Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Diego B. Alcala"'
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
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:
Diego B, Alcala, Brian D, Haldeman, Richard K, Brizendine, Agata K, Krenc, Josh E, Baker, Ronald S, Rock, Christine R, Cremo
Publikováno v:
Cell biochemistry and function. 34(7)
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=pmid________::35394c82b79062b92cf59f583ece4d4c
https://pubmed.ncbi.nlm.nih.gov/27528075
https://pubmed.ncbi.nlm.nih.gov/27528075
Autor:
Diego B. Alcala, Michael S. Carter, Brian D. Haldeman, Kevin C. Facemyer, Richard K. Brizendine, Josh E. Baker, Christine R. Cremo
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 112(36)
It is not known which kinetic step in the acto-myosin ATPase cycle limits contraction speed in unloaded muscles (V0). Huxley’s 1957 model [Huxley AF (1957) Prog Biophys Biophys Chem 7:255–318] predicts that V0 is limited by the rate that myosin d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eec91862772f9e7a19e20221144ec3f2
https://pubmed.ncbi.nlm.nih.gov/26294254
https://pubmed.ncbi.nlm.nih.gov/26294254
Autor:
Diego B. Alcala, Richard K. Brizendine, Christine R. Cremo, Brian D. Haldeman, Josh E. Baker, Kevin C. Facemyer
Publikováno v:
Biophysical Journal. 108:296a-297a
Previously we have shown that the ATP-dependence of EDC-stabilized fluorescent smooth muscle myosin (SMM) filament motility is very similar to solution ATPase values (KATP = 8.5 and 9.2 µM, respectively). This suggests both processes are influenced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53c3bf1e340f510dad70149c855b3f17
https://doi.org/10.1016/j.bpj.2014.11.1613
https://doi.org/10.1016/j.bpj.2014.11.1613
Autor:
Diego B. Alcala, Feng Hong, Josh E. Baker, Michael S. Carter, Amy M. Chattin, Kevin C. Facemyer, Brian D. Haldeman, Richard K. Brizendine, Christine R. Cremo, Michael P. Walsh, Avery E. Brown
Publikováno v:
The Journal of General Physiology
One-dimensional diffusion of myosin light chain kinase along actin filaments enables the rapid phosphorylation of smooth muscle myosin.
Smooth muscle myosin (SMM) light chain kinase (MLCK) phosphorylates SMM, thereby activating the ATPase activi
Smooth muscle myosin (SMM) light chain kinase (MLCK) phosphorylates SMM, thereby activating the ATPase activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::703ba8fd2f21f8a16485d890692dda51
https://doi.org/10.1083/jcb.2111oia229
https://doi.org/10.1083/jcb.2111oia229