A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production (Q42503419)

1 November 2017

title

A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production (English)

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1 November 2017

3

Alexandra C Newton

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1 November 2017

Daniel R Dries

1

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1 November 2017

Lisa L Gallegos

series ordinal

2

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1 November 2017

language of work or name

English

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publication date

27 October 2006

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Journal of Biological Chemistry

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published in

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volume

282

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issue

2

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1 November 2017

page(s)

826-830

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The extended protein kinase C superfamily

1 November 2017

cites work

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Increased membrane affinity of the C1 domain of protein kinase Cdelta compensates for the lack of involvement of its C2 domain in membrane recruitment

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A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C

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Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling

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21 January 2018

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Role of hydrophobic residues in the C1b domain of protein kinase C delta on ligand and phospholipid interactions

21 January 2018

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How proteins adapt to a membrane-water interface

21 January 2018

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21 January 2018

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Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms

21 January 2018

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Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C).

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.C600268200

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1 November 2017

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