Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria. - Wikidata - awgldk - TriplyDB

Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria.

Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria.

http://www.wikidata.org/entity/Q34979021

about

Mechanism of coupling drug transport reactions located in two different membranes Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirocheteBorrelia burgdorferi The ins and outs of RND efflux pumps in Escherichia coli Membrane fusion proteins of type I secretion system and tripartite efflux pumps share a binding motif for TolC in gram-negative bacteria Interaction mediated by the putative tip regions of MdsA and MdsC in the formation of a Salmonella-specific tripartite efflux pump Genetic assessment of the role of AcrB β-hairpins in the assembly of the TolC-AcrAB multidrug efflux pump of Escherichia coli Structure-function analysis of the ATP-driven glycolipid efflux pump DevBCA reveals complex organization with TolC/HgdD.A data-driven approach to modeling the tripartite structure of multidrug resistance efflux pumps.Architecture and roles of periplasmic adaptor proteins in tripartite eﬄux assemblies An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump Structure of the tripartite multidrug efflux pump AcrAB-TolC suggests an alternative assembly mode Mechanism and Function of the Outer Membrane Channel TolC in Multidrug Resistance and Physiology of Enterobacteria.Interaction of antibacterial compounds with RND eﬄux pumps in Pseudomonas aeruginosa Reversal of the Drug Binding Pocket Defects of the AcrB Multidrug Efflux Pump Protein of Escherichia coli.Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa.Focus on the Outer Membrane Factor OprM, the Forgotten Player from Efflux Pumps Assemblies.Molecular Dynamics Computer Simulations of Multidrug RND Efflux Pumps Efflux pump-mediated antibiotics resistance: insights from computational structural biology.Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model.Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump.Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3:6:3.The α-barrel tip region of Escherichia coli TolC homologs of Vibrio vulnificus interacts with the MacA protein to form the functional macrolide-specific efflux pump MacAB-TolC.Interaction between the α-barrel tip of Vibrio vulnificus TolC homologs and AcrA implies the adapter bridging model.Molecular Modeling of Multidrug Properties of Resistance Nodulation Division (RND) Transporters.Functional analysis of Vibrio vulnificus RND efflux pumps homologous to Vibrio cholerae VexAB and VexCD, and to Escherichia coli AcrAB.Functional analysis of TolC homologs in Vibrio vulnificus.Accumulation and efflux of polychlorinated biphenyls in Escherichia coli.

P2860

Q27025780-DFA9228B-7DE9-4264-B2A6-C07016D417BC Q27677094-F00E7034-CE9D-49A4-8531-71469E36506D Q27679079-6F7A1A7D-87BE-474D-BEB8-DE793EF2DBFF Q28084596-2E2D9681-04AB-41D4-B118-BDB5FCF0123C Q28481159-01F34FCF-744D-41B9-8982-4BE42B3EC0D4 Q28489987-36903BE7-2EBB-4F3B-B446-113CDAAE45FF Q30153455-00154264-5D30-4B8E-B266-62EFB358FD40 Q30153464-D82989A9-803A-487F-8AB2-1BD9CBDA3D2C Q30832957-144709D9-E96B-42F7-A763-6CAAC08886A0 Q33360920-1851893D-0BA1-49F9-AA9F-F34DF3C7909C Q33602956-C2291CE3-BE18-46AC-A4BD-6855DEC60369 Q35093818-EF10848E-F3BF-4928-AF27-55FDC3E8F7A7 Q35216438-AC0ED60F-6BBC-40BF-B5A5-9E330586AC74 Q35830489-4B72729C-3A58-4964-BF17-04FDA12966B4 Q36070064-F546B0C2-4AD5-4FB3-B873-33AE8183F1AE Q36403070-3AD1114E-668F-4122-901F-A3092F90626D Q36683523-E1BC8821-B391-497C-B478-C44AB84842DA Q37655085-E4CE66D2-5F2A-415F-BEE8-B05913FB6AAD Q38182018-019FD1AB-A678-4277-B882-EB31049F6F7D Q38508059-66915314-F622-4BD9-9C63-F5E1B9C823A4 Q41058185-4E76ED48-FE15-4555-9426-F1DD85D56370 Q41358824-1A578E72-2005-424B-AA08-16777082276B Q42052070-9D13A663-BE16-4AF9-BD99-311BD60F708C Q42596970-977C8DF9-7292-4CB3-9E9C-29BB855BFC68 Q45819610-059FC12E-E734-4353-8D3E-F50459AA2279 Q47362097-1E2892A5-EC64-4EE7-AD91-369A8EBAF14B Q54272654-F31DFDD9-A27F-4A6B-9851-95B93D06455B Q54295322-4A4EDD2A-EA13-4292-A194-318C20E8C938 Q54342035-D5938B32-4209-47A6-A63F-0F3D383F6DC4

P2860

Funnel-like hexameric assembly of the periplasmic adapter protein in the tripartite multidrug efflux pump in gram-negative bacteria.

http://www.wikidata.org/entity/Q34979021

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@ast

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@en

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@nl

type

label

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@ast

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@en

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@nl

prefLabel

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@ast

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@en

Funnel-like hexameric assembly ...... ump in gram-negative bacteria.

