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Similar articles for PubMed (Select 19737354)

1.

ZipN, an FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803.

Marbouty M, Saguez C, Cassier-Chauvat C, Chauvat F.

Mol Microbiol. 2009 Oct;74(2):409-20. doi: 10.1111/j.1365-2958.2009.06873.x. Epub 2009 Sep 8.

PMID:
19737354
2.

Characterization of the Synechocystis strain PCC 6803 penicillin-binding proteins and cytokinetic proteins FtsQ and FtsW and their network of interactions with ZipN.

Marbouty M, Mazouni K, Saguez C, Cassier-Chauvat C, Chauvat F.

J Bacteriol. 2009 Aug;191(16):5123-33. doi: 10.1128/JB.00620-09. Epub 2009 Jun 19.

3.

Characterization of the FtsZ-interacting septal proteins SepF and Ftn6 in the spherical-celled cyanobacterium Synechocystis strain PCC 6803.

Marbouty M, Saguez C, Cassier-Chauvat C, Chauvat F.

J Bacteriol. 2009 Oct;191(19):6178-85. doi: 10.1128/JB.00723-09. Epub 2009 Jul 31.

4.

Molecular analysis of the key cytokinetic components of cyanobacteria: FtsZ, ZipN and MinCDE.

Mazouni K, Domain F, Cassier-Chauvat C, Chauvat F.

Mol Microbiol. 2004 May;52(4):1145-58.

PMID:
15130131
5.

Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins.

D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L.

Microbiology. 2007 Jan;153(Pt 1):124-38.

PMID:
17185541
6.

A large-scale protein protein interaction analysis in Synechocystis sp. PCC6803.

Sato S, Shimoda Y, Muraki A, Kohara M, Nakamura Y, Tabata S.

DNA Res. 2007 Oct 31;14(5):207-16. Epub 2007 Nov 13.

7.

A conserved residue at the extreme C-terminus of FtsZ is critical for the FtsA-FtsZ interaction in Staphylococcus aureus.

Yan K, Pearce KH, Payne DJ.

Biochem Biophys Res Commun. 2000 Apr 13;270(2):387-92.

PMID:
10753635
9.

The Escherichia coli FtsK functional domains involved in its interaction with its divisome protein partners.

Grenga L, Luzi G, Paolozzi L, Ghelardini P.

FEMS Microbiol Lett. 2008 Oct;287(2):163-7. doi: 10.1111/j.1574-6968.2008.01317.x. Epub 2008 Aug 28.

10.

The rpaC gene product regulates phycobilisome-photosystem II interaction in cyanobacteria.

Joshua S, Mullineaux CW.

Biochim Biophys Acta. 2005 Aug 15;1709(1):58-68.

11.

Identification of cyanobacterial cell division genes by comparative and mutational analyses.

Miyagishima SY, Wolk CP, Osteryoung KW.

Mol Microbiol. 2005 Apr;56(1):126-43.

PMID:
15773984
12.

The cyanobacterial cell division factor Ftn6 contains an N-terminal DnaD-like domain.

Marbouty M, Saguez C, Chauvat F.

BMC Struct Biol. 2009 Aug 21;9:54. doi: 10.1186/1472-6807-9-54.

13.

Identification of a region of FtsA required for interaction with FtsZ.

Pichoff S, Lutkenhaus J.

Mol Microbiol. 2007 May;64(4):1129-38.

PMID:
17501933
14.

Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.

Tavares JR, de Souza RF, Meira GL, Gueiros-Filho FJ.

J Bacteriol. 2008 Nov;190(21):7096-107. doi: 10.1128/JB.00064-08. Epub 2008 Sep 5.

15.

Interaction between cell division proteins FtsE and FtsZ.

Corbin BD, Wang Y, Beuria TK, Margolin W.

J Bacteriol. 2007 Apr;189(8):3026-35. Epub 2007 Feb 16.

16.

Role of two essential domains of Escherichia coli FtsA in localization and progression of the division ring.

Rico AI, García-Ovalle M, Mingorance J, Vicente M.

Mol Microbiol. 2004 Sep;53(5):1359-71.

PMID:
15387815
17.
18.

A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.

Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N.

Mol Microbiol. 2006 Jun;60(6):1364-80.

PMID:
16796675
19.

Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.

Shiomi D, Margolin W.

Mol Microbiol. 2007 Dec;66(6):1396-415. Epub 2007 Nov 6.

PMID:
17986188
20.

FtsN-like proteins are conserved components of the cell division machinery in proteobacteria.

Möll A, Thanbichler M.

Mol Microbiol. 2009 May;72(4):1037-53. doi: 10.1111/j.1365-2958.2009.06706.x. Epub 2009 Apr 21.

PMID:
19400794
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