Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Deborah J. Anselma"'
Autor:
Ping Zhu, Paul W. H. I. Parren, Paul J. Maddon, Norbert Schülke, Anthony R. Villa, James M. Binley, Deborah J. Anselma, Kenneth H. Roux, Mika Vesanen, Rogier W. Sanders, John P. Moore, Min Lu, William C. Olson
Publikováno v:
Journal of virology, 76(15), 7760-7776. American Society for Microbiology
The native, fusion-competent form of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein complex is a trimeric structure composed of three gp120 subunits and three gp41 subunits; the receptor-binding (CD4 and coreceptor) sites are l
Autor:
Brian Clas, Deborah J. Anselma, James M. Binley, Aditi Master, Francis Kajumo, Yong Guo, Paul J. Maddon, John P. Moore, Rogier W. Sanders, Norbert Schuelke, William C. Olson
Publikováno v:
Journal of virology. 74(2):627-643
The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein epitopes exposed on infectious virions. These native envelope glycoprotein complexes comprise three gp12
Autor:
Diep N. H. Tran, Tatjana Dragic, Jeremy P. Segal, Paul J. Maddon, Simon Monard, John P. Moore, Kirsten A. Nagashima, Daniah A. D. Thompson, Deborah J. Anselma, Francis Kajumo, Gwénaël Rabut, Yong Guo, William C. Olson
The CC-chemokine receptor CCR5 mediates fusion and entry of the most commonly transmitted human immunodeficiency virus type 1 (HIV-1) strains. We have isolated six new anti-CCR5 murine monoclonal antibodies (MAbs), designated PA8, PA9, PA10, PA11, PA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc0644230089ae9c514e563753a402d1
https://europepmc.org/articles/PMC104194/
https://europepmc.org/articles/PMC104194/