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190 related items for PubMed ID: 12180984

  • 1. Functional characterization of the maltose ATP-binding-cassette transporter of Salmonella typhimurium by means of monoclonal antibodies directed against the MalK subunit.
    Stein A, Seifert M, Volkmer-Engert R, Siepelmeyer J, Jahreis K, Schneider E.
    Eur J Biochem; 2002 Aug; 269(16):4074-85. PubMed ID: 12180984
    [Abstract] [Full Text] [Related]

  • 2. 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; 22(4):655-66. PubMed ID: 8951813
    [Abstract] [Full Text] [Related]

  • 3. 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; 266(2):420-30. PubMed ID: 10561582
    [Abstract] [Full Text] [Related]

  • 4. 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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  • 5. Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly.
    Böhm A, Diez J, Diederichs K, Welte W, Boos W.
    J Biol Chem; 2002 Feb 01; 277(5):3708-17. PubMed ID: 11709552
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  • 8. Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. The maltose transport system of Escherichia coli.
    Panagiotidis CH, Reyes M, Sievertsen A, Boos W, Shuman HA.
    J Biol Chem; 1993 Nov 05; 268(31):23685-96. PubMed ID: 8226895
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  • 9. Large-scale purification, dissociation and functional reassembly of the maltose ATP-binding cassette transporter (MalFGK(2)) of Salmonella typhimurium.
    Landmesser H, Stein A, Blüschke B, Brinkmann M, Hunke S, Schneider E.
    Biochim Biophys Acta; 2002 Sep 20; 1565(1):64-72. PubMed ID: 12225853
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  • 10. Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli.
    Davidson AL, Sharma S.
    J Bacteriol; 1997 Sep 20; 179(17):5458-64. PubMed ID: 9287001
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  • 11. 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 20; 173(7):2180-6. PubMed ID: 2007546
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  • 12. The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon.
    Panagiotidis CH, Boos W, Shuman HA.
    Mol Microbiol; 1998 Nov 20; 30(3):535-46. PubMed ID: 9822819
    [Abstract] [Full Text] [Related]

  • 13. Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex.
    Samanta S, Ayvaz T, Reyes M, Shuman HA, Chen J, Davidson AL.
    J Biol Chem; 2003 Sep 12; 278(37):35265-71. PubMed ID: 12813052
    [Abstract] [Full Text] [Related]

  • 14. Domain structure of the ATP-binding-cassette protein MalK of salmonella typhimurium as assessed by coexpressed half molecules and LacK'-'MalK chimeras.
    Schmees G, Schneider E.
    J Bacteriol; 1998 Oct 12; 180(20):5299-305. PubMed ID: 9765559
    [Abstract] [Full Text] [Related]

  • 15. Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter.
    Alvarez FJ, Orelle C, Huang Y, Bajaj R, Everly RM, Klug CS, Davidson AL.
    Mol Microbiol; 2015 Dec 12; 98(5):878-94. PubMed ID: 26268698
    [Abstract] [Full Text] [Related]

  • 16. Mapping putative contact sites between subunits in a bacterial ATP-binding cassette (ABC) transporter by synthetic peptide libraries.
    Blüschke B, Eckey V, Kunert B, Berendt S, Landmesser H, Portwich M, Volkmer R, Schneider E.
    J Mol Biol; 2007 Jun 01; 369(2):386-99. PubMed ID: 17434534
    [Abstract] [Full Text] [Related]

  • 17. MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants.
    Lippincott J, Traxler B.
    J Bacteriol; 1997 Feb 01; 179(4):1337-43. PubMed ID: 9023220
    [Abstract] [Full Text] [Related]

  • 18. Mode of Interaction of the Signal-Transducing Protein EIIA(Glc) with the Maltose ABC Transporter in the Process of Inducer Exclusion.
    Wuttge S, Licht A, Timachi MH, Bordignon E, Schneider E.
    Biochemistry; 2016 Sep 27; 55(38):5442-52. PubMed ID: 27571040
    [Abstract] [Full Text] [Related]

  • 19. MalK forms a dimer independent of its assembly into the MalFGK2 ATP-binding cassette transporter of Escherichia coli.
    Kennedy KA, Traxler B.
    J Biol Chem; 1999 Mar 05; 274(10):6259-64. PubMed ID: 10037713
    [Abstract] [Full Text] [Related]

  • 20. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator malt by antagonizing inducer binding.
    Joly N, Böhm A, Boos W, Richet E.
    J Biol Chem; 2004 Aug 06; 279(32):33123-30. PubMed ID: 15180985
    [Abstract] [Full Text] [Related]

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