Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (Q28616082)

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English	Protein kinase C is regulated in vivo by three functionally distinct phosphorylations	scientific journal article

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3 February 2017

Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (English)

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3 February 2017

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L. M. Keranen

1

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3 February 2017

E. M. Dutil

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2

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3 February 2017

A. C. Newton

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3

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3 February 2017

language of work or name

English

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publication date

1 December 1995

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3 February 2017

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3 February 2017

5

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3 February 2017

12

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1394–1403

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3 February 2017

Three protein kinase structures define a common motif

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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Crystal structure of cyclin-dependent kinase 2

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Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

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Crystal structure of the tyrosine kinase domain of the human insulin receptor

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

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Threonine-497 is a critical site for permissive activation of protein kinase C alpha

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Autophosphorylation of protein kinase C at three separated regions of its primary sequence

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Determination of in Vivo Phosphorylation Sites in Protein Kinase C

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Protein kinase C association with the retinal cytoskeleton and phosphorylation of vimentin

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Rhodopsin kinase autophosphorylation. Characterization of site-specific mutations

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The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

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Internal protein sequence analysis: enzymatic digestion for less than 10 micrograms of protein bound to polyvinylidene difluoride or nitrocellulose membranes

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Examination of automated polypeptide sequencing using standard phenyl isothiocyanate reagent and subpicomole high-performance liquid chromatographic analysis

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Protein kinase C: structure, function, and regulation

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Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing.

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Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart

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Isolation and characterization of two new drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells

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Identifiers

DOI

10.1016/S0960-9822(95)00277-6

1 reference

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4792953

OpenCitations bibliographic resource ID

4792953

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4792953

Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (Q28616082)

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Protein kinase C is regulated in vivo by three functionally distinct phosphorylations (Q28616082)

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