Activation of the N-Terminally Truncated Form of the Stk Receptor Tyrosine Kinase Sf-Stk by Friend Virus-Encoded gp55 Is Mediated by Cysteine Residues in the Ecotropic Domain of gp55 and the Extracellular Domain of Sf-Stk

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Veröffentlicht in:	Journal of Virology 2010-03, Vol.84 (5), p.2223-2235
Hauptverfasser:	He, Shihan, Ni, Shuang, Hegde, Shailaja, Wang, Xin, Sharda, Daniel R, August, Avery, Paulson, Robert F, Hankey, Pamela A
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biological and medical sciences Cell Membrane - metabolism Cells, Cultured Cysteine - genetics Cysteine - metabolism Erythroid Precursor Cells - cytology Erythroid Precursor Cells - metabolism Erythropoietin - genetics Erythropoietin - metabolism Fundamental and applied biological sciences. Psychology Humans Mice Mice, Inbred C57BL Microbiology Mutagenesis, Site-Directed Protein Conformation Protein Structure, Tertiary Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - genetics Receptor Protein-Tyrosine Kinases - metabolism Receptors, Erythropoietin - genetics Receptors, Erythropoietin - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Transformation and Oncogenesis Viral Envelope Proteins - chemistry Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Virology
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Zusammenfassung:	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI
ISSN:	0022-538X 1098-5514
DOI:	10.1128/JVI.02090-09