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Phospholipase C

Known as: phosphatidylcholine cholinephosphohydrolase, alpha-toxin, PLC 
An enzyme found in the alpha-toxin of Clostridium welchii and other strains of clostridia and bacilli. It hydrolyzes glycerophosphatidates with the… Expand
National Institutes of Health

Papers overview

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Review
2008
Review
2008
Phosphoinositide-specific phospholipase C is an effector molecule in the signal transduction process. It generates two second… Expand
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Review
2001
Review
2001
  • S. Rhee
  • Annual review of biochemistry
  • 2001
  • Corpus ID: 21158219
Eleven distinct isoforms of phosphoinositide-specific phospholipase C (PLC), which are grouped into four subfamilies (beta, gamma… Expand
Review
2000
Review
2000
Phosphoinositide-specific phospholipase C (PLC) subtypes beta, gamma, and delta comprise a related group of multidomain… Expand
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Highly Cited
1998
Highly Cited
1998
The linker molecule LAT is a critical substrate of the tyrosine kinases activated upon TCR engagement. Phosphorylated LAT binds… Expand
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Highly Cited
1997
Highly Cited
1997
A variety of extracellular signals are transduced across the cell membrane by the enzyme phosphoinositide-specific phospholipase… Expand
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Highly Cited
1995
Highly Cited
1995
The X-ray crystal structure of the high affinity complex between the pleckstrin homology (PH) domain from rat phospholipase C… Expand
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Review
1993
Review
1993
  • R. Titball
  • Microbiological reviews
  • 1993
  • Corpus ID: 28286895
A variety of pathogenic bacteria produce phospholipases C, and since the discovery in 1944 that a bacterial toxin (Clostridium… Expand
Highly Cited
1992
Highly Cited
1992
In this paper, we describe a phospholipid transmission pathway mediating tumor necrosis factor (TNF) activation of the nuclear… Expand
Highly Cited
1992
Highly Cited
1992
HYDROLYSIS by phospholipase C (PLC) of phosphatidylinositol 4,5-bisphosphate is a key mechanism by which many extracellular… Expand
Highly Cited
1988
Highly Cited
1988
Severe norpA mutations in Drosophila eliminate the photoreceptor potential and render the fly completely blind. Recent… Expand