WorldCat Identities

Boisbouvier, Jérôme

Overview
Works: 15 works in 16 publications in 2 languages and 28 library holdings
Roles: Author, Thesis advisor, Other
Publication Timeline
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Most widely held works by Jérôme Boisbouvier
Etude du repliement des protéines au sein d'une chaperonine by Elisa Colas Debled( )

1 edition published in 2019 in English and held by 2 WorldCat member libraries worldwide

Les chaperonines sont des machines moléculaires impliquées dans la protection des protéines contre le mauvais repliement et l'agrégation. Ces macromolécules de tailleimportante (environ 1 MDa) sont présentes dans tous les domaines du vivant et sontorganisées en deux anneaux concentriques et empilés l'un sur l'autre, possèdent chacun une cavité en leur centre. Les chaperonines sont particulièrement intéressantes car peu caractérisées par rapport aux autres chaperones, notamment dû à leur grande taille et à leur complexité intrinsèque. Leur mécanisme d'action reste donc assez flou.Ce travail de thèse est centré sur l'étude de PhCPN, la chaperonine de Pyrococcushorikoshii, et son interaction avec différentes protéines substrats, grâce à une combinaison d'outils biochimiques et biophysiques tels que la RMN. En effet, la spectroscopie RMN est un outil particulièrement adapté à l'étude des interactions moléculaires transitoires à l'échelle atomique. L'utilisation dans ce cadre du marquage isotopique spécifique des groupements méthyles permet d'étudier des ensembles protéiques de taille importante tels que PhCPN, tandis que la RMN plus classique reste limitée à des poidsmoléculaires inférieurs à 30 kDa. Afin d'étudier le repliement des protéines à l'intérieur des cavités de PhCPN, deux protéines substrats de taille hétérogène et d'activité différentes ont été sélectionnées.En particulier, l'un de ces deux substrats (laMalate Synthase G ou MSG), formedes agrégats amorphes lorsqu'elle elle chauffée tandis que la seconde (l'Amyline) est capable de s'auto associer de manière plus organisée, créant des fibres amyloïdes de haut poids moléculaire. J'ai observé lors de cette étude que PhCPN est capable d'empêcher l'agrégation de ces deux substrats.En effet, la Chaperonine PhCPN est capable de se lier de manière irreversible à laproteine MSG, dépliée par une augmentation de la temperature, dans un ratio stoechiométrique 1/1. Le complexMSG/PhCPN a été isolé et characterisé. En particulier, la surface d'interaction entre PhCPN et cette large protéine substrat a été déterminée grâce à la RMN et la mciroscopie électronique.De plus, l'inhibition de la formation de fibres amyloïdes issues de l'Amyline parla Chaperonine a été étudiée par RMN et fluorescence de la ThT. Il a été notammentmontré que la Chaperonine retarde l'apparition des fibres amyloïdes, quelque soit l'état oligomerique de PhCPN. Le rôle de la Chaperonine sur les méchanismes de nucléation et d'élongation des fibres amyloïdes de l'Amylin a également été étudié
Etude structurale et fonctionnelle par RMN d'une chaperonine de 1 MDa en action by Guillaume Mas( )

1 edition published in 2015 in French and held by 2 WorldCat member libraries worldwide

Chaperonins are essential molecular chaperons for the refolding of proteins in the cells. Size and complexity of these biological machineries make complex the study of their structural and functional properties. NMR spectroscopy offers an unique ability to monitor structural and dynamic changes in real-time and at atomic resolution. However, the NMR studies of large proteins and complexes has been a real challenge for a long time. In the first part of this thesis, it has been shown that the combination of methyl specific labeling, optimized NMR spectroscopy for large assemblies and electron microscopy can be used to monitor the different states of the functional cycle of a 1 MDa chaperonin. To study this mechanism, the native chaperonin was reconstituted with a labeling of the methionines and valines methyl groups. Methionines residues have been used as probes to identify the NMR spectra corresponding to intermediates states and active species of the functional cycle. Thanks to theses probes, it has been possible to follow in real time the structural rearrangements corresponding to the different conformations of the chaperonin during its functional cycle. The second part deals with the characterization of the interaction between the chaperonin and an unfolded protein. Observation of the stabilization of the unfolded protein by the chaperonin allowed to identify the holdase activity of the chaperonin. Using a clever combination of a differential methyl labeling and optimized NMR spectroscopy for large assemblies, it has been possible to follow the refolding of the unfolded protein by the chaperonin and the effects of the unfolded protein on the functional cycle of the chaperonin in action
Resolution-optimized NMR measurement of 1DCH, 1DCC and 2DCH residual dipolar couplings in nucleic acid bases by Jérôme Boisbouvier( )

