Zobrazeno 1 - 10
of 59
pro vyhledávání: '"D J, Hartshorne"'
Publikováno v:
Scopus-Elsevier
The objective of this study was to relate the toxicity of several cantharidin-derivative pesticides with their abilities to inhibit protein phosphatases-1 (PP1) and -2A (PP2A). Cantharidin (CA), endothall, and endothall thioanhydride (ETA) inhibited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b2e898c8fda44d66e0c4ad4a01aba47
https://doi.org/10.1152/ajpcell.1995.269.5.c1176
https://doi.org/10.1152/ajpcell.1995.269.5.c1176
Publikováno v:
Journal of Biological Chemistry. 268:25948-25951
The actin-activated ATPase activities of subfragment 1 (S1) produced from gizzard myosin by papain or Staphylococcus aureus protease are different. The activity of the latter is lower, in spite of the presence of intact 20,000-dalton light chains. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07ea096baa9a69378f1ef96563bd67c7
https://doi.org/10.1016/s0021-9258(19)74478-0
https://doi.org/10.1016/s0021-9258(19)74478-0
Publikováno v:
Journal of Biological Chemistry. 266:7030-7036
Limited proteolysis of gizzard myosin by alpha-chymotrypsin converted the heavy chain doublet pattern, seen by gel electrophoresis, to a single band. Light chain degradation was not observed and only minor cleavage occurred at other heavy chain sites
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7cfaa790d52d4024f8597167d47d73e
https://doi.org/10.1016/s0021-9258(20)89605-7
https://doi.org/10.1016/s0021-9258(20)89605-7
Publikováno v:
European journal of biochemistry. 267(6)
The interactions of the catalytic subunit of type 1 protein phosphatase (PP1c) and the N-terminal half (residues 1-511) of myosin phosphatase target subunit 1 (MYPT1) were studied. Biotinylated MYPT1 derivatives were immobilized on streptavidin-biose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7b33bc50818c411c1285dc494c156e27
https://pubmed.ncbi.nlm.nih.gov/10712600
https://pubmed.ncbi.nlm.nih.gov/10712600
Autor:
D J, Hartshorne, K, Hirano
Publikováno v:
Molecular and cellular biochemistry. 190(1-2)
It has been established for many years that MLCK is regulated by the intracellular Ca2+ concentration via the formation of the Ca2+ -calmodulin-MLCK complex. A more recent discovery has been that the myosin phosphatase may also be regulated. This is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::82c5b7759af1337e3ef32fc419d0904f
https://pubmed.ncbi.nlm.nih.gov/10098973
https://pubmed.ncbi.nlm.nih.gov/10098973
Autor:
D J, Hartshorne
Publikováno v:
Acta physiologica Scandinavica. 164(4)
Myosin phosphorylation is an important mechanism in regulating contractile activity of smooth muscle. The level of myosin phosphorylation depends on the balance of two enzymes, myosin light chain kinase and myosin phosphatase. Recently it has been di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::afbb900dcca38eca7757be8457137787
https://pubmed.ncbi.nlm.nih.gov/9887971
https://pubmed.ncbi.nlm.nih.gov/9887971
Publikováno v:
Journal of muscle research and cell motility. 19(4)
This review has presented some of the recent data on myosin phosphatase from smooth muscle. Although it is not conclusive, it is likely that most of the myosin phosphatase activity is represented by a holoenzyme composed of three subunits. These are:
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0c3996824098a0f88e31599a7e79190f
https://pubmed.ncbi.nlm.nih.gov/9635276
https://pubmed.ncbi.nlm.nih.gov/9635276
Autor:
M J, Siegman, S U, Mooers, C, Li, S, Narayan, L, Trinkle-Mulcahy, S, Watabe, D J, Hartshorne, T M, Butler
Publikováno v:
Journal of muscle research and cell motility. 18(6)
A unique property of smooth muscle is its ability to maintain force with a very low expenditure of energy. This characteristic is highly expressed in molluscan smooth muscles, such as the anterior byssus retractor muscle (ABRM) of Mytilus edulis, dur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b32c76cfb46bdb94d33b1602465d1d92
https://pubmed.ncbi.nlm.nih.gov/9429159
https://pubmed.ncbi.nlm.nih.gov/9429159
Publikováno v:
Scopus-Elsevier
ResearcherID
ResearcherID
Myosin II light chains (MLC20) are phosphorylated by a Ca2+/calmodulin-activated kinase and dephosphorylated by a phosphatase that has been purified as a trimer containing the delta isoform of type 1 catalytic subunit (PP1C delta), a myosin-binding 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa1b9ea448db90e7930ced3b90cb679a
https://pubmed.ncbi.nlm.nih.gov/9247646
https://pubmed.ncbi.nlm.nih.gov/9247646
Autor:
Masaaki Ito, Masatoshi Miyahara, Kazuhito Ichikawa, Michiko Naka, Hiroyuki Shimizu, Tokuji Konishi, Toshio Tanaka, D J Hartshorne, Setsuya Okubo, Katsuya Hirano
Publikováno v:
The Journal of biological chemistry. 269(48)
A myosin phosphatase was purified from chicken gizzard smooth muscle. The holoenzyme is a trimer and consists of 130,000-, 38,000-, and 20,000-Da subunits (in agreement with the results of Alessi et al.: Alessi, D., MacDougall, L. K., Sola, M. M., Ik
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::812510535e51bb83d0792b3b4f837618
https://pubmed.ncbi.nlm.nih.gov/7982954
https://pubmed.ncbi.nlm.nih.gov/7982954