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156 related items for PubMed ID: 18445585

  • 1. The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner.
    Pinheiro BA, Proctor MR, Martinez-Fleites C, Prates JA, Money VA, Davies GJ, Bayer EA, Fontesm CM, Fierobe HP, Gilbert HJ.
    J Biol Chem; 2008 Jun 27; 283(26):18422-30. PubMed ID: 18445585
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  • 2. Indirect ELISA-based approach for comparative measurement of high-affinity cohesin-dockerin interactions.
    Slutzki M, Barak Y, Reshef D, Schueler-Furman O, Lamed R, Bayer EA.
    J Mol Recognit; 2012 Nov 27; 25(11):616-22. PubMed ID: 23108621
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  • 3. Crucial roles of single residues in binding affinity, specificity, and promiscuity in the cellulosomal cohesin-dockerin interface.
    Slutzki M, Reshef D, Barak Y, Haimovitz R, Rotem-Bamberger S, Lamed R, Bayer EA, Schueler-Furman O.
    J Biol Chem; 2015 May 29; 290(22):13654-66. PubMed ID: 25833947
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  • 5. A cellulosomal double-dockerin module from Clostridium thermocellum shows distinct structural and cohesin-binding features.
    Chen C, Yang H, Dong S, You C, Moraïs S, Bayer EA, Liu YJ, Xuan J, Cui Q, Mizrahi I, Feng Y.
    Protein Sci; 2024 Apr 29; 33(4):e4937. PubMed ID: 38501488
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  • 6. Unraveling enzyme discrimination during cellulosome assembly independent of cohesin-dockerin affinity.
    Borne R, Bayer EA, Pagès S, Perret S, Fierobe HP.
    FEBS J; 2013 Nov 29; 280(22):5764-79. PubMed ID: 24033928
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  • 12. Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition.
    Spinelli S, Fiérobe HP, Belaïch A, Belaïch JP, Henrissat B, Cambillau C.
    J Mol Biol; 2000 Nov 24; 304(2):189-200. PubMed ID: 11080455
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  • 15. Cohesin-dockerin interaction in cellulosome assembly: a single hydroxyl group of a dockerin domain distinguishes between nonrecognition and high affinity recognition.
    Mechaly A, Fierobe HP, Belaich A, Belaich JP, Lamed R, Shoham Y, Bayer EA.
    J Biol Chem; 2001 Mar 30; 276(13):9883-8. PubMed ID: 11148206
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  • 16. Revisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation.
    Chen C, Cui Z, Xiao Y, Cui Q, Smith SP, Lamed R, Bayer EA, Feng Y.
    J Struct Biol; 2014 Nov 30; 188(2):188-93. PubMed ID: 25270376
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  • 19. Species-specificity of the cohesin-dockerin interaction between Clostridium thermocellum and Clostridium cellulolyticum: prediction of specificity determinants of the dockerin domain.
    Pagès S, Bélaïch A, Bélaïch JP, Morag E, Lamed R, Shoham Y, Bayer EA.
    Proteins; 1997 Dec 30; 29(4):517-27. PubMed ID: 9408948
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  • 20. Functional asymmetry in cohesin binding belies inherent symmetry of the dockerin module: insight into cellulosome assembly revealed by systematic mutagenesis.
    Karpol A, Barak Y, Lamed R, Shoham Y, Bayer EA.
    Biochem J; 2008 Mar 01; 410(2):331-8. PubMed ID: 18021074
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