Large FK506-Binding Proteins Shape the Pharmacology of Rapamycin

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Veröffentlicht in:Molecular and Cellular Biology 2013-04, Vol.33 (7), p.1357-1367
Hauptverfasser: März, Andreas M, Fabian, Anne-Katrin, Kozany, Christian, Bracher, Andreas, Hausch, Felix
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container_end_page 1367
container_issue 7
container_start_page 1357
container_title Molecular and Cellular Biology
container_volume 33
creator März, Andreas M
Fabian, Anne-Katrin
Kozany, Christian
Bracher, Andreas
Hausch, Felix
description 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       
doi_str_mv 10.1128/MCB.00678-12
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subjects Cell Line
Cell Line, Tumor
HEK293 Cells
HeLa Cells
Humans
Immunosuppressive Agents - pharmacology
Phosphorylation - drug effects
Protein Binding
Proto-Oncogene Proteins c-akt - metabolism
Saccharomyces cerevisiae - metabolism
Sirolimus - chemistry
Sirolimus - pharmacology
Tacrolimus - metabolism
Tacrolimus - pharmacology
Tacrolimus Binding Proteins - chemistry
Tacrolimus Binding Proteins - metabolism
TOR Serine-Threonine Kinases - antagonists & inhibitors
TOR Serine-Threonine Kinases - metabolism
title Large FK506-Binding Proteins Shape the Pharmacology of Rapamycin
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