G
Glen R. Nemerow
Researcher at Scripps Research Institute
Publications - 172
Citations - 15743
Glen R. Nemerow is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Integrin & Virus. The author has an hindex of 64, co-authored 172 publications receiving 15184 citations. Previous affiliations of Glen R. Nemerow include University of California & Purdue University.
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Journal ArticleDOI
Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
TL;DR: In this article, the vitronectin-binding integrins α v β 3 and β 5 promote viral infection in a novel way since antibodies against these receptors or soluble penton base block virus internalization without affecting attachment.
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Differential regulation of cell motility and invasion by FAK
Datsun A. Hsia,Satyajit Sujit Kumar Mitra,Christof R. Hauck,Christof R. Hauck,Christof R. Hauck,Daniel N. Streblow,Jay A. Nelson,Dusko Ilic,Shuang Huang,Erguang Li,Glen R. Nemerow,Jay Leng,Kathryn S. R. Spencer,David A. Cheresh,David D. Schlaepfer +14 more
TL;DR: It is shown that viral Src transformation of FAK−/− cells promotes integrin-stimulated motility equal to stable FAK reexpression, and a dual role for FAK in promoting cell motility and invasion through the activation of distinct signaling pathways.
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Adenovirus Protein VI Mediates Membrane Disruption following Capsid Disassembly
TL;DR: A new model of Ad entry is proposed based on the present observations of capsid disassembly and membrane penetration, which possessed membrane lytic activity similar to partially disassembled virions.
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Integrin alpha v beta 5 selectively promotes adenovirus mediated cell membrane permeabilization.
TL;DR: Evidence is provided for the involvement of a cellular receptor in virus- mediated membrane permeabilization and a novel biological role for integrin alpha v beta 5 in the infectious pathway of a human adenovirus is suggested.
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Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: sequence homology of gp350 and C3 complement fragment C3d.
TL;DR: A computer-generated comparison of the deduced gp350 amino acid sequence with that of the human C3d complement fragment revealed two regions of significant primary sequence homology, a finding which suggests that a common region on these two unrelated proteins may be involved in CR2 binding.