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202 related items for PubMed ID: 19307717
41. Crystal structure of peroxide stress regulator from Streptococcus pyogenes provides functional insights into the mechanism of oxidative stress sensing. Makthal N, Rastegari S, Sanson M, Ma Z, Olsen RJ, Helmann JD, Musser JM, Kumaraswami M. J Biol Chem; 2013 Jun 21; 288(25):18311-24. PubMed ID: 23645680 [Abstract] [Full Text] [Related]
42. An autoinhibited state in the structure of Thermotoga maritima NusG. Drögemüller J, Stegmann CM, Mandal A, Steiner T, Burmann BM, Gottesman ME, Wöhrl BM, Rösch P, Wahl MC, Schweimer K. Structure; 2013 Mar 05; 21(3):365-75. PubMed ID: 23415559 [Abstract] [Full Text] [Related]
43. Crystal structure of an HEPN domain protein (TM0613) from Thermotoga maritima at 1.75 A resolution. Erlandsen H, Canaves JM, Elsliger MA, von Delft F, Brinen LS, Dai X, Deacon AM, Floyd R, Godzik A, Grittini C, Grzechnik SK, Jaroszewski L, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Robb A, Quijano K, Schwarzenbacher R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA. Proteins; 2004 Mar 01; 54(4):806-9. PubMed ID: 14997578 [No Abstract] [Full Text] [Related]
44. NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure. Penhoat CH, Li Z, Atreya HS, Kim S, Yee A, Xiao R, Murray D, Arrowsmith CH, Szyperski T. J Struct Funct Genomics; 2005 Mar 01; 6(1):51-62. PubMed ID: 15965736 [Abstract] [Full Text] [Related]
46. Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA. Resch M, Schiltz E, Titgemeyer F, Muller YA. Nucleic Acids Res; 2010 Apr 16; 38(7):2485-97. PubMed ID: 20047956 [Abstract] [Full Text] [Related]
47. Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding. Franco IS, Mota LJ, Soares CM, de Sá-Nogueira I. J Bacteriol; 2006 Apr 16; 188(8):3024-36. PubMed ID: 16585763 [Abstract] [Full Text] [Related]
48. Members of the IclR family of bacterial transcriptional regulators function as activators and/or repressors. Molina-Henares AJ, Krell T, Eugenia Guazzaroni M, Segura A, Ramos JL. FEMS Microbiol Rev; 2006 Mar 16; 30(2):157-86. PubMed ID: 16472303 [Abstract] [Full Text] [Related]
52. A new glimpse of FadR-DNA crosstalk revealed by deep dissection of the E. coli FadR regulatory protein. Zhang Y, Gao R, Ye H, Wang Q, Feng Y. Protein Cell; 2014 Dec 16; 5(12):928-39. PubMed ID: 25311842 [Abstract] [Full Text] [Related]
53. Identification and characterization of Rv0494: a fatty acid-responsive protein of the GntR/FadR family from Mycobacterium tuberculosis. Biswas RK, Dutta D, Tripathi A, Feng Y, Banerjee M, Singh BN. Microbiology (Reading); 2013 May 16; 159(Pt 5):913-923. PubMed ID: 23475950 [Abstract] [Full Text] [Related]
54. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins. Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP. J Mol Biol; 2003 Oct 31; 333(4):683-95. PubMed ID: 14568530 [Abstract] [Full Text] [Related]
55. Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor. Lynch MJ, Levenson R, Kim EA, Sircar R, Blair DF, Dahlquist FW, Crane BR. Structure; 2017 Feb 07; 25(2):317-328. PubMed ID: 28089452 [Abstract] [Full Text] [Related]
56. Transcriptional and DNA binding activity of the Foxp1/2/4 family is modulated by heterotypic and homotypic protein interactions. Li S, Weidenfeld J, Morrisey EE. Mol Cell Biol; 2004 Jan 07; 24(2):809-22. PubMed ID: 14701752 [Abstract] [Full Text] [Related]
60. A conserved π-helix plays a key role in thermoadaptation of catalysis in the glycoside hydrolase family 4. Mohapatra SB, Manoj N. Biochim Biophys Acta Proteins Proteom; 2021 Jan 07; 1869(1):140523. PubMed ID: 32853774 [Abstract] [Full Text] [Related] Page: [Previous] [Next] [New Search]