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Sandra Winter

Researcher at Humboldt University of Berlin

Publications -  8
Citations -  696

Sandra Winter is an academic researcher from Humboldt University of Berlin. The author has contributed to research in topics: G protein & Synaptic vesicle. The author has an hindex of 8, co-authored 8 publications receiving 653 citations. Previous affiliations of Sandra Winter include Charité.

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Journal ArticleDOI

Serotonylation of small GTPases is a signal transduction pathway that triggers platelet α-granule release

TL;DR: It is shown that mice selectively deficient in peripheral TPH and serotonin exhibit impaired hemostasis, resulting in a reduced risk of thrombosis and thromboembolism, although the ultrastructure of the platelets is not affected.
Journal ArticleDOI

The first luminal domain of vesicular monoamine transporters mediates G-protein-dependent regulation of transmitter uptake.

TL;DR: Vesicular content is involved in the activation of vesicle associated G-proteins via a structure sensing the luminal monoamine content through the first luminal loop of VMATs, which may represent a G-protein-coupled receptor that adapts vesicular filling.
Journal ArticleDOI

The Vesicular Monoamine Content Regulates VMAT2 Activity through Gαq in Mouse Platelets EVIDENCE FOR AUTOREGULATION OF VESICULAR TRANSMITTER UPTAKE

TL;DR: It is concluded that in platelets the vesicle itself regulates transmitter transporter activity via its content and vesicles-associated Gαq, mediating the down-regulation of VMAT2 activity.
Journal ArticleDOI

G alpha(o2) regulates vesicular glutamate transporter activity by changing its chloride dependence

TL;DR: It is shown that VGLUTs are exclusively regulated by G αo2, and Gαo2 acts on a putative regulatory chloride binding domain that appears to modulate transport activity of vesicular glutamate transporters.
Book ChapterDOI

Regulation of vesicular neurotreansmitter transporters

TL;DR: It appears that the vesicular content activates the G protein, suggesting a signal transduction form the luminal site which might be mediated by a vESicular G-protein coupled receptor or, as an alternative, possibly by the transporter itself.