Year |
Citation |
Score |
2011 |
Lepore BW, Indic M, Pham H, Hearn EM, Patel DR, van den Berg B. Ligand-gated diffusion across the bacterial outer membrane. Proceedings of the National Academy of Sciences of the United States of America. 108: 10121-6. PMID 21593406 DOI: 10.1073/Pnas.1018532108 |
0.333 |
|
2010 |
Lepore BW, Liu D, Peng Y, Fu M, Yasuda C, Manning JM, Silverman RB, Ringe D. Chiral discrimination among aminotransferases: Inactivation by 4-amino-4,5-dihydrothiophenecarboxylic Acid Biochemistry. 49: 3138-3147. PMID 20192272 DOI: 10.1021/Bi902052X |
0.606 |
|
2009 |
Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B. Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature. 458: 367-70. PMID 19182779 DOI: 10.1038/Nature07678 |
0.345 |
|
2007 |
Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D. Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms". Biochemistry. 46: 10517-27. PMID 17713924 DOI: 10.1021/Bi700663N |
0.602 |
|
2006 |
Chen D, Frey PA, Lepore BW, Ringe D, Ruzicka FJ. Identification of structural and catalytic classes of highly conserved amino acid residues in lysine 2,3-aminomutase. Biochemistry. 45: 12647-53. PMID 17042481 DOI: 10.1021/Bi061329L |
0.559 |
|
2005 |
Lepore BW, Ruzicka FJ, Frey PA, Ringe D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proceedings of the National Academy of Sciences of the United States of America. 102: 13819-24. PMID 16166264 DOI: 10.1073/Pnas.0505726102 |
0.576 |
|
2005 |
Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proceedings of the National Academy of Sciences of the United States of America. 102: 11882-7. PMID 16087890 DOI: 10.1073/Pnas.0505255102 |
0.584 |
|
2002 |
Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R. Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 41: 10454-61. PMID 12173932 DOI: 10.1021/Bi026052D |
0.604 |
|
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