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Biochemistry|April 9, 1985
Conformational flexibility of neurophysin as investigated by local motions of fluorophores. Relationships with neurohypophyseal hormone bindingM Rholam, P NicolasFEBS Letters|October 20, 1986
Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sitesM Rholam, P Nicolas, P CohenBiochemistry|June 18, 1985
Salt-dependent structural changes of neurohormones: lithium ions induce conformational rearrangements of ocytocin to a vasopressin-like structureM Rholam, P Nicolas, P CohenBiochemistry|September 28, 1982
Binding of neurohypophyseal peptides to neurophysin dimer promotes formation of compact and spherical complexesM Rholam, P Nicolas, P CohenEuropean Journal of Biochemistry|March 11, 2000
Favourable side-chain orientation of cleavage site dibasic residues of prohormone in proteolytic processing by prohormone convertase 1/3N Brakch, M Rholam, M Simonetti, et al.The Journal of Biological Chemistry|September 25, 1989
Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin modelN Brakch, H Boussetta, M Rholam, et al.Biochemistry|May 11, 1993
Role of beta-turn in proteolytic processing of peptide hormone precursors at dibasic sitesN Brakch, M Rholam, H Boussetta, et al.Journal of Chromatography|May 25, 1988
Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzymeC Créminon, M Rholam, H Boussetta, et al.FEBS Letters|May 6, 1991
Differential processing of hormone precursor. Independent production of somatostatins 14 and 28 in transfected neuroblastoma 2A cellsN Brakch, M Rholam, C Nault, et al.Biochemistry|March 21, 1989
Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitorI Plevrakis, C Clamagirand, C Créminon, et al.Pageof 2