Heme-albumin: an honorary enzyme. - Wikidata - awgldk - TriplyDB

Heme-albumin: an honorary enzyme.

Heme-albumin: an honorary enzyme.

http://www.wikidata.org/entity/Q42268220

about

Absorbance and redox based approaches for measuring free heme and free hemoglobin in biological matrices.

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P2860

Heme-albumin: an honorary enzyme.

http://www.wikidata.org/entity/Q42268220

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Heme-albumin: an honorary enzyme.

@en

Heme-albumin: an honorary enzyme.

@nl

type

label

Heme-albumin: an honorary enzyme.

@en

Heme-albumin: an honorary enzyme.

@nl

prefLabel

Heme-albumin: an honorary enzyme.

@en

Heme-albumin: an honorary enzyme.

@nl

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Cell Death and Disease

P1476

Heme-albumin: an honorary enzyme.

@en

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A di Masi

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G Fanali

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P Ascenzi

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P2860

Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin

Heme-based catalytic properties of human serum albumin

Functional role of transient conformations: Rediscovering "chronosteric effects" thirty years later

Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation

The five-to-six-coordination transition of ferric human serum heme-albumin is allosterically-modulated by ibuprofen and warfarin: a combined XAS and MD study

Artificial oxygen carriers, hemoglobin vesicles and albumin-hemes, based on bioconjugate chemistry.

Human serum albumin: from bench to bedside.

Enzymatic properties of human hemalbumin.

Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation.

Warfarin modulates the nitrite reductase activity of ferrous human serum heme-albumin.

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e1895

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scholarly article

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10.1038/CDDIS.2015.287

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6

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2015-10-08T00:00:00Z

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