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المؤلفون: Benjamin W. Parker, Mónika Bálint, Attila Reményi, Eric L. Weiss, Csaba Hetényi, Gergő Gógl
المساهمون: University of Illinois at Urbana-Champaign [Urbana], University of Illinois System, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institute of Organic Chemistry [Budapest], Research Centre for Natural Sciences, Hungarian Academy of Sciences (MTA)-Hungarian Academy of Sciences (MTA), University of Pecs, Northwestern University [Evanston], univOAK, Archive ouverte
المصدر: Biochemistry
Biochemistry, 2020, 59 (17), pp.1688-1700. ⟨10.1021/acs.biochem.9b01096⟩مصطلحات موضوعية: Models, Molecular, Saccharomyces cerevisiae Proteins, Protein Conformation, Allosteric regulation, Saccharomyces cerevisiae, Morphogenesis, Nerve Tissue Proteins, [SDV.CAN]Life Sciences [q-bio]/Cancer, Plasma protein binding, Protein Serine-Threonine Kinases, Biochemistry, Article, Cofactor, Substrate Specificity, Conserved sequence, 03 medical and health sciences, Protein structure, [SDV.CAN] Life Sciences [q-bio]/Cancer, Coactivator, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Conserved Sequence, 030304 developmental biology, 0303 health sciences, Cofactor binding, biology, Chemistry, Kinase, 030302 biochemistry & molecular biology, Intracellular Signaling Peptides and Proteins, biology.organism_classification, Cell biology, biology.protein, Signal transduction, Protein Binding
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المساهمون: Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1), Université de Lille-Centre National de la Recherche Scientifique (CNRS)
المصدر: Biochemical Journal
Biochemical Journal, Portland Press, 2017, 474 (6), pp.907-921. ⟨10.1042/BCJ20161052⟩
Biochemical Journal, 2017, 474 (6), pp.907-921. ⟨10.1042/BCJ20161052⟩مصطلحات موضوعية: 0301 basic medicine, chemistry.chemical_classification, Cofactor binding, biology, Mycobacterium smegmatis, [SDV]Life Sciences [q-bio], Mutant, Cell Biology, Reductase, biology.organism_classification, Biochemistry, Molecular biology, Complementation, 03 medical and health sciences, 030104 developmental biology, Enzyme, chemistry, Oxidoreductase, Dehydratase, lipids (amino acids, peptides, and proteins), Molecular Biology, ComputingMilieux_MISCELLANEOUS
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edf6b70710436af88a02257bbab827af
https://hal.archives-ouvertes.fr/hal-02137584 -
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المؤلفون: Claude Didierjean, Hélène Dubourg-Gerecke, François Talfournier, Raphael Bchini, André Aubry, Sophie Rahuel-Clermont, Guy Branlant
المساهمون: ARN-RNP, structure-fonction-maturation (AREMS), Université Henri Poincaré - Nancy 1 (UHP)-Centre National de la Recherche Scientifique (CNRS), Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Cristallographie et modélisation des matériaux minéraux et biologiques (CMMMB), Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS), Cristallographie, Résonance Magnétique et Modélisations (CRM2), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL)
المصدر: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (37), pp.31095-31103. ⟨10.1074/jbc.M112.350272⟩مصطلحات موضوعية: Stereochemistry, Aldehyde dehydrogenase, Dehydrogenase, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, 03 medical and health sciences, Structure-Activity Relationship, Protein structure, Bacterial Proteins, Enzyme kinetics, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, 030304 developmental biology, 0303 health sciences, Cofactor binding, Adenine binding, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Methylmalonate-Semialdehyde Dehydrogenase (Acylating), Adenine, Hydrolysis, 030302 biochemistry & molecular biology, Cell Biology, Enzyme structure, 3. Good health, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Kinetics, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], biology.protein, Enzymology, NAD+ kinase, NADP, Bacillus subtilis
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::582667311ceafd1f9a729c260112fe1a
https://hal.univ-lorraine.fr/hal-01682573 -
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المؤلفون: Ronen Marmorstein, Guoping Da, Catherine Dargemont, Batool Ossareh-Nazari, Keqin Li, Kehao Zhao
المساهمون: University of Pennsylvania [Philadelphia], Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Department of Chemistry
المصدر: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280(32), pp.29176-29185. ⟨10.1074/jbc.M502975200⟩مصطلحات موضوعية: Models, Molecular, Protein Folding, Saccharomyces cerevisiae Proteins, Protein Conformation, Dimer, Protein domain, Molecular Sequence Data, Saccharomyces cerevisiae, Calorimetry, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Deubiquitinating enzyme, Protein–protein interaction, 03 medical and health sciences, chemistry.chemical_compound, Endopeptidases, Escherichia coli, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Molecular Biology, 030304 developmental biology, Cell Proliferation, Glutathione Transferase, 0303 health sciences, Cofactor binding, Binding Sites, biology, Sequence Homology, Amino Acid, Chemistry, 030302 biochemistry & molecular biology, Isothermal titration calorimetry, Cell Biology, Culture Media, Protein Structure, Tertiary, Dissociation constant, Crystallography, Sedimentation equilibrium, Biophysics, biology.protein, Mutagenesis, Site-Directed, Carrier Proteins, Dimerization, Protein Binding
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e088dc7053408df023a834b8e2089ed8
https://hal.archives-ouvertes.fr/hal-00068948