Membrane fusion.
By R. Jahn, Helmut Grubmüller. Current Opinion in Cell Biology, 2002
1,515 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/2bffcb7fc600a9c52bf4a9aa48f9960340715acb
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Citations in the corpus
- SNAREs and traffic. (2005, background): “The neuronal SNARE complex consisting of Syn1, SNAP-25, and VAMP2 is the best studied and has served as a paradigm for other vesicular transport events [2,7,18,19].”
- Short-term presynaptic plasticity. (2012, background): “The magnitude of synaptic strength is steeply dependent upon calcium levels, because calcium binds to multiple low-affinity sites on synaptotagmin to trigger vesicle fusion (Jahn et al. 2003; Schneggenburger and Neher 2005; Sudhof and Rothman 2009).”
- Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, positive): “The now burgeoning fi eld of oxidants in biological systems rose from obscurity with the cardinal discovery that the common red cell enzyme erythrocuprein was both ubiquitous and protective , functioning as a superoxide dismutase (SOD; McCord and Fridovich, 1969).”
- Biological and synthetic membranes: What can be learned from a coarse-grained description? (2006, background): “There is evidence that this second step is dictated by the amphiphilic nature of the bilayer constituents [26,372,373], for fusion occurs in very different systems ranging from tiny, highly curved, synaptic vesicles to whole cells.”
- Molecular machines governing exocytosis of synaptic vesicles (2012, background): “Priming II involves arrest after positioning of the vesicle with the aid of active zone components and (possibly) contact of synaptotagmin with PI(4,5)P2 in the plasma membrane, but no contact between the SNAREs.”
- Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation (2004, background): “This process is tightly controlled by specific proteins that interact with each other and with lipids, as well as with other proteins, to form a complex at the fusion site (reviewed in Jahn et al, 2003).”