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.
185 related articles for article (PubMed ID: 11023787)
1. Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. Solà M; López-Hernández E; Cronet P; Lacroix E; Serrano L; Coll M; Párraga A J Mol Biol; 2000 Oct; 303(2):213-25. PubMed ID: 11023787 [TBL] [Abstract][Full Text] [Related]
2. Phosphorylation and binding interactions of CheY studied by use of Badan-labeled protein. Stewart RC; VanBruggen R Biochemistry; 2004 Jul; 43(27):8766-77. PubMed ID: 15236585 [TBL] [Abstract][Full Text] [Related]
3. Analysis of ATP binding to CheA containing tryptophan substitutions near the active site. Stewart RC Biochemistry; 2005 Mar; 44(11):4375-85. PubMed ID: 15766267 [TBL] [Abstract][Full Text] [Related]
4. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. McEvoy MM; Muhandiram DR; Kay LE; Dahlquist FW Biochemistry; 1996 May; 35(18):5633-40. PubMed ID: 8639521 [TBL] [Abstract][Full Text] [Related]
5. Mutations in the chemotactic response regulator, CheY, that confer resistance to the phosphatase activity of CheZ. Sanna MG; Swanson RV; Bourret RB; Simon MI Mol Microbiol; 1995 Mar; 15(6):1069-79. PubMed ID: 7623663 [TBL] [Abstract][Full Text] [Related]
6. Active site mutations in CheA, the signal-transducing protein kinase of the chemotaxis system in Escherichia coli. Hirschman A; Boukhvalova M; VanBruggen R; Wolfe AJ; Stewart RC Biochemistry; 2001 Nov; 40(46):13876-87. PubMed ID: 11705377 [TBL] [Abstract][Full Text] [Related]
7. Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM. Dyer CM; Dahlquist FW J Bacteriol; 2006 Nov; 188(21):7354-63. PubMed ID: 17050923 [TBL] [Abstract][Full Text] [Related]
8. Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY. Smith JG; Latiolais JA; Guanga GP; Citineni S; Silversmith RE; Bourret RB J Bacteriol; 2003 Nov; 185(21):6385-91. PubMed ID: 14563873 [TBL] [Abstract][Full Text] [Related]
9. Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. Bourret RB; Hess JF; Simon MI Proc Natl Acad Sci U S A; 1990 Jan; 87(1):41-5. PubMed ID: 2404281 [TBL] [Abstract][Full Text] [Related]
10. Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Swanson RV; Lowry DF; Matsumura P; McEvoy MM; Simon MI; Dahlquist FW Nat Struct Biol; 1995 Oct; 2(10):906-10. PubMed ID: 7552716 [TBL] [Abstract][Full Text] [Related]
11. Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli. Thakor H; Nicholas S; Porter IM; Hand N; Stewart RC J Bacteriol; 2011 Aug; 193(15):3894-903. PubMed ID: 21642453 [TBL] [Abstract][Full Text] [Related]
12. The response regulators CheB and CheY exhibit competitive binding to the kinase CheA. Li J; Swanson RV; Simon MI; Weis RM Biochemistry; 1995 Nov; 34(45):14626-36. PubMed ID: 7578071 [TBL] [Abstract][Full Text] [Related]
13. Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor. Swain KE; Gonzalez MA; Falke JJ Biochemistry; 2009 Oct; 48(39):9266-77. PubMed ID: 19705835 [TBL] [Abstract][Full Text] [Related]
14. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM. McEvoy MM; Bren A; Eisenbach M; Dahlquist FW J Mol Biol; 1999 Jun; 289(5):1423-33. PubMed ID: 10373376 [TBL] [Abstract][Full Text] [Related]
15. The CheZ-binding surface of CheY overlaps the CheA- and FliM-binding surfaces. Zhu X; Volz K; Matsumura P J Biol Chem; 1997 Sep; 272(38):23758-64. PubMed ID: 9295320 [TBL] [Abstract][Full Text] [Related]
16. Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching. Coleman MD; Bass RB; Mehan RS; Falke JJ Biochemistry; 2005 May; 44(21):7687-95. PubMed ID: 15909983 [TBL] [Abstract][Full Text] [Related]
17. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Stock AM; Mottonen JM; Stock JB; Schutt CE Nature; 1989 Feb; 337(6209):745-9. PubMed ID: 2645526 [TBL] [Abstract][Full Text] [Related]
18. The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides. McAdams K; Casper ES; Matthew Haas R; Santarsiero BD; Eggler AL; Mesecar A; Halkides CJ Arch Biochem Biophys; 2008 Nov; 479(2):105-13. PubMed ID: 18801331 [TBL] [Abstract][Full Text] [Related]
19. 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 Biochemistry; 2004 Jun; 43(22):6909-16. PubMed ID: 15170328 [TBL] [Abstract][Full Text] [Related]