Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
about
Expanded roles for multicargo and class 1B effector chaperones in type III secretionStructural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella entericaCommon architecture of the flagellar type III protein export apparatus and F- and V-type ATPasesStructural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motilityRearrangements of α-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III exportIsolation of Salmonella mutants resistant to the inhibitory effect of Salicylidene acylhydrazides on flagella-mediated motilityInteraction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein exportProtein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.The role of the FliD C-terminal domain in pentamer formation and interaction with FliT.Genetic and molecular characterization of flagellar assembly in Shewanella oneidensis.Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhAThe flagellar regulator fliT represses Salmonella pathogenicity island 1 through flhDC and fliZ.FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis.Periplasmic flagellar export apparatus protein, FliH, is involved in post-transcriptional regulation of FlaB, motility and virulence of the relapsing fever spirochete Borrelia hermsii.An energy transduction mechanism used in bacterial flagellar type III protein export.Mutations in the Borrelia burgdorferi Flagellar Type III Secretion System Genes fliH and fliI Profoundly Affect Spirochete Flagellar Assembly, Morphology, Motility, Structure, and Cell Division.A translocator-specific export signal establishes the translocator-effector secretion hierarchy that is important for type III secretion system function.Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella.Recognition and targeting mechanisms by chaperones in flagellum assembly and operationHigh-Resolution pH Imaging of Living Bacterial Cells To Detect Local pH Differences.Building a flagellum outside the bacterial cell.The EAL-like protein STM1697 regulates virulence phenotypes, motility and biofilm formation in Salmonella typhimurium.Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion.Chaperones: needed for both the good times and the bad times.RpoN2- and FliA-regulated fliTX is indispensible for flagellar motility and virulence in Xanthomonas oryzae pv. oryzae.Crystallization and preliminary X-ray analysis of FlgA, a periplasmic protein essential for flagellar P-ring assembly.Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus.Structural stability of flagellin subunit affects the rate of flagellin export in the absence of FliS chaperone.Structural plasticity of the Salmonella FliS flagellar export chaperone.Interactions of bacterial flagellar chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament.Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export.Dynamics and Control of Flagella Assembly in Salmonella typhimurium.Structural insights on two hypothetical secretion chaperones from Xanthomonas axonopodis pv. citri.In Vitro Reconstitution of Functional Type III Protein Export and Insights into Flagellar Assembly.Flagella-mediated secretion of a novel cytotoxin affecting both vertebrate and invertebrate hostsNovel insight into an energy transduction mechanism of the bacterial flagellar type III protein export
P2860
Q26858982-AC5B50AA-A542-4922-8798-A21EED619265Q27345193-C9E4DB7B-9E43-49C3-8DC9-5EF7475FCE3AQ27666617-7BA42244-4D6C-40F2-A289-1BC6DCD6AD10Q27673555-53A5DEBC-9AC5-4360-9EF2-F6CC4F5D9A8BQ27704861-4C1B8262-23DD-439F-BC24-BAFC9BB7B48CQ28484814-F1AD7833-B3FB-4E2D-B681-526106636AA8Q28490035-676F0872-068A-47BB-B3AE-E0131BE29F68Q30318075-6504A2BA-F440-402A-816F-DA2090FDF1A0Q33861084-F15F59A6-6FFE-4752-8695-9507E29BCD71Q33952495-65F4A464-4E35-439D-97CC-1C8250B90063Q33979924-F844F019-84D4-4B30-80F7-33D7E13262D7Q34222261-E4220AA3-C514-4BC4-9A93-7347B4EFAB6BQ34552812-1E758172-9F4E-4D3B-B3C8-BCB3B2F51201Q34755400-48FD786E-EAD4-43E9-9FA6-837698D59A81Q34979571-C8732E6D-066B-4566-BF68-0A1F1037BAB2Q35367067-07232BC5-4865-4855-8F38-99427FD016F6Q35620167-80588D74-599B-47F2-8EFC-DC094A087C66Q36472851-4D579575-2757-4046-914F-C5A8C54DF122Q36770466-397AD08D-6222-493E-9855-644B64D87665Q36999741-B5E8BD61-152A-4276-9E33-1D76E3A23110Q37258436-96E33953-1F0A-4FD2-A511-C87618A25F8EQ37481747-079C8B2B-E88E-4309-B112-7870306AD7AEQ38224001-67991F95-8CC0-480A-94EE-492C092B1C58Q39078192-66FA7933-8672-406B-896D-42F26D04418CQ39464419-56CEDF03-2003-489A-BC4B-4D0322E75835Q40183775-43A5076E-47D2-4727-9200-88776A007B81Q41336612-A772741A-3AC0-45F5-B62E-9069CCCBE4CFQ42000075-DF7441BB-AEE5-42F7-B4BD-E8A91E7A036AQ42958279-C83E0200-3168-43CA-9E11-B6C658602B81Q49960688-3F2DB402-58D1-41E7-B1BA-667B633D97E6Q49967370-B08670A1-9B65-45DA-9420-17841006C478Q50004876-F15014C2-4055-48A9-A5D9-C05C36E7FE17Q50034341-847D33EC-4D1A-4FF9-A4C4-FD649FC5E1AAQ50286878-69FEF0BB-3544-467A-AB28-AAA26B1BE823Q54360365-FA0B8EA3-E91D-4FFE-A751-AA272D52F19BQ55385008-A8D7DD53-F433-4EE5-A275-DE4003EC7B52Q57144305-1AA76F18-6318-44A2-ACAE-ED6D6667FA42Q58717983-E7D7DF58-A36E-499F-A20E-1DAF956F5562
P2860
Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural insight into the re ...... FliT with its binding partners
@ast
Structural insight into the re ...... FliT with its binding partners
@en
Structural insight into the re ...... FliT with its binding partners
@nl
type
label
Structural insight into the re ...... FliT with its binding partners
@ast
Structural insight into the re ...... FliT with its binding partners
@en
Structural insight into the re ...... FliT with its binding partners
@nl
prefLabel
Structural insight into the re ...... FliT with its binding partners
@ast
Structural insight into the re ...... FliT with its binding partners
@en
Structural insight into the re ...... FliT with its binding partners
@nl
P2093
P2860
P3181
P356
P1476
Structural insight into the re ...... FliT with its binding partners
@en
P2093
Katsumi Imada
Miki Kinoshita
Tohru Minamino
Yukio Furukawa
P2860
P304
P3181
P356
10.1073/PNAS.1001866107
P407
P577
2010-05-11T00:00:00Z