Mechanisms of SNARE proteins in membrane fusion
R Jahn, DC Cafiso, LK Tamm - Nature Reviews Molecular Cell Biology, 2024 - nature.com
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are a
family of small conserved eukaryotic proteins that mediate membrane fusion between …
family of small conserved eukaryotic proteins that mediate membrane fusion between …
Chaperoning SNARE folding and assembly
Y Zhang, FM Hughson - Annual review of biochemistry, 2021 - annualreviews.org
SNARE proteins and Sec1/Munc18 (SM) proteins constitute the core molecular engine that
drives nearly all intracellular membrane fusion and exocytosis. While SNAREs are known to …
drives nearly all intracellular membrane fusion and exocytosis. While SNAREs are known to …
SNAREs—engines for membrane fusion
R Jahn, RH Scheller - Nature reviews Molecular cell biology, 2006 - nature.com
Since the discovery of SNARE proteins in the late 1980s, SNAREs have been recognized as
key components of protein complexes that drive membrane fusion. Despite considerable …
key components of protein complexes that drive membrane fusion. Despite considerable …
[HTML][HTML] Membrane fusion
R Jahn, T Lang, TC Südhof - Cell, 2003 - cell.com
Membrane fusion, one of the most fundamental processes in life, occurs when two separate
lipid membranes merge into a single continuous bilayer. Fusion reactions share common …
lipid membranes merge into a single continuous bilayer. Fusion reactions share common …
Chaperoning SNARE assembly and disassembly
Intracellular membrane fusion is mediated in most cases by membrane-bridging complexes
of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) …
of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) …
Single reconstituted neuronal SNARE complexes zipper in three distinct stages
Soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) proteins
drive membrane fusion by assembling into a four-helix bundle in a zippering process. Here …
drive membrane fusion by assembling into a four-helix bundle in a zippering process. Here …
The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices—guilty as charged?
J Rizo, TC Südhof - Annual review of cell and developmental …, 2012 - annualreviews.org
Neurotransmitter release is governed by proteins that have homo-logs in most types of
intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the …
intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the …
Munc13 mediates the transition from the closed syntaxin–Munc18 complex to the SNARE complex
C Ma, W Li, Y Xu, J Rizo - Nature structural & molecular biology, 2011 - nature.com
During the priming step that leaves synaptic vesicles ready for neurotransmitter release, the
SNARE syntaxin-1 transitions from a closed conformation that binds Munc18-1 tightly to an …
SNARE syntaxin-1 transitions from a closed conformation that binds Munc18-1 tightly to an …
Protein kinetic stability
JM Sanchez-Ruiz - Biophysical chemistry, 2010 - Elsevier
The relevance of protein stability for biological function and molecular evolution is widely
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …
Helical extension of the neuronal SNARE complex into the membrane
Neurotransmission relies on synaptic vesicles fusing with the membrane of nerve cells to
release their neurotransmitter content into the synaptic cleft, a process requiring the …
release their neurotransmitter content into the synaptic cleft, a process requiring the …