Works matching IS 0950382X AND DT 2015 AND VI 95 AND IP 6
Results: 12
A role for the Fts QLB complex in cytokinetic ring activation revealed by an fts L allele that accelerates division.
- Published in:
- Molecular Microbiology, 2015, v. 95, n. 6, p. 925, doi. 10.1111/mmi.12905
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- Article
Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in E scherichia coli.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 945, doi. 10.1111/mmi.12906
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- Article
The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA- FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 971, doi. 10.1111/mmi.12907
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- Article
Last but not least: new insights into how FtsN triggers constriction during E scherichia coli cell division.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 903, doi. 10.1111/mmi.12925
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- Article
Identification of NoxD/ Pro41 as the homologue of the p22<sup>phox</sup> NADPH oxidase subunit in fungi.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 1006, doi. 10.1111/mmi.12876
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- Article
Conservation of fungal and animal nicotinamide adenine dinucleotide phosphate oxidase complexes.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 910, doi. 10.1111/mmi.12946
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- Article
Hybrid histidine kinases in pathogenic fungi.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 914, doi. 10.1111/mmi.12911
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- Article
The Bacterial signal transduction protein GlnB regulates the committed step in fatty acid biosynthesis by acting as a dissociable regulatory subunit of acetyl- CoA carboxylase.
- Published in:
- Molecular Microbiology, 2015, v. 95, n. 6, p. 1025, doi. 10.1111/mmi.12912
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- Publication type:
- Article
Post-transcriptional regulation of transcript abundance by a conserved member of the tristetraprolin family in C andida albicans.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 1036, doi. 10.1111/mmi.12913
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- Article
L egionella pneumophila utilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization.
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- Molecular Microbiology, 2015, v. 95, n. 6, p. 1054, doi. 10.1111/mmi.12914
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- Article
The DsbA2 disulfide-bond oxidase/isomerase system from Legionella pneumophila is coupled to two membrane spanning DsbD proteins and two DsbB oxidases. Homodimeric DsbA2 is partially reduced (thereby providing both DsbA oxidase and DsbC-like protein disulfide isomerase functions) and is required to manage disulfide bonding in DotG, a core component of the Dot/Icm secretion system. For details, see the article by Kpadeh et al. on pp. 1054-1069 of this issue.
- Published in:
- Molecular Microbiology, 2015, v. 95, n. 6, p. i, doi. 10.1111/mmi.12980
- Publication type:
- Article
BcNoxD, a putative ER protein, is a new component of the NADPH oxidase complex in B otrytis cinerea.
- Published in:
- Molecular Microbiology, 2015, v. 95, n. 6, p. 988, doi. 10.1111/mmi.12869
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- Article