Agency
National Institute of Health (NIH)
Institute
National Institute of Neurological Disorders and Stroke (NINDS)
Type
Research Project (R01)
Project #
5R01NS009878-26
Application #
2261866
Study Section
Neurological Sciences Subcommittee 1 (NLS)
Project Start
1978-09-01
Project End
1999-08-31
Budget Start
1996-09-01
Budget End
1997-08-31
Support Year
26
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of California San Francisco
Department
Internal Medicine/Medicine
Type
Schools of Medicine
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143
Jarousse, Nadine; Wilson, Joshua D; Arac, Demet et al. (2003) Endocytosis of synaptotagmin 1 is mediated by a novel, tryptophan-containing motif. Traffic 4:468-78
Dasgupta, Shoumita; Kelly, Regis B (2003) Internalization signals in synaptotagmin VII utilizing two independent pathways are masked by intramolecular inhibitions. J Cell Sci 116:1327-37
Blumstein, J; Faundez, V; Nakatsu, F et al. (2001) The neuronal form of adaptor protein-3 is required for synaptic vesicle formation from endosomes. J Neurosci 21:8034-42
de Wit, H; Lichtenstein, Y; Kelly, R B et al. (2001) Rab4 regulates formation of synaptic-like microvesicles from early endosomes in PC12 cells. Mol Biol Cell 12:3703-15
Jarousse, N; Kelly, R B (2001) The AP2 binding site of synaptotagmin 1 is not an internalization signal but a regulator of endocytosis. J Cell Biol 154:857-66
Jarousse, N; Kelly, R B (2001) Endocytotic mechanisms in synapses. Curr Opin Cell Biol 13:461-9
Qualmann, B; Kelly, R B (2000) Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J Cell Biol 148:1047-62
Faundez, V V; Kelly, R B (2000) The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform. Mol Biol Cell 11:2591-604
Qualmann, B; Kessels, M M; Kelly, R B (2000) Molecular links between endocytosis and the actin cytoskeleton. J Cell Biol 150:F111-6
Marullo, S; Faundez, V; Kelly, R B (1999) Beta 2-adrenergic receptor endocytic pathway is controlled by a saturable mechanism distinct from that of transferrin receptor. Receptors Channels 6:255-69

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