Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit.
about
Evidence that the gamma-glutamyl cycle functions in vivo using intracellular glutathione: effects of amino acids and selective inhibition of enzymesTranslocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: glutathionuria after inhibition of transpeptidaseDiazo Compounds: Versatile Tools for Chemical BiologyStructural, functional, and clinical aspects of gamma-glutamyltransferase.Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase.Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit.Glutathione conjugates and their synthetic derivatives as inhibitors of glutathione-dependent enzymes involved in cancer and drug resistance.Mechanism of translational control by hemin in reticulocyte lysatesSelective inhibition of gamma-glutamyl-cycle enzymes by substrate analogs.Inactivation of renal gamma-glutamyl transferase by 6-diazo-5-oxo-L-norleucylglycine, an inactive precursor of affinity-labeling reagent.Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase.Translocation of glutathione from lymphoid cells that have markedly different gamma-glutamyl transpeptidase activitiesHigh-level expression of enzymatically active mature human gamma-glutamyltransferase in transgenic V79 Chinese hamster cells.gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties.Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilisInhibiting Glutathione Metabolism in Lung Lining Fluid as a Strategy to Augment Antioxidant Defense.Cloning and expression of a novel type (III) of human gamma-glutamyltransferase truncated mRNA.gamma-Glutamyltranspeptidase-catalysed acyl-transfer to the added acceptor does not proceed via the ping-pong mechanism.gamma-Glutamyltransferase is not involved in the bulk uptake of amino acids, peptides or gamma-glutamyl-amino acids in yeast (Saccharomyces cerevisiae).The effect of azaserine on glutamine uptake by rat renal brush-border membranes.The covalently bound diazo group as an infrared probe for hydrogen bonding environments.Structure of 6-diazo-5-oxo-norleucine-bound human gamma-glutamyl transpeptidase 1, a novel mechanism of inactivation.Processing of the propeptide form of rat renal gamma-glutamyltranspeptidase.
P2860
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P2860
Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit.
description
1977 nî lūn-bûn
@nan
1977 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի մարտին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年論文
@yue
1977年論文
@zh-hant
1977年論文
@zh-hk
1977年論文
@zh-mo
1977年論文
@zh-tw
1977年论文
@wuu
name
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@ast
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@en
type
label
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@ast
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@en
prefLabel
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@ast
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@en
P2860
P356
P1476
Affinity labeling of gamma-glu ...... ing site on the light subunit.
@en
P2093
P2860
P304
P356
10.1073/PNAS.74.3.931
P407
P577
1977-03-01T00:00:00Z