The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Membrane fusion
Open accessAbstract
Subcellular compartmentalization, cell growth, hormone secretion and neurotransmission require rapid, targeted, and regulated membrane fusion. Fusion entails extensive lipid rearrangements by two apposed (docked) membrane vesicles, joining their membrane proteins and lipids and mixing their luminal contents without lysis. Fusion of membranes in the secretory pathway involves Rab GTPases; their bound 'effector' proteins, which mediate downstream steps; SNARE proteins, which can 'snare' each other, in cis (bound to one membrane) or in trans (anchored to apposed membranes); and SNARE-associated proteins (SM proteins; NSF or Sec18p; SNAP or Sec17p; and others) cooperating with specific lipids to catalyze fusion. In contrast, mitochondrial and cell-cell fusion events are regulated by and use distinct catalysts.
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Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,547
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417
Rabs and their effectors: achieving specificity in membrane traffic
Grosshans, B. L., Ortiz, D., & Novick, P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601617103 · Cited by 1,005
The Rab5 effector EEA1 is a core component of endosome docking
Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854
McBride, H. M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., & Zerial, M. (1999) · Cell · doi:10.1016/s0092-8674(00)81966-2 · Cited by 520
Wurmser, A. E., Sato, T. K., & Emr, S. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.3.551 · Cited by 425
Cited by
Chernomordik, L. V., & Kozlov, M. M. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1455 · Cited by 1,037
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586
Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis
Zhou, Q., Lai, Y., Bacaj, T., Zhao, M., Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Brewster, A. S., Sauter, N. K., Cohen, A. E., et al. (2015) · Nature · doi:10.1038/nature14975 · Cited by 348
Lőrincz, P., & Juhász, G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.028 · Cited by 328
Wang, Z., Miao, G., Xue, X., Guo, X., Yuan, C., Wang, Z., Zhang, G., Chen, Y., Feng, D., Hu, J., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.021 · Cited by 321
Metadata
- Authors
- Wickner, W., & Schekman, R.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2008-07
- Volume
- 15
- Issue
- 7
- Pages
- 658-664
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W4211197456
- Cited by
- 435
- References
- 6
- FWCI
- 13.14
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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