The role of Rab3A in neurotransmitter release

[1]  S. Siegelbaum,et al.  Postsynaptic induction and presynaptic expression of hippocampal long-term depression. , 1994, Science.

[2]  T. Südhof,et al.  Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis. , 1994, The Journal of biological chemistry.

[3]  G. Augustine,et al.  Synaptic vesicle exocytosis: Molecules and models , 1994, Cell.

[4]  R. Malinow,et al.  The probability of transmitter release at a mammalian central synapse , 1993, Nature.

[5]  Thomas C. Südhof,et al.  Short-term synaptic plasticity is altered in mice lacking synapsin I , 1993, Cell.

[6]  M. Zerial,et al.  Rab proteins and the road maps for intracellular transport , 1993, Neuron.

[7]  P. De Camilli,et al.  Relative properties and localizations of synaptic vesicle protein isoforms: the case of the synaptophysins , 1993, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[8]  Christian Rosenmund,et al.  Nonuniform probability of glutamate release at a hippocampal synapse. , 1993, Science.

[9]  T. Südhof,et al.  Structure of the murine rab3A gene: correlation of genomic organization with antibody epitopes. , 1993, The Biochemical journal.

[10]  Paul Tempst,et al.  SNAP receptors implicated in vesicle targeting and fusion , 1993, Nature.

[11]  P. Novick,et al.  A mammalian guanine-nucleotide-releasing protein enhances function of yeast secretory protein Sec4 , 1993, Nature.

[12]  T. Bliss,et al.  A synaptic model of memory: long-term potentiation in the hippocampus , 1993, Nature.

[13]  E. Kandel,et al.  Learning to modulate transmitter release: themes and variations in synaptic plasticity. , 1993, Annual review of neuroscience.

[14]  K. Kaibuchi,et al.  A possible target protein for smg-25A/rab3A small GTP-binding protein. , 1992, The Journal of biological chemistry.

[15]  H. Lodish,et al.  Cloning of a Rab3 isotype predominantly expressed in adipocytes. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[16]  P. De Camilli,et al.  Ca2+ stores in Purkinje neurons: endoplasmic reticulum subcompartments demonstrated by the heterogeneous distribution of the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin , 1992, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[17]  P. De Camilli,et al.  Association of Rab3A with synaptic vesicles at late stages of the secretory pathway , 1991, The Journal of cell biology.

[18]  Thomas C. Südhof,et al.  Proteins of synaptic vesicles involved in exocytosis and membrane recycling , 1991, Neuron.

[19]  Allan Bradley,et al.  Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice , 1991, Cell.

[20]  T. Südhof,et al.  A small GTP-binding protein dissociates from synaptic vesicles during exocytosis , 1991, Nature.

[21]  A. Hall,et al.  The cellular functions of small GTP-binding proteins. , 1990, Science.

[22]  T. Südhof,et al.  rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[23]  Arnold R. Kriegstein,et al.  Whole cell recording from neurons in slices of reptilian and mammalian cerebral cortex , 1989, Journal of Neuroscience Methods.

[24]  T. Südhof,et al.  Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor , 1989, Nature.

[25]  T. Südhof,et al.  Transmembrane topography and evolutionary conservation of synaptophysin. , 1989, The Journal of biological chemistry.

[26]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[27]  P. Greengard,et al.  Synapsin I (protein I), a nerve terminal-specific phosphoprotein. I. Its general distribution in synapses of the central and peripheral nervous system demonstrated by immunofluorescence in frozen and plastic sections , 1983, The Journal of cell biology.

[28]  V. Tennyson The Fine Structure of the Nervous System. , 1970 .