about
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycleMalonate-bound structure of the glycerophosphodiesterase fromEnterobacter aerogenes(GpdQ) and characterization of the native Fe2+metal-ion preferenceThe organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysisPhosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacterBacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycleStructural and functional analysis of a FeoB A143S G5 loop mutant explains the accelerated GDP release rateCrystal structure of Mycobacterium tuberculosis ketol-acid reductoisomerase at 1.0 Å resolution - a potential target for anti-tuberculosis drug discoveryPurple acid phosphatases from bacteria: similarities to mammalian and plant enzymesBinuclear metal centers in plant purple acid phosphatases: Fe-Mn in sweet potato and Fe-Zn in soybeanIdentification of a non-purple tartrate-resistant acid phosphatase: an evolutionary link to Ser/Thr protein phosphatases?Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.The identification of new metallo-β-lactamase inhibitor leads from fragment-based screening.Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic rate of GDP release.The catalytic mechanisms of binuclear metallohydrolases.Product release is rate-limiting for catalytic processing by the Dengue virus proteaseBinuclear metallohydrolases: complex mechanistic strategies for a simple chemical reaction.Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes.The applications of binuclear metallohydrolases in medicine: recent advances in the design and development of novel drug leads for purple acid phosphatases, metallo-β-lactamases and arginases.X-ray absorption spectroscopy of dinuclear metallohydrolases.Catalytic mechanisms of metallohydrolases containing two metal ions.Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics.Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community.Progress toward inhibitors of metallo-β-lactamases.Unique spectral signatures of the nucleic acid dye acridine orange can distinguish cell death by apoptosis and necroptosis.Reaction mechanism of the metallohydrolase CpsB from Streptococcus pneumoniae, a promising target for novel antimicrobial agents.Mechanistic Insight from Calorimetric Measurements of the Assembly of the Binuclear Metal Active Site of Glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes.Highly efficient synthetic iron-dependent nucleases activate both intrinsic and extrinsic apoptotic death pathways in leukemia cancer cells.Electronic structure and spectro-structural correlations of Fe(III)Zn(II) biomimetics for purple acid phosphatases: relevance to DNA cleavage and cytotoxic activity.Ca(II) Binding Regulates and Dominates the Reactivity of a Transition-Metal-Ion-Dependent Diesterase from Mycobacterium tuberculosis.The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysisIron, copper, and manganese complexes with in vitro superoxide dismutase and/or catalase activities that keep Saccharomyces cerevisiae cells alive under severe oxidative stress.Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site.A GTPase chimera illustrates an uncoupled nucleotide affinity and release rate, providing insight into the activation mechanism.Electronic structure analysis of the dinuclear metal center in the bioremediator glycerophosphodiesterase (GpdQ) from Enterobacter aerogenes.The bioremediator glycerophosphodiesterase employs a non-processive mechanism for hydrolysis.Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis.Immobilization of the enzyme GpdQ on magnetite nanoparticles for organophosphate pesticide bioremediation.Rapid-freeze-quench magnetic circular dichroism of intermediate X in ribonucleotide reductase: new structural insight.Reactivity of M(II) metal-substituted derivatives of pig purple acid phosphatase (uteroferrin) with phosphate.Spectroscopic and catalytic characterization of a functional Fe(III)Fe(II) biomimetic for the active site of uteroferrin and protein cleavage.
P50
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P50
description
hulumtues
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gary Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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Gerhard Schenk
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P106
P1960
osWYIgkAAAAJ
P21
P31
P496
0000-0001-8619-0631