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


261 related items for PubMed ID: 23256840

  • 1. Identification of c-di-GMP derivatives resistant to an EAL domain phosphodiesterase.
    Shanahan CA, Gaffney BL, Jones RA, Strobel SA.
    Biochemistry; 2013 Jan 15; 52(2):365-77. PubMed ID: 23256840
    [Abstract] [Full Text] [Related]

  • 2. Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP.
    Christen M, Christen B, Folcher M, Schauerte A, Jenal U.
    J Biol Chem; 2005 Sep 02; 280(35):30829-37. PubMed ID: 15994307
    [Abstract] [Full Text] [Related]

  • 3. Structural insight into the mechanism of c-di-GMP hydrolysis by EAL domain phosphodiesterases.
    Tchigvintsev A, Xu X, Singer A, Chang C, Brown G, Proudfoot M, Cui H, Flick R, Anderson WF, Joachimiak A, Galperin MY, Savchenko A, Yakunin AF.
    J Mol Biol; 2010 Sep 24; 402(3):524-38. PubMed ID: 20691189
    [Abstract] [Full Text] [Related]

  • 4. The bacterial second messenger c-di-GMP: probing interactions with protein and RNA binding partners using cyclic dinucleotide analogs.
    Shanahan CA, Strobel SA.
    Org Biomol Chem; 2012 Dec 14; 10(46):9113-29. PubMed ID: 23108253
    [Abstract] [Full Text] [Related]

  • 5. Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication.
    Yadav M, Pal K, Sen U.
    Biochem J; 2019 Nov 15; 476(21):3333-3353. PubMed ID: 31647518
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains.
    Schmidt AJ, Ryjenkov DA, Gomelsky M.
    J Bacteriol; 2005 Jul 15; 187(14):4774-81. PubMed ID: 15995192
    [Abstract] [Full Text] [Related]

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

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

  • 10.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12. Oligoribonuclease is a central feature of cyclic diguanylate signaling in Pseudomonas aeruginosa.
    Cohen D, Mechold U, Nevenzal H, Yarmiyhu Y, Randall TE, Bay DC, Rich JD, Parsek MR, Kaever V, Harrison JJ, Banin E.
    Proc Natl Acad Sci U S A; 2015 Sep 08; 112(36):11359-64. PubMed ID: 26305928
    [Abstract] [Full Text] [Related]

  • 13.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15. Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa.
    Rao F, Yang Y, Qi Y, Liang ZX.
    J Bacteriol; 2008 May 08; 190(10):3622-31. PubMed ID: 18344366
    [Abstract] [Full Text] [Related]

  • 16. Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases.
    Grigorenko BL, Knyazeva MA, Nemukhin AV.
    Proteins; 2016 Nov 08; 84(11):1670-1680. PubMed ID: 27479508
    [Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18. Insights into the GTP-dependent allosteric control of c-di-GMP hydrolysis from the crystal structure of PA0575 protein from Pseudomonas aeruginosa.
    Mantoni F, Paiardini A, Brunotti P, D'Angelo C, Cervoni L, Paone A, Cappellacci L, Petrelli R, Ricciutelli M, Leoni L, Rampioni G, Arcovito A, Rinaldo S, Cutruzzolà F, Giardina G.
    FEBS J; 2018 Oct 08; 285(20):3815-3834. PubMed ID: 30106221
    [Abstract] [Full Text] [Related]

  • 19.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 20.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]


    Page: [Next] [New Search]
    of 14.