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L Cocquerel

Showing results (1-10 of 8) with videos related to

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Virologie (Montrouge, France)|September 22, 2022
[Entry of HCV into target cells]F Helle, L Cocquerel
Journal 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.
Journal 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.
Journal 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.
The Journal of Biological Chemistry|May 16, 2000
The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerizationA Op De Beeck, R Montserret, S Duvet, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Virologie (Montrouge, France)|September 22, 2022
[Entry of HCV into target cells]F Helle, L Cocquerel
Journal 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.
Journal 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.
Journal 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.
The Journal of Biological Chemistry|May 16, 2000
The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerizationA Op De Beeck, R Montserret, S Duvet, et al.
Pageof 1