Using tandem mass spectrometry to quantify site-specific chlorination and nitration of proteins: model system studies with high-density lipoprotein oxidized by myeloperoxidase. (Q37142318)

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scientific article published on January 2008

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English	Using tandem mass spectrometry to quantify site-specific chlorination and nitration of proteins: model system studies with high-density lipoprotein oxidized by myeloperoxidase.	scientific article published on January 2008

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scholarly article

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6 January 2020

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Europe PubMed Central

Using tandem mass spectrometry to quantify site-specific chlorination and nitration of proteins: model system studies with high-density lipoprotein oxidized by myeloperoxidase (English)

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6 January 2020

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mass spectrometry

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6 January 2020

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Jay W Heinecke

2

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6 January 2020

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1 January 2008

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6 January 2020

Methods in Enzymology

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6 January 2020

440

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6 January 2020

33-63

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6 January 2020

Mass spectrometry-based proteomics

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Oxidative chemistry of peroxynitrite

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Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein

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The structure of apolipoprotein A-I in high density lipoproteins.

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Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils

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Assessment of chlorination by human neutrophils

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Myeloperoxidase produces nitrating oxidants in vivo

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Hypochlorite-induced oxidation of amino acids, peptides and proteins.

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Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation

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3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima

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Oxidants and antioxidants in the pathogenesis of atherosclerosis: implications for the oxidized low density lipoprotein hypothesis

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Large-scale purification of myeloperoxidase from HL60 promyelocytic cells: characterization and comparison to human neutrophil myeloperoxidase

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Identifiers

10.1016/S0076-6879(07)00803-8

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18423210%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18423210%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

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