Intrinsic negative feedback governs activation surge in two-component regulatory systems. - Wikidata - awgldk - TriplyDB

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

http://www.wikidata.org/entity/Q37019367

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Crystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiont Temporal and evolutionary dynamics of two-component signaling pathways The two-component sensor KinB acts as a phosphatase to regulate Pseudomonas aeruginosa Virulence Quantitative Kinetic Analyses of Shutting Off a Two-Component System Negative feedback in genetic circuits confers evolutionary resilience and capacitance.Bacterial nucleoid-associated protein uncouples transcription levels from transcription timing.Evolutionary tuning of protein expression levels of a positively autoregulated two-component system.The auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus.Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Missense substitutions reflecting regulatory control of transmitter phosphatase activity in two-component signalling Strong cross-system interactions drive the activation of the QseB response regulator in the absence of its cognate sensor.Cyclic di-GMP mediates a histidine kinase/phosphatase switch by noncovalent domain cross-linking Signal-specific temporal response by the Salmonella PhoP/PhoQ regulatory system.Antibacterial mechanisms of polymyxin and bacterial resistance.Signal transduction in histidine kinases: insights from new structures.The Histidine Residue of QseC Is Required for Canonical Signaling between QseB and PmrB in Uropathogenic Escherichia coli.Conformational dynamics of the essential sensor histidine kinase WalK Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide.Signaling by two-component system noncognate partners promotes intrinsic tolerance to polymyxin B in uropathogenic Escherichia coli.Tuning transcription of nutrient utilization genes to catabolic rate promotes growth in a gut bacterium.The small membrane protein MgrB regulates PhoQ bifunctionality to control PhoP target gene expression dynamics.Overcoming the Cost of Positive Autoregulation by Accelerating the Response with a Coupled Negative Feedback

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Intrinsic negative feedback governs activation surge in two-component regulatory systems.

http://www.wikidata.org/entity/Q37019367

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on February 2012

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@en

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@nl

type

label

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@en

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@nl

prefLabel

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@en

Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@nl

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J.MOLCEL.2011.12.027

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Intrinsic negative feedback governs activation surge in two-component regulatory systems.

@en

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Akinori Kato

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

Dongwoo Shin

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

Eduardo A Groisman

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

Henry V Huang

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

Igor Zwir

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

Won-Sik Yeo

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

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Structure of rat BCKD kinase: Nucleotide-induced domain communication in a mitochondrial protein kinase

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NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ

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409-421

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scholarly article

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10.1016/J.MOLCEL.2011.12.027

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3

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45

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2012-02-01T00:00:00Z

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221823793

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22325356

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3713471

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