Zobrazeno 1 - 10
of 75
pro vyhledávání: '"R S, Adelstein"'
Publikováno v:
American Journal of Physiology-Cell Physiology. 259:C258-C265
At near-threshold substance P concentrations, the isometric tension response of bovine tracheal strips is almost completely abolished by atropine, indicating mediation of contraction via substance P-stimulated release of acetylcholine from prejunctio
Publikováno v:
Cell motility and the cytoskeleton. 46(1)
To understand the role of nonmuscle myosin II in cardiac and skeletal muscle, we used a number of polyclonal antibodies, three detecting nonmuscle myosin heavy chain II-B (NMHC II-B) and two detecting NMHC II-A, to examine the localization of these t
Autor:
P P, Liu, C, Wijmenga, A, Hajra, T B, Blake, C A, Kelley, R S, Adelstein, A, Bagg, J, Rector, J, Cotelingam, C L, Willman, F S, Collins
Publikováno v:
Genes, chromosomescancer. 16(2)
An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid
Publikováno v:
The Journal of biological chemistry. 271(5)
We have expressed two truncated isoforms of chicken nonmuscle myosin II-B using the baculovirus expression system. One of the expressed heavy meromyosins (HMMexp) consists of two 150-kDa myosin heavy chains (MHCs), comprising amino acids 1-1231 as we
Publikováno v:
The Journal of biological chemistry. 269(1)
The phosphorylation of myosin light chains and heavy chains by protein kinase C is known to be temporally correlated with Ca(2+)-dependent secretion of granules from RBL-2H3 cells (Ludowyke, R. I., Peleg, I., Beaven, M. A., and Adelstein, R. S. (1989
Publikováno v:
The Journal of biological chemistry. 268(17)
The molecular mechanisms underlying the heterogeneity in contractile properties observed among smooth muscle tissues are unknown. We examined whether part of this diversity might be intrinsic to myosin by comparing structural and enzymatic properties
Publikováno v:
The Journal of laboratory and clinical medicine. 120(5)
Publikováno v:
The Journal of biological chemistry. 267(25)
The complete amino acid sequence of a vertebrate nonmuscle myosin heavy chain-B isoform (MHC-B, 1976 amino acids, 229 kDa) has been deduced by using cDNA clones from chicken brain libraries. The chicken nonmuscle MHC-B shows overall similarity in pri
Publikováno v:
The Journal of biological chemistry. 267(4)
Vertebrate smooth muscle myosin heavy chains (MHCs) exist as two isoforms with molecular masses of 204 and 200 kDa (MHC204 and MHC200) that are generated from a single gene by alternative splicing of mRNA (Nagai, R., Kuro-o, M., Babij, P., and Perias
Autor:
M A, Conti, R S, Adelstein
Publikováno v:
Methods in enzymology. 196