An artificial di-iron oxo-protein with phenol oxidase activity. - Wikidata - awgldk - TriplyDB

An artificial di-iron oxo-protein with phenol oxidase activity.

An artificial di-iron oxo-protein with phenol oxidase activity.

http://www.wikidata.org/entity/Q37254936

about

Computational enzyme design approaches with significant biological outcomes: progress and challenges Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Protein design: toward functional metalloenzymes Design of a switchable eliminase Human carbonic anhydrase II as a host for piano-stool complexes bearing a sulfonamide anchor Hydrolytic catalysis and structural stabilization in a designed metalloprotein Crystal Structure, Exogenous Ligand Binding, and Redox Properties of an Engineered Diiron Active Site in a Bacterial Hemerythrin H 2 O 2 -dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin A designed supramolecular protein assembly with in vivo enzymatic activity Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure Designed metalloprotein stabilizes a semiquinone radical Computational protein engineering: bridging the gap between rational design and laboratory evolution.The accommodation index measures the perturbation associated with insertions and deletions in coiled-coils: Application to understand signaling in histidine kinases.Biomimetic peptide-based models of [FeFe]-hydrogenases: utilization of phosphine-containing peptides.Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions.Engineering of biocatalysts - from evolution to creation.Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.An automated flow for directed evolution based on detection of promiscuous scaffolds using spatial and electrostatic properties of catalytic residues.A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues Design of a three-helix bundle capable of binding heavy metals in a triscysteine environment.Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.OptZyme: computational enzyme redesign using transition state analogues Covalent Anchor Positions Play an Important Role in Tuning Catalytic Properties of a Rationally Designed MnSalen-containing Metalloenzyme Light-driven oxygen production from superoxide by Mn-binding bacterial reaction centers.Design and engineering of a man-made diffusive electron-transport protein Shaping quaternary assemblies of water-soluble non-peptide helical foldamers by sequence manipulation.Catalysis by a de novo zinc-mediated protein interface: implications for natural enzyme evolution and rational enzyme engineering.Designing a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coils Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.Designing functional metalloproteins: from structural to catalytic metal sites.Computational design of protein-ligand interfaces: potential in therapeutic development.Constructing manmade enzymes for oxygen activation.De novo design of functional proteins: Toward artificial hydrogenases.Design and engineering of artificial oxygen-activating metalloenzymes.Alteration of the oxygen-dependent reactivity of de novo Due Ferri proteins.Designed multi-stranded heme binding β-sheet peptides in membrane.De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.Computational design of a self-assembling β-peptide oligomer.A de novo designed metalloenzyme for the hydration of CO2.Directed evolution induces tributyrin hydrolysis in a virulence factor of Xylella fastidiosa using a duplicated gene as a template.

P2860

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P2860

An artificial di-iron oxo-protein with phenol oxidase activity.

http://www.wikidata.org/entity/Q37254936

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

An artificial di-iron oxo-protein with phenol oxidase activity.

@en

An artificial di-iron oxo-protein with phenol oxidase activity.

@nl

type

label

An artificial di-iron oxo-protein with phenol oxidase activity.

@en

An artificial di-iron oxo-protein with phenol oxidase activity.

@nl

prefLabel

An artificial di-iron oxo-protein with phenol oxidase activity.

@en

An artificial di-iron oxo-protein with phenol oxidase activity.

@nl

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P1433

Nature Chemical Biology

P1476

An artificial di-iron oxo-protein with phenol oxidase activity.

@en

P2093

Concetta Andreozzi

http://www.w3.org/2001/XMLSchema#string

Flavia Nastri

http://www.w3.org/2001/XMLSchema#string

Marina Faiella

http://www.w3.org/2001/XMLSchema#string

Ornella Maglio

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Rafael Torres Martin de Rosales

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Vincenzo Pavone

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P2860

De novo computational design of retro-aldol enzymes

Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins

Sliding helix and change of coordination geometry in a model di-MnII protein

Preorganization of molecular binding sites in designed diiron proteins

Kemp elimination catalysts by computational enzyme design

New insight into the structure and function of the alternative oxidase

Membrane-bound diiron carboxylate proteins

Synthetic models of the active site of catechol oxidase: mechanistic studies

Protein design: a hierarchic approach.

Engineering novel metalloproteins: design of metal-binding sites into native protein scaffolds.

P2888

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882-884

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scholarly article

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10.1038/NCHEMBIO.257

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12

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5

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Angela Lombardi

William DeGrado

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2009-11-08T00:00:00Z

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38091457

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1041249755

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19915535

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3808167

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