M
Michael Brunner
Researcher at Heidelberg University
Publications - 138
Citations - 13264
Michael Brunner is an academic researcher from Heidelberg University. The author has contributed to research in topics: Circadian clock & Circadian rhythm. The author has an hindex of 53, co-authored 116 publications receiving 12441 citations. Previous affiliations of Michael Brunner include Memorial Sloan Kettering Cancer Center & Princeton University.
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Journal ArticleDOI
SNAP receptors implicated in vesicle targeting and fusion
Thomas H. Söllner,Sidney W. Whiteheart,Michael Brunner,Hediye Erdjument-Bromage,Scott J. Geromanos,Paul Tempst,James E. Rothman +6 more
TL;DR: The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicles or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesICLE-to-target specificity.
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ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
Tito Serafini,Tito Serafini,Lelio Orci,Mylène Amherdt,Michael Brunner,Richard A. Kahn,James E. Rothmant +6 more
TL;DR: In this paper, the ADP-ribosylation factor (ARF) was found to be highly concentrated in non-clathrin-coated transport vesicles and are coat proteins.
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Genome-wide and phase-specific DNA-binding rhythms of BMAL1 control circadian output functions in mouse liver.
Guillaume Rey,François Cesbron,Jacques Rougemont,Jacques Rougemont,Hans Reinke,Hans Reinke,Hans Reinke,Michael Brunner,Felix Naef,Felix Naef +9 more
TL;DR: Temporal mapping during a circadian day of binding sites for the BMAL1 transcription factor in mouse liver reveals genome-wide daily rhythms in DNA binding and uncovers output functions that are controlled by the circadian oscillator.
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N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion.
TL;DR: It is demonstrated that the ability of the D1 domain to hydrolyze ATP is required for NSF activity and, therefore, required for membrane fusion.
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Mitochondrial Hsp70/MIM44 complex facilitates protein import
Hans-Christoph Schneider,Jutta Berthold,Matthias F. Bauer,Klaus Dietmeier,Klaus Dietmeier,Bernard Guiard,Bernard Guiard,Michael Brunner,Walter Neupert +8 more
TL;DR: The MIM44/Hsp70 complex appears to act as a molecular ratchet which is energetically driven by the hydrolysis of ATP and facilitates stepwise vectorial translocation of proteins across the mitochondrial membranes.