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FlhD/FlhC-regulated promoters analyzed by gene array and lacZ gene fusions.
Prüss BM, Liu X, Hendrickson W, Matsumura P. Prüss BM, et al. Among authors: matsumura p. FEMS Microbiol Lett. 2001 Apr 1;197(1):91-7. doi: 10.1111/j.1574-6968.2001.tb10588.x. FEMS Microbiol Lett. 2001. PMID: 11287152
Gene array analysis of Yersinia enterocolitica FlhD and FlhC: regulation of enzymes affecting synthesis and degradation of carbamoylphosphate.
Kapatral V, Campbell JW, Minnich SA, Thomson NR, Matsumura P, Prüß BM. Kapatral V, et al. Among authors: matsumura p. Microbiology (Reading). 2004 Jul;150(Pt 7):2289-2300. doi: 10.1099/mic.0.26814-0. Microbiology (Reading). 2004. PMID: 15256571
Increased motility of Escherichia coli by insertion sequence element integration into the regulatory region of the flhD operon.
Barker CS, Prüss BM, Matsumura P. Barker CS, et al. Among authors: matsumura p. J Bacteriol. 2004 Nov;186(22):7529-37. doi: 10.1128/JB.186.22.7529-7537.2004. J Bacteriol. 2004. PMID: 15516564 Free PMC article.
FlhD/FlhC is a regulator of anaerobic respiration and the Entner-Doudoroff pathway through induction of the methyl-accepting chemotaxis protein Aer.
Prüss BM, Campbell JW, Van Dyk TK, Zhu C, Kogan Y, Matsumura P. Prüss BM, et al. Among authors: matsumura p. J Bacteriol. 2003 Jan;185(2):534-43. doi: 10.1128/jb.185.2.534-543.2003. J Bacteriol. 2003. PMID: 12511500 Free PMC article.
The accessibility of cys-120 in CheA(S) is important for the binding of CheZ and enhancement of CheZ phosphatase activity.
O'Connor C, Matsumura P. O'Connor C, et al. Among authors: matsumura p. Biochemistry. 2004 Jun 8;43(22):6909-16. doi: 10.1021/bi035592n. Biochemistry. 2004. PMID: 15170328
Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli.
Shukla D, Zhu XY, Matsumura P. Shukla D, et al. Among authors: matsumura p. J Biol Chem. 1998 Sep 11;273(37):23993-9. doi: 10.1074/jbc.273.37.23993. J Biol Chem. 1998. PMID: 9727015
Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106.
Zhu X, Rebello J, Matsumura P, Volz K. Zhu X, et al. Among authors: matsumura p. J Biol Chem. 1997 Feb 21;272(8):5000-6. doi: 10.1074/jbc.272.8.5000. J Biol Chem. 1997. PMID: 9030562
Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate.
Wang H, Matsumura P. Wang H, et al. Among authors: matsumura p. Mol Microbiol. 1996 Feb;19(4):695-703. doi: 10.1046/j.1365-2958.1996.393934.x. Mol Microbiol. 1996. PMID: 8820640
CheZ specifically facilitates CheY-phosphate (CheY-P) dephosphorylation and generates a smooth swimming signal. A physical interaction was detected between CheZ and CheAS in wild-type cell lysates by immunoprecipitation. ...Finally, the CheAS/CheZ complex formed in vitro s …
CheZ specifically facilitates CheY-phosphate (CheY-P) dephosphorylation and generates a smooth swimming signal. A physical interactio …
Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli.
Zhu X, Amsler CD, Volz K, Matsumura P. Zhu X, et al. Among authors: matsumura p. J Bacteriol. 1996 Jul;178(14):4208-15. doi: 10.1128/jb.178.14.4208-4215.1996. J Bacteriol. 1996. PMID: 8763950 Free PMC article.
Mutations leading to altered CheA binding cluster on a face of CheY.
Shukla D, Matsumura P. Shukla D, et al. Among authors: matsumura p. J Biol Chem. 1995 Oct 13;270(41):24414-9. doi: 10.1074/jbc.270.41.24414. J Biol Chem. 1995. PMID: 7592655
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