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platelet protein P47

Known as: 47KDa platelet protein, platelet 47k protein, pleckstrin 
National Institutes of Health

Related topics

Related topics

5 relations

Broader (2)

Blood ProteinsPhosphoproteins
PLEK gene

Narrower (2)

PLEK protein, humanPlek protein, mouse

Papers overview

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Highly Cited
2008
Highly Cited
2008
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Proteasomal receptors that recognize ubiquitin chains attached to substrates are key mediators of selective protein degradation… 
Highly Cited
2008
Highly Cited
2008
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Targeted protein degradation is largely performed by the ubiquitin–proteasome pathway, in which substrate proteins are marked by… 
Highly Cited
2004
Highly Cited
2004
Association of CBFA2 mutation with decreased platelet PKC-theta and impaired receptor-mediated activation of GPIIb-IIIa and pleckstrin phosphorylation: proteins regulated by CBFA2 play a role in…
The mechanisms by which agonists activate glycoprotein (GP) IIb-IIIa function remain unclear. We have reported data on a patient… 
Highly Cited
2004
Highly Cited
2004
Genetically encoded FRET probe for PKC activity based on pleckstrin.
We developed a probe for investigating protein kinase C (PKC) activity in living cells. The probe is based on a fragment of… 
Highly Cited
1997
Highly Cited
1997
Pleckstrin Associates with Plasma Membranes and Induces the Formation of Membrane Projections: Requirements for Phosphorylation and the NH2-terminal PH Domain
Pleckstrin homology (PH) domains are sequences of ∼100 amino acids that form “modules” that have been proposed to facilitate… 
Highly Cited
1995
Highly Cited
1995
Protein Kinase C Regulates Pleckstrin by Phosphorylation of Sites Adjacent to the N-terminal Pleckstrin Homology Domain (*)
Pleckstrin is a substrate for protein kinase C in activated platelets that contains at its N and C termini two of the pleckstrin… 
Highly Cited
1995
Highly Cited
1995
Phosphatidylinositol(3, 4, 5) -Trisphosphate Stimulates Phosphorylation of Pleckstrin in Human Platelets (*)
We have reported that platelets exposed to thrombin or thrombin receptor-directed ligand activate phospholipase C and rapidly… 
Review
1994
Review
1994
Pleckstrin homology (PH) domains in signal transducton
A diverse array of molecules involved in signal transduction have recently been recognised as containing a new homology domain… 
1992
1992
Suppression by wortmannin of platelet responses to stimuli due to inhibition of pleckstrin phosphorylation.
Studies were made of inhibition by wortmannin, a fungal metabolite, of human platelet responses to various stimuli. Wortmannin at… 
Highly Cited
1989
Highly Cited
1989
Molecular analysis of pleckstrin: The major protein kinase c substrate of platelets
Activation of protein kinase C (PKC) in platelets causes the immediate phosphorylation of pleckstrin, an apparent Mr 40–47,000… 
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