Kidney Dysfunction : Excessive use of glutathione, especially in IV form, can strain the kidneys
Peptides can interfere with microbial growth and complement the bodys defense mechanism against infections (Nabti et al
The K122 loop of wild-type PTPN2 adopts a completely different conformation C216S - phosphatase-dead mutant of TCPTP C227S - site-directed mutagenesis, catalytically inactive mutant comprising residues 1-294, specific interaction between the Lyp substrate-trapping mutant and SKAP-HOM C231S - phosphatase-dead mutant of PEST C258M - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition C270A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C270S inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C270S/T106D inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) C377S catalytically inactive Cdc25C C433S - phosphatase-dead mutant of PTPalpha C455S crystallization data C459S - substrate-trapping mutant of SHP2 C473D active site mutant, weak substrate affinity and dissociates rapidly C473S strong substrate affinity and dissociates slowly C488S catalytically inactive Cdc25B C92A site-directed mutagenesis, affects inhibition by abietic acid and 2-[(carboxycarbonyl)amino]-4,5,6,7-tetrahydro-thieno[2,3-c]-pyridine-3-carboxylic acid C945S - site-directed mutagenesis of the essential cysteine residue to a serine in the islet cell antigen-related PTP results in the expression of the intracellular region which does not catalyze hydrolysis of 4-nitrophenyl phosphate D195A/C227S - optimized substrate-trap mutant, used for identification of physiological enzyme substrates D236A substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 420fold reduced activity compared to the wild type enzyme D236A/C270A/Q314A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) D236A/C270S/Q314A inactive, substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339) D236A/Q314A substrate-trapping mutant of the HePTP catalytic domain (HePTP residues 44-339), shows 1255fold reduced activity compared to the wild type enzyme D284A - catalytically inactive, no significant effect on proliferation in human umbilical vein endothelial cells D48N - isoform PTP1B, mutation turns 1B isoform to PTPalpha-like enzyme in substrate recognition D61G - the mutation causes hyperactivation of the SHP2 catalytic activity D811A/C842S site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B D811A/H812F/C842S/M883G site-directed mutagenesis, analysis of binding structure of substrate Eps15846-854 compared to wild-type enzyme and enzyme PTP1B
Cholesterol stimulates the cellular uptake of L-carnitine by the carnitine/organic cation transporter novel 2 (OCTN2)
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