Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Weiwei Kuo"'
Autor:
Upneet Kaur, Kyle C. Kihn, Haiping Ke, Weiwei Kuo, Lila M. Gierasch, Daniel N. Hebert, Patrick L. Wintrode, Daniel Deredge, Anne Gershenson
Many multi-domain proteins including the serpin family of serine protease inhibitors contain non-sequential domains composed of regions that are far apart in sequence. Because proteins are translated vectorially from N-to C-terminus, such domains pos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2de98a94a1a2dfc8cfa68e0d48ae20c
https://doi.org/10.1101/2023.04.24.537978
https://doi.org/10.1101/2023.04.24.537978
Autor:
Adam Lanzarotta, Sara Kern, JaCinta Batson, Brian Boyd, Martin M. Kimani, Weiwei Kuo, Donna LaGarde, Mark Loh, Laurenee L. Adeoshun, Lisa Lorenz, Rebeca Melendez, Flavia Morales-Garcia, Michael Thatcher, Anthony E. Wetherby Jr., Mark R. Witkowski
Publikováno v:
Journal of pharmaceutical and biomedical analysis. 224
A satellite laboratory "toolkit" consisting of a handheld Raman spectrometer, portable direct analysis in real-time mass spectrometer (DART-MS) and portable Fourier transform infrared (FT-IR) spectrometer was employed to examine 926 pharmaceutical, u
Publikováno v:
Biochemistry. 50:2633-2641
Synaptotagmin 1 (syt1) is a synaptic vesicle-anchored membrane protein that acts as the calcium sensor for the synchronous component of neuronal exocytosis. Using site-directed spin labeling, the position and membrane interactions of a fragment of sy
Autor:
Hao Huang, Dawn Z. Herrick, David S. Cafiso, Jeffrey F. Ellena, Charles D. Schwieters, Weiwei Kuo
Publikováno v:
Journal of Molecular Biology. 390:913-923
Synaptotagmin 1 (syt1) is a synaptic vesicle membrane protein that functions as the Ca(2)(+) sensor in neuronal exocytosis. Here, site-directed spin labeling was used to generate models for the solution and membrane-bound structures of a soluble frag
Autor:
Cameron J. Kilcoyne, Weiwei Kuo, Daniel Deredge, Lila M. Gierasch, Anne Gershenson, Patrick L. Wintrode, Upneet Kaur, Eugenia M. Clerico
Publikováno v:
Biophysical Journal. 112:167a
Circulating inhibitory serpins regulate important physiological processes including inflammation. Misfolding and polymerization of serpins in the endoplasmic reticulum (ER) can lead to both loss-of-function and gain-of-function diseases. The topology
The Ca2+-independent membrane interactions of the soluble C2 domains from synaptotagmin 1 (syt1) were characterized using a combination of site-directed spin labeling and vesicle sedimentation. The second C2 domain of syt1, C2B, binds to membranes co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae2b1af17af2177e9d527b75ede64f08
https://europepmc.org/articles/PMC2669496/
https://europepmc.org/articles/PMC2669496/
Publikováno v:
Biophysical Journal. 96:102a
Synaptotagmin I (Syt I) appears to act as the Ca2+ sensor in neuronal exocytosis and it is known to interact both with membranes and with SNAREs, which form the conserved core protein machinery for the fusion process. The interactions of Syt I with m
Publikováno v:
Biochemistry; 4/5/2011, Vol. 50 Issue 13, p2633-2641, 9p
Publikováno v:
Biophysical Journal. (3):508a
Signaling in the central nervous system depends on the fusion of synaptic vesicles to the presynaptic membrane of the neuron. This fusion event is mediated by membrane-anchored SNAREs (Soluble NSF Attachment Protein Receptors), but requires a number
Publikováno v:
Biophysical Journal. (3):144a
Synaptotagmin 1 (syt1) is a synaptic vesicle protein believed to act as the Ca2+ sensor for neuronal exocytosis. It consists of one N-terminal transmembrane helical segment and two C2 domains (C2A and C2B) that are connected by a short, flexible link