Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain (Q24310550)

GOA release 2020-03-11

Pleckstrin

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phosphatidylinositol metabolic process

GOA release 2020-03-11

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Journal of Biological Chemistry

GOA release 2020-03-11

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C S Abrams

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W Zhao

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E Belmonte

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L F Brass

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language of work or name

English

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publication date

6 October 1995

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published in

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volume

270

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issue

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page(s)

23317-21

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cites work

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Pleckstrin domain homology

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A putative modular domain present in diverse signaling proteins

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Solution structure of a pleckstrin-homology domain

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Structure of the pleckstrin homology domain from beta-spectrin.

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Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin

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Crystal structure of the pleckstrin homology domain from dynamin

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Three-dimensional solution structure of the pleckstrin homology domain from dynamin

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Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy

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The PH domain: a common piece in the structural patchwork of signalling proteins

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Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate.

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Pleckstrin inhibits phosphoinositide hydrolysis initiated by G-protein-coupled and growth factor receptors. A role for pleckstrin's PH domains

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o-Iodosobenzoic oxidation and cleavage of myosin subfragment 1

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Protein kinase C contains a pseudosubstrate prototope in its regulatory domain

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