Results 11 to 20 of about 2,487,706 (262)

Towards Understanding the Angiomotin Membrane Fusion Activity [PDF]

, 2021
Angiomotins (Amot) are a family of adaptor proteins that regulate cellular differentiation and proliferation signaling. These cellular events are linked to the initiation of invasive ductal carcinoma, the most common form of breast cancer.
Brenner, Evans, Ann, Kimble-Hill, Seth, Sears   +2 more
core   +1 more source

A supramolecular system mimicking the infection process of an enveloped virus through membrane fusion

Scientific Reports, 2023
Membrane fusion is an essential step for the entry of enveloped viruses, such as human immunodeficiency virus and influenza virus, into the host cell, often triggered by the binding of membrane proteins on the viral envelope to host cell membrane ...
Hiroto Furukawa, Yuuna Kimura, Hiroshi Inaba, Kazunori Matsuura   +3 more
doaj   +1 more source

Membrane Binding of α-Synuclein Stimulates Expansion of SNARE-Dependent Fusion Pore

Frontiers in Cell and Developmental Biology, 2021
SNARE-dependent membrane fusion is essential for neurotransmitter release at the synapse. Recently, α-synuclein has emerged as an important regulator for membrane fusion. Misfolded α-synuclein oligomers are potent fusion inhibitors. However, the function
Ryan Khounlo, Brenden J. D. Hawk, Tung-Mei Khu, Gyeongji Yoo, Nam Ki Lee, Josh Pierson, Yeon-Kyun Shin   +6 more
doaj   +1 more source

TRIM67 regulates exocytic mode and neuronal morphogenesis via SNAP47

Cell Reports, 2021
Summary: Neuronal morphogenesis involves dramatic plasma membrane expansion, fueled by soluble N-ethylmaleimide-sensitive factor attachment protein eceptors (SNARE)-mediated exocytosis.
Fabio L. Urbina, Shalini Menon, Dennis Goldfarb, Reginald Edwards, M. Ben Major, Patrick Brennwald, Stephanie L. Gupton   +6 more
doaj   +1 more source

A virus-encoded cell-cell fusion machine dependent on surrogate adhesins. [PDF]

PLoS Pathogens, 2008
The reovirus fusion-associated small transmembrane (FAST) proteins function as virus-encoded cellular fusogens, mediating efficient cell-cell rather than virus-cell membrane fusion. With ectodomains of only approximately 20-40 residues, it is unclear how
Jayme Salsman, Deniz Top, Christopher Barry, Roy Duncan   +3 more
doaj   +1 more source

LegC3, an effector protein from Legionella pneumophila, inhibits homotypic yeast vacuole fusion in vivo and in vitro. [PDF]

PLoS ONE, 2013
During infection, the intracellular pathogenic bacterium Legionella pneumophila causes an extensive remodeling of host membrane trafficking pathways, both in the construction of a replication-competent vacuole comprised of ER-derived vesicles and plasma ...
Terry L Bennett, Shannon M Kraft, Barbara J Reaves, Joji Mima, Kevin M O'Brien, Vincent J Starai   +5 more
doaj   +1 more source

Fusion of secretory vesicles isolated from rat liver [PDF]

, 1978
Secretory vesicles isolated from rat liver were found to fuse after exposure to Ca2+. Vescle fusion is characterized by the occurrence of twinned vesicles with a continuous cleavage plane between two vesicles in freeze-fracture electron microscopy.
Dahl, Gerhard, Dahl, G., Gratzl, Manfred   +2 more
core   +1 more source

Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE

Cell Reports, 2019
Summary: Intracellular vesicle fusion is mediated by soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18 (SM) proteins. It is generally accepted that membrane fusion occurs when the vesicle and target membranes
Shailendra S. Rathore, Yinghui Liu, Haijia Yu, Chun Wan, MyeongSeon Lee, Qian Yin, Michael H.B. Stowell, Jingshi Shen   +7 more
doaj   +1 more source

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

The structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex reveals the protein-membrane and lateral protein-protein interaction [PDF]

, 2013
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex.
Topf, Maya, Huiskonen, JT, Topf, M., Maurer, U., Whitbeck, J., Maurer, U.E., Gruenewald, Kay, Cohen, G., Cairns, T.M., Eisenberg, R.J., Huiskonen, Juha T., Whitbeck, J.C., Zeev-Ben-Mordehai, T, Cohen, Gary H., Cohen, GH, Cairns, Tina M., Hannah, BP, Hannah, B.P., Cohen, G.H., Pandurangan, A., Zeev-Ben-Mordehai, T., Grünewald, K, Eisenberg, Roselyn J., Cairns, T., Huiskonen, J.T., Maurer, Ulrike E., Grünewald, Kay, Eisenberg, RJ, Topf, M, Grünewald, K., Maurer, UE, Pandurangan, Arun Prasad, Whitbeck, JC, Zeev-Ben-Mordehai, Tzviya, Huiskonen, J., Hannah, Brian P., Hannah, B., Pandurangan, Arun, Pandurangan, AP, Eisenberg, R., Whitbeck, J. Charles, Cairns, TM   +41 more
core   +2 more sources