Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes. (Q30486705)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18728007%20AND%20SRC:MED&resulttype=core&format=json

12 January 2020

title

Tyrosine residues as redox cofactors in human hemoglobin: implications for engineering nontoxic blood substitutes (English)

1 reference

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12 January 2020

author

Radu Silaghi-Dumitrescu

3

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12 January 2020

Dimitri A Svistunenko

4

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12 January 2020

Chris E. Cooper

6

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12 January 2020

Brandon J Reeder

1

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12 January 2020

author name string

Marie Grey

2

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12 January 2020

Leif Bülow

5

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12 January 2020

Michael T Wilson

7

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12 January 2020

language of work or name

English

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publication date

26 August 2008

1 reference

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12 January 2020

number of pages

8

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Journal of Biological Chemistry

inferred from page(s)

published in

1 reference

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12 January 2020

volume

283

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12 January 2020

page(s)

30780-30787

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12 January 2020

issue

45

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Cell-free hemoglobin-based blood substitutes and risk of myocardial infarction and death: a meta-analysis

12 January 2020

cites work

1 reference

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First-generation blood substitutes: what have we learned? Biochemical and physiological perspectives

20 June 2018

1 reference

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Current status of oxygen carriers ('blood substitutes'): 2006.

20 June 2018

1 reference

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Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease States

20 June 2018

1 reference

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Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide

20 June 2018

1 reference

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A role for the myoglobin redox cycle in the induction of endothelial cell apoptosis

20 June 2018

1 reference

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

20 June 2018

1 reference

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Detection of ferryl myoglobin in the isolated ischemic rat heart

20 June 2018

1 reference

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Oxidative modification by low levels of HOOH can transform myoglobin to an oxidase

20 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662160

Hemoglobin M equon beta 41 (C7) phenylalanine leads to tyrosine

20 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662160

Redox equilibria of liganded forms of methemoglobin

20 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2662160

Toxicity of myoglobin and haemoglobin: oxidative stress in patients with rhabdomyolysis and subarachnoid haemorrhage.

20 June 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

The reaction of ascorbic acid with different heme iron redox states of myoglobin. Antioxidant and prooxidant aspects.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

Characteristics and mechanism of formation of peroxide-induced heme to protein cross-linking in myoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

A new sensitive assay reveals that hemoglobin is oxidatively modified in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

Desferrioxamine inhibits production of cytotoxic heme to protein cross-linked myoglobin: a mechanism to protect against oxidative stress without iron chelation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

Iron chelators can protect against oxidative stress through ferryl heme reduction.

21 January 2018

1 reference

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Tyrosine as a redox-active center in electron transfer to ferryl heme in globins.

21 January 2018

1 reference

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Autoreduction of ferryl myoglobin: discrimination among the three tyrosine and two tryptophan residues as electron donors

21 January 2018

1 reference

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Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

Hb(αα,ββ): A novel fusion construct for a dimeric, four-domain hemoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804709200

Enhanced lipid oxidation by oxidatively modified myoglobin: role of protein-bound heme

21 January 2018

1 reference

12 December 2020

Oxidation of myoglobin in isolated adult rat cardiac myocytes by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid

1 reference

12 December 2020

Site-directed mutagenesis in haemoglobin. Functional role of tyrosine-42(C7) alpha at the alpha 1-beta 2 interface

1 reference

12 December 2020

A hydrogen-donating monohydroxamate scavenges ferryl myoglobin radicals

1 reference

12 December 2020

The globin-based free radical of ferryl hemoglobin is detected in normal human blood

1 reference

12 December 2020

Increased lipid peroxidation in patients with rhabdomyolysis

1 reference

12 December 2020

Identifiers

DOI

10.1074/JBC.M804709200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18728007%20AND%20SRC:MED&resulttype=core&format=json

12 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18728007%20AND%20SRC:MED&resulttype=core&format=json

12 January 2020

1 reference