G
Gina E. Sosinsky
Researcher at University of California, San Diego
Publications - 80
Citations - 6173
Gina E. Sosinsky is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Connexin & Gap junction. The author has an hindex of 37, co-authored 80 publications receiving 5792 citations. Previous affiliations of Gina E. Sosinsky include University of California, Santa Barbara & University of California, Berkeley.
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Journal ArticleDOI
Multicolor and Electron Microscopic Imaging of Connexin Trafficking
Guido M. Gaietta,Thomas J. Deerinck,Stephen R. Adams,James C. Bouwer,Oded Tour,Dale W. Laird,Gina E. Sosinsky,Roger Y. Tsien,Mark H. Ellisman +8 more
TL;DR: This approach was used to show that newly synthesized connexin43 was transported predominantly in 100- to 150-nanometer vesicles to the plasma membrane and incorporated at the periphery of existing gap junctions, whereas older connexins were removed from the center of the plaques into pleiomorphic vesicle of widely varying sizes.
Journal ArticleDOI
Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy
Jeffrey D. Martell,Thomas J. Deerinck,Yasemin Sancak,Yasemin Sancak,Thomas L. Poulos,Vamsi K. Mootha,Vamsi K. Mootha,Gina E. Sosinsky,Mark H. Ellisman,Alice Y. Ting +9 more
TL;DR: APEX as discussed by the authors is a monomeric 28-kDa peroxidase that withstands strong EM fixation to give excellent ultrastructural preservation and can be used for high-resolution EM imaging of a variety of mammalian organelles and specific proteins using a simple and robust labeling procedure.
Journal ArticleDOI
Isolation, Characterization and Structure of Bacterial Flagellar Motors Containing the Switch Complex
TL;DR: Evidence is provided that the thickened M ring contains FliG and that the C ring complex may contain FliM and FliN, and the large diameter of the CRing complex may permit interaction with the M ring and with the circlet of studs thought to be the MotA/MotB complex.
Journal ArticleDOI
Pannexin channels are not gap junction hemichannels
Gina E. Sosinsky,Daniela Boassa,Rolf Dermietzel,Heather S. Duffy,Dale W. Laird,Brian A. MacVicar,Christian C. Naus,Silvia Penuela,Eliana Scemes,David C. Spray,Roger J. Thompson,Hong-Bo Zhao,Gerhard Dahl +12 more
TL;DR: It is presented the case that unlike the connexin gap junction inter cellular channels, so far, pannexin oligomers have repeatedly been shown to be channels that are functional in single membranes, but not as intercellular channels in appositional membranes, hence, they should be referred to as channels and not hemichannels.
Journal ArticleDOI
Pannexin1 Channels Contain a Glycosylation Site That Targets the Hexamer to the Plasma Membrane
TL;DR: It is shown for the first time that Pannexin1 is glycosylated at Asn-254 and that this residue is important for plasma membrane targeting, and proposed that N-glycosylation of Pan Nexin1 could be a significant mechanism for regulating the trafficking of these membrane proteins to the cell surface in different tissues.