Year |
Citation |
Score |
2015 |
Kuiper BD, Keusch BJ, Dewdney TG, Chordia P, Ross K, Brunzelle JS, Kovari IA, MacArthur R, Salimnia H, Kovari LC. The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops. Biochemistry and Biophysics Reports. 2: 160-165. PMID 29124158 DOI: 10.1016/J.Bbrep.2015.06.003 |
0.84 |
|
2015 |
Kuiper BD, Keusch BJ, Dewdney TG, Chordia P, Ross K, Brunzelle JS, Kovari IA, MacArthur R, Salimnia H, Kovari LC. The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops Biochemistry and Biophysics Reports. 2: 160-165. DOI: 10.1016/j.bbrep.2015.06.003 |
0.825 |
|
2014 |
Chordia P, Dewdney TG, Keusch B, Kuiper BD, Ross K, Kovari IA, MacArthur R, Salimnia H, Kovari LC. The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics. Discoveries (Craiova, Romania). 2: e27. PMID 32309558 DOI: 10.15190/d.2014.19 |
0.835 |
|
2014 |
Fribourgh JL, Nguyen HC, Matreyek KA, Alvarez FJD, Summers BJ, Dewdney TG, Aiken C, Zhang P, Engelman A, Xiong Y. Structural insight into HIV-1 restriction by MxB. Cell Host & Microbe. 16: 627-638. PMID 25312384 DOI: 10.1016/J.Chom.2014.09.021 |
0.613 |
|
2013 |
Dewdney TG, Wang Y, Liu Z, Sharma SK, Reiter SJ, Brunzelle JS, Kovari IA, Woster PM, Kovari LC. Ligand modifications to reduce the relative resistance of multi-drug resistant HIV-1 protease Bioorganic and Medicinal Chemistry. 21: 7430-7434. PMID 24128815 DOI: 10.1016/J.Bmc.2013.09.045 |
0.736 |
|
2013 |
Dewdney TG, Wang Y, Kovari IA, Reiter SJ, Kovari LC. Reduced HIV-1 integrase flexibility as a mechanism for raltegravir resistance. Journal of Structural Biology. 184: 245-50. PMID 23891838 DOI: 10.1016/J.Jsb.2013.07.008 |
0.823 |
|
2013 |
Liu Z, Yedidi RS, Wang Y, Dewdney TG, Reiter SJ, Brunzelle JS, Kovari IA, Kovari LC. Crystallographic study of multi-drug resistant HIV-1 protease lopinavir complex: mechanism of drug recognition and resistance. Biochemical and Biophysical Research Communications. 437: 199-204. PMID 23792096 DOI: 10.1016/J.Bbrc.2013.06.027 |
0.792 |
|
2013 |
Liu Z, Yedidi RS, Wang Y, Dewdney TG, Reiter SJ, Brunzelle JS, Kovari IA, Kovari LC. Insights into the mechanism of drug resistance: X-ray structure analysis of multi-drug resistant HIV-1 protease ritonavir complex. Biochemical and Biophysical Research Communications. 431: 232-8. PMID 23313846 DOI: 10.1016/J.Bbrc.2012.12.127 |
0.807 |
|
2013 |
Liu Z, Wang Y, Yedidi RS, Dewdney TG, Reiter SJ, Brunzelle JS, Kovari IA, Kovari LC. Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes. Biochemical and Biophysical Research Communications. 430: 1022-7. PMID 23261453 DOI: 10.1016/J.Bbrc.2012.12.045 |
0.79 |
|
2012 |
Wang Y, Dewdney TG, Liu Z, Reiter SJ, Brunzelle JS, Kovari IA, Kovari LC. Higher Desolvation Energy Reduces Molecular Recognition in Multi-Drug Resistant HIV-1 Protease. Biology. 1: 81-93. PMID 24832048 DOI: 10.3390/Biology1010081 |
0.863 |
|
2011 |
Wang Y, Liu Z, Brunzelle JS, Kovari IA, Dewdney TG, Reiter SJ, Kovari LC. The higher barrier of darunavir and tipranavir resistance for HIV-1 protease. Biochemical and Biophysical Research Communications. 412: 737-42. PMID 21871444 DOI: 10.1016/J.Bbrc.2011.08.045 |
0.856 |
|
2011 |
Wang Y, Dewdney TG, Liu Z, Reiter SJ, Brunzelle JS, Kovari IA, Kovari LC. X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions Studia Universitatis Babes-Bolyai Chemia. 221-230. |
0.832 |
|
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