• Publications
  • Influence
Role of amino acid sequences flanking dibasic cleavage sites in precursor proteolytic processing The importance of the first residue C-terminal of the cleavage site
: The amino acid sequences flanking 352 dibasic moieties contained in 83 prohormones and pro-proteins listed in a database were examined. Frequency calculations on the occurrence of given residues atExpand
  • 52
  • 3
Processing of peptide and hormone precursors at the dibasic cleavage sites
  • M. Rholam, C. Fahy
  • Biology, Medicine
  • Cellular and Molecular Life Sciences
  • 20 March 2009
Many functionally important cellular peptides and proteins, including hormones, neuropeptides, and growth factors, are synthesized as inactive precursor polypeptides, which require post-translationalExpand
  • 66
  • 3
Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro‐ocytocin model.
Bioactivation of pro‐proteins by limited proteolysis is a general mechanism in the biosynthesis of hormones, receptors and viral protein precursors. This proceeds by cleavage of peptide bonds at theExpand
  • 35
  • 2
Binding of neurohypophyseal peptides to neurophysin dimer promotes formation of compact and spherical complexes.
Previous hydrodynamic studies [Rholam, M., & Nicolas, P. (1981) Biochemistry 20, 5837-5843] have demonstrated that the dimerization of a neurophysin monomer (prolate ellipsoid with an axial ratio,Expand
  • 29
  • 1
Role of amino acid sequences flanking dibasic cleavage sites in precursor proteolytic processing. The importance of the first residue C-terminal of the cleavage site.
The amino acid sequences flanking 352 dibasic moieties contained in 83 prohormones and pro-proteins listed in a database were examined. Frequency calculations on the occurrence of given residues atExpand
  • 46
  • 1
Role of beta-turn in proteolytic processing of peptide hormone precursors at dibasic sites.
Proteolytic activation of prohormones and proproteins occurs most frequently at the level of basic amino acids arranged in doublets. Previous predictions by Rholam et al. [Rholam, M., Nicolas, P., &Expand
  • 47
  • 1
Salt-dependent structural changes of neurohormones: lithium ions induce conformational rearrangements of ocytocin to a vasopressin-like structure.
The preferred average conformation and structural subdomain interactions of the nonapeptide hormones vasopressin and ocytocin have been analyzed through the determination of their hydrodynamic volumeExpand
  • 11
  • 1
The somatostatin-28(1-12)-NPAMAP sequence: an essential helical-promoting motif governing prosomatostatin processing at mono- and dibasic sites.
Proline residues, known to have special structural properties, induce particular conformations which participate in some biological functions. Two prolines (Pro(-9), Pro(-5)) located near theExpand
  • 7
  • 1
Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sites
We have analyzed the amino acid sequences situated around the putative proteolytic cleavage sites in twenty different biosynthetic precursors of peptide hormones by processing enzymes. The predictionExpand
  • 129
  • PDF