The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes

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Bibliographic Details
Published in:	Molecular and Cellular Biology Vol. 15; no. 5; pp. 2393 - 2401
Main Authors:	Gervais, F G, Veillette, A
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-05-1995
Subjects:	3T3 Cells Amino Acid Sequence Animals Base Sequence Binding Sites - genetics Cell Line DNA Primers - genetics Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Mice Molecular Sequence Data Mutation Phosphorylation Protein Tyrosine Phosphatases - metabolism Protein-Tyrosine Kinases - genetics Protein-Tyrosine Kinases - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism T-Lymphocytes - enzymology
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Summary:	Article Usage Stats Services MCB 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 MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology. For an alternate route to MCB .asm.org, visit: MCB
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0270-7306 1098-5549