Ligand-binding PAS domains in a genomic, cellular, and structural context
about
The DSF Family of Cell-Cell Signals: An Expanding Class of Bacterial Virulence RegulatorsTwo quorum sensing systems control biofilm formation and virulence in members of the Burkholderia cepacia complexCyclic di-GMP: the first 25 years of a universal bacterial second messengerRegulating the ARNT/TACC3 Axis: Multiple Approaches to Manipulating Protein/Protein Interactions with Small MoleculesArchitecture of the Soluble Receptor Aer2 Indicates an In-Line Mechanism for PAS and HAMP Domain SignalingAllosteric inhibition of hypoxia inducible factor-2 with small moleculesMechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor DomainsStructural properties of PAS domains from the KCNH potassium channelsCrystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator ComplexCoiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 fromArabidopsis thalianaAdaptor-Dependent Degradation of a Cell-Cycle Regulator Uses a Unique Substrate ArchitectureStructure and proposed mechanism for the pH-sensing Helicobacter pylori chemoreceptor TlpBMulti-PAS domain-mediated protein oligomerization of PpsR fromRhodobacter sphaeroidesPAS kinase: a nutrient sensing regulator of glucose homeostasis.Structural analysis of an oxygen-regulated diguanylate cyclaseGeneral Stress Signaling in the AlphaproteobacteriaCyclic Di-GMP phosphodiesterases RmdA and RmdB are involved in regulating colony morphology and development in Streptomyces coelicolorCache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in ProkaryotesMolecular Insights into Toluene Sensing in the TodS/TodT Signal Transduction SystemStructural basis for ligand recognition by a Cache chemosensory domain that mediates carboxylate sensing in Pseudomonas syringaeProtein structural dynamics revealed by time-resolved X-ray solution scattering.Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus.Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.Crystal structures of the F and pSLT plasmid TraJ N-terminal regions reveal similar homodimeric PAS folds with functional interchangeability.Influence of PAS domain flanking regions on oligomerisation and redox signalling by NifL.Small molecule modifiers of circadian clocks.The Brucella abortus virulence regulator, LovhK, is a sensor kinase in the general stress response signalling pathwayRole of the PAS sensor domains in the Bacillus subtilis sporulation kinase KinA.Complex two-component signaling regulates the general stress response in Alphaproteobacteria.The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function RelationshipsLigand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations.Activation of gab cluster transcription in Bacillus thuringiensis by γ-aminobutyric acid or succinic semialdehyde is mediated by the Sigma 54-dependent transcriptional activator GabRCharacterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmissionReductive evolution and the loss of PDC/PAS domains from the genus Staphylococcus.Domain shuffling in a sensor protein contributed to the evolution of insect pathogenicity in plant-beneficial Pseudomonas protegens.The Drosophila juvenile hormone receptor candidates methoprene-tolerant (MET) and germ cell-expressed (GCE) utilize a conserved LIXXL motif to bind the FTZ-F1 nuclear receptor.Genome-wide survey of two-component signal transduction systems in the plant growth-promoting bacterium AzospirillumMolecular Mechanisms of Transcription Activation by Juvenile Hormone: A Critical Role for bHLH-PAS and Nuclear Receptor Proteins.Cis-2-dodecenoic acid receptor RpfR links quorum-sensing signal perception with regulation of virulence through cyclic dimeric guanosine monophosphate turnoverThe auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus.
