Conserved Pattern of Interactions in a Protein Revealed by Local Thermal Expansion Properties
Dellarole M, Caro JA, Roche J, Fossat M, Barthe P, Garcia-Moreno E B, Royer CA, Roumestand C, J Am Chem Soc, 2015
Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies
Roche J, Dellarole M, Royer CA, Roumestand C, Subcell Biochem, 2015
2014
(1)H, (15)N and (13)C Backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide
Yang Y, Allemand F, Guca E, Vallone B, Delbecq S, Roumestand C, Biomol NMR Assign, 2014
Prioritizing targets for structural biology through the lens of proteomics: The archaeal protein TGAM_1934 from Thermococcus gammatolerans
Yang YS, Fernandez B, Lagorce A, Aloin V, deGuillen KM, Boyer JB, Dedieu A, Confalonieri F, Armengaud J, Roumestand C, Proteomics, 2014
2013
Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy
Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno B, Roumestand C, Royer CA, J Am Chem Soc, 2013
Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure
Sibille N, Dellarole M, Royer C, Roumestand C, J Biomol NMR, 2013
Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations
Roche J, Caro JA, Dellarole M, Guca E, Royer CA, Garcia-Moreno BE, Garcia AE, Roumestand C, Proteins, 2013
Equivalence between Euler angle conventions for the description of tensorial interactions in liquid NMR: application to different software programs
Dosset P, Barthe P, Cohen-Gonsaud M, Roumestand C, Demene H, J Biomol NMR, 2013
1H, 1aN and 13C Backbone resonance assignments of a conformational mutant of the adhesion protein a-Bd37 from Babesia divergens
Barthe P, Murciano B, Schetters T, Gorenflot A, Delbecq S, Roumestand C, Biomol NMR Assign, 2013
Volumetric properties underlying ligand binding in a monomeric hemoglobin: a high-pressure NMR study
Dellarole M, Roumestand C, Royer C, Lecomte JT, Biochim Biophys Acta, 2013
Low-cost equilibrium unfolding of heme proteins using 2 mul samples
Guca E, Roumestand C, Vallone B, Royer CA, Dellarole M, Anal Biochem, 2013
2012
Cavities determine the pressure unfolding of proteins
Roche J, Caro JA, Norberto DR, Barthe P, Roumestand C, Schlessman JL, Garcia AE, Garcia-Moreno BE, Royer CA, Proc Natl Acad Sci U S A, 2012
Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations.
Roche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang Y, Garcia AE, Roumestand C, Garcia-Moreno B, Royer CA, Biochemistry, 2012
Structural and functional characterization of Bc28.1, major erythrocyte-binding protein from Babesia canis merozoite surface
Yang YS, Murciano B, Moubri K, Cibrelus P, Schetters T, Gorenflot A, Delbecq S, Roumestand C, J Biol Chem, 2012
2011
Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH
Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti MS, Garcia-Moreno EB, Schroer MA, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet deGuillen K, Royer CA, Proteins, 2011
Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase
Roumestand C, Leiba J, Galophe N, Margeat E, Padilla A, Bessin Y, Barthe P, Molle V, Cohen-Gonsaud M, Structure, 2011
Structure of the Mycobacterium tuberculosis OmpATb protein: a model of an oligomeric channel in the mycobacterial cell wall
Yang Y, Auguin D, Delbecq S, Dumas E, Molle G, Molle V, Roumestand C, Saint N, Proteins, 2011
2010
2009
Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism
Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M, Structure, 2009
The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation
Cohen-Gonsaud M, Barthe P, Canova MJ, Stagier-Simon C, Kremer L, Roumestand C, Molle V, J Biol Chem, 2009
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
Ropars V, Barthe P, Wang CS, Chen W, Tzou DL, Descours A, Martin L, Noguchi M, Roumestand C, Open Spect J, 2009
The TCL1A oncoprotein interacts directly with the NF-kappaB inhibitor IkappaB
Ropars V, Despouy G, Stern MH, Benichou S, Roumestand C, Arold ST, PLoS One, 2009
2008
Analysis of the C12A-p8MTCP1 protein internal motions using Fast Density Mapping at multiple magnetic fields
Ropars V, Roche J, Barthe P, Roumestand C, C.R. Chimie, 2008
The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking
Delbecq S, Auguin D, Yang YS, Lohr F, Arold ST, Schetters T, Precigout E, Gorenflot A, Roumestand C, J Mol Biol, 2008
2007
Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola
Barthe P, Pujade-Renaud V, Breton F, Gargani D, Thai R, Roumestand C, de Lamotte F, J Mol Biol, 2007
Proto-oncogene TCL1: more than just a coactivator for Akt
Noguchi M, Ropars V, Roumestand C, Suizu F, Faseb J, 2007
Unraveling protein dynamics through fast spectral density mapping
Ropars V, Bouguet-Bonnet S, Auguin D, Barthe P, Canet D, Roumestand C, J Biomol NMR, 2007
2006
DYNAMOF: a program for the dynamics analysis of relaxation data obtained at multiple magnetic fields.
