about
The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactionsRaman spectroscopy differentiates squamous cell carcinoma (SCC) from normal skin following treatment with a high-powered CO2 laser.Solid-phase synthesis, characterization, and cellular activities of collagen-model nanodiamond-peptide conjugatesAmmonium catalyzed cyclitive additions: evidence for a cation-π interaction with alkynes.Human indoleamine 2,3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide.Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization.Role of indoleamine 2,3-dioxygenase in health and disease.A continuous spectrophotometric assay and nonlinear kinetic analysis of methionine γ-lyase catalysis.Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ(1-23) using an unnatural amino acid.Oxidized lipid accumulates in the presence of alpha-tocopherol in atherosclerosis.Vitamin E oxidation in human atherosclerotic lesions.Peptide detection and structure determination in live cells using confocal Raman microscopy.Label-Free Confocal Raman Mapping of Transportan in Melanoma Cells.Post-translational Regulation of Human Indoleamine 2,3-Dioxygenase Activity by Nitric OxideHuman Indoleamine 2,3-Dioxygenase 1 Is an Efficient Mammalian Nitrite Reductase
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P50
description
researcher ORCID ID = 0000-0001-6137-8275
@en
wetenschapper
@nl
name
Andrew C Terentis
@ast
Andrew C Terentis
@en
Andrew C Terentis
@es
Andrew C Terentis
@nl
type
label
Andrew C Terentis
@ast
Andrew C Terentis
@en
Andrew C Terentis
@es
Andrew C Terentis
@nl
prefLabel
Andrew C Terentis
@ast
Andrew C Terentis
@en
Andrew C Terentis
@es
Andrew C Terentis
@nl
P1153
6602563779
P31
P496
0000-0001-6137-8275