(Q28749528)

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Protein modification by acrolein: formation and stability of cysteine adducts

scientific article (publication date: April 2009)

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Protein modification by acrolein: formation and stability of cysteine adducts (English)

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author name string

Jian Cai

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1

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Aruni Bhatnagar

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2

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William M Pierce

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3

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language of work or name

English

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publication date

April 2009

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published in

Chemical Research in Toxicology

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volume

22

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issue

4

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page(s)

708-16

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cites work

Acrolein is a major cigarette-related lung cancer agent: Preferential binding at p53 mutational hotspots and inhibition of DNA repair

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Kinetics and mechanism of protein tyrosine phosphatase 1B inactivation by acrolein

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Acrolein impairs ATP binding cassette transporter A1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I.

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Fluorine-18 radiolabeling of low-density lipoproteins: a potential approach for characterization and differentiation of metabolism of native and oxidized low-density lipoproteins in vivo.

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1,N2-deoxyguanosine adducts of acrolein, crotonaldehyde, and trans-4-hydroxynonenal cross-link to peptides via Schiff base linkage

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The molecular effects of acrolein

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Protein-bound acrolein: potential markers for oxidative stress

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Acrolein mercapturates: synthesis, characterization, and assessment of their role in the bladder toxicity of cyclophosphamide

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N(epsilon)-(3-methylpyridinium)lysine, a major antigenic adduct generated in acrolein-modified protein

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DNA interchain cross-links formed by acrolein and crotonaldehyde.

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Acrolein is a product of lipid peroxidation reaction. Formation of free acrolein and its conjugate with lysine residues in oxidized low density lipoproteins

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Kinetic analysis of the nonenzymatic glycosylation of hemoglobin

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12 December 2020

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PubMed publication ID

19231900

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ResearchGate publication ID

24029724

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(Q28749528)

Protein modification by acrolein: formation and stability of cysteine adducts

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