1 edition published in 2004 in English and held by 2 WorldCat member libraries worldwide

Simultaneous determination of disulphide bridge topology and three-dimensional structure using ambiguous intersulphur distance restraints: Possibilities and limitations by Jérôme Boisbouvier( )

1 edition published in 2000 in English and held by 2 WorldCat member libraries worldwide

Resolution-Enhanced Base-Type-Edited HCN Experiment for RNA by Hélène Van Melckebeke( )

1 edition published in 2005 in English and held by 2 WorldCat member libraries worldwide

Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids by Jerome Boisbouvier( )

1 edition published in 2018 in English and held by 2 WorldCat member libraries worldwide

Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins by Rodolfo M Rasia( )

1 edition published in 2011 in English and held by 2 WorldCat member libraries worldwide

Utilisation de la corrélation croisée CSA-Dipolaire pour l'étude RMN des acides ribonucléiques : détermination simultanée de la structure des protéines et de la topologie des ponts disulfures par modélisation moléculaire sous contraintes RMN by Jérôme Boisbouvier( Book )

2 editions published in 2000 in French and held by 2 WorldCat member libraries worldwide

L'ETUDE DES ARN PAR RMN EST LIMITEE PAR LEUR DISTRIBUTION INHOMOGENE DE PROTONS ET LA FAIBLE RESOLUTION DES SPECTRES DE CORRELATIONS 1 3C- 1H, RENDANT PARTICULIEREMENT DIFFICILE L'ATTRIBUTION ET LEUR CARACTERISATION STRUCTURALE. IL EST DEMONTRE QUE L'UTILISATION DE LA CORRELATION CROISEE CSA-DIPOLAIRE APPORTE UN IMPORTANT GAIN EN RESOLUTION ET EN SENSIBILITE POUR CES EXPERIENCES. CES AVANTAGES ONT ETE APPLIQUES AUX PRINCIPALES EXPERIENCES PERMETTANT L'ATTRIBUTION ET LA MESURE DES PARAMETRES STRUCTURAUX ET DYNAMIQUES DANS LES ARN DE TAILLES IMPORTANTES. L'ETUDE QUANTITATIVE DES PHENOMENES DE RELAXATION INDUITS PAR CETTE CORRELATION CROISEE PERMET, D'UNE PART, DE DETERMINER SIMPLEMENT LA CONFORMATION DES SUCRES, ET D'AUTRE PART, APPORTE LA PREMIERE CARACTERISATION EXPERIMENTALE DES CSA DANS LES BASES NUCLEIQUES DES ARN EN SOLUTION. DANS LES BIOMOLECULES PARAMAGNETIQUES LA MESURE DE CES VITESSES DE RELAXATION CROISEE PERMET D'OBTENIR DE NOUVELLES CONTRAINTES STRUCTURALES A LONGUE PORTEE, PARTICULIEREMENT INTERESSANTES POUR LA DETERMINATION DE LA STRUCTURE DES ARN. UNE APPROCHE EST PROPOSEE POUR GENERALISER CETTE METHODE AUX BIOMOLECULES NE POSSEDANT PAS DE SITE NATUREL DE FIXATION AUX IONS PARAMAGNETIQUES. DANS UNE SECONDE PARTIE, IL EST PROPOSE UN PROTOCOLE DE CALCUL DE STRUCTURE OPTIMISE POUR LA DETERMINATION DE LA TOPOLOGIE DES PONTS DISULFURES A PARTIR DES CONTRAINTES RMN. UNE ETUDE DES POSSIBILITES ET LIMITATIONS DE CETTE METHODE, INDIQUE QU'ELLE EST GENERALE ET PEUT ETRE APPLIQUEE DES LES PREMIERS STADES DES ETUDES RMN DES PROTEINES RICHES EN PONTS DISULFURES. LES APPLICATIONS A DEUX TOXINES RICHES EN PONTS DISULFURES RESISTANTES AUX ENDOPROTEASES, APPORTENT DE NOUVELLES INFORMATIONS STRUCTURALES ET BIOCHIMIQUES POUR CES FAMILLES DE PROTEINES
Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins by Guillaume Mas( )

1 edition published in 2013 in English and held by 2 WorldCat member libraries worldwide

