Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 09/2006, Volume 7, Issue 9, pp. 631 - 643
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...
3-DIMENSIONAL STRUCTURE | COMPLEX-FORMATION | NEUROTRANSMITTER RELEASE | CRYSTAL-STRUCTURE | N-TERMINAL DOMAIN | ALPHA-SNAP | PROTEIN-PROTEIN INTERACTIONS | SYNAPTIC VESICLE DOCKING | ENDOPLASMIC-RETICULUM | HOMOTYPIC VACUOLE FUSION | CELL BIOLOGY | Multiprotein Complexes - metabolism | Animals | Synapses - metabolism | SNARE Proteins - genetics | Humans | Cell Growth Processes - physiology | Signal Transduction - physiology | Synapses - genetics | Membrane Fusion - physiology | SNARE Proteins - metabolism
3-DIMENSIONAL STRUCTURE | COMPLEX-FORMATION | NEUROTRANSMITTER RELEASE | CRYSTAL-STRUCTURE | N-TERMINAL DOMAIN | ALPHA-SNAP | PROTEIN-PROTEIN INTERACTIONS | SYNAPTIC VESICLE DOCKING | ENDOPLASMIC-RETICULUM | HOMOTYPIC VACUOLE FUSION | CELL BIOLOGY | Multiprotein Complexes - metabolism | Animals | Synapses - metabolism | SNARE Proteins - genetics | Humans | Cell Growth Processes - physiology | Signal Transduction - physiology | Synapses - genetics | Membrane Fusion - physiology | SNARE Proteins - metabolism
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 07/2008, Volume 15, Issue n7, pp. 658 - 664
Subcellular compartmentalization, cell growth, hormone secretion and neurotransmission require rapid, targeted, and regulated membrane fusion. Fusion entails...
MITOCHONDRIAL FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | VERTEX RING DOMAIN | SECRETORY PATHWAY | CELL BIOLOGY | YEAST SACCHAROMYCES-CEREVISIAE | BIOPHYSICS | SNARE COMPLEX | VESICULAR TRANSPORT | DYNAMIN-RELATED GTPASE | SYNAPTIC VESICLE EXOCYTOSIS | INFLUENZA HEMAGGLUTININ | CELL-FUSION | Cell Fusion | Animals | Synapses - metabolism | Models, Biological | Neurons - cytology | Mitochondria - metabolism | Neurons - metabolism | Membrane Fusion - physiology | Physiological aspects | Membrane fusion | Cellular signal transduction | Research | Protein kinases
MITOCHONDRIAL FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | VERTEX RING DOMAIN | SECRETORY PATHWAY | CELL BIOLOGY | YEAST SACCHAROMYCES-CEREVISIAE | BIOPHYSICS | SNARE COMPLEX | VESICULAR TRANSPORT | DYNAMIN-RELATED GTPASE | SYNAPTIC VESICLE EXOCYTOSIS | INFLUENZA HEMAGGLUTININ | CELL-FUSION | Cell Fusion | Animals | Synapses - metabolism | Models, Biological | Neurons - cytology | Mitochondria - metabolism | Neurons - metabolism | Membrane Fusion - physiology | Physiological aspects | Membrane fusion | Cellular signal transduction | Research | Protein kinases
Journal Article
Annual Review of Cell and Developmental Biology, ISSN 1081-0706, 11/2012, Volume 28, Issue 1, pp. 279 - 308
Neurotransmitter release is governed by proteins that have homo-logs in most types of intracellular membrane fusion, including the Sec1 Munc18 protein Munc18-1...
presynaptic plasticity | synaptic vesicle exocytosis | molecular chaperones | neurotransmitter release | active zone | CRYSTAL-STRUCTURE | DEVELOPMENTAL BIOLOGY | T-SNARE | CLOSED CONFORMATION | CELL BIOLOGY | 3-DIMENSIONAL STRUCTURE | DENSE CORE VESICLES | N-TERMINAL PEPTIDE | SYNTAXIN 1A | SYNAPTIC-VESICLE FUSION | Protein Structure, Tertiary | Molecular Chaperones - metabolism | SNARE Proteins - physiology | Membrane Fusion | Humans | Models, Molecular | Munc18 Proteins - metabolism | Cell Membrane - physiology | Molecular Chaperones - physiology | Animals | Protein Structure, Quaternary | Cell Membrane - metabolism | Munc18 Proteins - physiology | SNARE Proteins - metabolism | Physiological aspects | Neural circuitry | Molecular chaperones | Health aspects | Membrane proteins
presynaptic plasticity | synaptic vesicle exocytosis | molecular chaperones | neurotransmitter release | active zone | CRYSTAL-STRUCTURE | DEVELOPMENTAL BIOLOGY | T-SNARE | CLOSED CONFORMATION | CELL BIOLOGY | 3-DIMENSIONAL STRUCTURE | DENSE CORE VESICLES | N-TERMINAL PEPTIDE | SYNTAXIN 1A | SYNAPTIC-VESICLE FUSION | Protein Structure, Tertiary | Molecular Chaperones - metabolism | SNARE Proteins - physiology | Membrane Fusion | Humans | Models, Molecular | Munc18 Proteins - metabolism | Cell Membrane - physiology | Molecular Chaperones - physiology | Animals | Protein Structure, Quaternary | Cell Membrane - metabolism | Munc18 Proteins - physiology | SNARE Proteins - metabolism | Physiological aspects | Neural circuitry | Molecular chaperones | Health aspects | Membrane proteins
Journal Article