The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity

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Veröffentlicht in:	Molecular and Cellular Biology 1994-04, Vol.14 (4), p.2675-2685
Hauptverfasser:	KLIPPEL, A, ESCOBEDO, J. A, HIRANO, M, WILLIAMS, L. T
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3 Cells Analytical, structural and metabolic biochemistry Animals Base Sequence Binding Sites Biological and medical sciences Cell Line Cloning, Molecular DNA Primers DNA, Complementary - metabolism Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Escherichia coli Fundamental and applied biological sciences. Psychology Gene Library Kinetics Macromolecular Substances Mice Mice, Inbred BALB C Molecular Sequence Data Phosphatidylinositol 3-Kinases Phosphotransferases (Alcohol Group Acceptor) - biosynthesis Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Binding Protein Biosynthesis Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping Sequence Deletion Transcription, Genetic Transfection Transferases
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Zusammenfassung:	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
ISSN:	0270-7306 1098-5549
DOI:	10.1128/MCB.14.4.2675