These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Journal Abstract Search


145 related items for PubMed ID: 11148206

  • 1. 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
    [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
    [Abstract] [Full Text] [Related]

  • 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
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 6. Cohesin-dockerin interaction in cellulosome assembly: a single Asp-to-Asn mutation disrupts high-affinity cohesin-dockerin binding.
    Handelsman T, Barak Y, Nakar D, Mechaly A, Lamed R, Shoham Y, Bayer EA.
    FEBS Lett; 2004 Aug 13; 572(1-3):195-200. PubMed ID: 15304347
    [Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 9.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 10. Interaction between a type-II dockerin domain and a type-II cohesin domain from Clostridium thermocellum cellulosome.
    Jindou S, Kajino T, Inagaki M, Karita S, Beguin P, Kimura T, Sakka K, Ohmiya K.
    Biosci Biotechnol Biochem; 2004 Apr 13; 68(4):924-6. PubMed ID: 15118324
    [Abstract] [Full Text] [Related]

  • 11. 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
    [Abstract] [Full Text] [Related]

  • 12. 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 19; 29(4):517-27. PubMed ID: 9408948
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
    Lytle BL, Volkman BF, Westler WM, Heckman MP, Wu JH.
    J Mol Biol; 2001 Mar 30; 307(3):745-53. PubMed ID: 11273698
    [Abstract] [Full Text] [Related]

  • 15. 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
    [Abstract] [Full Text] [Related]

  • 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 24; 188(2):188-93. PubMed ID: 25270376
    [Abstract] [Full Text] [Related]

  • 17. 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]

  • 18. 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]

  • 19. The Dock tag, an affinity tool for the purification of recombinant proteins, based on the interaction between dockerin and cohesin domains from Clostridium josui cellulosome.
    Kamezaki Y, Enomoto C, Ishikawa Y, Koyama T, Naya S, Suzuki T, Sakka K.
    Protein Expr Purif; 2010 Mar 08; 70(1):23-31. PubMed ID: 19836451
    [Abstract] [Full Text] [Related]

  • 20. 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 08; 280(22):5764-79. PubMed ID: 24033928
    [Abstract] [Full Text] [Related]


    Page: [Next] [New Search]
    of 8.