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Wen Wei, Ph.D. - Publications

Affiliations: 
2003 Rutgers The State University of New Jersey - Newark, United States 
Area:
Molecular Biology
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5 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
2006 Joseph E, Wei W, Tittmann K, Jordan F. Function of a conserved loop of the beta-domain, not involved in thiamin diphosphate binding, in catalysis and substrate activation in yeast pyruvate decarboxylase. Biochemistry. 45: 13517-27. PMID 17087505 DOI: 10.1021/Bi0615588  0.602
2004 Park YH, Wei W, Zhou L, Nemeria N, Jordan F. Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit. Biochemistry. 43: 14037-46. PMID 15518552 DOI: 10.1021/Bi049027B  0.609
2003 Wei W, Li H, Nemeria N, Jordan F. Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase. Protein Expression and Purification. 28: 140-50. PMID 12651118 DOI: 10.1016/S1046-5928(02)00674-5  0.545
2002 Nemeria N, Arjunan P, Brunskill A, Sheibani F, Wei W, Yan Y, Zhang S, Jordan F, Furey W. Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. Biochemistry. 41: 15459-67. PMID 12501174 DOI: 10.1021/Bi0205909  0.572
2002 Wei W, Liu M, Jordan F. Solvent kinetic isotope effects monitor changes in hydrogen bonding at the active center of yeast pyruvate decarboxylase concomitant with substrate activation: the substituent at position 221 can control the state of activation. Biochemistry. 41: 451-61. PMID 11781083 DOI: 10.1021/Bi0112964  0.526
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