Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Josh E, Baker"'
Autor:
Josh E. Baker
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-7 (2023)
Abstract As Nature’s version of machine learning, evolution has solved many extraordinarily complex problems, none perhaps more remarkable than learning to harness an increase in chemical entropy (disorder) to generate directed chemical forces (ord
Externí odkaz:
https://doaj.org/article/81d148af50ba48b7bef60617b33e62c3
Publikováno v:
The Journal of Biological Chemistry
Molecular motors such as kinesin and myosin often work in groups to generate the directed movements and forces critical for many biological processes. Although much is known about how individual motors generate force and movement, surprisingly little
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e66384b8794c95be4f2bf62e78fc2ea1
http://europepmc.org/articles/PMC8560993
http://europepmc.org/articles/PMC8560993
Publikováno v:
Biophysical Journal. 120:60a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8038a842347a8869cf4d9eef730a5f84
https://doi.org/10.1016/j.bpj.2020.11.595
https://doi.org/10.1016/j.bpj.2020.11.595
Autor:
Josh E. Baker
Publikováno v:
Biophysical Journal. 120:60a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64a5076b53837397ed5bc2d5b3235cd4
https://doi.org/10.1016/j.bpj.2020.11.596
https://doi.org/10.1016/j.bpj.2020.11.596
Autor:
Josh E. Baker, Brian D. Haldeman, Diego B. Alcala, Agata K. Krenc, Christine R. Cremo, Richard K. Brizendine, Ronald S. Rock
Publikováno v:
Cell Biochemistry and Function. 34:469-474
Myosin light chain kinase (MLCK) phosphorylates S19 of the myosin regulatory light chain (RLC), which is required to activate myosin's ATPase activity and contraction. Smooth muscles are known to display plasticity in response to factors such as infl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::035822c97970b26685b80debc5717f17
https://doi.org/10.1002/cbf.3209
https://doi.org/10.1002/cbf.3209
Publikováno v:
Biophysical Journal. 118:435a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab5393138481a1ce05e8a33aa6396062
https://doi.org/10.1016/j.bpj.2019.11.2442
https://doi.org/10.1016/j.bpj.2019.11.2442
Publikováno v:
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
Tocolytics show limited efficacy to prevent preterm delivery. In uterine smooth muscle cGMP accumulation following addition of nitric oxide (NO) has little effect on relaxation suggesting a role for protein S-nitrosation. In human myometrial tissues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e3bd90267b73718b944fd95e5cb96b7
https://doi.org/10.1038/s41598-018-23371-w
https://doi.org/10.1038/s41598-018-23371-w
Autor:
Christine R. Cremo, Sabrina I. Novenschi, Gabriel Sheehy, Diego B. Alcala, Josh E. Baker, Richard K. Brizendine
Publikováno v:
Science Advances
Reconstituted muscle-like assays reveal novel mechanisms that control the speed of muscle contraction.
In vitro motility assays, where purified myosin and actin move relative to one another, are used to better understand the mechanochemistry of
In vitro motility assays, where purified myosin and actin move relative to one another, are used to better understand the mechanochemistry of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30b025b37d79a488f9eab59748f998d3
https://doi.org/10.1126/sciadv.aao2267
https://doi.org/10.1126/sciadv.aao2267
Autor:
Richard K. Brizendine, Brian D. Haldeman, Josh E. Baker, Kevin C. Facemyer, Christine R. Cremo
Publikováno v:
Journal of Biological Chemistry. 289:21055-21070
Actin-myosin interactions are well studied using soluble myosin fragments, but little is known about effects of myosin filament structure on mechanochemistry. We stabilized unphosphorylated smooth muscle myosin (SMM) and phosphorylated smooth muscle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67657f0e0471da0c087872872765167f
https://doi.org/10.1074/jbc.m114.564740
https://doi.org/10.1074/jbc.m114.564740
Autor:
Michael S. Carter, Travis J. Stewart, Milad Webb, Travis Phillips, Del R. Jackson, Christine R. Cremo, Josh E. Baker
Publikováno v:
Archives of Biochemistry and Biophysics. :74-82
To determine the mechanism by which sucrose slows in vitro actin sliding velocities, V, we used stopped flow kinetics and a single molecule binding assay, SiMBA. We observed that in the absence of ATP, sucrose (880 mM) slowed the rate of actin-myosin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d3bb2fac4455166bd9f180dba3063b5
https://doi.org/10.1016/j.abb.2013.12.012
https://doi.org/10.1016/j.abb.2013.12.012