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Journal Abstract Search


770 related items for PubMed ID: 9287001

  • 1.
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  • 3. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits.
    Mourez M, Hofnung M, Dassa E.
    EMBO J; 1997 Jun 02; 16(11):3066-77. PubMed ID: 9214624
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  • 4. A putative helical domain in the MalK subunit of the ATP-binding-cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool.
    Wilken S, Schmees G, Schneider E.
    Mol Microbiol; 1996 Nov 02; 22(4):655-66. PubMed ID: 8951813
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  • 5. ATP modulates subunit-subunit interactions in an ATP-binding cassette transporter (MalFGK2) determined by site-directed chemical cross-linking.
    Hunke S, Mourez M, Jehanno M, Dassa E, Schneider E.
    J Biol Chem; 2000 May 19; 275(20):15526-34. PubMed ID: 10809785
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  • 7. MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants.
    Lippincott J, Traxler B.
    J Bacteriol; 1997 Feb 19; 179(4):1337-43. PubMed ID: 9023220
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  • 9. Functional consequences of mutations in the conserved 'signature sequence' of the ATP-binding-cassette protein MalK.
    Schmees G, Stein A, Hunke S, Landmesser H, Schneider E.
    Eur J Biochem; 1999 Dec 19; 266(2):420-30. PubMed ID: 10561582
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  • 10. The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations.
    Kühnau S, Reyes M, Sievertsen A, Shuman HA, Boos W.
    J Bacteriol; 1991 Apr 19; 173(7):2180-6. PubMed ID: 2007546
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  • 11. Maltose transport in Escherichia coli: mutations that uncouple ATP hydrolysis from transport.
    Panagiotidis CH, Shuman HA.
    Methods Enzymol; 1998 Apr 19; 292():30-9. PubMed ID: 9711544
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  • 12. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins.
    Davidson AL, Shuman HA, Nikaido H.
    Proc Natl Acad Sci U S A; 1992 Mar 15; 89(6):2360-4. PubMed ID: 1549599
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  • 13. Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli.
    Dean DA, Hor LI, Shuman HA, Nikaido H.
    Mol Microbiol; 1992 Aug 15; 6(15):2033-40. PubMed ID: 1406246
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  • 14. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex.
    Hor LI, Shuman HA.
    J Mol Biol; 1993 Oct 20; 233(4):659-70. PubMed ID: 8411172
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  • 15. Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli.
    Merino G, Shuman HA.
    J Biol Chem; 1998 Jan 23; 273(4):2435-44. PubMed ID: 9442094
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  • 16. Maltose transport system of Escherichia coli: an ABC-type transporter.
    Nikaido H.
    FEBS Lett; 1994 Jun 06; 346(1):55-8. PubMed ID: 8206159
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  • 17. Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter.
    Covitz KM, Panagiotidis CH, Hor LI, Reyes M, Treptow NA, Shuman HA.
    EMBO J; 1994 Apr 01; 13(7):1752-9. PubMed ID: 8157012
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  • 18. Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.
    Merino G, Shuman HA.
    J Bacteriol; 1997 Dec 01; 179(24):7687-94. PubMed ID: 9401026
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  • 19. Demonstration of conformational changes associated with activation of the maltose transport complex.
    Mannering DE, Sharma S, Davidson AL.
    J Biol Chem; 2001 Apr 13; 276(15):12362-8. PubMed ID: 11150310
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  • 20. ATP-driven MalK dimer closure and reopening and conformational changes of the "EAA" motifs are crucial for function of the maltose ATP-binding cassette transporter (MalFGK2).
    Daus ML, Grote M, Müller P, Doebber M, Herrmann A, Steinhoff HJ, Dassa E, Schneider E.
    J Biol Chem; 2007 Aug 03; 282(31):22387-96. PubMed ID: 17545154
    [Abstract] [Full Text] [Related]


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