The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
about
Microbial cellulose utilization: fundamentals and biotechnologyStructure, function, and evolution of bacterial ATP-binding cassette systemsThe crystal structure of the MJ0796 ATP-binding cassette. Implications for the structural consequences of ATP hydrolysis in the active site of an ABC transporterThe alternating ATPase domains of MutS control DNA mismatch repairMolecular properties of bacterial multidrug transportersOptimized purification of a heterodimeric ABC transporter in a highly stable form amenable to 2-D crystallizationThe Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding DomainsATP-dependent substrate transport by the ABC transporter MsbA is proton-coupledXenobiotic efflux in bacteria and fungi: a genomics updateA novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein.Determinants of the activity and substrate recognition of breast cancer resistance protein (ABCG2).Catalytic and transport cycles of ABC exporters.Small molecules that dramatically alter multidrug resistance phenotype by modulating the substrate specificity of P-glycoproteinGlutathione stimulates sulfated estrogen transport by multidrug resistance protein 1.Distinct functions of the ATP binding cassettes of transporters associated with antigen processing: a mutational analysis of Walker A and B sequences.NorA functions as a multidrug efflux protein in both cytoplasmic membrane vesicles and reconstituted proteoliposomesThe ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities.Molecular cloning and characterization of an ABC multidrug efflux pump, VcaM, in Non-O1 Vibrio choleraeDrug-lipid A interactions on the Escherichia coli ABC transporter MsbA.Multiple drugbinding sites on the R482G isoform of the ABCG2 transporter.A multidrug ABC transporter with a taste for salt.The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificityStructural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody.Symmetry and structure in P-glycoprotein and ABC transporters what goes around comes around.Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport.Mechanism of ABC transporters: a molecular dynamics simulation of a well characterized nucleotide-binding subunit.EfrAB, an ABC multidrug efflux pump in Enterococcus faecalis.Multidrug transporters in prokaryotic and eukaryotic cells: physiological functions and transport mechanisms.Multidrug resistance ABC transporters.Vibrio cholerae strains with mutations in an atypical type I secretion system accumulate RTX toxin intracellularlyUncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transportersUnderstanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1A new GntR family transcriptional regulator in streptomyces coelicolor is required for morphogenesis and antibiotic production and controls transcription of an ABC transporter in response to carbon sourceNative mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.Structure and function of efflux pumps that confer resistance to drugsTetrandrine reverses drug resistance in isoniazid and ethambutol dual drug-resistant Mycobacterium tuberculosis clinical isolates.TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitansHow do ABC transporters drive transport?The emerging pharmacotherapeutic significance of the breast cancer resistance protein (ABCG2).
P2860
Q24533239-D31160E7-064C-4BA3-95F5-C8A7C140D08CQ24643436-0A2EF4DE-3EA6-4484-8F14-E53E74FEFEC4Q27632558-D78CF264-937D-4F28-8D7F-A5D61D82FA4CQ27640375-B0BEC72E-8303-4593-BC75-CBC33E0C566AQ28139376-A8278106-6843-44EC-9B44-83F53F0732B1Q28478129-4F7B922A-E795-43C3-90EB-9B59DD157DD3Q28545890-664FC989-AE2E-493C-988D-B145911DA3E9Q28830840-F10DFBAD-FB90-4900-8E9D-A866A48E3C0FQ28834633-0E1253B0-0BB2-421B-8935-92AE970B89A5Q30309937-C6754323-F962-4995-A0F3-4395A47C763BQ30364846-3D42B31E-A6E1-4708-A36F-076B3EA50CD8Q30454423-9BBE54D0-3343-4D6C-8C8A-66B8A7EB0F0FQ31030101-34E59924-F0C7-4EB5-B625-FE5A367310C2Q31645457-66567102-43A3-4CD6-BFA3-0D4DE5DBCE4DQ33181866-53BF480E-1E18-477D-88B5-D09F80ACD839Q33183378-A24463F5-45F7-4244-9F82-F49D8341CABFQ33187645-FAB0DCE2-B2C2-4275-966C-2103A9A84C1DQ33187852-9184DE40-CD62-4658-A26F-E982E6823941Q33223264-08B674C0-38E0-45BD-B132-BA12254C58E9Q33257856-5C2003DE-7D8D-4ED1-BF9B-9A510F9661C5Q33481004-FFB0A422-81A7-4997-9C31-7FD6F4A7E866Q33556191-FC6220AD-BB09-4DD2-8467-53AD9572F6BBQ33577108-2B942054-98A4-44B8-B53C-BA59856EED54Q34010123-E6E3D045-0E10-46F2-A5FA-E569D41D9934Q34087117-448048EC-5341-4FFC-9B59-30E343B4F114Q34188954-7A4C97D7-6CA8-4AC5-BAB9-A39B816356D5Q34230365-F9630C6E-8095-4C82-B859-1A34B7EDBCBAQ34276400-E343EE95-8C37-4122-8161-6D41C0B9DD42Q34278138-8B21A901-D9DB-4F89-AF2D-A49CED4C8393Q34368464-952EC13D-A3F7-4B42-860E-D25D4C2E2A93Q34400982-5C7451B7-13A2-4490-AF10-1BE9C11A2AD1Q34530785-C30250D1-B129-4053-BA66-114DDD0E5C55Q35007411-15704BDC-D636-412E-8153-C7E439DD536CQ35130232-8FDA54BE-DBEF-40C5-A8B7-A37355BEAAF9Q35259130-4C4C7C29-10A3-4B37-8388-E77A25E6B03BQ35294152-A16D9A84-F0F0-438C-91CC-78CDB2C6BAFEQ35562635-1886C928-3AE0-4C16-BBFD-814377828D42Q35696412-EC5C2786-5AB5-4722-91D1-FD3EAD90EE86Q35954774-846A6EC2-F15E-49A5-B89B-0F4B5F051835Q36052743-EE506334-6ED5-4D3C-AA68-760186F029B4
P2860
The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@ast
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@en
type
label
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@ast
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@en
prefLabel
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@ast
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@en
P2093
P2860
P3181
P356
P1433
P1476
The homodimeric ATP-binding ca ...... two-cylinder engine) mechanism
@en
P2093
A Margolles
C F Higgins
W N Konings
P2860
P304
P3181
P356
10.1093/EMBOJ/19.11.2503
P407
P577
2000-06-01T00:00:00Z