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Journal Abstract Search

295 related items for PubMed ID: 23108621

  • 1. 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; 25(11):616-22. PubMed ID: 23108621
    [Abstract] [Full Text] [Related]

  • 2. Measurements of relative binding of cohesin and dockerin mutants using an advanced ELISA technique for high-affinity interactions.
    Slutzki M, Barak Y, Reshef D, Schueler-Furman O, Lamed R, Bayer EA.
    Methods Enzymol; 2012 Nov; 510():417-28. PubMed ID: 22608739
    [Abstract] [Full Text] [Related]

  • 3. Engineered proteins containing the cohesin and dockerin domains from Clostridium thermocellum provides a reversible, high affinity interaction for biotechnology applications.
    Craig SJ, Foong FC, Nordon R.
    J Biotechnol; 2006 Jan 24; 121(2):165-73. PubMed ID: 16111782
    [Abstract] [Full Text] [Related]

  • 4. Analysis of cohesin-dockerin interactions using mutant dockerin proteins.
    Sakka K, Sugihara Y, Jindou S, Sakka M, Inagaki M, Sakka K, Kimura T.
    FEMS Microbiol Lett; 2011 Jan 24; 314(1):75-80. PubMed ID: 21054503
    [Abstract] [Full Text] [Related]

  • 5. 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 24; 280(22):5764-79. PubMed ID: 24033928
    [Abstract] [Full Text] [Related]

  • 6. Probing the mechanism of cellulosome attachment to the Clostridium thermocellum cell surface: computer simulation of the Type II cohesin-dockerin complex and its variants.
    Xu J, Smith JC.
    Protein Eng Des Sel; 2010 Oct 24; 23(10):759-68. PubMed ID: 20682763
    [Abstract] [Full Text] [Related]

  • 7. Characterization of a dockerin-based affinity tag: application for purification of a broad variety of target proteins.
    Demishtein A, Karpol A, Barak Y, Lamed R, Bayer EA.
    J Mol Recognit; 2010 Oct 24; 23(6):525-35. PubMed ID: 21038354
    [Abstract] [Full Text] [Related]

  • 8. 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
    [Abstract] [Full Text] [Related]

  • 9. Insights into higher-order organization of the cellulosome revealed by a dissect-and-build approach: crystal structure of interacting Clostridium thermocellum multimodular components.
    Adams JJ, Currie MA, Ali S, Bayer EA, Jia Z, Smith SP.
    J Mol Biol; 2010 Mar 05; 396(4):833-9. PubMed ID: 20070943
    [Abstract] [Full Text] [Related]

  • 10. 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
    [Abstract] [Full Text] [Related]

  • 11. Functional insights into the role of novel type I cohesin and dockerin domains from Clostridium thermocellum.
    Pinheiro BA, Gilbert HJ, Sakka K, Sakka K, Fernandes VO, Prates JA, Alves VD, Bolam DN, Ferreira LM, Fontes CM.
    Biochem J; 2009 Dec 10; 424(3):375-84. PubMed ID: 19758121
    [Abstract] [Full Text] [Related]

  • 12. 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
    [Abstract] [Full Text] [Related]

  • 13. Determination of binding affinity upon mutation for type I dockerin-cohesin complexes from Clostridium thermocellum and Clostridium cellulolyticum using deep sequencing.
    Kowalsky CA, Whitehead TA.
    Proteins; 2016 Dec 27; 84(12):1914-1928. PubMed ID: 27699856
    [Abstract] [Full Text] [Related]

  • 14. Cell-surface Attachment of Bacterial Multienzyme Complexes Involves Highly Dynamic Protein-Protein Anchors.
    Cameron K, Najmudin S, Alves VD, Bayer EA, Smith SP, Bule P, Waller H, Ferreira LM, Gilbert HJ, Fontes CM.
    J Biol Chem; 2015 May 22; 290(21):13578-90. PubMed ID: 25855788
    [Abstract] [Full Text] [Related]

  • 15. Novel Clostridium thermocellum type I cohesin-dockerin complexes reveal a single binding mode.
    Brás JL, Alves VD, Carvalho AL, Najmudin S, Prates JA, Ferreira LM, Bolam DN, Romão MJ, Gilbert HJ, Fontes CM.
    J Biol Chem; 2012 Dec 28; 287(53):44394-405. PubMed ID: 23118225
    [Abstract] [Full Text] [Related]

  • 16. Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA.
    Carvalho AL, Pires VM, Gloster TM, Turkenburg JP, Prates JA, Ferreira LM, Romão MJ, Davies GJ, Fontes CM, Gilbert HJ.
    J Mol Biol; 2005 Jun 24; 349(5):909-15. PubMed ID: 15913653
    [Abstract] [Full Text] [Related]

  • 17. Escherichia coli expression, purification, crystallization, and structure determination of bacterial cohesin-dockerin complexes.
    Brás JL, Carvalho AL, Viegas A, Najmudin S, Alves VD, Prates JA, Ferreira LM, Romão MJ, Gilbert HJ, Fontes CM.
    Methods Enzymol; 2012 Jun 24; 510():395-415. PubMed ID: 22608738
    [Abstract] [Full Text] [Related]

  • 18. Structural characterization of type II dockerin module from the cellulosome of Clostridium thermocellum: calcium-induced effects on conformation and target recognition.
    Adams JJ, Webb BA, Spencer HL, Smith SP.
    Biochemistry; 2005 Feb 15; 44(6):2173-82. PubMed ID: 15697243
    [Abstract] [Full Text] [Related]

  • 19. 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 15; 33(4):e4937. PubMed ID: 38501488
    [Abstract] [Full Text] [Related]

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