Year |
Citation |
Score |
2020 |
Orans J, Kovach AR, Hoff KE, Horstmann NM, Brennan RG. Crystal structure of an Escherichia coli Hfq Core (residues 2-69)-DNA complex reveals multifunctional nucleic acid binding sites. Nucleic Acids Research. PMID 32133526 DOI: 10.1093/Nar/Gkaa149 |
0.365 |
|
2014 |
Kovach AR, Hoff KE, Canty JT, Orans J, Brennan RG. Recognition of U-rich RNA by Hfq from the Gram-positive pathogen Listeria monocytogenes. Rna (New York, N.Y.). 20: 1548-59. PMID 25150227 DOI: 10.1261/Rna.044032.113 |
0.352 |
|
2014 |
Robinson KE, Orans J, Kovach AR, Link TM, Brennan RG. Mapping Hfq-RNA interaction surfaces using tryptophan fluorescence quenching. Nucleic Acids Research. 42: 2736-49. PMID 24288369 DOI: 10.1093/Nar/Gkt1171 |
0.329 |
|
2012 |
Horstmann N, Orans J, Valentin-Hansen P, Shelburne SA, Brennan RG. Structural mechanism of Staphylococcus aureus Hfq binding to an RNA A-tract. Nucleic Acids Research. 40: 11023-35. PMID 22965117 DOI: 10.1093/Nar/Gks809 |
0.349 |
|
2011 |
Tseng Q, Orans J, Hast MA, Iyer RR, Changela A, Modrich PL, Beese LS. Purification, crystallization and preliminary X-ray diffraction analysis of the human mismatch repair protein MutSβ. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 947-52. PMID 21821902 DOI: 10.1107/S1744309111019300 |
0.4 |
|
2011 |
Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS. Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell. 145: 212-23. PMID 21496642 DOI: 10.1016/J.Cell.2011.03.005 |
0.372 |
|
2011 |
Orans J, McSweeney E, Modrich P, Beese LS. Crystal Structures of Human Exonuclease I with DNA Provides Insight into Substrate Selectivity and Mechanism Biophysical Journal. 100: 241a. DOI: 10.1016/J.Bpj.2010.12.1533 |
0.382 |
|
2010 |
Wallace BD, Wang H, Lane KT, Scott JE, Orans J, Koo JS, Venkatesh M, Jobin C, Yeh LA, Mani S, Redinbo MR. Alleviating cancer drug toxicity by inhibiting a bacterial enzyme. Science (New York, N.Y.). 330: 831-5. PMID 21051639 DOI: 10.1126/Science.1191175 |
0.624 |
|
2010 |
Orans J, Johnson MD, Coggan KA, Sperlazza JR, Heiniger RW, Wolfgang MC, Redinbo MR. Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility. Proceedings of the National Academy of Sciences of the United States of America. 107: 1065-70. PMID 20080557 DOI: 10.1073/Pnas.0911616107 |
0.623 |
|
2010 |
Orans J, Johnson MDL, Coggan KA, Sperlazza JR, Heiniger RW, Wolfgang MC, Redinbo MR. Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 3 (1065-1070) DOI:10.1073/pnas.0911616107) Proceedings of the National Academy of Sciences of the United States of America. 107: 5260. DOI: 10.1073/Pnas.1000441107 |
0.572 |
|
2007 |
Xue Y, Moore LB, Orans J, Peng L, Bencharit S, Kliewer SA, Redinbo MR. Crystal structure of the pregnane X receptor-estradiol complex provides insights into endobiotic recognition. Molecular Endocrinology (Baltimore, Md.). 21: 1028-38. PMID 17327420 DOI: 10.1210/Me.2006-0323 |
0.701 |
|
2007 |
Xue Y, Moore LB, Orans J, Peng L, Bencharit S, Kliewer SA, Redinbo MR. Erratum: Crystal structure of the pregnane X receptor-estradiol complex provides insights into endobiotic recognition (Molecular Endocrinology (2007) 21, 5, (1028-1038)) Molecular Endocrinology. 21: 1488-1489. DOI: 10.1210/Me.2007-0000 |
0.682 |
|
2005 |
Orans J, Teotico DG, Redinbo MR. The nuclear xenobiotic receptor pregnane X receptor: recent insights and new challenges. Molecular Endocrinology (Baltimore, Md.). 19: 2891-900. PMID 15961506 DOI: 10.1210/Me.2005-0156 |
0.648 |
|
2005 |
Chrencik JE, Orans J, Moore LB, Xue Y, Peng L, Collins JL, Wisely GB, Lambert MH, Kliewer SA, Redinbo MR. Structural disorder in the complex of human pregnane X receptor and the macrolide antibiotic rifampicin. Molecular Endocrinology (Baltimore, Md.). 19: 1125-34. PMID 15705662 DOI: 10.1210/Me.2004-0346 |
0.672 |
|
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