The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B

10.1016/j.cellsig.2005.07.005

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Main Authors:	Zhu Yimin, Smith, D., Verma, C., Lim, W.G., Tan, B.J., Armstrong, J.S., Zhou, S., Chan, E., Tan, S.-L., Zhu Yi Zhun, Cheung Nam Sang, Duan Wei
Other Authors:	BIOLOGICAL SCIENCES
Format:	Article
Published:	2014
Subjects:	Hydrophobic motif PDK-1 Phosphorylation PKCε Signal transduction V5 domain
Online Access:	http://scholarbank.nus.edu.sg/handle/10635/109712
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Institution:	National University of Singapore

id	sg-nus-scholar.10635-109712
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spelling	sg-nus-scholar.10635-1097122024-11-15T15:58:26Z The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B Zhu Yimin Smith, D. Verma, C. Lim, W.G. Tan, B.J. Armstrong, J.S. Zhou, S. Chan, E. Tan, S.-L. Zhu Yi Zhun Cheung Nam Sang Duan Wei BIOLOGICAL SCIENCES BIOCHEMISTRY PHARMACY Hydrophobic motif PDK-1 Phosphorylation PKCε Signal transduction V5 domain 10.1016/j.cellsig.2005.07.005 Cellular Signalling 18 6 807-818 CESIE 2014-11-26T07:49:07Z 2014-11-26T07:49:07Z 2006-06 Article Zhu Yimin, Smith, D., Verma, C., Lim, W.G., Tan, B.J., Armstrong, J.S., Zhou, S., Chan, E., Tan, S.-L., Zhu Yi Zhun, Cheung Nam Sang, Duan Wei (2006-06). The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B. Cellular Signalling 18 (6) : 807-818. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cellsig.2005.07.005 08986568 http://scholarbank.nus.edu.sg/handle/10635/109712 000235728000006 Scopus
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	Hydrophobic motif PDK-1 Phosphorylation PKCε Signal transduction V5 domain
spellingShingle	Hydrophobic motif PDK-1 Phosphorylation PKCε Signal transduction V5 domain Zhu Yimin Smith, D. Verma, C. Lim, W.G. Tan, B.J. Armstrong, J.S. Zhou, S. Chan, E. Tan, S.-L. Zhu Yi Zhun Cheung Nam Sang Duan Wei The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
description	10.1016/j.cellsig.2005.07.005
author2	BIOLOGICAL SCIENCES
author_facet	BIOLOGICAL SCIENCES Zhu Yimin Smith, D. Verma, C. Lim, W.G. Tan, B.J. Armstrong, J.S. Zhou, S. Chan, E. Tan, S.-L. Zhu Yi Zhun Cheung Nam Sang Duan Wei
format	Article
author	Zhu Yimin Smith, D. Verma, C. Lim, W.G. Tan, B.J. Armstrong, J.S. Zhou, S. Chan, E. Tan, S.-L. Zhu Yi Zhun Cheung Nam Sang Duan Wei
author_sort	Zhu Yimin
title	The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
title_short	The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
title_full	The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
title_fullStr	The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
title_full_unstemmed	The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B
title_sort	very c-terminus of protein kinase cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 b
publishDate	2014
url	http://scholarbank.nus.edu.sg/handle/10635/109712
_version_	1821200310854483968

The very C-terminus of protein kinase Cε is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1 B

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