Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Elena L, Vilitkevich"'
Autor:
Asker Y. Khapchaev, Vladimir P. Shirinsky, A. A. Az’muko, Elena L. Vilitkevich, V. N. Bushuev, A. S. Molokoedov, Zhanna D. Bespalova, Olga A. Kazakova, Mikhail V. Samsonov, Maria Sidorova
Publikováno v:
Journal of Peptide Science. 22:673-681
Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility including smooth muscle contraction, cell migration, cytokinesis, receptor capping, secretion, etc. Inhibition of MLCK activity in endothelial and epithelial monola
Autor:
Asker Y, Khapchaev, Olga A, Kazakova, Mikhail V, Samsonov, Maria V, Sidorova, Valery N, Bushuev, Elena L, Vilitkevich, Andrey A, Az'muko, Alexander S, Molokoedov, Zhanna D, Bespalova, Vladimir P, Shirinsky
Publikováno v:
Journal of peptide science : an official publication of the European Peptide Society. 22(11-12)
Myosin light chain kinase (MLCK) is a key regulator of various forms of cell motility including smooth muscle contraction, cell migration, cytokinesis, receptor capping, secretion, etc. Inhibition of MLCK activity in endothelial and epithelial monola
Autor:
Mikhail V. Samsonov, A. S. Molokoedov, A. A. Az’muko, Asker Y. Khapchaev, Olga A. Kazakova, Maria Sidorova, Elena L. Vilitkevich, Zh. D. Bespalova, Vladimir P. Shirinsky
Publikováno v:
Biophysics. 57:587-591
Novel peptides originating from the peptide inhibitor of myosin light chain kinase (MLCK), L-PIK (Arg-Lys-Lys-Tyr-Lys-Tyr-Arg-Arg-Lys), have been studied for their ability to attenuate the thrombin-induced hyperpermeability of an endothelial cell mon
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
Autor:
Elena L. Vilitkevich, Olga V. Stepanova, Tatyana A Nikonenko, Linda J. Van Eldik, Vladimir P. Shirinsky, Thomas J. Lukas, N. A. Shanina, D. Martin Watterson, Dmitry S. Kudryashov, Elena S. Nadezhdina
Publikováno v:
Experimental cell research. 298(2)
Recently discovered 210-kDa myosin light chain kinase (MLCK-210) is identical to 108-130 kDa MLCK, the principal regulator of the myosin II molecular motor, except for the presence of a unique amino terminal extension. Our in vitro experiments and tr