The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor. - Wikidata - wikimedia - TriplyDB

The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor.

The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor.

http://www.wikidata.org/entity/Q33564100

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Structural and energetic basis of allostery The ensemble nature of allostery Transcriptional Repression Mediated by a TetR Family Protein, PfmR, from Thermus thermophilus HB8 The crystal structure of the TetR family transcriptional repressor SimR bound to DNA and the role of a flexible N-terminal extension in minor groove binding Structural Requirements for Cooperativity in Ileal Bile Acid-binding Proteins Structural activation of the transcriptional repressor EthR from Mycobacterium tuberculosis by single amino acid change mimicking natural and synthetic ligands Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2)Modular organisation of inducer recognition and allostery in the tetracycline repressor Mechanism of Iron-Dependent Repressor (IdeR) Activation and DNA Binding: A Molecular Dynamics and Protein Structure Network Study Regulating transcription regulators via allostery and flexibility Induced fit, conformational selection and independent dynamic segments: an extended view of binding events The Role of Protein-Ligand Contacts in Allosteric Regulation of the Escherichia coli Catabolite Activator Protein Interplay between allostery and intrinsic disorder in an ensemble Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I.Structural and functional characterization of a ketosteroid transcriptional regulator of Mycobacterium tuberculosis Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC.Crystal Structure of Fad35R from Mycobacterium tuberculosis H37Rv in the Apo-State.Agonism/antagonism switching in allosteric ensembles.Crystal Structures of the Global Regulator DasR from Streptomyces coelicolor: Implications for the Allosteric Regulation of GntR/HutC Repressors Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor.The TetR family of regulators.Synthetic Biology-The Synthesis of Biology.Metallochaperones and metalloregulation in bacteria.Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme.Positions 94-98 of the lactose repressor N-subdomain monomer-monomer interface are critical for allosteric communication.Ligand binding specificity of RutR, a member of the TetR family of transcription regulators in Escherichia coli.A two-step mechanism for the activation of actinorhodin export and resistance in Streptomyces coelicolor.Sequence-function relationships in folding upon binding.Streptomyces coelicolor XdhR is a direct target of (p)ppGpp that controls expression of genes encoding xanthine dehydrogenase to promote purine salvage.Crystallization and preliminary X-ray analysis of the TetR-like efflux pump regulator SimR.Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding.Minimal genetic device with multiple tunable functions.Structural and genomic DNA analysis of the putative TetR transcriptional repressor SCO7518 from Streptomyces coelicolor A3(2).Structural insights into simocyclinone as an antibiotic, effector ligand, and substrate.Molecular dynamics simulation unveils the conformational flexibility of the interdomain linker in the bacterial transcriptional regulator GabR from Bacillus subtilis bound to pyridoxal 5'-phosphate.Isoenergic modification of whey protein structure by denaturation and crosslinking using transglutaminase.Functional Mechanism of the Efflux Pumps Transcription Regulators From Pseudomonas aeruginosa Based on 3D Structures.

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P2860

The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor.

http://www.wikidata.org/entity/Q33564100

description

2009 nî lūn-bûn

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2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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The induction of folding coope ...... nse of tetracycline repressor.

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The induction of folding coope ...... nse of tetracycline repressor.

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The induction of folding coope ...... nse of tetracycline repressor.

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The induction of folding coope ...... nse of tetracycline repressor.

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The induction of folding coope ...... nse of tetracycline repressor.

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PNAS.0911566106

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Proceedings of the National Academy of Sciences of the United States of America

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The induction of folding coope ...... nse of tetracycline repressor.

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Alan R Davidson

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Sean E Reichheld

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P2860

Exploring the sequence space for tetracycline-dependent transcriptional activators: novel mutations yield expanded range and sensitivity

Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system

Crystal structures of the Streptomyces coelicolor TetR-like protein ActR alone and in complex with actinorhodin or the actinorhodin biosynthetic precursor (S)-DNPA

A protein functional leap: how a single mutation reverses the function of the transcription regulator TetR

The complex formed between Tet repressor and tetracycline-Mg2+ reveals mechanism of antibiotic resistance

Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance

Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions

Conformational changes of the Tet repressor induced by tetracycline trapping

Crystal structure of the tet repressor in complex with a novel tetracycline, 9-(N,N-dimethylglycylamido)- 6-demethyl-6-deoxy-tetracycline

The TetR family of transcriptional repressors.

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22263-22268

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scholarly article

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10.1073/PNAS.0911566106

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52

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