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Imma Fernandez
Researcher at University of Texas Southwestern Medical Center
Publications - 11
Citations - 2130
Imma Fernandez is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Synaptotagmin I & Syntaxin. The author has an hindex of 10, co-authored 11 publications receiving 2032 citations. Previous affiliations of Imma Fernandez include University of Barcelona.
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Journal ArticleDOI
A conformational switch in syntaxin during exocytosis: role of munc18
Irina Dulubova,Shuzo Sugita,Sandra Hill,Masahiro Hosaka,Imma Fernandez,Thomas C. Südhof,Josep Rizo +6 more
TL;DR: The results indicate that syntaxin binds to munc18‐1 in a closed conformation and suggest that this conformation represents an essential intermediate in exocytosis, and suggest a model whereby syntaxin undergoes a large conformational switch that mediates the transition between the syntaxin–munc 18‐1 complex and the core complex.
Journal ArticleDOI
Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine.
Imma Fernandez,Demet Araç,Josep Ubach,Stefan H. Gerber,Ok Ho Shin,Yan Gao,Richard G.W. Anderson,Thomas C. Südhof,Josep Rizo +8 more
TL;DR: A novel view of synaptotagmin function is suggested whereby the two C2-domains cooperate in a common activity, Ca2+-dependent phospholipid binding, to trigger neurotransmitter release.
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Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.
TL;DR: NMR spectroscopy is used to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure, indicating a specific role in exocytosis.
Journal ArticleDOI
Synaptotagmin–Syntaxin Interaction: The C2 Domain as a Ca2+-Dependent Electrostatic Switch
TL;DR: A model is proposed whereby synaptotagmin acts as an electrostatic switch in Ca2+-triggered synaptic vesicle exocytosis, promoting a structural rearrangement in the fusion machinery that is effected by its interaction with syntaxin.
Journal ArticleDOI
Solution Structures of the Ca2+-free and Ca2+-bound C2A Domain of Synaptotagmin I: Does Ca2+ Induce a Conformational Change?†
TL;DR: The results support a model whereby the C2A domain functions as an electrostatic switch in neurotransmitter release, and the similarity between the structures of the synaptotagmin I C1A domain and the PLC-delta1 C2 domain suggests that the latter binds four Ca2+ ions and acts by a similar mechanism.