Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation. [electronic resource]
Producer: 20050225Description: 55051-9 p. digitalISSN:- 0021-9258
- Alanine -- chemistry
- Amino Acid Motifs
- Animals
- Azetidinecarboxylic Acid -- chemistry
- Baculoviridae -- metabolism
- Cell Line
- Chromatography, Liquid
- Culture Media, Serum-Free -- pharmacology
- Glutamic Acid -- chemistry
- Humans
- Hydroxylation
- Hypoxia-Inducible Factor 1, alpha Subunit
- Insecta
- Ketoglutaric Acids -- chemistry
- Kinetics
- Leucine -- chemistry
- Mass Spectrometry
- Methionine -- chemistry
- Models, Chemical
- Peptides -- chemistry
- Procollagen-Proline Dioxygenase -- chemistry
- Proline -- analogs & derivatives
- Protein Structure, Tertiary
- Substrate Specificity
- Time Factors
- Transcription Factors -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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