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Items: 1 to 20 of 130

1.

The single-domain globin from the pathogenic bacterium Campylobacter jejuni: novel D-helix conformation, proximal hydrogen bonding that influences ligand binding, and peroxidase-like redox properties.

Shepherd M, Barynin V, Lu C, Bernhardt PV, Wu G, Yeh SR, Egawa T, Sedelnikova SE, Rice DW, Wilson JL, Poole RK.

J Biol Chem. 2010 Apr 23;285(17):12747-54. doi: 10.1074/jbc.M109.084509. Epub 2010 Feb 17.

2.
3.

The globins of Campylobacter jejuni.

Tinajero-Trejo M, Shepherd M.

Adv Microb Physiol. 2013;63:97-145. doi: 10.1016/B978-0-12-407693-8.00004-2. Review.

PMID:
24054796
4.

Nitric oxide reactivities of the two globins of the foodborne pathogen Campylobacter jejuni: roles in protection from nitrosative stress and analysis of potential reductants.

Tinajero-Trejo M, Vreugdenhil A, Sedelnikova SE, Davidge KS, Poole RK.

Nitric Oxide. 2013 Nov 1;34:65-75. doi: 10.1016/j.niox.2013.06.002. Epub 2013 Jun 11.

PMID:
23764490
5.

Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni.

Lu C, Mukai M, Lin Y, Wu G, Poole RK, Yeh SR.

J Biol Chem. 2007 Aug 31;282(35):25917-28. Epub 2007 Jul 2.

6.

Structural and functional properties of a truncated hemoglobin from a food-borne pathogen Campylobacter jejuni.

Lu C, Egawa T, Wainwright LM, Poole RK, Yeh SR.

J Biol Chem. 2007 May 4;282(18):13627-36. Epub 2007 Mar 5.

7.

Ferrous Campylobacter jejuni truncated hemoglobin P displays an extremely high reactivity for cyanide - a comparative study.

Bolli A, Ciaccio C, Coletta M, Nardini M, Bolognesi M, Pesce A, Guertin M, Visca P, Ascenzi P.

FEBS J. 2008 Feb;275(4):633-45. doi: 10.1111/j.1742-4658.2007.06223.x. Epub 2008 Jan 10.

8.

Expression and purification of Cgb and Ctb, the NO-inducible globins of the foodborne bacterial pathogen C. jejuni.

Pickford JL, Wainwright L, Wu G, Poole RK.

Methods Enzymol. 2008;436:289-302. doi: 10.1016/S0076-6879(08)36016-9.

PMID:
18237639
9.

Role of the distal hydrogen-bonding network in regulating oxygen affinity in the truncated hemoglobin III from Campylobacter jejuni.

Arroyo Mañez P, Lu C, Boechi L, Martí MA, Shepherd M, Wilson JL, Poole RK, Luque FJ, Yeh SR, Estrin DA.

Biochemistry. 2011 May 17;50(19):3946-56. doi: 10.1021/bi101137n. Epub 2011 Apr 25.

10.

Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni.

Nardini M, Pesce A, Labarre M, Richard C, Bolli A, Ascenzi P, Guertin M, Bolognesi M.

J Biol Chem. 2006 Dec 8;281(49):37803-12. Epub 2006 Oct 5.

11.

NssR, a member of the Crp-Fnr superfamily from Campylobacter jejuni, regulates a nitrosative stress-responsive regulon that includes both a single-domain and a truncated haemoglobin.

Elvers KT, Turner SM, Wainwright LM, Marsden G, Hinds J, Cole JA, Poole RK, Penn CW, Park SF.

Mol Microbiol. 2005 Aug;57(3):735-50.

12.

Functional implications of the proximal site hydrogen bonding network in Vitreoscilla hemoglobin (VHb): role of Tyr95 (G5) and Tyr126 (H12).

Kaur R, Ahuja S, Anand A, Singh B, Stark BC, Webster DA, Dikshit KL.

FEBS Lett. 2008 Oct 15;582(23-24):3494-500. doi: 10.1016/j.febslet.2008.09.018. Epub 2008 Sep 18.

13.

Globin-mediated nitric oxide detoxification in the foodborne pathogenic bacterium Campylobacter jejuni proceeds via a dioxygenase or denitrosylase mechanism.

Shepherd M, Bernhardt PV, Poole RK.

Nitric Oxide. 2011 Aug 1;25(2):229-33. doi: 10.1016/j.niox.2010.12.006. Epub 2011 Jan 5.

PMID:
21215320
14.

Redox-mediated interactions of VHb (Vitreoscilla haemoglobin) with OxyR: novel regulation of VHb biosynthesis under oxidative stress.

Anand A, Duk BT, Singh S, Akbas MY, Webster DA, Stark BC, Dikshit KL.

Biochem J. 2010 Feb 24;426(3):271-80. doi: 10.1042/BJ20091417.

PMID:
20025616
15.

The NO-responsive hemoglobins of Campylobacter jejuni: concerted responses of two globins to NO and evidence in vitro for globin regulation by the transcription factor NssR.

Smith HK, Shepherd M, Monk C, Green J, Poole RK.

Nitric Oxide. 2011 Aug 1;25(2):234-41. doi: 10.1016/j.niox.2010.12.009. Epub 2011 Jan 1.

PMID:
21199674
16.

Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.

Ouellet YH, Daigle R, Lagüe P, Dantsker D, Milani M, Bolognesi M, Friedman JM, Guertin M.

J Biol Chem. 2008 Oct 3;283(40):27270-8. doi: 10.1074/jbc.M804215200. Epub 2008 Aug 2.

17.

Structural basis of human cytoglobin for ligand binding.

Sugimoto H, Makino M, Sawai H, Kawada N, Yoshizato K, Shiro Y.

J Mol Biol. 2004 Jun 11;339(4):873-85.

PMID:
15165856
18.

The roles of Tyr(CD1) and Trp(G8) in Mycobacterium tuberculosis truncated hemoglobin O in ligand binding and on the heme distal site architecture.

Ouellet H, Milani M, LaBarre M, Bolognesi M, Couture M, Guertin M.

Biochemistry. 2007 Oct 16;46(41):11440-50. Epub 2007 Sep 22.

PMID:
17887774
19.
20.

Structural characterization of the proximal and distal histidine environment of cytoglobin and neuroglobin.

Sawai H, Makino M, Mizutani Y, Ohta T, Sugimoto H, Uno T, Kawada N, Yoshizato K, Kitagawa T, Shiro Y.

Biochemistry. 2005 Oct 11;44(40):13257-65.

PMID:
16201751

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