Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis.
about
Site-specific and synergistic stimulation of methylation on the bacterial chemotaxis receptor Tsr by serine and CheWNutrient-sensing mechanisms across evolutionThe role of membrane-mediated interactions in the assembly and architecture of chemoreceptor latticesAn agent-based model of signal transduction in bacterial chemotaxisThe 3.2 Å Resolution Structure of a Receptor:CheA:CheW Signaling Complex Defines Overlapping Binding Sites and Key Residue Interactions within Bacterial Chemosensory ArraysConstruction of a genetic multiplexer to toggle between chemosensory pathways in Escherichia coliPositioning of chemosensory clusters in E. coli and its relation to cell division.SecA, the motor of the secretion machine, binds diverse partners on one interactive surface.Molecular architecture of chemoreceptor arrays revealed by cryoelectron tomography of Escherichia coli minicells.Mapping out regions on the surface of the aspartate receptor that are essential for kinase activationCheA Kinase of bacterial chemotaxis: chemical mapping of four essential docking sites.Role of translational coupling in robustness of bacterial chemotaxis pathway.Interaction between individual protein components of the GerA and GerB nutrient receptors that trigger germination of Bacillus subtilis sporesStructure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteinsConformation and dynamics of the [3-(13)C]Ala, [1-(13)C]Val-labeled truncated pharaonis transducer, pHtrII(1-159), as revealed by site-directed (13)C solid-state NMR: changes due to association with phoborhodopsin (sensory rhodopsin II)The protein interaction network of a taxis signal transduction system in a halophilic archaeonCysteine-scanning analysis of the chemoreceptor-coupling domain of the Escherichia coli chemotaxis signaling kinase CheAElectron microscopic analysis of membrane assemblies formed by the bacterial chemotaxis receptor Tsr.Core unit of chemotaxis signaling complexes.Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis.Self-assembly of receptor/signaling complexes in bacterial chemotaxisFundamental constraints on the abundances of chemotaxis proteinsDirect visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy.CheA-receptor interaction sites in bacterial chemotaxis.Crosslinking snapshots of bacterial chemoreceptor squads.Chemoreceptor VfcA mediates amino acid chemotaxis in Vibrio fischeri.Ligand affinity and kinase activity are independent of bacterial chemotaxis receptor concentration: insight into signaling mechanisms.Excitation and adaptation in bacteria-a model signal transduction system that controls taxis and spatial pattern formationDifferent signaling roles of two conserved residues in the cytoplasmic hairpin tip of Tsr, the Escherichia coli serine chemoreceptorBacterial chemoreceptors: high-performance signaling in networked arraysDynamic map of protein interactions in the Escherichia coli chemotaxis pathwayThree-dimensional structure and organization of a receptor/signaling complex.Spatial organization in bacterial chemotaxis.The PICM chemical scanning method for identifying domain-domain and protein-protein interfaces: applications to the core signaling complex of E. coli chemotaxis.Isolated bacterial chemosensory array possesses quasi- and ultrastable components: functional links between array stability, cooperativity, and order.Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli.Stochastic assembly of chemoreceptor clusters in Escherichia coli.Integration of the second messenger c-di-GMP into the chemotactic signaling pathway.Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA
P2860
Q24793956-D3836154-7BAF-4D35-B2F3-0F2FE48CFEF4Q27015819-01486603-19C6-429F-B21C-58C58C68A943Q27320561-15C5B009-BB6B-4C71-BA21-D034FE2D1591Q27333948-78B323A8-A2A3-448D-B23A-E60B7F0B3FD6Q27678118-1E467F32-B64D-433F-A176-33AB59AF7C45Q28914734-95687A48-326C-4AC0-ADD9-063AF5914120Q30479125-8479D884-49C8-4468-9380-44937530F2D0Q30485740-73F65261-2109-4E1D-8AB5-05FE6EC427FFQ30518239-304E6239-7A58-4516-8F72-19D7FE476A7DQ30894653-84C4E520-8472-4871-86FB-63E3D4C94D51Q33250403-7DCF5A0C-E408-467A-A34A-AF1248C968CBQ33494496-A08A2F02-AD11-4DF2-A928-2FDE4517B42AQ33716703-0F0F477A-DEB4-4517-9AE7-B82F2B4F8F4CQ34107640-6AC3754D-211A-4DB7-9D09-BE841FF2D1EAQ34166081-4B223C52-E5BF-4B16-8758-9B83E8FC8C4EQ34185701-F170F092-8505-4C3B-A4DF-3AA6E41E2C33Q34484501-E1F59E81-6B05-4770-BE63-1C94AA5AB55EQ34697302-1129D0BB-1580-4B6E-AAC8-C0991558ACFBQ35021206-7C2D2097-D3A4-4127-AD25-0A1AAC7BCAD5Q35035138-6C06B8F9-22E5-4FFB-B5AF-D976FB45186EQ35070683-04726937-4A6D-44BF-A723-2BB3AB4D75E0Q35080611-43AC1B06-6E70-4CC0-BF0C-D5147856541FQ35221688-48863C17-F9B9-4CA0-8C5B-3B42FADDC480Q35676633-C41125DA-08B7-41B3-8125-FEE4EBABCC03Q36162080-B3FB5F6F-BECC-418F-988C-70A80078C103Q36604915-A2C2C988-CCAB-4846-8D8E-69259F23D436Q36668170-BB0791A6-3425-4F50-B7D5-CD593FE03F17Q36727802-CEB8BA10-2522-4B49-908C-2E125176361AQ36913571-E20D0F27-0745-44E4-90BA-CD36305D6A3FQ36994336-DB909223-5A24-419B-9E9E-E9C36221ADD7Q37047302-3E5E1BDE-B7AD-427A-8973-1AD0E9447A3CQ37101011-A26F76B4-8A31-485E-ACC0-F72855F90F48Q37713948-58651CDB-B936-4725-A171-070A9F8B427EQ37780681-35210945-67DB-47A1-BAEB-0A8FC8E2FBFAQ38300348-C2CADC69-1DBE-4F2C-8036-90398458C483Q39297839-A4DF60C0-F8BB-43BB-8D8F-DE72E5F2E0DDQ39995603-0A203AFE-4DEF-4866-A855-9BA446758553Q40092338-E1C6F21B-9895-4C13-ADA2-32AAAD62334CQ41814076-8460C7B6-5FDE-410D-8980-EC6DBA239C7EQ42078600-41CF33D3-2B20-4ABB-910A-B71B71802FB3
P2860
Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@en
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@nl
type
label
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@en
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@nl
prefLabel
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@en
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@nl
P2093
P2860
P356
P1476
Organization of the receptor-k ...... s Escherichia coli chemotaxis.
@en
P2093
Jeffry B Stock
Mikhail N Levit
Thorsten W Grebe
P2860
P304
36748-36754
P356
10.1074/JBC.M204317200
P407
P577
2002-07-15T00:00:00Z