Results 11 to 20 of about 55,518 (304)

SNARE Modulators and SNARE Mimetic Peptides

Biomolecules, 2022
The soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) proteins play a central role in most forms of intracellular membrane trafficking, a key process that allows for membrane and biocargo shuffling between ...
Mikhail Khvotchev, Mikhail Soloviev
doaj   +4 more sources

SNARE protein mimicry by an intracellular bacterium. [PDF]

PLoS Pathogens, 2008
Many intracellular pathogens rely on host cell membrane compartments for their survival. The strategies they have developed to subvert intracellular trafficking are often unknown, and SNARE proteins, which are essential for membrane fusion, are possible ...
Cédric Delevoye, Michael Nilges, Pierre Dehoux, Fabienne Paumet, Stéphanie Perrinet, Alice Dautry-Varsat, Agathe Subtil   +6 more
doaj   +2 more sources

α-SNAP Enhances SNARE Zippering by Stabilizing the SNARE Four-Helix Bundle [PDF]

Cell Reports, 2016
Intracellular membrane fusion is mediated by dynamic assembly and disassembly of soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors (SNAREs). α-SNAP guides NSF to disassemble SNARE complexes after membrane fusion.
Lu Ma, Yuhao Kang, Junyi Jiao, Aleksander A. Rebane, Hyo Keun Cha, Zhiqun Xi, Hong Qu, Yongli Zhang   +7 more
doaj   +2 more sources

Model of SNARE-mediated membrane adhesion kinetics. [PDF]

PLoS ONE, 2009
SNARE proteins are conserved components of the core fusion machinery driving diverse membrane adhesion and fusion processes in the cell. In many cases micron-sized membranes adhere over large areas before fusion. Reconstituted in vitro assays have helped
Jason M Warner, Erdem Karatekin, Ben O'Shaughnessy   +2 more
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SNARE zippering [PDF]

Bioscience Reports, 2016
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been
Lou, Xiaochu, Shin, Yeon-Kyun
openaire   +2 more sources

SNAREs-SAP: SNARE Proteins Identification With PSSM Profiles [PDF]

Frontiers in Genetics, 2021
Soluble N-ethylmaleimide sensitive factor activating protein receptor (SNARE) proteins are a large family of transmembrane proteins located in organelles and vesicles. The important roles of SNARE proteins include initiating the vesicle fusion process and activating and fusing proteins as they undergo exocytosis activity, and SNARE proteins are also ...
Zixiao Zhang, Yue Gong, Bo Gao, Hongfei Li, Wentao Gao, Yuming Zhao, Benzhi Dong   +6 more
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The Sec1/Munc18 protein Vps45 regulates cellular levels of its SNARE binding partners Tlg2 and Snc2 in Saccharomyces cerevisiae [PDF]

, 2012
Intracellular membrane trafficking pathways must be tightly regulated to ensure proper functioning of all eukaryotic cells. Central to membrane trafficking is the formation of specific SNARE (soluble N-ethylmeleimide-sensitive factor attachment protein ...
Marion S Struthers, Nia J Bryant, Lindsay N Carpp, Carpp Lindsay N., Shanks, S.G., McCann Rebecca K., Carpp, L.N., Struthers, M.S., Bryant, N.J., Scott G Shanks, Struthers Marion S., McCann, R.K., Bryant Nia J., Hong, W., Shanks Scott G., Rebecca K McCann   +15 more
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Secretory vesicles are preferentially targeted to areas of low molecular SNARE density [PDF]

, 2012
Intercellular communication is commonly mediated by the regulated fusion, or exocytosis, of vesicles with the cell surface. SNARE (soluble N-ethymaleimide sensitive factor attachment protein receptor) proteins are the catalytic core of the secretory ...
Weiping Lu (120665), Dun, Alison R., Lu, Weiping, Rory R. Duncan (120667), Weiping Lu, Gabriel J. Lord (120664), Colin Rickman (120669), Andrew Dunn, Gabriel J Lord, Martin, Kirsty J, Lei Yang (102719), Qiu, Zhen, Rickman, Colin; id_orcid, Kirsty J Martin, Lei Yang, Duncan, Rory R, Duncan, Rory R., Alison R. Dun (120660), Zhen Qiu (120662), Rickman, Colin, Dun, Alison, Qiu, Zhen; id_orcid, Colin Rickman, Rory R Duncan, Lord, Gabriel J, Kirsty J. Martin (120661), Alison R Dun, Lord, Gabriel J., Yang, Lei, Martin, Kirsty J., Andrew Dunn (120663), Dunn, Andrew, Zhen Qiu   +32 more
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A TONSIL SNARE. [PDF]

JAMA: The Journal of the American Medical Association, 1906
In presenting this tonsil snare to the profession I wish to recommend its simplicity, strength, lightness and cheapness. The instrument consists of three parts: The shaft, with handle, the stylet and the tip. In place of the straight tip the different size Vedder tips can be used, all of which are easily taken apart and cleaned. Wire from Nos. 5 to 8
openaire   +2 more sources

Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c In Vitro [PDF]

, 2008
Background: Translocation of the facilitative glucose transporter GLUT4 from an intracellular store to the plasma membrane is responsible for the increased rate of glucose transport into fat and muscle cells in response to insulin.
Nia J Bryant, Gould, G.W., Veronica Aran, James A McNew, Gwyn W Gould, McNew, J.A., Bryant, N.J., Aran Veronica, Avani Verma, Gould Gwyn W., Aran-Ponte, V., Fiona M Brandie, Bryant Nia J., Verma Avani, Brandie Fiona M., McNew James A., Brandie, F.M., Verma, A.   +17 more
core   +2 more sources