A systematic mutagenesis-driven strategy for site-resolved NMR studies of supramolecular assemblies by Carlos Amero( )

1 edition published in 2011 in English and held by 2 WorldCat member libraries worldwide

Spectral editing of intra- and inter-chain methyl-methyl NOEs in protein complexes by Ricarda Törner( )

1 edition published in 2020 in English and held by 2 WorldCat member libraries worldwide

<> by Rime Kerfah( )

1 edition published in 2014 in English and held by 2 WorldCat member libraries worldwide

Etudes biophysiques de l'interaction entre la protéine humaine TRBP et un précurseur de microARN oncogène by Matthieu Benoit( )

1 edition published in 2013 in French and held by 2 WorldCat member libraries worldwide

MicroRNAs (miRNA) are a class of small non-coding RNAs that regulate gene expression through RNA interference (RNAi). Human miRNAs are generated via a series of enzymatic processing steps. In particular, in the cytoplasm, the precursor miRNA (pre-miRNA) is recognized and cleaved by a complex containing the RNase III enzyme Dicer and several non-catalytic accessory proteins. HIV TAR element-binding protein (TRBP) is a constituent of the Dicer complex, which augments complex stability, has effect on the cleavage kinetics and on the cleavage site and potentially functions in substrate recognition and product transfer to the RNA-induced silencing complex (RISC). TRBP is composed of three double stranded RNA binding domains (dsRBDs). The RNA binding region of TRBP is composed of the first two dsRBDs and an uncharacterized interdomain region. The present study reports the in vitro biophysical characterization of the RNA binding region of TRBP in the apo state and in the RNA bound state with the two successive cytoplasmic precursors of the oncogenic human microRNA miR-155, the hairpin pre-miR-155 and the related Dicer product miR-155/miR-155* duplex. The study shows that the RNA binding region of TRBP is monomeric and comprises two independent double-stranded RNA-binding domains connected by a 60 residues flexible linker. The first dsRBD, uncharacterized previously in solution, undergoes a full folding/unfolding equilibrium in a wide range of physico-chemical conditions. The two first dsRBDs of TRBP can interact with one microRNA precursor and two RNA binding regions can interact with one precursor molecule. The RNA-binding region of TRBP interacts with both pre-miR-155 and miR-155/miR-155* duplex with similar affinities. In the complex with one RNA binding region of TRBP bound to either pre-miR-155 or miR-155/miR-155* duplex, no evidence of contact between the two dsRBDs were observed and the protein interacts with both precursors via the same protein binding surface. The data presented here suggest that the RNA binding region of TRBP can play a role before and after processing of pre-miRNAs by Dicer, including in the RISC loading complex
Specific labeling strategies for new developments in liquid state protein NMR by Rachel Lenoir-Capello( )

1 edition published in 2020 in English and held by 1 WorldCat member library worldwide

Nuclear Magnetic Resonance (NMR) provides valuable structural and dynamic information at the atomic scale, however, the low sensitivity and resolution of signals rapidly preclude investigations of larger molecular objects. We present three isotopic labeling strategies for different protein-solution NMR experiments and demonstrate their potential for the structural study of biomolecules in solution. Among the strategies considered, two are based on the use of in vitro protein expression to obtain selectively labeled proteins of a certain chemical group and/or amino acid in a perdeuterated environment. Perdeuteration is essential for the optimal use of Transverse Relaxation Optimized Spectroscopy pulse sequences. They allowed significant spectral gains when samples were specifically labeled on amide groups or on the methylene of glycines while maintaining a very high rate of deuteration on the other chemical functions of the proteins. The third protein labeling strategy employed is based on in vivo protocols but used in innovative NMR applications: a technique of hyperpolarization of nuclei in solution which increases their sensitivity by several orders of magnitude. The lifetime of this hyperpolarization is governed by the longitudinal relaxation time of nuclei, which are reduced for proteins at room temperature. By isolating the nuclei of interest in a perdeuterated environment, dipolar interactions created by neighboring protons were eliminated and hyperpolarized nuclei relaxed much more slowly. Hyperpolarization of a small protein domain was successfully undertaken at 1K but the dissolution conditions need to be improved in order to preserve a homogeneous aqueous phase
Recent developments in biomolecular NMR by Marcellus Ubbink( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

This text draws together experts in the field to discuss advances in nuclear magnetic resonance methods that have occurred or had an impact on the biomolecular field in the last few years
 
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Recent developments in biomolecular NMR
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French (4)