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-1B

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-1B

Cellular Signalling

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Main Authors: Zhu, Y., Lim, W.G., Tan, B.J., Armstrong, J.S., Cheung, N.S., Duan, W., Smith, D., Verma, C., Zhou, S., Chan, E., Tan, S.-L., Zhu, Y.-Z.
Other Authors: BIOCHEMISTRY
Format: Article
Published: 2011
Subjects:
Hydrophobic motif
PDK-1
Phosphorylation
PKCε
Signal transduction
V5 domain
Online Access:http://scholarbank.nus.edu.sg/handle/10635/28943
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Institution: National University of Singapore
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spelling sg-nus-scholar.10635-289432023-08-21T22:49:01Z 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-1B Zhu, Y. Lim, W.G. Tan, B.J. Armstrong, J.S. Cheung, N.S. Duan, W. Smith, D. Verma, C. Zhou, S. Chan, E. Tan, S.-L. Zhu, Y.-Z. BIOCHEMISTRY PHARMACY PHARMACOLOGY BIOLOGICAL SCIENCES Hydrophobic motif PDK-1 Phosphorylation PKCε Signal transduction V5 domain Cellular Signalling 18 6 807-818 CESIE 2011-11-29T06:11:18Z 2011-11-29T06:11:18Z 2006 Article Zhu, Y., Lim, W.G., Tan, B.J., Armstrong, J.S., Cheung, N.S., Duan, W., Smith, D., Verma, C., Zhou, S., Chan, E., Tan, S.-L., Zhu, Y.-Z. (2006). 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-1B. Cellular Signalling 18 (6) : 807-818. ScholarBank@NUS Repository. 08986568 http://scholarbank.nus.edu.sg/handle/10635/28943 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, Y.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Cheung, N.S.
Duan, W.
Smith, D.
Verma, C.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
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-1B
description Cellular Signalling
author2 BIOCHEMISTRY
author_facet BIOCHEMISTRY
Zhu, Y.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Cheung, N.S.
Duan, W.
Smith, D.
Verma, C.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
format Article
author Zhu, Y.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Cheung, N.S.
Duan, W.
Smith, D.
Verma, C.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
author_sort Zhu, Y.
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-1B
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-1B
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-1B
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-1B
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-1B
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-1b
publishDate 2011
url http://scholarbank.nus.edu.sg/handle/10635/28943
_version_ 1775625566008901632

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