@nl

P1433

Q34979021-3722466F-0B28-47A9-82A1-0FDA34AA2E77

P1476

Q34979021-78B8CAC1-F132-4677-85C2-EFEC4EC91912

P2093

Q34979021-3AF5A426-1F1E-40AB-A969-06203A1974FF

Q34979021-5616FA5F-1C0F-4922-8B03-DE2A4B7DE721

Q34979021-6F6CA940-DF0B-4C65-9780-CCF736D37B7E

Q34979021-76805670-708D-4CE5-806A-8808E9B23FB3

Q34979021-855414C5-98E6-405A-B53A-FD2BE52F19C1

Q34979021-92F0AF20-0B16-4217-A7F9-615CC18EEAA7

Q34979021-DB4E4E87-2F76-4E77-885E-1F152678823B

Q34979021-FDFDF9EF-C8DF-4E4A-92EB-E29747705989

P2860

Q34979021-03F2C437-3BF8-4ADF-8B74-F267B905A6C0

Q34979021-0AD5FF4B-AC50-43D6-9A36-D235DF327B01

Q34979021-0F720ECE-9513-47D6-AB97-A7CF6FA2B9B4

Q34979021-1453DD6E-C886-47B6-A329-455E92747555

Q34979021-171791BA-9117-40F7-8961-B67695D9F80E

Q34979021-171CE5E6-FF7D-44D8-80D4-4B44E51D6389

Q34979021-23648FF3-45A7-42CC-BB89-D28996908AD3

Q34979021-35863B83-F3F4-42A3-9B05-7C24F3604FD7

Q34979021-3B349E02-8222-4216-BA4E-C30834153F2B

Q34979021-41A4CC3F-D715-445A-A37C-8CD968D816DB

P304

Q34979021-B3E97AB3-2ED8-41B7-A644-62A2662051EE

P31

Q34979021-CC4EC458-A87F-464B-B2CC-73BFFB00E784

P356

Q34979021-677B7E7E-6D78-48A6-A726-857DB6B2E8B6

P407

Q34979021-D0196186-1ACB-4275-B2B5-9B5DF7B67121

P433

Q34979021-D1E07BD2-D6DA-4073-AFDC-BDA1E2CB1464

P478

Q34979021-FCEE6E90-F909-4D4A-9365-F8D41C2CA6CE

P50

Q34979021-4B8958A0-C439-40F4-B51C-CA9CD57AFEE1

P577

Q34979021-BC2CB387-4F67-409A-8574-BF9CBBB304A8

P5875

Q34979021-D84EEF91-5660-4003-937E-C98292F16032

P698

Q34979021-73A0DF48-278B-4A72-BC87-E4ED79D6AE95

P921

Q34979021-0917EF6C-A861-406B-9872-866CE1CAE58F

P932

Q34979021-A5984C7F-4BDE-4BED-80FA-CEB42DA6D4E3

P356

JBC.M111.238535

P1433

Journal of Biological Chemistry

P1476

Funnel-like hexameric assembly ...... pump in gram-negative bacteria

@en

P2093

Bo-Young Yoon

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

Hong-Man Kim

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

Kangseok Lee

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

Minho Lee

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

Nam-Chul Ha

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

Saemee Song

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

So-Young Jun

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

Yongbin Xu

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

P2860

Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export

Crystal structure of bacterial multidrug efflux transporter AcrB

Assembly and Channel Opening in a Bacterial Drug Efflux Machine

Crystal structure of the periplasmic component of a tripartite macrolide-specific efflux pump

The assembled structure of a complete tripartite bacterial multidrug efflux pump

Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa

Crystal structure of the periplasmic region of MacB, a noncanonic ABC transporter

Crystal Structure of the Membrane Fusion Protein CusB from Escherichia coli

Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems

PHENIX: building new software for automated crystallographic structure determination

P304

17910-17920

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

P31

scholarly article

P356

10.1074/JBC.M111.238535

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

P407

P433

20

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

P478

286

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

P50

P577

2011-03-29T00:00:00Z

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

P5875

50939890

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

P698

21454662

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

P921

Gram-negative bacteria

P932

3093866

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