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

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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Bibliographic Details
Main Authors: Zhu, Y., Smith, D., Verma, C., Lim, W.G., Tan, B.J., Armstrong, J.S., Zhou, S., Chan, E., Tan, S.-L., Zhu, Y.-Z., Cheung, N.S., Duan, W.
Other Authors: PHARMACY
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
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spelling sg-nus-scholar.10635-1097122023-10-30T07:08:07Z 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, Y. Smith, D. Verma, C. Lim, W.G. Tan, B.J. Armstrong, J.S. Zhou, S. Chan, E. Tan, S.-L. Zhu, Y.-Z. Cheung, N.S. Duan, W. PHARMACY BIOLOGICAL SCIENCES BIOCHEMISTRY 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, Y., Smith, D., Verma, C., Lim, W.G., Tan, B.J., Armstrong, J.S., Zhou, S., Chan, E., Tan, S.-L., Zhu, Y.-Z., Cheung, N.S., Duan, W. (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, Y.
Smith, D.
Verma, C.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
Cheung, N.S.
Duan, W.
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 PHARMACY
author_facet PHARMACY
Zhu, Y.
Smith, D.
Verma, C.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
Cheung, N.S.
Duan, W.
format Article
author Zhu, Y.
Smith, D.
Verma, C.
Lim, W.G.
Tan, B.J.
Armstrong, J.S.
Zhou, S.
Chan, E.
Tan, S.-L.
Zhu, Y.-Z.
Cheung, N.S.
Duan, W.
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-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_ 1781788738468184064

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