Identification of human glutaminyl cyclase as a metalloenzyme. Potent inhibition by imidazole derivatives and heterocyclic chelators
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Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.Human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active siteStructure of glutaminyl cyclase fromDrosophila melanogasterin space groupI4Structural and functional analyses of a glutaminyl cyclase from Ixodes scapularis reveal metal-independent catalysis and inhibitor bindingSoluble variants of human recombinant glutaminyl cyclasePurification and Characterization of Recombinant N-Terminally Pyroglutamate-Modified Amyloid-β Variants and Structural Analysis by Solution NMR SpectroscopyNatural Products from Microalgae with Potential against Alzheimer's Disease: Sulfolipids Are Potent Glutaminyl Cyclase Inhibitors.Probing secondary glutaminyl cyclase (QC) inhibitor interactions applying an in silico-modeling/site-directed mutagenesis approach: implications for drug development.Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution.Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions.Pyroglutamate amyloid-β (Aβ): a hatchet man in Alzheimer diseaseThe isoenzyme of glutaminyl cyclase is an important regulator of monocyte infiltration under inflammatory conditions.Identification of potential glutaminyl cyclase inhibitors from lead-like libraries by in silico and in vitro fragment-based screening.Peptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function.Signaling from the secretory granule to the nucleus.Peripheral blood gene expression profiling in rheumatoid arthritis.High-level expression, purification, and characterization of Staphylococcus aureus dihydroorotase (PyrC) as a cleavable His-SUMO fusion.Mammalian glutaminyl cyclases and their isoenzymes have identical enzymatic characteristics.Structural and functional investigation into acetyl-coenzyme A synthase and methyltransferase from human pathogen Clostridium difficile.Pronounced influence of pH, metal-ion and solvent isotope on the thermoresponse of synthetic amphiphilic polypeptides
P2860
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P2860
Identification of human glutaminyl cyclase as a metalloenzyme. Potent inhibition by imidazole derivatives and heterocyclic chelators
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Identification of human glutam ...... ves and heterocyclic chelators
@ast
Identification of human glutam ...... ves and heterocyclic chelators
@en
Identification of human glutam ...... ves and heterocyclic chelators
@nl
type
label
Identification of human glutam ...... ves and heterocyclic chelators
@ast
Identification of human glutam ...... ves and heterocyclic chelators
@en
Identification of human glutam ...... ves and heterocyclic chelators
@nl
prefLabel
Identification of human glutam ...... ves and heterocyclic chelators
@ast
Identification of human glutam ...... ves and heterocyclic chelators
@en
Identification of human glutam ...... ves and heterocyclic chelators
@nl
P2093
P2860
P50
P356
P1476
Identification of human glutam ...... ves and heterocyclic chelators
@en
P2093
André J Niestroj
Katrin Zunkel
Michael Wermann
Stephan Schilling
Torsten Hoffmann
P2860
P304
P356
10.1074/JBC.M309077200
P407
P577
2003-12-12T00:00:00Z