Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
By J. McNew, F. Parlati, R. Fukuda, Robert J. Johnston Jr., K. Paz, F. Paumet, T. Söllner, J. Rothman. Nature, 2000
704 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/1150b0a88449fbc9cf343d61c01c9cfb9edebe81
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Citations in the corpus
- Secretory granule exocytosis. (2003, background): “controlled, at least in part, by distinct SNARE combinations, in keeping with observations on reconstituted liposome fusion (483, 583).”
- Bi-directional protein transport between the ER and Golgi. (2004, background): “In vitro fusion experiments with SNAREs reconstituted into synthetic liposomes have been instrumental in defining the specific combinations of SNAREs that mediate membrane fusion (Fukuda et al. 2000, McNew et al. 2000, Parlati et al. 2000).”
- SNAREs and traffic. (2005, background): “Most Qc SNAREs act as a light chain of t-SNARE, but some Qc SNAREs (such as GS15, Bet1 and likely Slt1) may function as v-SNAREs [3,5,34,35].”
- Rab proteins as membrane organizers (2001, background): “Rab5 • Ligand sequestration at plasma Rabaptin-5 • Stabilizes Rabex-5 Rab5–GTP Rabex-5 • Nucleotide exchange factor membrane Rabaptin-5β recruitment Rab4–GTP Rabphilin-3 • CCV–EE and EE–EE fusion EEA1 • Tethering, core fusion Rab5–GTP Syntaxin13 • t-SNAREs essential for • Endosome motility component”