Zobrazeno 1 - 10
of 575
pro vyhledávání: '"I R Gibbons"'
Autor:
GUNDERSEN, G
Publikováno v:
Cell; October 1989, Vol. 59 Issue: 2 p244-244, 1p
Autor:
Anthony J. Roberts, Reiko Ohkura, Peter J. Knight, Kazuo Sutoh, I R Gibbons, Kenji Imamula, Stan A. Burgess, Takahide Kon
Publikováno v:
Nature structural & molecular biology
Coupling between ATPase and track-binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled-coil stalk which must mediate communication between them, yet the underlying me
Autor:
Joan E. Garbarino, Ronald A. Milligan, Ronald D. Vale, Wesley E. Shipley, Andrew P. Carter, Carol Cho, Elizabeth M. Wilson-Kubalek, I. R. Gibbons
Publikováno v:
Science. 322:1691-1695
Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphos
Autor:
Blair J. Rossetti, Judkins Km, Robert A. Obar, Leone Ad, Rawson Ap, Musante Am, Robert L. Morris, Cool J, Hoffman Mp, I. R. Gibbons, David R. Burgess, McCafferty Ss, Allgood El
Publikováno v:
Developmental Biology. 300(1):219-237
The sea urchin embryo is a classical model system for studying the role of the cytoskeleton in such events as fertilization, mitosis, cleavage, cell migration and gastrulation. We have conducted an analysis of gene models derived from the Strongyloce
Autor:
Gabor Mocz, I. R. Gibbons
Publikováno v:
Structure. 9:93-103
Background: Recent iterative methods for sequence alignment have indicated that the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases . These alignments indicate that the core of the 380 kDa motor unit contains a concate
Publikováno v:
Biochemistry. 37:9862-9869
MantATP [2'(3')-O-(-N-methylanthraniloyl)-adenosine 5'-triphosphate] was employed as a fluorescence probe of the nucleotide-binding sites of dynein from sea urchin sperm flagella. MantATP binds specifically with enhanced fluorescence (approximately 2
Autor:
J. Richard McIntosh, Erika L.F. Holzbaur, Mary E. Porter, Stephen M. King, Richard B. Vallee, Elizabeth M. C. Fisher, Trina A. Schroer, K. Kevin Pfister, Kevin T. Vaughan, Thomas S. Hays, George B. Witman, I. R. Gibbons
Publikováno v:
The Journal of Cell Biology
A variety of names has been used in the literature for the subunits of cytoplasmic dynein complexes. Thus, there is a strong need for a more definitive consensus statement on nomenclature. This is especially important for mammalian cytoplasmic dynein
Publikováno v:
The Journal of Cell Biology
The Saccharomyces cerevisiae kinesin-related gene products Cin8p and Kip1p function to assemble the bipolar mitotic spindle. The cytoplasmic dynein heavy chain homologue Dyn1p (also known as Dhc1p) participates in proper cellular positioning of the s
Autor:
I. R. Gibbons
Publisher Summary This chapter examines the research carried out on the dynein motor protein reflecting its role in the life of a cell. It describes how Ian Gibbons, as the first person of his family to attend a university, participated in discoverin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::582a0b8cf954f4100a396c7f31b8cbbc
https://doi.org/10.1016/b978-0-12-382004-4.10001-9
https://doi.org/10.1016/b978-0-12-382004-4.10001-9
Autor:
Eric L. Eisenstein, Ying R. Yang, Howard K. Schachman, T.S. Woo, J.M. Ritchey, I. R. Gibbons, M.S. Han
Publikováno v:
Journal of Biological Chemistry. 267:22148-22155
A comprehensive set of hybrid molecules of aspartate transcarbamylase (ATCase) from Escherichia coli has been constructed of wild-type and mutationally altered catalytic chains. The mutant enzymes that were virtually devoid of activity contained a re