Zobrazeno 21 - 30
of 39
pro vyhledávání: '"Michael R. Wasserman"'
Publikováno v:
Biophysical Journal. 116:76a
The eukaryotic replicative helicase CMG is assembled at replication origins and is thought to remain topologically closed until termination. Upon encountering a lesion, CMG must vacate a stalled fork to allow DNA repair. However, the fate of CMG unde
Autor:
Daniel S. Terry, Roger B. Altman, Chad M. Kurylo, Scott C. Blanchard, Matt M. Parks, Manuel F. Juette, Boris Zinshteyn, Jose L. Alejo Amaya, Theresa Vincent, Michael R. Wasserman
Publikováno v:
Biophysical Journal. 116:12a
Publikováno v:
Annals of the New York Academy of Sciences. 1241:E1-E16
Single-molecule fluorescence imaging has provided unprecedented access to the dynamics of ribosome function, revealing transient intermediate states that are critical to ribosome activity. Imaging platforms have now been developed that are capable of
Autor:
Robert A. Bailey, Gregory Reardon, Michael R. Wasserman, R. Scott McKenzie, R. Steve Hord, Brett S. Kilpatrick
Publikováno v:
Health Outcomes Research in Medicine. 2:e227-e240
Purpose To evaluate the association between anemia and the clinical endpoints of pressure ulcers, falls, and hospital admissions in long-term care residents. Methods Data were derived retrospectively from the AnalytiCare (Glenview, IL) proprietary da
Publikováno v:
Nature structural & molecular biology
In bacteria, the translocation of tRNA and mRNA with respect to the ribosome is catalyzed by the conserved GTPase, elongation factor-G (EF-G). In order to probe the rate determining features in this process, EF-G-catalyzed translocation was imaged fr
Autor:
Jeffrey J. Fredberg, Michael R. Wasserman, James P. Butler, Thomas E. Angelini, David A. Weitz, Xavier Trepat, Emil Millet
Publikováno v:
Nature Physics. 5:426-430
It has been thought that sheets of cells move by traction forces exerted by the cells at the leading edge of the sheet. Using traction microscopy to create a map of physical forces, it is now shown that in fact it is cells many rows from the front th
Autor:
Jamie H. D. Cate, Sylvie Garneau-Tsodikova, Arto Pulk, Scott C. Blanchard, John C. Zinder, Keith D. Green, Roger B. Altman, Michael R. Wasserman, Zhou Zhou
Publikováno v:
Nature Communications
Wasserman, Michael R.; Pulk, Arto; Zhou, Zhou; Altman, Roger B.; Zinder, John C.; Green, Keith D.; et al.(2015). Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions. Nature Communications, 6. UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/3jf9k6m1
Wasserman, Michael R.; Pulk, Arto; Zhou, Zhou; Altman, Roger B.; Zinder, John C.; Green, Keith D.; et al.(2015). Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions. Nature Communications, 6. UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/3jf9k6m1
Dynamic remodelling of intersubunit bridge B2, a conserved RNA domain of the bacterial ribosome connecting helices 44 (h44) and 69 (H69) of the small and large subunit, respectively, impacts translation by controlling intersubunit rotation. Here we s
Autor:
Zhou Zhou, Michael R. Wasserman, Benjamin J. Burnett, Roger B. Altman, Scott C. Blanchard, Angelica Ferguson
During protein synthesis, elongation factor-Tu (EF-Tu) bound to GTP chaperones the entry of aminoacyl-tRNA (aa-tRNA) into actively translating ribosomes. In so doing, EF-Tu increases the rate and fidelity of the translation mechanism. Recent evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94ecb1ca83b814c87201dd451b69fc5f
https://europepmc.org/articles/PMC4156062/
https://europepmc.org/articles/PMC4156062/
Autor:
Qinsi Zheng, Michael R. Wasserman, Steffen Jockusch, Scott C. Blanchard, Manuel F. Juette, Roger B. Altman, Zhou Zhou
Fluorescence provides a mechanism for achieving contrast in biological imaging that enables investigations of molecular structure, dynamics, and function at high spatial and temporal resolution. Small-molecule organic fluorophores have proven essenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac9dd2c43126d623079021c4bb8a3ee4
https://europepmc.org/articles/PMC3946787/
https://europepmc.org/articles/PMC3946787/
Autor:
Michael R. Wasserman
Publikováno v:
Journal of the American Geriatrics SocietyReferences. 61(6)