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Virologie (Montrouge, France)|September 22, 2022
[Entry of HCV into target cells]F Helle, L CocquerelCancer Gene Therapy|February 11, 2012
Germ cell DNA-repair systems-possible tools in cancer research?F HelleJournal of Virology|March 23, 2000
Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteinsL Cocquerel, C Wychowski, F Minner, et al.Hospital Materiel Management Quarterly|February 8, 2000
Creativity: the key to breakthrough changes, how teaming can harness collective knowledgeP F HelleJournal of Virology|March 14, 1998
A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2L Cocquerel, J C Meunier, A Pillez, et al.Cellular and Molecular Life Sciences : CMLS|October 5, 2007
Hepatitis C virus entry into host cellsF Helle, J DubuissonJournal of Virology|March 12, 1999
The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulumL Cocquerel, S Duvet, J C Meunier, et al.The Journal of Biological Chemistry|November 21, 1998
Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrievalS Duvet, L Cocquerel, A Pillez, et al.The Journal of General Virology|April 22, 1999
Analysis of the glycosylation sites of hepatitis C virus (HCV) glycoprotein E1 and the influence of E1 glycans on the formation of the HCV glycoprotein complexJ C Meunier, A Fournillier, A Choukhi, et al.The Journal of Biological Chemistry|July 7, 2000
Glycosylation of the hepatitis C virus envelope protein E1 is dependent on the presence of a downstream sequence on the viral polyproteinJ Dubuisson, S Duvet, J C Meunier, et al.Pageof 2