Mireille Boyer

Stress Environnementaux et Biosurveillance des Milieux Aquatiques

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Yves Benyamin

Université de Montpellier

Claude Roustan

Université de Montpellier

Caroline Méjean

Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement

Magali Jullien

Inserm

Catherine A. Royer

Rensselaer Polytechnic Institute

Jérôme Labbé

Pierre Fabre (France)

Marie‐Odile Roy

Euroscreen (Belgium)

Jean-Pierre Labbé

Centre National de la Recherche Scientifique

Kim S. Wise

J. Craig Venter Institute

Raoul Bertrand

Centre de Recherche en Biologie cellulaire de Montpellier

Cooperative Institutions

Centre National de la Recherche Scientifique

Inserm

Université de Montpellier

Centre de Recherche en Biologie cellulaire de Montpellier

École Pratique des Hautes Études

Université Paris Cité

Centre de Biologie Structurale

Centre National pour la Recherche Scientifique et Technique (CNRST)

Sorbonne Université

Hôpital Purpan

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Equilibrium and Pressure-jump Relaxation Studies of the Conformational Transitions of P13MTCP1

Journal of Molecular Biology (2002)

Ryo Kitahara Catherine A. Royer Hiroaki Yamada Mireille Boyer Jean-Louis Saldana

Conformational isomerism

Equilibrium unfolding

10.1016/s0022-2836(02)00516-8

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Citations (51)

DNAse I – actin complex: An immunological study

Bioscience Reports (1985)

Mireille Boyer Claude Roustan Yves Benyamin

DNAse I – actin complex formation is studied in the presence of different anti actin antibody populations. The binding of DNAse I to actin is shown to be affected by antibodies specific to a central region in actin sequence (168–226). The C- and N-extremities of actin are shown to be in spatial proximity at the surface of the actin monomer and far from the binding area of DNAse I.

Actin-binding protein

Actin remodeling

Actina

Sequence (biology)

10.1007/bf01117439

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Citations (32)

μ‐Opioid Receptors and Not K‐Opioid Receptors Are Coupled to the Adenylate Cyclase in the Cerebellum

Journal of Neurochemistry (1990)

Jocelyne Polastron Mireille Boyer Y. Quertermont J Thouvenot Jean‐Christophe Meunier

The putative regulatory effect of opioids on adenylate cyclase was investigated in two different preparations containing, respectively, two different populations of opioid receptors: the rabbit cerebellum (greater than 75% mu-opioid receptors) and the guinea pig cerebellum (greater than 80% kappa-opioid receptors). In the mu-preparation, but not in the kappa-preparation, opioids inhibited the basal and the forskolin-stimulated adenylate cyclase activity in a dose-dependent manner and stereospecifically. The inhibition was in the 20-30% range, required the presence in the assay medium of Mg2+ and of GTP, but was independent of the presence of Na+. Pharmacological characterization of the inhibitory response in the rabbit cerebellum clearly showed that it was under the control of a mu-opioid binding site, with the effect being elicited by non-selective (etorphine and morphine) and mu-selective (Tyr-D-Ala-Gly-Me-Phe-Gly-ol) agonists, whereas delta- and kappa-selective agonists were almost totally ineffective. ADP ribosylation of inhibitory GTP-binding protein by pertussis toxin failed to block the inhibitory effect of opioids, and data presented suggest that this failure is likely to be the consequence of a limited access of the toxin to its substrate in rabbit cerebellum membranes.

Etorphine

10.1111/j.1471-4159.1990.tb01908.x

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Citations (32)

Two identical hydrophobic clusters are present on the same actin monomer: interaction between one myosin subfragment‐1 and two actin monomers

FEBS Letters (1995)

Jean-Pierre Labbé Mireille Boyer Yves Benyamin

Two‐dimensional hydrophobic clusters analysis (HCA) was used to compare the distribution of hydrophobic clusters along various actin sequence. HCA‐deduced patterns were not altered by amino‐acid variations throughout the evolution of actin and we observed similar hydrophobic motifs comprising myosin subfragment‐1 ATP‐independent binding sites. HCA suggested the presence of two groups of identical hydrophobic motifs (A 1 and A 2 ) which bound on each side of the S1 (63 kDa‐31 kDa) connecting segment in relation with two actin monomers. This connection is important in communications between actin‐ and nucleotide‐binding sites. We postulate that some relation and message between the two motifs A 1 and A 2 take place through myosin subfragment‐1 (63 kDa‐31 kDa) connecting segment.

Actin-binding protein

Actin remodeling

10.1016/0014-5793(95)01044-f

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Citations (5)

Biochemical evidence for the presence of an unconventional actin protein in a prokaryotic organism

Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology (1996)

Jean-Pierre Labbé Marie-Cécile Harricane Mireille Boyer Jean Derancourt Claude Roustan

10.1016/0305-0491(96)00034-x

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Citations (7)

Conformational changes induced by Mg²⁺ on actin monomers

FEBS Letters (1985)

Claude Roustan Yves Benyamin Mireille Boyer Raoul Bertrand Etienne Audemard

The effect of Mg 2+ ions on the conformation of G‐actin and in particular on the accessibility of its antigenic regions has been tested. Experiments were performed with G‐actin coupled to Sepharose 4B which was, therefore, maintained in the monomeric state. The results presented her show that the 2mM MgCl 2 ‐perturbed antigenic site is located in a central region of the actin sequence.

Sequence (biology)

Sepharose

Actina

Conformational change

10.1016/0014-5793(85)81125-x

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Citations (29)

Antigenic probes locate the myosin subfragment 1 interaction site on the N-terminal part of actin

Bioscience Reports (1986)

Caroline Méjean Mireille Boyer Jérôme Labbé Jean Derancourt Yves Benyamin

The interaction of two different anti-actin antibody populations with the myosin subfragment 1-F-actin rigor complex has been studied. In contrast with the 1–7 sequence, the 18–28 sequence appears to be strongly implicated in the contact area of the myosin head on the actin polypeptide chain.

Actina

Sequence (biology)

Actin remodeling

10.1007/bf01116141

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Citations (38)

Les possibilités de composter les renouées asiatiques

Mireille Boyer Louise Barthod

10.14758/set-revue.2019.1.14

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Citations (1)

Structural variations in actins. Biochemical and immunological tools for probing the structure of rabbit skeletal-muscle and bovine aortic actins

Biochemical Journal (1985)

J C Cavadore Claude Roustan Yves Benyamin Mireille Boyer Jacques Haiech

Structural differences between skeletal-muscle and aortic actins were studied by using biochemical and immunological approaches. By using proteinase digestion we found that three regions of actin show structural differences: (a) in the C-terminal part, (b) the region around residue 227 and (c) the region around residue 167. By using antibodies specific to particular actin conformations we can discriminate between monomeric and filamentous forms of the two actins. Our results show that the minor sequence variations of the N- and C-terminal regions induce structural change in these regions, but also some long-range structural variations in other regions.

Residue (chemistry)

Actina

10.1042/bj2310363

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Citations (8)

Induction by chemically modified actin derivatives of antibody specificity

FEBS Letters (1983)

Yves Benyamin Claude Roustan Mireille Boyer

A comparison of specific antibodies induced by unfolded actins modified either by oxidation or by arylation of lysine residues was reported. We have focused our work on binding properties with filamentous actin and located its preferential antigenic sites for the anti‐arylated‐actin antibodies in the C‐part of the molecule. An interference of anti‐oxidized actin antibodies upon actin polymerisation has also been reported.

Actin-binding protein

10.1016/0014-5793(83)80932-6

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Citations (15)