Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation.

No abstract is available for this paper.

• Publication year

  1997

• Venue

  Biochemical and Biophysical Research Communications - BBRC

• Publication date

  1997-07-09

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1006/BBRC.1997.6921PMID 9223444
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• And still they are moving… Dynamic properties of caveolae

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• Discovery of a Novel, Potent, and Src Family-selective Tyrosine Kinase Inhibitor

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• Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling.

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• Phosphorylation of endothelial nitric oxide synthase in response to fluid shear stress.

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  1995cited by this paper
• Oligomeric structure of caveolin: implications for caveolae membrane organization.

  1995cited by this paper
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• The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide(*)

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• Guilty by insolubility--does a protein's detergent insolubility reflect a caveolar location?

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