Zobrazeno 1 - 10
of 83
pro vyhledávání: '"D. M. Watterson"'
Autor:
D. M. Watterson, A. V. Nikashin, Asker Y. Khapchaev, Thomas J. Lukas, Vladimir P. Shirinsky, Elena L. Vilitkevich, James P. Schavocky, Dmitri S. Kudryashov
Publikováno v:
Biochemistry. Biokhimiia. 80(10)
High molecular weight myosin light chain kinase (MLCK210) is a multifunctional protein involved in myosin II activation and integration of cytoskeletal components in cells. MLCK210 possesses actin-binding regions both in the central part of the molec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2452d47f4c865947d3fbeff2a2edbd14
https://pubmed.ncbi.nlm.nih.gov/26567572
https://pubmed.ncbi.nlm.nih.gov/26567572
Autor:
T. V. Dudnakova, V. P. Shirinsky, D. M. Watterson, B. V. Shekhonin, O. V. Stepanova, K. V. Dergilev, A. V. Chadin
Publikováno v:
Cell Motility and the Cytoskeleton. 63:375-383
Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility involving actin and myosin II. MLCK is widely present in vertebrate tissues including the myocardium. However, the role of MLCK in cardiomyocyte function is not kno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eecf88ef1d4454f3276cbe91a3ea936d
https://doi.org/10.1002/cm.20127
https://doi.org/10.1002/cm.20127
Publikováno v:
Journal of Biological Chemistry. 268:4120-4125
Calmodulin (CaM) is an integral subunit, called delta, of the phosphorylase kinase hexadecamer, and the activity of the isolated catalytic gamma-subunit of the kinase is stimulated by CaM. We report here the first analysis of functionally important f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9ea593f74845c9d8d68630d567c1c0c
https://doi.org/10.1016/s0021-9258(18)53588-2
https://doi.org/10.1016/s0021-9258(18)53588-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1160:8-15
The heterodimer complex of calmodulin (CaM) and the protein kinase catalytic subunit of myosin light chain kinase from vertebrate smooth muscle and non-muscle tissues (sm/nmMLCK) is one of the most extensively characterized CaM-regulated enzyme compl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c4a0056343fcd8e8359e582b520aee0
https://doi.org/10.1016/0167-4838(92)90033-a
https://doi.org/10.1016/0167-4838(92)90033-a
Autor:
D M Watterson, L J Van Eldik, P E Matrisian, Thomas J. Lukas, R L Shattuck, Warren E. Zimmer, M Collinge
Publikováno v:
Scopus-Elsevier
We have determined the first genomic structure and characterized the mRNA and protein products of a novel vertebrate gene that encodes a calcium-binding protein with amino acid sequence identity to a protein kinase domain. The elucidation of the comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1262d28ca2368673242b7553140a80e5
https://doi.org/10.1128/mcb.12.5.2359
https://doi.org/10.1128/mcb.12.5.2359
Autor:
A V, Marchenko, M V, Sidorova, A V, Sekridova, V N, Bushuev, V L, Lakomkin, Ts R, Orlova, O V, Stepanova, V I, Kapel'ko, D M, Watterson, L J, Van Eldik, Zh D, Bespalova, V P, Shirinskiĭ
Publikováno v:
Rossiiskii fiziologicheskii zhurnal imeni I.M. Sechenova. 95(5)
Nonapeptide H-Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys-NH2 corresponding to a modified sequence of autoinhibitory region of myosin light chain kinase (MLCK) was synthesized from L-amino acids and from D-amino acids. Using nuclear magnetic resonance spectr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::62f66ef98cf6b470c03b8f2c39d680a3
https://pubmed.ncbi.nlm.nih.gov/19569527
https://pubmed.ncbi.nlm.nih.gov/19569527
Publikováno v:
Biochemistry. 30:663-667
Trifluoperazine (TFP) binding by 14 calmodulins, including 12 produced by site-directed mutagenesis, was determined. While vertebrate calmodulin binds 4.2 +/- 0.2 equiv of TFP, Escherichia coli expressed but unmutated calmodulins bind about 5.0 +/- 0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fccb7a4505a518f0e76bd0737454cf3
https://doi.org/10.1021/bi00217a011
https://doi.org/10.1021/bi00217a011
Autor:
Keyuan Jiang, D M Watterson, L J Van Eldik, J. Z Heng, Thomas J. Lukas, S.B. Higgins, T. A. Craig
Publikováno v:
Bioinformatics. 6:205-212
Presented in this paper is a knowledge-based experimental design system that incorporates the domain expertise used in nucleic acid engineering, thus automating the processing of error-prone, laborious low-level work, and many decision-making steps,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92ea03cbd5e9a2f73ef74b4eefc60abb
https://doi.org/10.1093/bioinformatics/6.3.205
https://doi.org/10.1093/bioinformatics/6.3.205
Autor:
R L Shattuck, D M Watterson, L J Van Eldik, Thomas J. Lukas, W. Lau, M.O. Shoemaker, Emily Wilson, L. Guerra-Santos, A P Kwiatkowski, P E Matrisian
Publikováno v:
The Journal of Cell Biology
Scopus-Elsevier
Scopus-Elsevier
The first primary structure for a nonmuscle myosin light chain kinase (nmMLCK) has been determined by elucidation of the cDNA sequence encoding the protein kinase from chicken embryo fibroblasts, and insight into the molecular mechanism of calmodulin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50d478fc2b92e29d337738e24d9d607e
http://europepmc.org/articles/PMC2116294
http://europepmc.org/articles/PMC2116294
Publikováno v:
Journal of muscle research and cell motility. 22(5)
KRP (telokin), an independently expressed C-terminal myosin-binding domain of smooth muscle myosin light chain kinase (MLCK), has been reported to have two related functions. First, KRP stabilizes myosin filaments (Shirinsky et al., 1993, J. Biol. Ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::64bc95ec78614af9d97e8990b83477e5
https://pubmed.ncbi.nlm.nih.gov/11964068
https://pubmed.ncbi.nlm.nih.gov/11964068