Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

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Coexpression of human alpha- and circularly permuted beta-globins yields a hemoglobin with normal R state but modified T state properties

P2860

Q37301645-0D61FDEF-B47B-4209-8749-EB998D4E3570

P2860

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

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http://www.wikidata.org/entity/Q36639420

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2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

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@zh-cn

name

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@ast

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

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type

Item

label

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@ast

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@en

prefLabel

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@ast

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@en

P1476

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

@en

P2093

Alexandru Babes

http://www.w3.org/2001/XMLSchema#string

Claude Poyart

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Donald J Abraham

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Laurent Kiger

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Marion Cabanes-Macheteau

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Martin K Safo

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Michael C Marden

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Nathalie Griffon

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Telih Boyiri

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P2860

A human recombinant haemoglobin designed for use as a blood substitute

Fixation of the quaternary structures of human adult haemoglobin by encapsulation in transparent porous silica gels.

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

Oxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids.

HbXL99 alpha: a hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute.

Oxygen delivery and autoxidation of hemoglobin.

Tetramer-dimer equilibrium of oxyhemoglobin mutants determined from auto-oxidation rates.

Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin.

Dependence of the quantum efficiency for photolysis of carboxyhemoglobin on the degree of ligation.

X-ray diffraction study of the binding of the antisickling agent 12C79 to human hemoglobin.

P304

1376-1383

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P31

scholarly article

P356

10.1110/PS.4880102

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P478

http://www.w3.org/2001/XMLSchema#string

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2002-06-01T00:00:00Z

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11351299

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12021436

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P932

2373633

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Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

about

P2860

P2860

Control of the allosteric equilibrium of hemoglobin by cross-linking agents.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932