Irreversible inactivation of protein kinase C by glutathione (Q48445043)

11 February 2018

title

Irreversible inactivation of protein kinase C by glutathione (English)

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11 February 2018

author name string

Ward NE

1

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11 February 2018

Pierce DS

2

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11 February 2018

Chung SE

3

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Gravitt KR

4

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11 February 2018

O'Brian CA

5

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11 February 2018

language of work or name

English

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publication date

1 May 1998

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11 February 2018

Journal of Biological Chemistry

published in

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volume

273

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11 February 2018

issue

20

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11 February 2018

page(s)

12558-12566

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11 February 2018

Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C

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Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Calpha.

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Ceramide inactivates cellular protein kinase Calpha

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The common structure and activities of four subspecies of rat brain protein kinase C family

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Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester

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Irreversible inactivation of protein kinase C by a peptide-substrate analog.

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Covalent modification of protein kinase C isozymes by the inactivating peptide substrate analog N-biotinyl-Arg-Arg-Arg-Cys-Leu-Arg-Arg-Leu. Evidence that the biotinylated peptide is an active-site affinity label

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Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation

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The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation

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Regulation of HIV-1 protease activity through cysteine modification.

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Characterization of a Ca2( )- and phospholipid-dependent ATPase reaction catalyzed by rat brain protein kinase C.

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Inhibition of protein kinase C by melittin: antagonism of binding interactions between melittin and the catalytic domain by active-site binding of MgATP.

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Overproduction of protein kinase C causes disordered growth control in rat fibroblasts

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Evidence that protein kinase C-alpha activation is a critical event in phorbol ester-induced multiple drug resistance in human colon cancer cells

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Protein kinase CK2: biphasic kinetics with peptide substrates.

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Sequence of human protein kinase C alpha

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Ca2 Differentially Regulates Conventional Protein Kinase Cs' Membrane Interaction and Activation

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Tumor necrosis factor increases hepatocellular glutathione by transcriptional regulation of the heavy subunit chain of gamma-glutamylcysteine synthetase.

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Retinoids inhibit the oxidative modification of protein kinase C induced by oxidant tumor promoters

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12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Calpha correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer

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Specifically targeted modification of human aldose reductase by physiological disulfides

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Inhibition of the neutral magnesium-dependent sphingomyelinase by glutathione

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N-Acetylcysteine-promoted Survival of PC12 Cells Is Glutathione-independent but Transcription-dependent

21 January 2018

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Inhibition of protein kinase C by N-myristoylated peptide substrate analogs

21 January 2018

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Partial reversal of multidrug resistance in human breast cancer cells by an N-myristoylated protein kinase C-alpha pseudosubstrate peptide

21 January 2018

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Protein kinase C contains a pseudosubstrate prototope in its regulatory domain

21 January 2018

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S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulfide

21 January 2018

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Substrate-induced translocation of PKC-alpha to the membrane

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Thiol Compounds Interact with Nitric Oxide in Regulating Heme Oxygenase-1 Induction in Endothelial Cells

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Modifications of cellular thiols during growth and squamous differentiation of cultured human bronchial epithelial cells

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hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.20.12558

1 reference

11 February 2018

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11 February 2018