Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: differences in molecular structure and physiological function.
about
Quantifying global tolerance of biochemical systems: design implications for moiety-transfer cyclesSplit histidine kinases enable ultrasensitivity and bistability in two-component signaling networksThe two-component sensor KinB acts as a phosphatase to regulate Pseudomonas aeruginosa VirulenceEnzyme Sequestration as a Tuning Point in Controlling Response Dynamics of Signalling NetworksConstruction of a genetic multiplexer to toggle between chemosensory pathways in Escherichia coliIdentifying quantitative operation principles in metabolic pathways: a systematic method for searching feasible enzyme activity patterns leading to cellular adaptive responses.Adaptable functionality of transcriptional feedback in bacterial two-component systems.Reciprocal regulation as a source of ultrasensitivity in two-component systems with a bifunctional sensor kinase.Use of physiological constraints to identify quantitative design principles for gene expression in yeast adaptation to heat shock.A sensor of the two-component system CpxA affects expression of the type III secretion system through posttranscriptional processing of InvE.Two-component signaling circuit structure and properties.How important is the phosphatase activity of sensor kinases?Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain.Genetic structure of three fosmid-fragments encoding 16S rRNA genes of the Miscellaneous Crenarchaeotic Group (MCG): implications for physiology and evolution of marine sedimentary archaea.Two component systems: physiological effect of a third component.Kinetic buffering of cross talk between bacterial two-component sensors.CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenesA survey of HK, HPt, and RR domains and their organization in two-component systems and phosphorelay proteins of organisms with fully sequenced genomes.Asymmetric cross-regulation between the nitrate-responsive NarX-NarL and NarQ-NarP two-component regulatory systems from Escherichia coli K-12Cyanobacterial two-component proteins: structure, diversity, distribution, and evolution.RodZ regulates the post-transcriptional processing of the Shigella sonnei type III secretion system.Deciphering Parameter Sensitivity in the BvgAS Signal TransductionThe WalKR system controls major staphylococcal virulence genes and is involved in triggering the host inflammatory responseA natural inactivating mutation in the CovS component of the CovRS regulatory operon in a pattern D Streptococcal pyogenes strain influences virulence-associated genesDistribution, structure and diversity of "bacterial" genes encoding two-component proteins in the Euryarchaeota.Biological insights from structures of two-component proteins.Mathematical formalisms based on approximated kinetic representations for modeling genetic and metabolic pathways.Cross-talk and specificity in two-component signal transduction pathways.Functions of the duplicated hik31 operons in central metabolism and responses to light, dark, and carbon sources in Synechocystis sp. strain PCC 6803Cross-talk suppression between the CpxA-CpxR and EnvZ-OmpR two-component systems in E. coli.Differential target gene activation by the Staphylococcus aureus two-component system saeRS.Control of Streptococcus pyogenes virulence: modeling of the CovR/S signal transduction system.Evolving a robust signal transduction pathway from weak cross-talk.Revisiting regulation of potassium homeostasis in Escherichia coli: the connection to phosphate limitation.KinD is a checkpoint protein linking spore formation to extracellular-matrix production in Bacillus subtilis biofilmsResponse dynamics of phosphorelays suggest their potential utility in cell signalling.Evidence that the essential response regulator YycF in Streptococcus pneumoniae modulates expression of fatty acid biosynthesis genes and alters membrane composition.Hysteretic and graded responses in bacterial two-component signal transduction.Integrating input from multiple signals: the VirA/VirG two-component system of Agrobacterium tumefaciens.Binding of the global response regulator protein CovR to the sag promoter of Streptococcus pyogenes reveals a new mode of CovR-DNA interaction.
P2860
Q28474957-C5004B28-CCF2-46E3-815D-4685216AB43CQ28487725-4A9A1680-2693-4831-855D-C02FB295CC54Q28493057-576CD2F7-B9C2-4AFF-A07E-51F252B5894BQ28551936-5577A0B1-8470-4CB5-94E4-5633BD0DDFA4Q28914734-71568852-D94B-438A-9FCF-9BF26D673E55Q30492576-7471BD81-712A-4429-9A3D-FFAF0C8EF0ADQ30978121-E871392C-CC26-42C4-BE33-CE3B6D455F68Q31160663-2203E3E9-5CE5-42AC-9919-82C161A968AAQ33238498-9BE89BB9-28D7-435E-8923-09C80F92AD5EQ33554160-5634DD7B-54FC-4B2D-B6CC-471A75B8E49DQ33762040-2C4E6989-0722-4648-99ED-DC2B254C726CQ33784260-3965F00B-7E07-40DE-A89E-DDF7F90209BFQ33825947-066EE025-F6DC-4A38-86CF-8B4D3787387DQ34083854-F5E4F374-05E6-4AC3-9C94-0A163F965CA7Q34170516-D4FF3998-5774-4687-8532-39B97332E314Q34282460-90BEEF5B-1D26-4C40-ACA0-04A282F66F4CQ34352002-54C4C049-5CD8-40D3-BDC6-307B209E5EE2Q34492520-90522C8E-D10E-457D-84DB-125BD5DDC494Q34554137-D49E3B5F-9395-4B90-8AA9-1A5699EC4CF1Q34720154-2328D689-D8E8-4E91-85D4-0330547469F6Q35194777-42166DDA-D0FC-4857-A44A-4C2298C0FE2FQ35904876-B635C83F-05E3-4620-9E94-F47EEB47AE80Q36277416-01A5F6FA-76CA-499B-8636-7A843EA44326Q36647385-14456A96-400E-4195-A587-8B2C713AADA0Q37200753-488646C4-64A3-47AC-8C51-5615A67E33FCQ37539921-DBF7A38A-32D5-4C4E-9233-9A39723241B9Q37853843-75C10750-F0C4-4246-8ECC-3217B4656A4AQ38829571-90889917-613F-47DC-B40F-4E91D58F6720Q40347419-852A9207-C1AD-4664-9530-19414A7683CCQ41929636-25B879CB-E208-452C-B624-6CFBDFD9B9DEQ41989725-DE1241C0-3777-4BC4-BA41-6318AFADA339Q42068488-98430DCD-9509-4964-AB4F-D1E8BB617E0CQ42158819-F0D0518A-6F0C-4D48-9DA3-650DC16B41A9Q42177696-F3B2AA09-35BE-441E-B7CF-6533D2010556Q42641273-FA0F72BA-B3CD-461D-B8F8-960BAABE1AFFQ42701156-BA5D40B7-3550-4911-BAEB-62D6F94F4695Q42705155-7FCDC844-ED6E-405E-851D-8C252F677B53Q43191527-D2BDF52A-D13D-4818-9E8C-3143F6E0C231Q45130658-EB2782CB-DCC2-4479-95CE-E8C0AA269F3FQ46713390-37E1067E-2ABF-4834-9B9F-563BF5097BF4
P2860
Comparative analysis of prototype two-component systems with either bifunctional or monofunctional sensors: differences in molecular structure and physiological function.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Comparative analysis of protot ...... re and physiological function.
@en
Comparative analysis of protot ...... re and physiological function.
@nl
type
label
Comparative analysis of protot ...... re and physiological function.
@en
Comparative analysis of protot ...... re and physiological function.
@nl
prefLabel
Comparative analysis of protot ...... re and physiological function.
@en
Comparative analysis of protot ...... re and physiological function.
@nl
P2860
P1476
Comparative analysis of protot ...... re and physiological function.
@en
P2093
Michael A Savageau
P2860
P356
10.1046/J.1365-2958.2003.03344.X
P407
P577
2003-04-01T00:00:00Z