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Journal Abstract Search

90 related items for PubMed ID: 15292269

  • 1. Pinpoint mapping of recognition residues on the cohesin surface by progressive homologue swapping.
    Nakar D, Handelsman T, Shoham Y, Fierobe HP, Belaich JP, Morag E, Lamed R, Bayer EA.
    J Biol Chem; 2004 Oct 08; 279(41):42881-8. PubMed ID: 15292269
    [Abstract] [Full Text] [Related]

  • 2. Cohesin-dockerin interactions within and between Clostridium josui and Clostridium thermocellum: binding selectivity between cognate dockerin and cohesin domains and species specificity.
    Jindou S, Soda A, Karita S, Kajino T, Béguin P, Wu JH, Inagaki M, Kimura T, Sakka K, Ohmiya K.
    J Biol Chem; 2004 Mar 12; 279(11):9867-74. PubMed ID: 14688277
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  • 4. 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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  • 6. 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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  • 7. Duplicated dockerin subdomains of Clostridium thermocellum endoglucanase CelD bind to a cohesin domain of the scaffolding protein CipA with distinct thermodynamic parameters and a negative cooperativity.
    Schaeffer F, Matuschek M, Guglielmi G, Miras I, Alzari PM, Béguin P.
    Biochemistry; 2002 Feb 19; 41(7):2106-14. PubMed ID: 11841200
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  • 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
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  • 11. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction.
    Barak Y, Handelsman T, Nakar D, Mechaly A, Lamed R, Shoham Y, Bayer EA.
    J Mol Recognit; 2005 May 29; 18(6):491-501. PubMed ID: 16167300
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  • 12. Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase.
    Chitayat S, Gregg K, Adams JJ, Ficko-Blean E, Bayer EA, Boraston AB, Smith SP.
    J Mol Biol; 2008 Jan 04; 375(1):20-8. PubMed ID: 17999932
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  • 14. Mapping by site-directed mutagenesis of the region responsible for cohesin-dockerin interaction on the surface of the seventh cohesin domain of Clostridium thermocellum CipA.
    Miras I, Schaeffer F, Béguin P, Alzari PM.
    Biochemistry; 2002 Feb 19; 41(7):2115-9. PubMed ID: 11841201
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  • 16. Cohesin-dockerin microarray: Diverse specificities between two complementary families of interacting protein modules.
    Haimovitz R, Barak Y, Morag E, Voronov-Goldman M, Shoham Y, Lamed R, Bayer EA.
    Proteomics; 2008 Mar 19; 8(5):968-79. PubMed ID: 18219699
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  • 18. Crystal structure of a type-II cohesin module from the Bacteroides cellulosolvens cellulosome reveals novel and distinctive secondary structural elements.
    Noach I, Frolow F, Jakoby H, Rosenheck S, Shimon LW, Lamed R, Bayer EA.
    J Mol Biol; 2005 Apr 22; 348(1):1-12. PubMed ID: 15808849
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  • 19. 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
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