Rong Fu - Publications

Affiliations: 
Georgia State University; Emory University 

7 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2013 Liu F, Rehmani I, Esaki S, Fu R, Chen L, de Serrano V, Liu A. Pirin is an iron-dependent redox regulator of NF-κB. Proceedings of the National Academy of Sciences of the United States of America. 110: 9722-7. PMID 23716661 DOI: 10.1073/Pnas.1221743110  0.589
2011 Fu R, Gupta R, Geng J, Dornevil K, Wang S, Zhang Y, Hendrich MP, Liu A. Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase. The Journal of Biological Chemistry. 286: 26541-54. PMID 21632548 DOI: 10.1074/Jbc.M111.253237  0.545
2010 Gupta R, Fu R, Liu A, Hendrich MP. EPR and Mössbauer spectroscopy show inequivalent hemes in tryptophan dioxygenase. Journal of the American Chemical Society. 132: 1098-109. PMID 20047315 DOI: 10.1021/Ja908851E  0.522
2009 Fu R, Liu F, Davidson VL, Liu A. Heme iron nitrosyl complex of MauG reveals an efficient redox equilibrium between hemes with only one heme exclusively binding exogenous ligands. Biochemistry. 48: 11603-5. PMID 19911786 DOI: 10.1021/Bi9017544  0.493
2008 Li X, Fu R, Lee S, Krebs C, Davidson VL, Liu A. A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical. Proceedings of the National Academy of Sciences of the United States of America. 105: 8597-600. PMID 18562294 DOI: 10.1073/Pnas.0801643105  0.508
2008 Li X, Fu R, Liu A, Davidson VL. Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry. 47: 2908-12. PMID 18220357 DOI: 10.1021/Bi702259W  0.48
2006 Li T, Iwaki H, Fu R, Hasegawa Y, Zhang H, Liu A. Alpha-amino-beta-carboxymuconic-epsilon-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily. Biochemistry. 45: 6628-34. PMID 16716073 DOI: 10.1021/Bi060108C  0.642
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