Zobrazeno 1 - 7
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pro vyhledávání: '"Daniel T. Giardina"'
Publikováno v:
Biophysical Journal. 121:546a
Publikováno v:
Biophysical Journal. 120:90a
Autor:
Hai T. Tran, Jefferson D. Knight, Kan Chantranuvatana, Matthew D. Coffman, Joseph K. Vasquez, Daniel T. Giardina
Publikováno v:
Biophysical Journal. 110(3)
Synaptotagmin 1 (Syt1), a Ca2+ sensor involved in exocytosis in pre-synaptic neurons, contains a characteristic tandem C2 sequence (C2AB) which inserts into anionic membranes in the presence of Ca2+. Previous studies have shown that the C2AB fragment
Publikováno v:
Biophysical Journal. 110(3)
Biomolecular interactions such as interfacial protein-membrane binding are often the cumulative effect of multivalent attractions. We have shown that the stoichiometry of peripheral protein-membrane interactions can be measured based on single-molecu
Autor:
Marissa DeLima, Jefferson D. Knight, Abena Watson-Siriboe, J. Ryan Osterberg, Daniel T. Giardina, Jack A. Henderson, Hai Lin
Publikováno v:
ResearcherID
Granuphilin, also known as synaptotagmin-like protein 4 (Slp4), is a Rab effector responsible for docking insulin secretory vesicles to the plasma membrane prior to exocytosis. Granuphilin binds vesicular Rab proteins via an N-terminal Slp homology (
Autor:
Daniel T. Giardina, Kan Chantranuvatana, Matthew D. Coffman, Jefferson D. Knight, Joseph K. Vasquez
Publikováno v:
Biochemistry
The synaptotagmin (Syt) family of proteins contains tandem C2 domains, C2A and C2B, which bind membranes in the presence of Ca(2+) to trigger vesicle fusion during exocytosis. Despite recent progress, the role and extent of interdomain interactions b
Publikováno v:
Biophysical Journal. (2):559a-560a
The synaptotagmin (Syt) family of proteins is characterized by the presence of tandem C2 domains, C2A and C2B, which sense Ca2+ to trigger vesicle fusion during exocytosis. The widely studied Syt1 is central to rapid neurotransmitter release, while S