Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Amy McGough"'
Autor:
Theodore G. Wensel, Amy McGough, Thomas J. Melia, Zhixian Zhang, Ching Yuan, Feng He, Michael F. Schmid
Publikováno v:
Journal of Biological Chemistry. 279:33937-33945
Heterotrimeric G proteins interact with receptors and effectors at the membrane-cytoplasm interface. Structures of soluble forms have not revealed how they interact with membranes. We have used electron crystallography to determine the structure in i
Publikováno v:
Biophysical Journal. 84(4):2585-2592
Bacteriophage assembly frequently begins with the formation of a precursor capsid that serves as a DNA packaging machine. The DNA packaging is accompanied by a morphogenesis of the small round precursor capsid into a large polyhedral DNA-containing m
Publikováno v:
Journal of Molecular Biology. 298:649-661
The actin depolymerizing factor (ADF)/cofilin family of proteins interact with actin monomers and filaments in a pH-sensitive manner. When ADF/cofilin binds F-actin it induces a change in the helical twist and fragmentation; it also accelerates the d
Publikováno v:
Trends in Cell Biology. 9:364-370
The actin-depolymerizing factor (ADF)/cofilins are a family of essential actin regulatory proteins, ubiquitous among eukaryotes, that enhance the turnover of actin by regulating the rate constants of polymerization and depolymerization at filament en
Autor:
Amy McGough, Wah Chiu
Publikováno v:
Journal of Molecular Biology. 291:513-519
Observed in vivo motility rates can only be accounted for if the rate of actin filament treadmilling in cells is considerably greater than has been quantified for purified actin in vitro. ADF/cofilin is uniquely suited to promote actin dynamics in ce
Autor:
Amy McGough, Justine A. Malinski, Wah Chiu, Barrie Greene, Peter E. Prevelige, Pamela A. Thuman-Commike, Michelle Burbea
Publikováno v:
Biophysical Journal. 76:3267-3277
Assembly of certain classes of bacterial and animal viruses requires the transient presence of molecules known as scaffolding proteins, which are essential for the assembly of the precursor procapsid. To assemble a procapsid of the proper size, each
Publikováno v:
Trends in Cell Biology. 9:154-159
Electron cryomicroscopy is a high-resolution imaging technique that is particularly appropriate for the structural determination of large macromolecular assemblies, which are difficult to study by X-ray crystallography or NMR spectroscopy. For some b
Autor:
Amy McGough
Publikováno v:
Current Opinion in Structural Biology. 8:166-176
The study of proteins that bind filamentous actin (F-actin) is entering an exciting stage as more and more structures are determined. After more than 50 years in which the focus was on muscle proteins, emphasis has recently shifted towards understand
Publikováno v:
Scopus-Elsevier
Gelsolin is a six-domain protein that regulates actin assembly by severing, capping, and nucleating filaments. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on F-actin. To obtain fully decorated filament
Autor:
Amy McGough, Michael Way
Publikováno v:
Journal of Structural Biology. 115:144-150
Gelsolin is a six-domain protein with a wide array of actin regulating activities. Despite the growing body of structural data on this protein, little is known about how it binds F-actin during severing and capping. In this paper we have combined dat