Zobrazeno 1 - 10
of 17
pro vyhledávání: '"L. P. Adam"'
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 24, Iss 3, Pp 328-335 (2011)
Verticillium wilt, caused by Verticillium dahliae Kleb., is a serious potato (Solanum tuberosum L.) disease worldwide, and biocontrol represents a promising eco-friendly strategy to reduce its impact. We used extracts from Canada milk vetch (CMV) and
Externí odkaz:
https://doaj.org/article/325f38d3a2284b75b66d19f1df7bfc74
Publikováno v:
New Zealand Dental Journal; Mar2023, Vol. 119 Issue 1, p27-36, 10p
Akademický článek
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Autor:
M. Finkbeiner, Elena, Micheli, Fiorenza, J. Bennett, Nathan, L. Ayers, Adam, Le Cornu, Elodie, N. Doerr, Angee
Publikováno v:
Marine Policy; Feb2018, Vol. 88, p359-364, 6p
Publikováno v:
Europe PubMed Central
Evidence suggests that the mechanical behavior of smooth muscle tissues is regulated by Ca(2+)-dependent changes in the phosphorylation of the 20,000-Da light chain of myosin (MLC). However, alternative mechanisms activated by specific kinases may be
Publikováno v:
The Journal of biological chemistry. 274(42)
Extracellular signal-regulated kinases (ERKs) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-CaD) at two sites (Ser(759) and Ser(789)) during smooth muscle stimulation. To investigate the role of phosphorylati
Publikováno v:
Europe PubMed Central
Reorganization of cytoskeletal-membrane interactions during contractile stimulation may contribute to the regulation of airway smooth muscle contraction. We investigated the effect of contractile stimulation on the phosphorylation of the actin-membra
Publikováno v:
Journal of biochemistry. 115(1)
The Ca(2+)-dependent protease, calpain II, isolated from vascular smooth muscle was found to be a substrate for Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) in vitro. Phosphorylation was dependent upon prior autolysis of the regulatory
Publikováno v:
The Biochemical journal. 294
It was reported that chicken gizzard smooth-muscle caldesmon Cys-580 can be disulphide-cross-linked to the C-terminal pen-ultimate residue (Cys-374) of actin, indicating that these residues are close in the protein complex [Graceffa, P. and Jancso, A
Autor:
D. Benny, Paul, L. Moore, Adam
Publikováno v:
Current Organic Synthesis; August 2011, Vol. 8 Issue: 4 p566-583, 18p