Barthe P, Ropars V, Roumestand C, C. R. Chimie, 2006
Structural basis for the Akt (PKB) kinase inhibition by the peptide Akt-in: an NMR study.
Ropars V, Guichou J-F, Auguin D, Barthe P, Noguchi M, Roumestand C, C. R. Chimie, 2006
2005
The concept of effective correlation times for describing backbone motions in proteins. Part I. A residue-per-residue self-consistent analysis of multifield N-15 relaxation parameters
Bouguet-Bonnet S, Mutzenhardt P, Roumestand C, Canet D, Concept in Magnetic Resonance Part A, 2005
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
Bouguet-Bonnet S, Mutzenhardt P, Roumestand C, Canet D, Concept in Magnetic Resonance Part A, 2005
The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes
Cohen-Gonsaud M, Barthe P, Bagneris C, Henderson B, Ward J, Roumestand C, Keep NH, Nat Struct Mol Biol, 2005
Scorpion-toxin mimics of CD4 in complex with human immunodeficiency virus gp120 crystal structures, molecular mimicry, and neutralization breadth
Huang CC, Stricher F, Martin L, Decker JM, Majeed S, Barthe P, Hendrickson WA, Robinson J, Roumestand C, Sodroski J, Wyatt R, Shaw GM, Vita C, Kwong PD, Structure, 2005
A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic
Stricher F, Martin L, Barthe P, Pogenberg V, Mechulam A, Menez A, Roumestand C, Veas F, Royer C, Vita C, Biochem J, 2005
1H, 15N and 13C Backbone resonance assignments of the 37 kDa surface antigen protein Bd37 from Babesia divergens
Yang YS, Delbecq S, Strub MP, Lohr F, Schetters T, Gorenflot A, Precigout E, Roumestand C, J Biomol NMR, 2005
2004
Inhibition of Akt kinase activity by a peptide spanning the betaA strand of the proto-oncogene TCL1
Hiromura M, Okada F, Obata T, Auguin D, Shibata T, Roumestand C, Noguchi M, J Biol Chem, 2004
(1)H, (15)N, and (13)C chemical shift assignments of the resuscitation promoting factor domain of Rv1009 from Mycobacterium tuberculosis
Cohen-Gonsaud M, Barthe P, Pommier F, Harris R, Driscoll PC, Keep NH, Roumestand C, J Biomol NMR, 2004
NMR determination of the Pleckstrin Homology domain oligomerisation state of the protein Akt2
Auguin D, Gostan T, Delsuc M-A, Roumestand C, C.R. Chimie, 2004
Design of an amphipatic a-helical hairpin peptide
Barthe P, Cohen-Gonsaud M, Aldrian-Herrada G, Chavanieu A, Labesse G, Roumestand C, Comptes Rendus Chimie, 2004
Structural basis for the co-activation of protein kinase B by T-cell leukemia-1 (TCL1) family proto-oncoproteins
Auguin D, Barthe P, Royer C, Stern MH, Noguchi M, Arold ST, Roumestand C, J Biol Chem, 2004
Determination de l'etat d'oligomerisation du domaine homologue a la pleckstrine de la proteine AKT2 par des techniques RMN
Auguin D, Gostan T, MA D, Roumestand C, C.R.A.S. Chimie, 2004
Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
Auguin D, Barthe P, Auge-Senegas MT, Stern MH, Noguchi M, Roumestand C, J Biomol NMR, 2004
2003
1H, (15)N and (13)C chemical shift assignments of the Pleckstrin Homology domain of the Human Protein Kinase B (Pkb/Akt)
Auguin D, Barthe P, Auge-Senegas MT, Hoh F, Noguchi M, Roumestand C, J. Biomol. NMR, 2003
Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes
Martin L, Stricher F, Misse D, Sironi F, Pugniere M, Barthe P, Prado-Gotor R, Freulon I, Magne X, Roumestand C, Menez A, Lusso P, Veas F, Vita C, Nat Biotechnol, 2003
2002
Helix motion in protein C12A-p8(MTCP1): comparison of molecular dynamics simulations and multifield NMR relaxation data
Barthe P, Roumestand C, Demene H, Chiche L, J. Comput. Chem., 2002
Structure refinement of flexible proteins using dipolar couplings: application to the protein p8MTCP1
Demene H, Ducat T, Barthe P, Delsuc MA, Roumestand C, J. Biomol. NMR., 2002
Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1
Kitahara R, Royer C, Yamada H, Boyer M, Saldana JL, Akasaka K, Roumestand C, J Mol Biol, 2002
Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1.
