Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase - Wikidata - wikimedia - TriplyDB

Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase

Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase

http://www.wikidata.org/entity/Q27681351

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X-ray Scattering Studies of Protein Structural Dynamics.The structural basis for the allosteric regulation of ribonucleotide reductase.LinkProt: a database collecting information about biological links.Evidence that the catenane form of CS2 hydrolase is not an artefact.Cellular Synthesis of Protein Catenanes.Allosteric Inhibition of Human Ribonucleotide Reductase by dATP Entails the Stabilization of a Hexamer.Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli.Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase.Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis.Targeting ribonucleotide reductase for cancer therapy.Catenanes: fifty years of molecular links.Natural supramolecular protein assemblies.Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.Diversity in Overall Activity Regulation of Ribonucleotide Reductase.A Solomon link through an interwoven molecular grid.Transmission electron microscopy enables the reconstruction of the catenane and ring forms of CS2 hydrolase.Self-Assembly of Catenanes from Lasso Peptides.Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains.Phylogenetic sequence analysis and functional studies reveal compensatory amino acid substitutions in loop 2 of human ribonucleotide reductase.Potent competitive inhibition of human ribonucleotide reductase by a nonnucleoside small molecule.3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound.Disruption of an oligomeric interface prevents allosteric inhibition of Escherichia coli class Ia ribonucleotide reductase.An endogenous dAMP ligand in Bacillus subtilis class Ib RNR promotes assembly of a noncanonical dimer for regulation by dATP.

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P2860

Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase

http://www.wikidata.org/entity/Q27681351

description

2012 nî lūn-bûn

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2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Tangled Up in Knots: Structure ...... ss Ia Ribonucleotide Reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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type

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Tangled Up in Knots: Structure ...... ss Ia Ribonucleotide Reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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Tangled Up in Knots: Structure ...... ss Ia Ribonucleotide Reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

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Tangled up in knots: structure ...... ss Ia ribonucleotide reductase

@en

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Catherine L Drennan

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

Christina M Zimanyi

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Edward J Brignole

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Francisco J Asturias

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Joanne Stubbe

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

Nozomi Ando

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P2860

Structure and function of the Escherichia coli ribonucleotide reductase protein R2

Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization

Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The BPTI decamer observed in acidic pH crystal forms pre-exists as a stable species in solution

Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase

Structure of ribonucleotide reductase protein R1

Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site

Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding

Phasercrystallographic software

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10.1016/J.STR.2012.05.009

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8

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Escherichia coli

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