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GRASP65, a protein involved in the stacking of Golgi cisternae
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scholarly article
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title
GRASP65, a protein involved in the stacking of Golgi cisternae
(English)
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author name string
F A Barr
series ordinal
1
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M Puype
series ordinal
2
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J Vandekerckhove
series ordinal
3
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G Warren
series ordinal
4
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language of work or name
English
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publication date
17 October 1997
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published in
Cell
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volume
91
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page(s)
253-62
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issue
2
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cites work
The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
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Reconstitution of vesiculated Golgi membranes into stacks of cisternae: requirement of NSF in stack formation
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Basic local alignment search tool
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Intercisternal material in the golgi body of Trichomonas
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Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport
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A monoclonal antibody against a 135-K Golgi membrane protein.
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Progress in unraveling pathways of Golgi traffic
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Inter- and intracisternal elements of the Golgi apparatus. A system of membrane-to-membrane cross-links
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Structural analysis and identification of gel-purified proteins, available in the femtomole range, using a novel computer program for peptide sequence assignment, by matrix-assisted laser desorption ionization-reflectron time-of-flight-mass spectrom
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Genetic and biochemical studies of protein N-myristoylation
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Nitric oxide modulates synaptic vesicle docking fusion reactions
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COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system
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Characterization of a cis-Golgi matrix protein, GM130
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The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
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Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
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Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
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Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
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An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
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Modulation of the Golgi apparatus in Saccharomyces cerevisiae sec7 mutants as seen by three-dimensional electron microscopy
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p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p
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Assembly of the ER to Golgi SNARE complex requires Uso1p
1 reference
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A possible docking and fusion particle for synaptic transmission
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Membrane partitioning during cell division
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Identifiers
DOI
10.1016/S0092-8674(00)80407-9
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3156374
OpenCitations bibliographic resource ID
3156374
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3156374
PubMed ID
9346242
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3156374
ResearchGate publication ID
13883159
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