Structure and heme environment of beef liver catalase at 2.5 A resolution.
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The structure and peroxidase activity of a 33-kDa catalase-related protein fromMycobacterium aviumssp.paratuberculosisInteraction of nitric oxide with catalase: structural and kinetic analysis.Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosaStructure of the monofunctional heme catalase DR1998 from Deinococcus radioduransThe NADPH binding site on beef liver catalaseRedox control of asthma: molecular mechanisms and therapeutic opportunities.Nitric oxide blocks cellular heme insertion into a broad range of heme proteinsTemporal variation for the expression of catalase in Drosophila melanogaster: correlations between rates of enzyme synthesis and levels of translatable catalase-messenger RNAAttractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria.Electron crystallography of ultrathin 3D protein crystals: atomic model with chargesAntioxidant responses to oxidant-mediated lung diseases.Arg354 in the catalytic centre of bovine liver catalase is protected from methylglyoxal-mediated glycation.Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicidaMössbauer and electron paramagnetic resonance studies of chloroperoxidase following mechanism-based inactivation with allylbenzeneNovel insights in mammalian catalase heme maturation: effect of NO and thioredoxin-1.The impact of transition metals on bacterial plant disease.Biological and physiological role of reactive oxygen species--the good, the bad and the ugly.Cloning and disruption of the antigenic catalase gene of Aspergillus fumigatus.Role of the conserved distal heme asparagine of coral allene oxide synthase (Asn137) and human catalase (Asn148): mutations affect the rate but not the essential chemistry of the enzymatic transformations.The grid sectioning technique: a study of catalase platelets.NADPH binding and control of catalase compound II formation: comparison of bovine, yeast, and Escherichia coli enzymes.Failure of benzene and phenol to serve as substrates for the peroxidatic action of catalase.Proteome wide identification of iron binding proteins of Xanthomonas translucens pv. undulosa: focus on secretory virulent proteins.Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach.Investigation on the interaction of catalase with sodium lauryl sulfonate and the underlying mechanisms.Comparison of the toxicity of the dyes Sudan II and Sudan IV to catalase.Iron chelators inhibit the heme-degradation reaction by HutZ from Vibrio cholerae.The in Vivo and in Vitro Inhibition of Catalase from Leaves of Nicotiana sylvestris by 3-Amino-1,2,4-Triazole.Fuel Cell Cathode Catalyst with Heme-Like Structure Formed from Nitrogen of Glycine and Iron
P2860
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P2860
Structure and heme environment of beef liver catalase at 2.5 A resolution.
description
1981 nî lūn-bûn
@nan
1981 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
name
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@ast
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@en
type
label
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@ast
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@en
prefLabel
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@ast
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@en
P2093
P2860
P356
P1476
Structure and heme environment of beef liver catalase at 2.5 A resolution.
@en
P2093
P2860
P304
P356
10.1073/PNAS.78.8.4767
P407
P577
1981-08-01T00:00:00Z