P2860
Q26800244-18DADDE5-F2C7-4AA5-A18D-B0CEFD84BCE1Q26827817-33DE6C58-F81F-4A18-AF67-E3E5672B6E29Q26850396-6AA9FEBB-2B10-407F-A492-568F20900B60Q27675499-BE4BE378-EB3E-4D5F-A3B2-16AB7460D670Q27675636-6DEF5A25-480B-485B-9AD1-FFEA46DB55D2Q27676596-5B7A7CB8-DCF0-409B-9726-D32DB038CBA7Q27676725-C10D4AA3-AE26-456D-B0BC-2A69296165F9Q27677199-003C5B61-3A17-480B-82DF-A7CD4F37C48DQ27679392-404D615D-A3AF-486F-BB0B-7E93D2E42E29Q27680819-E49DA058-61F6-4800-8B87-A62AC28949DCQ27681031-73CFDB33-F5DD-428E-ADD5-11CA96F869B3Q27681189-6C9D1C48-34B7-4EF1-8B7E-6B8819B4BCDFQ27682008-30DB67C9-FE3B-49CA-8C1A-3A19EE561916Q27691811-E775BC9E-FA2E-4B8D-840A-9871A6F2A60EQ27702555-3883DDAF-0A9A-427A-BD3F-94CA3E0DC75AQ28085365-53D3DC6D-104F-47C0-8322-2DDE2C03270BQ28504076-0404F16E-CA07-4922-A477-AD7DDFE85C71Q28551212-9170B03D-1B54-41EC-938A-27A0E6317178Q28603026-48DC8D14-F62D-45CA-9AEB-17F3911BAB3BQ28822122-F9F8E73D-0BC1-44D0-9655-F657E6832C41Q30376223-1AA303D1-B8E1-4E03-91BF-C903900BF504Q30387565-7E042BF9-BBA9-4FA2-B046-5E2E44AFA0E7Q30838981-FF2647DB-0E5F-4315-B2BE-8875F366788DQ34193860-51FFF1CF-5482-44A5-BE25-B2550BDA1B7DQ34441783-29E72AEE-40F7-48D8-A61C-1AAB1DD46C50Q34480532-3AB624CC-F501-4C29-9657-41274E883926Q34490455-22602C89-2039-441E-9C8C-C88EF7BAC75CQ34624767-DD7A4BE7-E267-4198-8FA9-8D6A17355D9BQ34661097-78FE75B7-F9CE-4A96-A303-B9B19A563421Q34680715-DCA6DB6D-65D0-4CF8-9407-FEA4CED2E208Q34754684-25518425-996C-4BFD-A98D-6FDCEA2F2D51Q34787524-8560D89D-38FF-48D6-ABB2-5BD43FADFB93Q34863387-695F6257-3DF1-42F1-8444-72A8AE4ED1EDQ34883534-ABDD2674-3543-48FE-B00F-D98676EA72C4Q35105660-470FF3C1-8B73-437D-8072-614D864FAFCEQ35801986-8ED26B86-3318-4DF4-B42F-BFBF6B6112DBQ35816553-09F19992-81FF-4B9D-B51A-4CD5AF091FC6Q36007710-6CAF1E6C-27F8-4983-A27A-FF03BBBEFF62Q36280043-5D96DCCD-B8F1-4833-B7AB-DA2D5C00DBC5Q36309811-5A0421AC-FAE8-485D-82DA-CD91F7C52714
P2860
Ligand-binding PAS domains in a genomic, cellular, and structural context
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
name
Ligand-binding PAS domains in a genomic, cellular, and structural context
@ast
Ligand-binding PAS domains in a genomic, cellular, and structural context
@en
Ligand-binding PAS domains in a genomic, cellular, and structural context
@nl
type
label
Ligand-binding PAS domains in a genomic, cellular, and structural context
@ast
Ligand-binding PAS domains in a genomic, cellular, and structural context
@en
Ligand-binding PAS domains in a genomic, cellular, and structural context
@nl
prefLabel
Ligand-binding PAS domains in a genomic, cellular, and structural context
@ast
Ligand-binding PAS domains in a genomic, cellular, and structural context
@en
Ligand-binding PAS domains in a genomic, cellular, and structural context
@nl
P2860
P1476
Ligand-binding PAS domains in a genomic, cellular, and structural context
@en
P2093
Jonathan T Henry
P2860
P304
P356
10.1146/ANNUREV-MICRO-121809-151631
P50
P577
2011-01-01T00:00:00Z