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Nils Brose

Researcher at Max Planck Society

Publications -  250
Citations -  27989

Nils Brose is an academic researcher from Max Planck Society. The author has contributed to research in topics: Synaptic vesicle & Neurotransmission. The author has an hindex of 84, co-authored 230 publications receiving 24975 citations. Previous affiliations of Nils Brose include Howard Hughes Medical Institute & University of Göttingen.

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Synaptotagmin: a calcium sensor on the synaptic vesicle surface

TL;DR: It is reported here that synaptotagmin, a highly conserved synaptic vesicle protein, binds calcium at physiological concentrations in a complex with negatively charged phospholipids, and this binding is specific for calcium and involves the cytoplasmic domain of synaptoagmin.
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Synaptotagmin I functions as a calcium regulator of release probability

TL;DR: A point mutation in synaptotagmin I is studied that causes a twofold decrease in overall Ca2+ affinity without inducing structural or conformational changes and participates in triggering neurotransmitter release at the synapse.
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Neuroligins Determine Synapse Maturation and Function

TL;DR: It is shown that deletion mutant mice lacking neuroligin expression die shortly after birth due to respiratory failure, and that neuroligins are required for proper synapse maturation and brain function, but not for the initial formation of synaptic contacts.
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Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles

TL;DR: It is shown that glutamatergic hippocampal neurons from mice lacking Munc13-1 form ultrastructurally normal synapses whose synaptic-vesicle cycle is arrested at the maturation step, demonstrating the existence of multiple and transmitter-specific synaptic vesicle maturation processes in synapses.
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Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses

TL;DR: It is shown that neuroligin 1 is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion.