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pro vyhledávání: '"Harold P. Erickson"'
Autor:
Harold P. Erickson
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
The cytoplasm of bacteria is maintained at a higher osmolality than the growth medium, which generates a turgor pressure. The cell membrane (CM) cannot support a large turgor, so there are two possibilities for transferring the pressure to the peptid
Externí odkaz:
https://doaj.org/article/95a2831d88c944ccb4d226181833ab99
Autor:
Kevin O. Saunders, Laurent K. Verkoczy, Chuancang Jiang, Jinsong Zhang, Robert Parks, Haiyan Chen, Max Housman, Hilary Bouton-Verville, Xiaoying Shen, Ashley M. Trama, Richard Scearce, Laura Sutherland, Sampa Santra, Amanda Newman, Amanda Eaton, Kai Xu, Ivelin S. Georgiev, M. Gordon Joyce, Georgia D. Tomaras, Mattia Bonsignori, Steven G. Reed, Andres Salazar, John R. Mascola, M. Anthony Moody, Derek W. Cain, Mireille Centlivre, Sandra Zurawski, Gerard Zurawski, Harold P. Erickson, Peter D. Kwong, S. Munir Alam, Yves Levy, David C. Montefiori, Barton F. Haynes
Publikováno v:
Cell Reports, Vol 21, Iss 13, Pp 3681-3690 (2017)
The events required for the induction of broad neutralizing antibodies (bnAbs) following HIV-1 envelope (Env) vaccination are unknown, and their induction in animal models as proof of concept would be critical. Here, we describe the induction of plas
Externí odkaz:
https://doaj.org/article/e81ea1bb367e416ea3dab564db722a4e
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
Abstract The cytokinetic division ring of Escherichia coli comprises filaments of FtsZ tethered to the membrane by FtsA and ZipA. Previous results suggested that ZipA is a Z-ring stabilizer, since in vitro experiments it is shown that ZipA enhanced F
Externí odkaz:
https://doaj.org/article/16b42d13f92846d8898a352de1dd6d64
Autor:
Masaki Osawa, Harold P. Erickson
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Bacterial cytokinesis begins with the assembly of FtsZ into a Z ring at the center of the cell. The Z-ring constriction in Gram-negative bacteria may occur in an environment where the periplasm and the cytoplasm are isoosmotic, but in Gram-positive b
Externí odkaz:
https://doaj.org/article/5d65b27b8a88491fa6c5cb5a16fcce5f
Publikováno v:
Biochemistry.
The trimeric spike protein of SARS-CoV-2 has been targeted by antibody mimics that bind near or at the receptor-binding domain to neutralize the virus. Several independent studies have reported enhanced binding avidity for dimers and trimers, where b
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0176643 (2017)
FtsZ is an essential protein for bacterial cell division, where it forms the cytoskeletal scaffold and may generate the constriction force. We have found previously that some mutant and foreign FtsZ that do not complement an ftsZ null can function fo
Externí odkaz:
https://doaj.org/article/12f9463bac6a4699a9d66341ab3548e9
Publikováno v:
Microbiology. 168
There has been recent debate as to the source of constriction force during cell division. FtsZ can generate a constriction force on tubular membranes in vitro, suggesting it may generate the constriction force in vivo. However, another study showed t
Publikováno v:
Endocrine Reviews
In 2002, a transmembrane protein—now known as FNDC5—was discovered and shown to be expressed in skeletal muscle, heart, and brain. It was virtually ignored for 10 years, until a study in 2012 proposed that, in response to exercise, the ectodomain
Autor:
Harold P. Erickson, Lauren C. Corbin
Publikováno v:
Biophys J
Bacterial cell division is tightly coupled to the dynamic behavior of FtsZ, a tubulin homolog. Recent experimental work in vitro and in vivo has attributed FtsZ's assembly dynamics to treadmilling, in which subunits add to the bottom and dissociate f
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
Escherichia coli has served as the main model system for examining cell division in bacteria; however, the structure of the central cytokinesis protein FtsZ has not been determined to date. Here, high-resolution structures of E. coli FtsZ in GDP-boun