Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Clinton Mathai"'
Autor:
Clinton Mathai, Frances Jourd'heuil, Le Gia Cat Pham, Kurrim Gilliard, Dennis Howard, Joseph Balnis, Ariel Jaitovich, Sridar V. Chittur, Mark Rilley, Ruben Peredo-Wende, Ibrahim Ammoura, Sandra J. Shin, Margarida Barroso, Jonathan Barra, Evgenia Shishkova, Joshua J. Coon, Reynold I. Lopez-Soler, David Jourd'heuil
Publikováno v:
Redox Biology, Vol 65, Iss , Pp 102838- (2023)
Identifying novel regulators of vascular smooth muscle cell function is necessary to further understand cardiovascular diseases. We previously identified cytoglobin, a hemoglobin homolog, with myogenic and cytoprotective roles in the vasculature. The
Externí odkaz:
https://doaj.org/article/e2ea6201c6364609aa8d71c26b37331d
Publikováno v:
Redox Biology, Vol 32, Iss , Pp - (2020)
Cytoglobin is an evolutionary ancient hemoglobin with poor functional annotation. Rather than constrained to penta coordination, cytoglobin's heme iron may exist either as a penta or hexacoordinated arrangement when exposed to different intracellular
Externí odkaz:
https://doaj.org/article/4644bbbfeae34ba7a8ae17b8f95debcd
Autor:
Clinton Mathai, Frances Jourd’heuil, Le Gia Cat Pham, Kurrim Gilliard, Joseph Balnis, Annie Jen, Katherine A. Overmyer, Joshua J Coon, Ariel Jatovich, Benoit Boivin, David Jourd’heuil
Publikováno v:
bioRxiv
The oxidant hydrogen peroxide serves as a signaling molecule that alters many aspects of cardiovascular functions. Recent studies suggest that cytoglobin – a hemoglobin expressed in the vasculature – may promote electron transfer reactions with p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d915a7377e55f06457fb2b6ac44cd7c0
https://europepmc.org/articles/PMC10081330/
https://europepmc.org/articles/PMC10081330/
Publikováno v:
Redox Biology
Redox Biology, Vol 32, Iss, Pp-(2020)
Redox Biology, Vol 32, Iss, Pp-(2020)
Cytoglobin is an evolutionary ancient hemoglobin with poor functional annotation. Rather than constrained to penta coordination, cytoglobin's heme iron may exist either as a penta or hexacoordinated arrangement when exposed to different intracellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::524484d8484321d814f793d66942989b
https://pubmed.ncbi.nlm.nih.gov/32087552
https://pubmed.ncbi.nlm.nih.gov/32087552
Publikováno v:
Nitric Oxide. 28:57-64
Recent studies indicate the formation of protein nitrosamines in vivo and tryptophan residues in proteins might represent important targets of nitrosative and oxidative stress. In the present work, we examined the mechanism by which xanthine oxidase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63c9f681e139c9d29b8a0d3b4e2bbbc0
https://doi.org/10.1016/j.niox.2012.10.004
https://doi.org/10.1016/j.niox.2012.10.004