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Xianghui Li, Ph.D. - Publications

Affiliations: 
2008 The University of Mississippi Medical Center 
Area:
Biochemistry

13 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
2016 Chen F, Zhang G, Yu L, Feng Y, Li X, Zhang Z, Wang Y, Sun D, Pradhan S. High-efficiency generation of induced pluripotent mesenchymal stem cells from human dermal fibroblasts using recombinant proteins. Stem Cell Research & Therapy. 7: 99. PMID 27473118 DOI: 10.1186/s13287-016-0358-4  0.8
2011 Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM. Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis. Journal of the American Chemical Society. 133: 5626-8. PMID 21438550 DOI: 10.1021/ja110492p  0.8
2010 Dey M, Li X, Kunz RC, Ragsdale SW. Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue. Biochemistry. 49: 10902-11. PMID 21090696 DOI: 10.1021/bi101562m  0.8
2010 Dey M, Li X, Zhou Y, Ragsdale SW. Evidence for organometallic intermediates in bacterial methane formation involving the nickel coenzyme F₄₃₀. Metal Ions in Life Sciences. 7: 71-110. PMID 20877805 DOI: 10.1039/BK9781847551771-00071  0.8
2010 Li X, Telser J, Kunz RC, Hoffman BM, Gerfen G, Ragsdale SW. Observation of organometallic and radical intermediates formed during the reaction of methyl-coenzyme M reductase with bromoethanesulfonate. Biochemistry. 49: 6866-76. PMID 20597483 DOI: 10.1021/bi100650m  0.8
2009 Lee S, Shin S, Li X, Davidson VL. Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 48: 2442-7. PMID 19196017 DOI: 10.1021/bi802166c  0.8
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  0.8
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  0.8
2006 Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 13276-83. PMID 17073448 DOI: 10.1021/bi061497d  0.8
2006 Pearson AR, Marimanikkuppam S, Li X, Davidson VL, Wilmot CM. Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase. Journal of the American Chemical Society. 128: 12416-7. PMID 16984182 DOI: 10.1021/ja064466e  0.8
2006 Li X, Feng M, Wang Y, Tachikawa H, Davidson VL. Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis. Biochemistry. 45: 821-8. PMID 16411758 DOI: 10.1021/bi052000n  0.8
2005 Wang Y, Li X, Jones LH, Pearson AR, Wilmot CM, Davidson VL. MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. Journal of the American Chemical Society. 127: 8258-9. PMID 15941239 DOI: 10.1021/ja051734k  0.8
2005 Sun D, Li X, Mathews FS, Davidson VL. Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled. Biochemistry. 44: 7200-6. PMID 15882058 DOI: 10.1021/bi050288a  0.8
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