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Items: 1 to 20 of 104


The structure of a reduced form of OxyR from Neisseria meningitidis.

Sainsbury S, Ren J, Nettleship JE, Saunders NJ, Stuart DI, Owens RJ.

BMC Struct Biol. 2010 May 17;10:10. doi: 10.1186/1472-6807-10-10.


Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.

Svintradze DV, Peterson DL, Collazo-Santiago EA, Lewis JP, Wright HT.

Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2091-103. doi: 10.1107/S0907444913019471. Epub 2013 Sep 20.


The major catalase gene (katA) of Pseudomonas aeruginosa PA14 is under both positive and negative control of the global transactivator OxyR in response to hydrogen peroxide.

Heo YJ, Chung IY, Cho WJ, Lee BY, Kim JH, Choi KH, Lee JW, Hassett DJ, Cho YH.

J Bacteriol. 2010 Jan;192(2):381-90. doi: 10.1128/JB.00980-09. Epub 2009 Nov 20.


A novel OxyR sensor and regulator of hydrogen peroxide stress with one cysteine residue in Deinococcus radiodurans.

Chen H, Xu G, Zhao Y, Tian B, Lu H, Yu X, Xu Z, Ying N, Hu S, Hua Y.

PLoS One. 2008 Feb 13;3(2):e1602. doi: 10.1371/journal.pone.0001602.


Structural basis of the redox switch in the OxyR transcription factor.

Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu SE.

Cell. 2001 Apr 6;105(1):103-13.


Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) from Neisseria meningitidis.

Sainsbury S, Ren J, Saunders NJ, Stuart DI, Owens RJ.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):730-7. doi: 10.1107/S1744309112010603. Epub 2012 Jun 22.


OxyR acts as a repressor of catalase expression in Neisseria gonorrhoeae.

Tseng HJ, McEwan AG, Apicella MA, Jennings MP.

Infect Immun. 2003 Jan;71(1):550-6.


Structural details of the OxyR peroxide-sensing mechanism.

Jo I, Chung IY, Bae HW, Kim JS, Song S, Cho YH, Ha NC.

Proc Natl Acad Sci U S A. 2015 May 19;112(20):6443-8. doi: 10.1073/pnas.1424495112. Epub 2015 Apr 30.


OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms.

Ieva R, Roncarati D, Metruccio MM, Seib KL, Scarlato V, Delany I.

Mol Microbiol. 2008 Dec;70(5):1152-65. doi: 10.1111/j.1365-2958.2008.06468.x.


Crystal structure of nitrogen regulatory protein IIANtr from Neisseria meningitidis.

Ren J, Sainsbury S, Berrow NS, Alderton D, Nettleship JE, Stammers DK, Saunders NJ, Owens RJ.

BMC Struct Biol. 2005 Aug 10;5:13.


The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases.

Wu J, Neiers F, Boschi-Muller S, Branlant G.

J Biol Chem. 2005 Apr 1;280(13):12344-50. Epub 2005 Jan 24.


OxyR acts as a transcriptional repressor of hydrogen peroxide-inducible antioxidant genes in Corynebacterium glutamicum R.

Teramoto H, Inui M, Yukawa H.

FEBS J. 2013 Jul;280(14):3298-312. doi: 10.1111/febs.12312. Epub 2013 Jun 3.


Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.

Ren J, Nettleship JE, Sainsbury S, Saunders NJ, Owens RJ.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):247-51. doi: 10.1107/S1744309108005411. Epub 2008 Mar 21.


The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.

Nichols CE, Sainsbury S, Ren J, Walter TS, Verma A, Stammers DK, Saunders NJ, Owens RJ.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):204-9. doi: 10.1107/S174430910900414X. Epub 2009 Feb 26.


DRA0336, another OxyR homolog, involved in the antioxidation mechanisms in Deinococcus radiodurans.

Yin L, Wang L, Lu H, Xu G, Chen H, Zhan H, Tian B, Hua Y.

J Microbiol. 2010 Aug;48(4):473-9. doi: 10.1007/s12275-010-0043-8. Epub 2010 Aug 20.


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