Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Gian Carlo Ochoa"'
Autor:
Mark A. McNiven, Vladimir I. Slepnev, Pietro De Camilli, Warren T. Kim, Gian-Carlo Ochoa, Kohji Takei, Lynn Neff, Roland Baron, Laurie Daniell, Niels Ringstad, Hong Cao
Publikováno v:
The Journal of Cell Biology
Cell transformation by Rous sarcoma virus results in a dramatic change of adhesion structures with the substratum. Adhesion plaques are replaced by dot-like attachment sites called podosomes. Podosomes are also found constitutively in motile nontrans
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::859b99d3c60d7d007d1858a9c6427146
https://doi.org/10.1083/jcb.150.2.377
https://doi.org/10.1083/jcb.150.2.377
Publikováno v:
Science. 281:821-824
Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc6cc23aa33c03cad8405bf09b440c8
https://doi.org/10.1126/science.281.5378.821
https://doi.org/10.1126/science.281.5378.821
Autor:
Melissa Marcucci, Eunkyung Lee, Gian Carlo Ochoa, Pietro De Camilli, Laurie Daniell, Ora A. Weisz, Khashayar Farsad, Markus R. Wenk, Marc Pypaert
Publikováno v:
Science (New York, N.Y.). 297(5584)
In striated muscle, the plasma membrane forms tubular invaginations (transverse tubules or T-tubules) that function in depolarization-contraction coupling. Caveolin-3 and amphiphysin were implicated in their biogenesis. Amphiphysin isoforms have a pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd60742397dbec3c072696e128fc4d13
https://pubmed.ncbi.nlm.nih.gov/12183633
https://pubmed.ncbi.nlm.nih.gov/12183633
Autor:
Elena B. Porro, Pietro De Camilli, Vladimir I. Slepnev, Gian-Carlo Ochoa, Scott R. Floyd, Li-Huei Tsai
Publikováno v:
The Journal of biological chemistry. 276(11)
Amphiphysin 1 is a phosphoprotein expressed at high levels in neurons, where it participates in synaptic vesicle endocytosis and neurite outgrowth. It is a substrate for cyclin-dependent kinase (cdk) 5, a member of the cyclin-dependent protein kinase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b1679b67063688a36f458bd3cd78284
https://pubmed.ncbi.nlm.nih.gov/11113134
https://pubmed.ncbi.nlm.nih.gov/11113134
Autor:
Pietro De Camilli, Gian Carlo Ochoa, O Mundigl, Vladimir I. Slepnev, Alexander V. Kabanov, Carol David
Publikováno v:
Scopus-Elsevier
Amphiphysin I is an SH3 domain-containing neuronal protein, enriched in axon terminals, which was reported to act as a physiological binding partner for dynamin I in synaptic vesicle endocytosis. Rvs167 and Rvs161, the yeast homologs of amphiphysin I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62395fd7a76c28a49c6ea37a6c07d6b6
https://europepmc.org/articles/PMC6793426/
https://europepmc.org/articles/PMC6793426/
Autor:
Gian Carlo Ochoa, Vladimir I. Slepnev, Laurie Daniell, Pietro De Camilli, Volker Haucke, Khashayar Farsad
Publikováno v:
Neuropharmacology. 46:297
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91f22d6578d891d76fe8a41ada21da16
https://doi.org/10.1016/j.neuropharm.2003.10.005
https://doi.org/10.1016/j.neuropharm.2003.10.005