| Year |
Citation |
Score |
| 2021 |
Forshaw TE, Reisz JA, Nelson KJ, Gumpena R, Lawson JR, Jönsson TJ, Wu H, Clodfelter JE, Johnson LC, Furdui CM, Lowther WT. Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants (Basel, Switzerland). 10. PMID 34208049 DOI: 10.3390/antiox10060946 |
0.361 |
|
| 2016 |
Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure (London, England : 1993). PMID 27594682 DOI: 10.1016/J.Str.2016.07.012 |
0.366 |
|
| 2015 |
Randall L, Manta B, Nelson KJ, Santos J, Poole LB, Denicola A. Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form. Archives of Biochemistry and Biophysics. PMID 26612102 DOI: 10.1016/J.Abb.2015.11.032 |
0.388 |
|
| 2015 |
Perkins A, Nelson KJ, Parsonage D, Poole LB, Karplus PA. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends in Biochemical Sciences. 40: 435-45. PMID 26067716 DOI: 10.1016/J.Tibs.2015.05.001 |
0.337 |
|
| 2015 |
Parsonage D, Nelson KJ, Ferrer-Sueta G, Alley S, Karplus PA, Furdui CM, Poole LB. Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC. Biochemistry. 54: 1567-75. PMID 25633283 DOI: 10.1021/Bi501515W |
0.33 |
|
| 2013 |
Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin. Biochemistry. 52: 8708-21. PMID 24175952 DOI: 10.1021/Bi4011573 |
0.385 |
|
| 2012 |
Perkins A, Gretes MC, Nelson KJ, Poole LB, Karplus PA. Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes. Biochemistry. 51: 7638-50. PMID 22928725 DOI: 10.1021/Bi301017S |
0.351 |
|
| 2011 |
Nelson KJ, Knutson ST, Soito L, Klomsiri C, Poole LB, Fetrow JS. Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis. Proteins. 79: 947-64. PMID 21287625 DOI: 10.1002/Prot.22936 |
0.316 |
|
| 2011 |
Hall A, Nelson K, Poole LB, Karplus PA. Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxidants & Redox Signaling. 15: 795-815. PMID 20969484 DOI: 10.1089/Ars.2010.3624 |
0.387 |
|
| 2008 |
Zhang L, Nelson KJ, Rajagopalan KV, George GN. Structure of the molybdenum site of Escherichia coli trimethylamine N-oxide reductase. Inorganic Chemistry. 47: 1074-8. PMID 18163615 DOI: 10.1021/Ic701956F |
0.515 |
|
| 2007 |
George GN, Nelson KJ, Harris HH, Doonan CJ, Rajagopalan KV. Interaction of product analogues with the active site of rhodobacter sphaeroides dimethyl sulfoxide reductase. Inorganic Chemistry. 46: 3097-104. PMID 17361996 DOI: 10.1021/Ic0619052 |
0.511 |
|
| 2004 |
Nelson KJ, Rajagopalan KV. Studies on the interaction of NADPH with Rhodobacter sphaeroides biotin sulfoxide reductase. Biochemistry. 43: 11226-37. PMID 15366932 DOI: 10.1021/Bi0490845 |
0.513 |
|
| 2003 |
Raitsimring AM, Astashkin AV, Feng C, Enemark JH, Nelson KJ, Rajagopalan KV. Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 95-104. PMID 12459903 DOI: 10.1007/S00775-002-0393-8 |
0.425 |
|
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