Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Pierre E. Garnaud"'
Publikováno v:
Biochemistry. 43:11035-11044
Electron transfer through neuronal nitric oxide synthase (nNOS) is regulated by the reversible binding of calmodulin (CaM) to the reductase domain of the enzyme, the conformation of which has been shown to be dependent on the presence of substrate, N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a22d6082dd167df48e87ca412ed8c0e4
https://doi.org/10.1021/bi049312v
https://doi.org/10.1021/bi049312v
Publikováno v:
Welland, A, Garnaud, P E, Kitamura, M, Miles, C S & Daff, S 2008, ' Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain ', Biochemistry, vol. 47, no. 37, pp. 9771-9780 . https://doi.org/10.1021/bi800787m
Calmodulin (CaM) activates NO synthase (NOS) by binding to a 20 amino acid interdomain hinge in the presence of Ca2+, inducing electrons to be transferred from the FAD to the heme of the enzyme via a mobile FMN domain. The activation process is influ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f232c969763f227b58a0a1d5e9d6551
https://doi.org/10.1021/bi800787m
https://doi.org/10.1021/bi800787m
Publikováno v:
University of St Andrews CRIS
Calmodulin (CaM) is an acidic ubiquitous calcium binding protein, involved in many intracellular processes, which often involve the formation of complexes with a variety of protein and peptide targets. One such system, activated by Ca 2+ loaded CaM,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88d8bd3baf71c4620fae7fe7ff4a30ec
https://risweb.st-andrews.ac.uk/portal/en/researchoutput/the-formation-of-a-complex-between-calmodulin-and-neuronal-nitric-oxide-synthase-is-determined-by-esims(6bfec503-ce2a-43b0-a200-f35792f4c576).html
https://risweb.st-andrews.ac.uk/portal/en/researchoutput/the-formation-of-a-complex-between-calmodulin-and-neuronal-nitric-oxide-synthase-is-determined-by-esims(6bfec503-ce2a-43b0-a200-f35792f4c576).html
