Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA - Wikidata - awgldk - TriplyDB

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

http://www.wikidata.org/entity/Q35751393

about

Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator fromBacillus subtilisreveal ligand-induced structural changes upon binding of several glycolytic intermediates Structural Basis for Phosphorylated Autoinducer-2 Modulation of the Oligomerization State of the Global Transcription Regulator LsrR from Escherichia coli Crystal Structures of the LsrR Proteins Complexed with Phospho-AI-2 and Two Signal-Interrupting Analogues Reveal Distinct Mechanisms for Ligand Recognition Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex.Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states.Transcriptomic and phenotypic analyses suggest a network between the transcriptional regulators HrcA and sigmaB in Listeria monocytogenes.Characterization of the control catabolite protein of gluconeogenic genes repressor by fluorescence cross-correlation spectroscopy and other biophysical approaches.Transcriptional regulation is insufficient to explain substrate-induced flux changes in Bacillus subtilis.Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO.Comparison of the regulation, metabolic functions, and roles in virulence of the glyceraldehyde-3-phosphate dehydrogenase homologues gapA and gapB in Staphylococcus aureus.Minimal genetic device with multiple tunable functions.The Bacillus subtilis mannose regulator, ManR, a DNA-binding protein regulated by HPr and its cognate PTS transporter ManP.

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P2860

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

http://www.wikidata.org/entity/Q35751393

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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name

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@ast

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@en

type

label

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@ast

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@en

prefLabel

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@ast

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

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BIOPHYSJ.106.095109

P1433

Biophysical Journal

P1476

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA

@en

P2093

Alvaro Ortega

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

Carlos Alfonso

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

Catherine A Royer

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

Emmanuel Margeat

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

Germán Rivas

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

Nathalie Declerck

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Silvia Zorrilla

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

Stéphane Aymerich

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

Thierry Doan

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

P2860

The complete genome sequence of the gram-positive bacterium Bacillus subtilis

Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase

Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR

Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain.

Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium

Numerical analysis of binding data: advantages, practical aspects, and implications.

The HPr kinase from Bacillus subtilis is a homo-oligomeric enzyme which exhibits strong positive cooperativity for nucleotide and fructose 1,6-bisphosphate binding.

The lac repressor.

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3215-3227

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scholarly article

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10.1529/BIOPHYSJ.106.095109

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9

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92

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2007-02-09T00:00:00Z

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6512615

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17293407

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1852337

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