Zobrazeno 1 - 10
of 229
pro vyhledávání: '"R. Cremo"'
Autor:
Joshua D. Smith, Jhonnathan Brawley, Kate C. Bordenave, Ryan K. Olsen, Amarawan Intasiri, Christine R. Cremo, Thomas W. Bell
Publikováno v:
European journal of medicinal chemistry. 247
Muscle myosin inhibition could be used to treat many medical conditions involving hypercontractile states, including muscle spasticity, chronic musculoskeletal pain, and hypertrophic cardiomyopathy. A series of 13 advanced analogs of 3-(N-butylethani
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33f40168643aa121715de1a1fd125b25
https://pubmed.ncbi.nlm.nih.gov/36543032
https://pubmed.ncbi.nlm.nih.gov/36543032
Autor:
Thomas W. Gould, Brandon M. Welcome, Joshua D. Smith, Richard K. Brizendine, Jhonnathan Brawley, Dante J. Heredia, Kyle Nennecker, Emily Etter, Christine R. Cremo, Thomas W. Bell, Amarawan Intasiri
Publikováno v:
J Med Chem
Inhibitors of muscle myosin ATPases are needed to treat conditions that could be improved by promoting muscle relaxation. The lead compound for this study ((3-(N-butylethanimidoyl)ethyl)-4-hydroxy-2H-chromen-2-one; BHC) was previously discovered to i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::895a098b9f4ddd54b8aab143967624d9
https://doi.org/10.1021/acs.jmedchem.0c01062
https://doi.org/10.1021/acs.jmedchem.0c01062
Publikováno v:
The Journal of General Physiology
The July 2021 issue of JGP is a collection of peer-reviewed articles focused on the function and dynamic regulation of contractile systems in muscle and non-muscle cells.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b528abba76c5eabc450a3e782afa802
https://doi.org/10.1085/jgp.202112972
https://doi.org/10.1085/jgp.202112972
Publikováno v:
The Journal of General Physiology
Brizendine et al. directly visualized quantum dot–labeled myosin heads and rods in vitro to understand the flexibility of the S2 subdomain. Their results confirm theoretical predictions about the range of motion of S2 and its effect on the relative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d915d92048df44de4ca11ca55e36372
https://doi.org/10.1085/jgp.202012751
https://doi.org/10.1085/jgp.202012751
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:
Cytoskeleton (Hoboken, N.J.). 76(2)
The regulatory light chain (RLC) of myosin is commonly tagged to monitor myosin behavior in vitro, in muscle fibers, and in cells. The goal of this study was to prepare smooth muscle myosin (SMM) filaments containing a single head labeled with a quan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fded1a6c078703870755439935a3078
https://pubmed.ncbi.nlm.nih.gov/30861328
https://pubmed.ncbi.nlm.nih.gov/30861328
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