A Novel mTOR-Regulated Phosphorylation Site in Elongation Factor 2 Kinase Modulates the Activity of the Kinase and Its Binding to Calmodulin

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...

Full description

Saved in:

Bibliographic Details
Published in:	Molecular and Cellular Biology Vol. 24; no. 7; pp. 2986 - 2997
Main Authors:	Browne, Gareth J., Proud, Christopher G.
Format:	Journal Article
Language:	English
Published:	United States American Society for Microbiology 01-04-2004 Taylor & Francis
Subjects:	3-Phosphoinositide-Dependent Protein Kinases Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino Acids - metabolism Animals Calcium-Calmodulin-Dependent Protein Kinases - chemistry Calcium-Calmodulin-Dependent Protein Kinases - genetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calmodulin - metabolism Cell Growth and Development Cell Line Cricetinae Elongation Factor 2 Kinase Humans Insulin - metabolism Mice mTOR protein Phosphorylation Protein Binding protein kinase phosphoinositide-dependent kinase 1 Protein Kinases - metabolism Protein Serine-Threonine Kinases - metabolism Recombinant Fusion Proteins - metabolism Repressor Proteins - metabolism Serine - metabolism TOR Serine-Threonine Kinases Tuberous Sclerosis Complex 2 Protein Tumor Suppressor Proteins
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
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-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Division of Molecular Physiology, Faculty of Life Sciences, University of Dundee, Dundee DD15EH, United Kingdom. Phone: 44 1382 344919. Fax: 44 1382 345507. E-mail: c.g.proud@dundee.ac.uk.
ISSN:	0270-7306 1098-5549 1098-5549
DOI:	10.1128/MCB.24.7.2986-2997.2004