Oxidative stress and antioxidants in beta-thalassemia/hemoglobin E. 1987

K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
Department of Biochemistry, Siriraj Hospital, Mahidol University, Bangkok, Thailand.

UI MeSH Term Description Entries
D008315 Malondialdehyde The dialdehyde of malonic acid. Malonaldehyde,Propanedial,Malonylaldehyde,Malonyldialdehyde,Sodium Malondialdehyde,Malondialdehyde, Sodium
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D005979 Glutathione Peroxidase An enzyme catalyzing the oxidation of 2 moles of GLUTATHIONE in the presence of HYDROGEN PEROXIDE to yield oxidized glutathione and water. Cytosolic Glutathione Peroxidase,Glutathione Lipoperoxidase,Selenoglutathione Peroxidase,Glutathione Peroxidase, Cytosolic,Lipoperoxidase, Glutathione,Peroxidase, Glutathione,Peroxidase, Selenoglutathione
D006446 Hemoglobin E An abnormal hemoglobin that results from the substitution of lysine for glutamic acid at position 26 of the beta chain. It is most frequently observed in southeast Asian populations.
D006455 Hemoglobins, Abnormal Hemoglobins characterized by structural alterations within the molecule. The alteration can be either absence, addition or substitution of one or more amino acids in the globin part of the molecule at selected positions in the polypeptide chains. Abnormal Hemoglobins
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D013482 Superoxide Dismutase An oxidoreductase that catalyzes the reaction between SUPEROXIDES and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. Hemocuprein,Ag-Zn Superoxide Dismutase,Cobalt Superoxide Dismutase,Cu-Superoxide Dismutase,Erythrocuprein,Fe-Superoxide Dismutase,Fe-Zn Superoxide Dismutase,Iron Superoxide Dismutase,Manganese Superoxide Dismutase,Mn-SOD,Mn-Superoxide Dismutase,Ag Zn Superoxide Dismutase,Cu Superoxide Dismutase,Dismutase, Ag-Zn Superoxide,Dismutase, Cobalt Superoxide,Dismutase, Cu-Superoxide,Dismutase, Fe-Superoxide,Dismutase, Fe-Zn Superoxide,Dismutase, Iron Superoxide,Dismutase, Manganese Superoxide,Dismutase, Mn-Superoxide,Dismutase, Superoxide,Fe Superoxide Dismutase,Fe Zn Superoxide Dismutase,Mn SOD,Mn Superoxide Dismutase,Superoxide Dismutase, Ag-Zn,Superoxide Dismutase, Cobalt,Superoxide Dismutase, Fe-Zn,Superoxide Dismutase, Iron,Superoxide Dismutase, Manganese
D013789 Thalassemia A group of hereditary hemolytic anemias in which there is decreased synthesis of one or more hemoglobin polypeptide chains. There are several genetic types with clinical pictures ranging from barely detectable hematologic abnormality to severe and fatal anemia. Thalassemias

Related Publications

K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
January 2000, Journal of pediatric hematology/oncology,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
January 2013, PloS one,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
February 2003, Free radical research,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
April 1985, Australian and New Zealand journal of medicine,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
April 1997, Indian pediatrics,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
April 2023, Hematology/oncology clinics of North America,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
April 2005, Indian pediatrics,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
June 1998, Annals of the New York Academy of Sciences,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
April 2012, Blood reviews,
K Suthipark, and S Ong-ajyooth, and D Shumnumsirivath, and A Likidlilid, and S Fucharoen, and C Siddhikol, and P Pootrakul, and B Niyomporn
January 1987, Birth defects original article series,
Copied contents to your clipboard!