Zobrazeno 1 - 10
of 125
pro vyhledávání: '"Richard M. Berry"'
Autor:
Michael V. Kiriakou, Amir Saeid Pakdel, Richard M. Berry, Todd Hoare, Marc A. Dubé, Emily D. Cranston
Publikováno v:
ACS Materials Au, Vol 2, Iss 2, Pp 176-189 (2021)
Externí odkaz:
https://doaj.org/article/6b00ca1f79b348c8958b140a5d61e913
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
Several new structures of three types of protein complexes, obtained by cryo-electron microscopy (cryo-EM) and published between 2019 and 2021, identify a new family of natural molecular wheels, the “5:2 rotary motors.” These span the cytoplasmic
Externí odkaz:
https://doaj.org/article/4600df7ecd1c431e8e1e6789e40024de
Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
Autor:
Meghna Sobti, James L. Walshe, Di Wu, Robert Ishmukhametov, Yi C. Zeng, Carol V. Robinson, Richard M. Berry, Alastair G. Stewart
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
F1Fo ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F1 and the transmembrane Fo. Here, the authors present cryo-EM structures of E. coli ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution an
Externí odkaz:
https://doaj.org/article/0173de1fc389481f868feeaeaacc4180
Publikováno v:
ACS Omega, Vol 4, Iss 1, Pp 2102-2110 (2019)
Externí odkaz:
https://doaj.org/article/67c6fc82df5b4897a28c5dc9ee8a6ef8
Autor:
Fatima Awan, Muhammad Shahidul Islam, Yeyu Ma, Cindy Yang, Zengqian Shi, Richard M. Berry, Kam C. Tam
Publikováno v:
ACS Omega, Vol 3, Iss 10, Pp 12403-12411 (2018)
Externí odkaz:
https://doaj.org/article/5d922eea70184e3088f38c3a183331c9
Autor:
Andrew L. Hook, James L. Flewellen, Jean-Frédéric Dubern, Alessandro M. Carabelli, Irwin M. Zaid, Richard M. Berry, Ricky D. Wildman, Noah Russell, Paul Williams, Morgan R. Alexander
Publikováno v:
mSystems, Vol 4, Iss 5 (2019)
ABSTRACT Bacteria sense chemicals, surfaces, and other cells and move toward some and away from others. Studying how single bacterial cells in a population move requires sophisticated tracking and imaging techniques. We have established quantitative
Externí odkaz:
https://doaj.org/article/fe0ad18bb1004ea5ada2c4ae39a439b1
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
Assembling multiple biological components into synthetic lipid vesicles is a limiting step in the manufacture of biomimetic cell-like structures. Here the authors use fusogenic proteoliposomes of opposite charge for fast assembly of a minimal electro
Externí odkaz:
https://doaj.org/article/79ab5c276ed346169bc8cceb064fb099
Publikováno v:
mBio, Vol 5, Iss 4 (2014)
ABSTRACT Some proteins in biological complexes exchange with pools of free proteins while the complex is functioning. Evidence is emerging that protein exchange can be part of an adaptive mechanism. The bacterial flagellar motor is one of the most co
Externí odkaz:
https://doaj.org/article/8b56e806756745b29fca346facbba8f6
Publikováno v:
mBio, Vol 4, Iss 4 (2013)
ABSTRACT It is becoming clear that the bacterial flagellar motor output is important not only for bacterial locomotion but also for mediating the transition from liquid to surface living. The output of the flagellar motor changes with the mechanical
Externí odkaz:
https://doaj.org/article/fc581c2868374af8b8a8041ce1cb0e12
Autor:
Yoshiaki Kinosita, Nagisa Mikami, Tessa E. F. Quax, Sonja-Verena Albers, Chris van der Does, Robert Ishmukhametov, Frank Braun, Richard M. Berry, Zhengqun Li
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 117(43), 26766-26772. NATL ACAD SCIENCES
Archaea swim using the archaellum (archaeal flagellum), a reversible rotary motor consisting of a torque-generating motor and a helical filament, which acts as a propeller. Unlike the bacterial flagellar motor (BFM), ATP (adenosine-5′-triphosphate)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78811ddac39f62a88d968401cacf9495
https://doi.org/10.1073/pnas.2009814117
https://doi.org/10.1073/pnas.2009814117