Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2

Analytical Biochemistry

Volumn 393, Issue 2, 2009, Pages 215-221

  Mecinović, Jasmin ^a   Chowdhury, Rasheduzzaman ^a   Flashman, Emily ^a   Schofield, Christopher J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Cysteine; Hypoxia; Mass spectrometry; Oxygen sensing; Prolyl hydroxylase domain 2; Protein modification

Indexed keywords

AMINO ACIDS; ELECTRODEPOSITION; ELECTROSPRAY IONIZATION; PARAMAGNETIC RESONANCE;

CYSTEINE; HYPOXIA; OXYGEN-SENSING; PROLYL HYDROXYLASE DOMAINS; PROTEIN MODIFICATIONS;

MASS SPECTROMETRY;

CYSTEINE; N ETHYLMALEIMIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE 2; THIOMESYLIC ACID METHYL ESTER; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTROSPRAY MASS SPECTROMETRY; MOLECULAR PROBE; NONHUMAN; OXYGEN SENSING; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MODIFICATION;

EID: 68349133481     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.06.029     Document Type: Article

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