메뉴 건너뛰기




Volumn 31, Issue 1, 2013, Pages 2-3

Haptoglobin: The hemoglobin detoxifier in plasma

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE AREA; CLINICAL SETTINGS; COMPLEX FORMATIONS; OXIDATIVE TOXICITY; PLASMA PROTEIN; STRESS CONDITION; THERAPEUTIC BENEFITS;

EID: 84871699041     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2012.10.003     Document Type: Letter
Times cited : (66)

References (12)
  • 1
    • 79953794760 scopus 로고    scopus 로고
    • Blood aging, safety, and transfusion: capturing the "radical" menace
    • Buehler P.W., et al. Blood aging, safety, and transfusion: capturing the "radical" menace. Antioxid. Redox Signal. 2011, 14:1713-1738.
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1713-1738
    • Buehler, P.W.1
  • 2
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: can we tame haemoglobin?
    • Alayash A.I. Oxygen therapeutics: can we tame haemoglobin?. Nat. Rev. Drug Discov. 2004, 3:152-159.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 3
    • 70350441470 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers: current status and future directions
    • Silverman T.A., Weiskopf R.B. Hemoglobin-based oxygen carriers: current status and future directions. Anesthesiology 2009, 111:946-963.
    • (2009) Anesthesiology , vol.111 , pp. 946-963
    • Silverman, T.A.1    Weiskopf, R.B.2
  • 4
    • 33947494971 scopus 로고    scopus 로고
    • Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway
    • Jia Y., et al. Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway. J. Biol. Chem. 2007, 282:4894-4907.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4894-4907
    • Jia, Y.1
  • 5
    • 34548842263 scopus 로고    scopus 로고
    • Effects of endogenous ascorbate on oxidation, oxygenation and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig
    • Buehler P.W., et al. Effects of endogenous ascorbate on oxidation, oxygenation and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig. J. Pharm. Exp. Ther. 2007, 323:49-60.
    • (2007) J. Pharm. Exp. Ther. , vol.323 , pp. 49-60
    • Buehler, P.W.1
  • 6
    • 79952763426 scopus 로고    scopus 로고
    • Blood-brain barrier disruption and oxidative stress in guinea pig after systemic exposure to modified cell-free hemoglobin
    • Butt O.I. Blood-brain barrier disruption and oxidative stress in guinea pig after systemic exposure to modified cell-free hemoglobin. Am. J. Pathol. 2011, 178:1316-1328.
    • (2011) Am. J. Pathol. , vol.178 , pp. 1316-1328
    • Butt, O.I.1
  • 7
    • 84871708157 scopus 로고    scopus 로고
    • Haptoglobin binding stabilizes hemoglobin ferryl iron and globin radical on Tyrosine β-145
    • (in press)
    • Cooper, E.C. et al. Haptoglobin binding stabilizes hemoglobin ferryl iron and globin radical on Tyrosine β-145. Antioxid. Redox Signal. (in press).
    • Antioxid. Redox Signal.
    • Cooper, E.C.1
  • 8
    • 84865325486 scopus 로고    scopus 로고
    • Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions
    • Banerjee S., et al. Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions. Free Radic. Biol. Med. 2012, 53:1317-1326.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1317-1326
    • Banerjee, S.1
  • 9
    • 84866504266 scopus 로고    scopus 로고
    • Structure of the haptoglobin-haemoglobin complex
    • Andersen C.B., et al. Structure of the haptoglobin-haemoglobin complex. Nature 2012, 489:456-459.
    • (2012) Nature , vol.489 , pp. 456-459
    • Andersen, C.B.1
  • 10
    • 84871704284 scopus 로고    scopus 로고
    • Molecular modeling of the human hemoglobin-haptoglobin complex shed light on the protective mechanisms of haptoglobin
    • (in press)
    • Natasenamat, C. et al. Molecular modeling of the human hemoglobin-haptoglobin complex shed light on the protective mechanisms of haptoglobin. PLoS ONE (in press).
    • PLoS ONE
    • Natasenamat, C.1
  • 11
    • 33847749415 scopus 로고    scopus 로고
    • A unique loop extension of the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex
    • Nielson M.J., et al. A unique loop extension of the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex. J. Biol. Chem. 2007, 282:1072-1079.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1072-1079
    • Nielson, M.J.1
  • 12
    • 84859712543 scopus 로고    scopus 로고
    • Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in guinea pigs by haptoglobin therapy
    • Baek J.H., et al. Hemoglobin-driven pathophysiology is an in vivo consequence of the red blood cell storage lesion that can be attenuated in guinea pigs by haptoglobin therapy. J. Clin. Invest. 2012, 122:1444-1458.
    • (2012) J. Clin. Invest. , vol.122 , pp. 1444-1458
    • Baek, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.