The Penultimate Tyrosine Residues are Critical for the Genotoxic Effect of Human Hemoglobin.

about

The Penultimate Tyrosine Residues are Critical for the Genotoxic Effect of Human Hemoglobin.

Item

http://www.wikidata.org/entity/Q52763305

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@en

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@nl

type

Item

label

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@en

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@nl

prefLabel

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@en

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@nl

P1476

The Penultimate Tyrosine Resid ...... ic Effect of Human Hemoglobin.

@en

P2093

Kisan Kodam

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

Leif Bülow

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

Sandeep Chakane

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

Vijay Markad

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

P2860

A simple technique for quantitation of low levels of DNA damage in individual cells

Updates of the HbVar database of human hemoglobin variants and thalassemia mutations.

Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes.

Dynamics of allostery in hemoglobin: roles of the penultimate tyrosine H bonds.

A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure.

Haptoglobin binding stabilizes hemoglobin ferryl iron and the globin radical on tyrosine β145

Pathological conditions involving extracellular hemoglobin: molecular mechanisms, clinical significance, and novel therapeutic opportunities for α(1)-microglobulin.

Trapping of human hemoglobin by haptoglobin: molecular mechanisms and clinical applications.

Redox reactions of hemoglobin: mechanisms of toxicity and control.

Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical.

P304

351-357

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

P31

scholarly article

P356

10.1007/978-3-319-55231-6_46

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

P407

English

P478

977

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

P577

2017-01-01T00:00:00Z

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

P698

28685465

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