Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
about
5-hydroxymethyl-2-furfural modifies intracellular sickle haemoglobin and inhibits sickling of red blood cellsTherapeutic strategies to alter the oxygen affinity of sickle hemoglobin.Crystallographic analysis of human hemoglobin elucidates the structural basis of the potent and dual antisickling activity of pyridyl derivatives of vanillin.X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin.New developments in anti-sickling agents: can drugs directly prevent the polymerization of sickle haemoglobin in vivo?Pharmacokinetics and pharmacodynamics of tucaresol, an antisickling agent, in healthy volunteers.Anti-sickling effect of MX-1520, a prodrug of vanillin: an in vivo study using rodents.Discovery of GBT440, an Orally Bioavailable R-State Stabilizer of Sickle Cell Hemoglobin.Sickle hemoglobin oxygen affinity-shifting strategies have unequal cerebrovascular risks.
P2860
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P2860
Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
@en
type
label
Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
@en
prefLabel
Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
@en
P2093
P2860
P356
P1433
P1476
Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
@en
P2093
P2860
P304
P356
10.1042/BJ2390387
P407
P577
1986-10-01T00:00:00Z