Kunstle G, Laine J, Pierron G, Kagami SS, Nakajima H, Hoh F, Roumestand C, Stern MH, M. N, Mol Cell Biol, 2002
2001
A comprehensive analysis of multifield 15N relaxation parameters in proteins: determination of 15N chemical shift anisotropies
Canet D, Barthe P, Mutzenhardt P, Roumestand C, J. Am. Chem. Soc., 2001
The use of sample rotation for minimizing convection effects in self- diffusion NMR measurements
Esturau N, Sanchez-Ferrando F, Gavin JA, Roumestand C, Delsuc MA, Parella T, J Magn Reson, 2001
Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13
Roumestand C, Boyer M, Guignard L, Barthe P, Royer CA, J. Mol. Biol., 2001
2000
Engineering novel bioactive mini-proteins on natural scaffolds
Martin L, Barthe P, Combes O, Roumestand C, Vita C, Tetrahedron, 2000
Extending the excitation sculpting concept for selective excitation
Roumestand C, Canet D, J Magn Reson, 2000
Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: comparison with X-ray data
Guignard L, Padilla A, Mispelter J, Yang YS, Stern MH, Lhoste JM, Roumestand C, J Biomol NMR, 2000
Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges
Barthe P, Rochette S, Vita C, Roumestand C, Protein Sci., 2000
1999
Backbone dynamics study of C12A-P8MTCP1 using the linear correlation approach at 2 magnetic field strength. Effect of protein aggregation
Bartes P, N.Declerck, Delsuc M-A, Lefevre J-F, Roumestand C, J.Chim.Phys., 1999
Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation
Barthe P, Chiche L, Declerck N, Delsuc MA, Lefevre JF, Malliavin T, Mispelter J, Stern MH, Lhoste JM, Roumestand C, J. Biomol. NMR., 1999
Backbone dynamics study of C12A-p8MTCP1 using the linear correlation approach at two magnetic field strengths. Effect of protein aggregation.
Barthe P, Declerck N, Delsuc MA, Lefevre JF, Roumestand C, J. Chim. Phys., 1999
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.
Roumestand C, Delay C, Gavin JA, Canet D, Magn. Reson. Chem., 1999
Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein
Vita C, Drakopoulou E, Vizzavona J, Rochette S, Martin L, Menez A, Roumestand C, Yang YS, Ylisastigui L, Benjouad A, Gluckman JC, Proc Natl Acad Sci U S A, 1999
1998
Formation of native disulfide bonds in endothelin-1. Structural evidence for the involvement of a highly specific salt bridge between the prosequence and the endothelin-1 sequence
Aumelas A, Kubo S, Chino N, Chiche L, Forest E, Roumestand C, Kobayashi Y, Biochemistry, 1998
The preliminary solution structure of human p8MTCP1, a protein encoded by the putative MTCP1 oncogene
Barthe P, Guignard L, Yang YS, Chiche L, Strub MP, Hoh F, Stern MH, Roumestand C, J. Chim. Phys., 1998
Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study
Roumestand C, Louis V, Aumelas A, Grassy G, Calas B, Chavanieu A, FEBS Lett, 1998
Solution structure of the recombinant human oncoprotein p13MTCP1
Yang YS, Guignard L, Padilla A, Hoh F, Strub MP, Stern MH, Lhoste JM, Roumestand C, J Biomol NMR, 1998
1997
Isolation and structure elucidation of a highly haemolytic saponin from the Merck saponin extract using high-field gradient-enhanced NMR techniques
Delay C, Gavin JA, Aumelas A, Bonnet PA, Roumestand C, Carbohydr Res, 1997
Solution structure of human p8MTCP1, a cysteine-rich protein encoded by the MTCP1 oncogene, reveals a new alpha-helical assembly motif
Barthe P, Yang YS, Chiche L, Hoh F, Strub MP, Guignard L, Soulier J, Stern MH, van Tilbeurgh H, Lhoste JM, Roumestand C, J. Mol. Biol., 1997
On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
Dauplais M, Lecoq A, Song J, Cotton J, Jamin N, Gilquin B, Roumestand C, Vita C, de Medeiros CL, Rowan EG, Harvey AL, Menez A, J Biol Chem, 1997
1996
Synthesis and solution structure of the antimicrobial peptide protegrin-1
Aumelas A, Mangoni M, Roumestand C, Chiche L, Despaux E, Grassy G, Calas B, Chavanieu A, Eur J Biochem, 1996
Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation
Mangoni ME, Aumelas A, Charnet P, Roumestand C, Chiche L, Despaux E, Grassy G, Calas B, Chavanieu A, FEBS Lett, 1996
Gradient-Enhanced Band-Filtering Experiments.
