Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Robyn G. Midwinter"'
Autor:
Stuart T. Fraser, Robyn G. Midwinter, Lucy A. Coupland, Stephanie Kong, Birgit S. Berger, Jia Hao Yeo, Osvaldo Cooley Andrade, Deborah Cromer, Cacang Suarna, Magda Lam, Ghassan J. Maghzal, Beng H. Chong, Christopher R. Parish, Roland Stocker
Publikováno v:
Haematologica, Vol 100, Iss 5 (2015)
Heme oxygenase-1 is critical for iron recycling during red blood cell turnover, whereas its impact on steady-state erythropoiesis and red blood cell lifespan is not known. We show here that in 8- to 14-week old mice, heme oxygenase-1 deficiency adver
Externí odkaz:
https://doaj.org/article/a784017e99d7465b947593a790120954
Publikováno v:
Advances in Hematology, Vol 2011 (2011)
The first mature cells to arise in the developing mammalian embryo belong to the erythroid lineage. This highlights the immediacy of the need for red blood cells during embryogenesis and for survival. Linked with this pressure is the necessity of the
Externí odkaz:
https://doaj.org/article/b4af3104f0f34a8e990d86bd894f5063
Autor:
James Cantley, Robyn G. Midwinter, Kim H. Chan, Weiyu Chen, Anita Ayer, Ghassan J. Maghzal, Stephanie M.Y. Kong, Louise L. Dunn, Martin K.C. Ng, Roland Stocker, Sergey Tumanov
Publikováno v:
Arteriosclerosis, thrombosis, and vascular biology. 41(1)
Objective: Hmox1 (heme oxygenase-1) is a stress-induced enzyme that catalyzes the degradation of heme to carbon monoxide, iron, and biliverdin. Induction of Hmox1 and its products protect against cardiovascular disease, including ischemic injury. Hmo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00ef5b0a5ed20e9680db4f96b4c82120
https://pubmed.ncbi.nlm.nih.gov/33207934
https://pubmed.ncbi.nlm.nih.gov/33207934
Autor:
Robyn G. Midwinter, Deborah Cromer, Roland Stocker, Ghassan J. Maghzal, Christopher R. Parish, Birgit S. Berger, Beng H. Chong, Osvaldo Cooley Andrade, Stuart T. Fraser, Lucy A. Coupland, Magdalena Lam, Cacang Suarna, Stephanie M.Y. Kong, Jia Hao Yeo
Publikováno v:
Haematologica. 100:601-610
Heme oxygenase-1 is critical for iron recycling during red blood cell turnover, whereas its impact on steady-state erythropoiesis and red blood cell lifespan is not known. We show here that in 8- to 14-week old mice, heme oxygenase-1 deficiency adver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c07db6b3a0b5d0ca8edc9e9c187ccc86
https://doi.org/10.3324/haematol.2014.116368
https://doi.org/10.3324/haematol.2014.116368
Autor:
Hafizah A. Hamid, Robyn G. Midwinter, Louise L. Dunn, Jun Ni, Christopher R. Parish, Roland Stocker
Publikováno v:
Antioxidants & Redox Signaling. 20:1723-1742
Significance: Heme oxygenase-1 (HMOX1) plays a critical role in the protection of cells, and the inducible enzyme is implicated in a spectrum of human diseases. The increasing prevalence of cardiovascular and metabolic morbidities, for which current
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23c85bb3e442737b5e99db8f53e332bd
https://doi.org/10.1089/ars.2013.5675
https://doi.org/10.1089/ars.2013.5675
Autor:
Levon M. Khachigian, Hong Cai, Ghassan J. Maghzal, Ben J. Wu, Valerian E. Kagan, Lan-Feng Dong, Alexandr A. Kapralov, Yulia Y. Tyurina, Robyn G. Midwinter, Roland Stocker, Jiri Neuzil, Natalia A. Belikova, Joanne M. Dennis
Publikováno v:
Free Radical Biology and Medicine. 52:871-879
Probucol inhibits the proliferation of vascular smooth muscle cells in vitro and in vivo, and the drug reduces intimal hyperplasia and atherosclerosis in animals via induction of heme oxygenase-1 (HO-1). Because the succinyl ester of probucol, succin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d22d2203811a7c0d0fc2c01db20468ee
https://doi.org/10.1016/j.freeradbiomed.2011.11.029
https://doi.org/10.1016/j.freeradbiomed.2011.11.029
Publikováno v:
Free Radical Biology and Medicine. 38:397-405
Hypochlorous acid formed by activated neutrophils reacts with amines to produce chloramines. Chloramines vary in stability, reactivity, and cell permeability. We have examined whether chloramine exchange occurs between physiologically important amine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3bb8fde1ef4eaac3490d5d74d525c95
https://doi.org/10.1016/j.freeradbiomed.2004.11.006
https://doi.org/10.1016/j.freeradbiomed.2004.11.006
Extracellular Oxidation by Taurine Chloramine Activates ERK via the Epidermal Growth Factor Receptor
Publikováno v:
Journal of Biological Chemistry. 279:32205-32211
Taurine is present in high concentrations in neutrophils, and when the cells are stimulated taurine can react with hypochlorous acid (HOCl) to form taurine-chloramine (Tau-Cl). This compound retains oxidant activity and can affect the neutrophil itse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0343fe19f4a5c2587f3c24507442621
https://doi.org/10.1074/jbc.m402070200
https://doi.org/10.1074/jbc.m402070200
Publikováno v:
Advances in Hematology, Vol 2011 (2011)
Advances in Hematology
Advances in Hematology
The first mature cells to arise in the developing mammalian embryo belong to the erythroid lineage. This highlights the immediacy of the need for red blood cells during embryogenesis and for survival. Linked with this pressure is the necessity of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56810a5ac3506bdea6b0e3427c579b7c
https://doaj.org/article/b4af3104f0f34a8e990d86bd894f5063
https://doaj.org/article/b4af3104f0f34a8e990d86bd894f5063
Autor:
Konstanze Beck, Ben J. Wu, Carlos Cassano, Jennifer R. Gamble, Robyn G. Midwinter, Roland Stocker, Dechaboon (Bernie) Changsiri, Yutang Wang
Publikováno v:
Arteriosclerosis, thrombosis, and vascular biology. 29(10)
Objectives— Induction of heme oxygenase-1 (HO-1) protects against atherosclerotic disease in part by promoting reendothelialization. As endothelial progenitor cells (EPCs) contribute to reendothelialization, we examined the role of HO-1 on bone mar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca3ae961f3c8b16806efd5652d93b5b4
https://pubmed.ncbi.nlm.nih.gov/19542024
https://pubmed.ncbi.nlm.nih.gov/19542024