J
Jean Gagnon
Researcher at Université de Montréal
Publications - 211
Citations - 9797
Jean Gagnon is an academic researcher from Université de Montréal. The author has contributed to research in topics: Peptide sequence & Amino acid. The author has an hindex of 50, co-authored 206 publications receiving 9408 citations. Previous affiliations of Jean Gagnon include European Synchrotron Radiation Facility & University of Washington.
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Cloning and expression of the rat prolactin receptor, a member of the growth hormone/prolactin receptor gene family
Jean-Marie Boutin,Christine Jolicoeur,Hiroaki Okamura,Jean Gagnon,Marc Edery,Mariko Shirota,Denis Banville,Isabelle Dusanter-Fourt,Jean Djiane,Paul A. Kelly +9 more
TL;DR: There is strong localized sequence identity between these two receptors in both the extracellular and cytoplasmic domains, suggesting that the two receptors originated from a common ancestor.
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Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin
Alan F. Williams,Jean Gagnon +1 more
TL;DR: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains, and preliminary evidence for an invertebrate Thy- 1 homolog supports this possibility.
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Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.
Jean-François Hernandez,Jean Gagnon,Laurent Chiche,Tuyet Mai Nguyen,Jean-Pierre Andrieu,Annie Heitz,Thai Trinh Hong,and T. Trân Châu Pham,Dung Le Nguyen +8 more
TL;DR: Three trypsin inhibitors, from the seeds of the squash Momordica cochinchinensis, have been isolated and purified and it was shown that their polypeptide backbones are cyclic, a structure that has never been described in squash TIs.
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Ovalbumin: a secreted protein without a transient hydrophobic leader sequence.
TL;DR: The sequence of 35 residues at the NH2 terminus of ovalbumin was determined by automated Edman degradation after a method was devised to prevent acetylation during protein synthesis in the reticulocyte lysate, and does not resemble the transient "signal peptides" associated with most secretory proteins.
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Molecular cloning of the CD9 antigen. A new family of cell surface proteins.
Claude Boucheix,P Benoit,Philippe Frachet,Martine Billard,Ronald E. Worthington,Jean Gagnon,Georges Uzan +6 more
TL;DR: Sequence and structural comparisons showed extensive similarity of the CD9 antigen with a 237-amino acid molecule described previously as the human melanoma-associated antigen ME491 and a Schistosoma mansoni membrane protein of 218 amino acids, which identify a new family of cell-surface proteins.