Zobrazeno 1 - 10
of 18
pro vyhledávání: '"J M, Chalovich"'
Publikováno v:
Frontiers in Physiology, Vol 13 (2022)
Striated muscle contraction is inhibited by the actin associated proteins tropomyosin, troponin T, troponin I and troponin C. Binding of Ca2+ to troponin C relieves this inhibition by changing contacts among the regulatory components and ultimately r
Externí odkaz:
https://doaj.org/article/a3547f6888014e16aa46eb703cf2716c
Publikováno v:
Journal of muscle research and cell motility. 21(8)
The troponin complex in a muscle fiber can be replaced with exogenous troponin by using a gentle exchange procedure in which the actin-tropomyosin complex is never devoid of a full complement of troponin (Brenner et al. (1999) Biophys J 77: 2677-2691
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6d2be33d018644451bc0bb051094a53e
https://pubmed.ncbi.nlm.nih.gov/11392555
https://pubmed.ncbi.nlm.nih.gov/11392555
Publikováno v:
Journal of muscle research and cell motility. 20(5-6)
A novel actin binding protein has been isolated from chicken gizzard muscle. When isolated, a pair of proteins with apparent molecular weights of 79 kDa and 103 kDa are obtained; both proteins have a pI near 9.3. Peptide mapping indicates that these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::be968d59ae02e285328579ba0dccaff2
https://pubmed.ncbi.nlm.nih.gov/10555072
https://pubmed.ncbi.nlm.nih.gov/10555072
Publikováno v:
Journal of muscle research and cell motility. 20(3)
Intact caldesmon and particularly the actin-binding C-terminal fragment (20-kDa) of caldesmon have been shown in skeletal muscle fibers to selectively displace low affinity, weakly bound cross-bridges from actin without significantly altering the act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5bc2291569769bc1ba3d17e0de0dbe8f
https://pubmed.ncbi.nlm.nih.gov/10471992
https://pubmed.ncbi.nlm.nih.gov/10471992
Autor:
S, Xu, S, Malinchik, S, Frisbie, J, Gu, T, Kraft, G, Rapp, J M, Chalovich, B, Brenner, L C, Yu
Publikováno v:
Advances in experimental medicine and biology. 453
Two dimensional x-ray diffraction was obtained from skinned rabbit psoas muscle fibers. The goal is to correlate structures of the cross-bridge population with various intermediate states in the cross-bridge cycle by using nucleotides and their analo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::773afeb6f467d1eecf0b0a47b88f61ce
https://pubmed.ncbi.nlm.nih.gov/9889839
https://pubmed.ncbi.nlm.nih.gov/9889839
Publikováno v:
Advances in experimental medicine and biology. 453
Using fluorescence of NBD-labelled troponin I incorporated into skinned fibers of the rabbit psoas muscle by chasing native troponin by troponin with the NBD-labelled TnI subunit we attempted to study kinetics of thin filament activation at different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::695af97d037def01b2744ec655404097
https://pubmed.ncbi.nlm.nih.gov/9889828
https://pubmed.ncbi.nlm.nih.gov/9889828
Publikováno v:
Acta physiologica Scandinavica. 164(4)
The actin binding protein caldesmon inhibits the actin-activation of myosin ATPase activity. The steps in the cycle of ATP hydrolysis that caldesmon could inhibit include: (1) the binding of myosin to actin, (2) the transition between any two actin-m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::503c5de82694a0ed6301e18a2de1ac2e
https://pubmed.ncbi.nlm.nih.gov/9887966
https://pubmed.ncbi.nlm.nih.gov/9887966
Publikováno v:
The Journal of biological chemistry. 268(20)
Caldesmon, an actin-binding protein from smooth muscle and non-muscle cells, has previously been shown to bind stoichiometrically to smooth muscle myosin in an ATP-dependent manner. We now show quantitatively the effects of Ca(2+)-calmodulin and phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::12caa38bcff82122f945dd4e55758b64
https://pubmed.ncbi.nlm.nih.gov/8325900
https://pubmed.ncbi.nlm.nih.gov/8325900
Publikováno v:
Biology of reproduction. 49(1)
Previous immunological studies have indicated that the molecular structure of hamster relaxin is quite different from that of porcine relaxin. In the present study, hamster relaxin was purified from placentas and characterized in order to investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5c41ce33cca37d33b13dbebd99a819fe
https://pubmed.ncbi.nlm.nih.gov/8353182
https://pubmed.ncbi.nlm.nih.gov/8353182
Publikováno v:
The Journal of biological chemistry. 268(1)
A mouse leukemia L1210 cell line was selected for resistance to deoxyguanosine. The deoxyguanosine-resistant cells (dGuo-R) were 126-fold less sensitive to deoxyguanosine than the wild-type cells. The IC50 values for araC and araG were increased, but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::10724136a30a45338966677cd70340b9
https://pubmed.ncbi.nlm.nih.gov/8380161
https://pubmed.ncbi.nlm.nih.gov/8380161