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Items: 1 to 20 of 124

1.

Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity.

Ausmees N, Mayer R, Weinhouse H, Volman G, Amikam D, Benziman M, Lindberg M.

FEMS Microbiol Lett. 2001 Oct 16;204(1):163-7.

2.

GGDEF domain is homologous to adenylyl cyclase.

Pei J, Grishin NV.

Proteins. 2001 Feb 1;42(2):210-6.

PMID:
11119645
3.

The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)(2) at the active site.

Yang CY, Chin KH, Chuah ML, Liang ZX, Wang AH, Chou SH.

Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):997-1008. doi: 10.1107/S090744491104039X. Epub 2011 Nov 18.

PMID:
22120736
4.

GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility.

Simm R, Morr M, Kader A, Nimtz M, Römling U.

Mol Microbiol. 2004 Aug;53(4):1123-34.

5.

Cyclic diguanylate turnover mediated by the sole GGDEF/EAL response regulator in Pseudomonas putida: its role in the rhizosphere and an analysis of its target processes.

Matilla MA, Travieso ML, Ramos JL, Ramos-González MI.

Environ Microbiol. 2011 Jul;13(7):1745-66. doi: 10.1111/j.1462-2920.2011.02499.x. Epub 2011 May 9.

PMID:
21554519
6.

Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation.

García B, Latasa C, Solano C, García-del Portillo F, Gamazo C, Lasa I.

Mol Microbiol. 2004 Oct;54(1):264-77.

7.
8.

Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli.

Weber H, Pesavento C, Possling A, Tischendorf G, Hengge R.

Mol Microbiol. 2006 Nov;62(4):1014-34. Epub 2006 Sep 29.

9.

An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control.

Tuckerman JR, Gonzalez G, Sousa EH, Wan X, Saito JA, Alam M, Gilles-Gonzalez MA.

Biochemistry. 2009 Oct 20;48(41):9764-74. doi: 10.1021/bi901409g.

PMID:
19764732
10.

A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum.

Qi Y, Rao F, Luo Z, Liang ZX.

Biochemistry. 2009 Nov 3;48(43):10275-85. doi: 10.1021/bi901121w.

PMID:
19785462
11.
12.

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 2;280(35):30829-37. Epub 2005 Jul 1.

13.

Comparative genomics of cyclic-di-GMP signalling in bacteria: post-translational regulation and catalytic activity.

Seshasayee AS, Fraser GM, Luscombe NM.

Nucleic Acids Res. 2010 Oct;38(18):5970-81. doi: 10.1093/nar/gkq382. Epub 2010 May 18.

14.
15.

A staphylococcal GGDEF domain protein regulates biofilm formation independently of cyclic dimeric GMP.

Holland LM, O'Donnell ST, Ryjenkov DA, Gomelsky L, Slater SR, Fey PD, Gomelsky M, O'Gara JP.

J Bacteriol. 2008 Aug;190(15):5178-89. doi: 10.1128/JB.00375-08. Epub 2008 May 23.

16.

The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain.

Malone JG, Williams R, Christen M, Jenal U, Spiers AJ, Rainey PB.

Microbiology. 2007 Apr;153(Pt 4):980-94.

PMID:
17379708
17.

Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities.

Liu N, Pak T, Boon EM.

Mol Biosyst. 2010 Sep;6(9):1561-4. doi: 10.1039/c002246b. Epub 2010 May 13.

PMID:
20467666
18.

Vibrio parahaemolyticus ScrC modulates cyclic dimeric GMP regulation of gene expression relevant to growth on surfaces.

Ferreira RB, Antunes LC, Greenberg EP, McCarter LL.

J Bacteriol. 2008 Feb;190(3):851-60. Epub 2007 Nov 9.

19.

Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli.

Zähringer F, Massa C, Schirmer T.

Appl Biochem Biotechnol. 2011 Jan;163(1):71-9. doi: 10.1007/s12010-010-9017-x. Epub 2010 Jun 29.

PMID:
20582742
20.

Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae.

Cruz DP, Huertas MG, Lozano M, Zárate L, Zambrano MM.

BMC Microbiol. 2012 Jul 9;12:139. doi: 10.1186/1471-2180-12-139.

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