Roumestand C, Mutzenhardt P, Delay C, Canet D, Magn. Reson. Chem., 1996
1995
Analytical Expressions for the DANTE Pulse Sequence.
Canet D, Brondeau J, Roumestand C, J Magn Reson, 1995
Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins
Dauplais M, Gilquin B, Possani LD, Gurrola-Briones G, Roumestand C, Menez A, Biochemistry, 1995
An NMR study of the interaction of cardiotoxin gamma from Naja nigricollis with perdeuterated dodecylphosphocholine micelles
Dauplais M, Neumann JM, Pinkasfeld S, Menez A, Roumestand C, Eur J Biochem, 1995
Suppression of Unwanted Side-Band Excitations in the DANTE-Z experiment.
Roumestand C, Canet D, J Magn Reson, 1995
The Use of Band-Filtering in Multidimensional NMR. Evaluation of Two User-Friendly methods.
Roumestand C, Mispelter J, Austruy C, Canet D, J Magn Reson, 1995
Solution structure of a green mamba toxin that activates muscarinic acetylcholine receptors, as studied by nuclear magnetic resonance and molecular modeling
Segalas I, Roumestand C, Zinn-Justin S, Gilquin B, Menez R, Menez A, Toma F, Biochemistry, 1995
Scorpion toxins as natural scaffolds for protein engineering
Vita C, Roumestand C, Toma F, Menez A, Proc Natl Acad Sci U S A, 1995
1994
DANTE-Z : an alternative to low-power soft pulses. Improvement of the selection scheme and applications to multidimensional NMR studies of proteins.
Roumestand C, Canet D, Mahieu N, Toma F, J Magn Reson, 1994
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
Roumestand C, Gilquin B, Tremeau O, Gatineau E, Mouawad L, Menez A, Toma F, J Mol Biol, 1994
A General Computer Program for Calculating Selectivity Profiles in NMR Spectroscopy.
Canet D, Roumestand C, Boubel J-C, Proc. Indian Acad. Sci. - Chem. Sci., 1994
NMR Spectral Selectivity by Radiofrequency Field Gradients.
Canet D, Mutzenhardt P, Brondeau J, Roumestand C, Chem. Phys. Letters, 1994
1993
Refined three-dimensional solution structure of a snake cardiotoxin: analysis of the side-chain organization suggests the existence of a possible phospholipid binding site
Gilquin B, Roumestand C, Zinn-Justin S, Menez A, Toma F, Biopolymers, 1993
Side reaction during the deprotection of (S-acetamidomethyl)cysteine in a peptide with a high serine and threonine content
Lamthanh H, Roumestand C, Deprun C, Menez A, Int J Pept Protein Res, 1993
Double-Selective {1H,31P} Editing of 1D or 2D spectra through small heteronuclear coupling constants based on Spin-Echo Difference spectroscopy.
Roumestand C, Boudot D, Canet D, J Magn Reson, 1993
Mapping of two neutralizing epitopes of a snake curaremimetic toxin by proton nuclear magnetic resonance spectroscopy
Zinn-Justin S, Roumestand C, Drevet P, Menez A, Toma F, Biochemistry, 1993
1992
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications
Bontems F, Gilquin B, Roumestand C, Menez A, Toma F, Biochemistry, 1992
Peptide inhibitors of E. collagenolyticum bacterial collagenase--effect of N-methylation. Consequences on biological activity and conformational properties
Dive V, Yiotakis A, Roumestand C, Gilquin B, Labadie J, Toma F, Int J Pept Protein Res, 1992
Structural basis for functional diversity of animal toxins.
Menez A, Bontems F, Roumestand C, Gilquin B, Toma F, Proceeding of the Royal Society of Edinburgh, 1992
Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study
Zinn-Justin S, Roumestand C, Gilquin B, Bontems F, Menez A, Toma F, Biochemistry, 1992
1991
Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins
Bontems F, Roumestand C, Boyot P, Gilquin B, Doljansky Y, Menez A, Toma F, Eur J Biochem, 1991
Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins
Bontems F, Roumestand C, Gilquin B, Menez A, Toma F, Science, 1991
1990
Pseudo-3D NMR of proteins with selective excitation by DANTE-Z. One-dimensional TOCSY-NOESY experiment.
Boudot D, Roumestand C, Toma F, Canet D, Journal of Magnetic Resonance, 1990
Do cardiotoxins possess a functional site? Structural and chemical modification studies reveal the functional site of the cardiotoxin from Naja nigricollis
Menez A, Gatineau E, Roumestand C, Harvey AL, Mouawad L, Gilquin B, Toma F, Biochimie, 1990