Year |
Citation |
Score |
2022 |
Peng C, Namanja AT, Munoz E, Wu H, Frederick TE, Maestre-Martinez M, Iglesias Fernandez I, Sun Q, Cobas C, Sun C, Petros AM. Efficiently driving protein-based fragment screening and lead discovery using two-dimensional NMR. Journal of Biomolecular Nmr. PMID 36512150 DOI: 10.1007/s10858-022-00410-3 |
0.312 |
|
2019 |
Namanja AT, Xu J, Wu H, Sun Q, Upadhyay AK, Sun C, Van Doren SR, Petros AM. NMR-based fragment screening and lead discovery accelerated by principal component analysis. Journal of Biomolecular Nmr. PMID 31541395 DOI: 10.1007/S10858-019-00279-9 |
0.395 |
|
2016 |
Namanja AT, Wang J, Buettner R, Colson L, Chen Y. Allosteric Communication Across STAT3 Domains Associated with STAT3 Function and Disease-causing Mutation. Journal of Molecular Biology. PMID 26774853 DOI: 10.1016/j.jmb.2016.01.003 |
0.335 |
|
2014 |
Chen CH, Namanja AT, Chen Y. Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding. Nature Communications. 5: 4968. PMID 25263960 DOI: 10.1038/Ncomms5968 |
0.471 |
|
2014 |
Namanja A, Chen C, Chen Y. Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19885 |
0.359 |
|
2014 |
Namanja AT, Buettner R, Jove R, Chen Y. Abstract 1636: NMR discovery and molecular-basis of small molecule inhibitors of STAT3 Cancer Research. 74: 1636-1636. DOI: 10.1158/1538-7445.Am2014-1636 |
0.305 |
|
2013 |
Madu IG, Namanja AT, Su Y, Wong S, Li YJ, Chen Y. Identification and characterization of a new chemotype of noncovalent SENP inhibitors. Acs Chemical Biology. 8: 1435-41. PMID 23614497 DOI: 10.1021/Cb400177Q |
0.34 |
|
2013 |
Namanja A, Chen C, Chen Y. Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for Mutant SENP1 C603S Catalytic Domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr19083 |
0.348 |
|
2012 |
Hu W, Namanja AT, Wong S, Chen Y. Selective editing of Val and Leu methyl groups in high molecular weight protein NMR. Journal of Biomolecular Nmr. 53: 113-24. PMID 22532128 DOI: 10.1007/S10858-012-9629-2 |
0.309 |
|
2012 |
Namanja AT, Li YJ, Su Y, Wong S, Lu J, Colson LT, Wu C, Li SS, Chen Y. Insights into high affinity small ubiquitin-like modifier (SUMO) recognition by SUMO-interacting motifs (SIMs) revealed by a combination of NMR and peptide array analysis. The Journal of Biological Chemistry. 287: 3231-40. PMID 22147707 DOI: 10.1074/Jbc.M111.293118 |
0.445 |
|
2011 |
Namanja AT, Wang XJ, Xu B, Mercedes-Camacho AY, Wilson KA, Etzkorn FA, Peng JW. Stereospecific gating of functional motions in Pin1. Proceedings of the National Academy of Sciences of the United States of America. 108: 12289-94. PMID 21746900 DOI: 10.1073/Pnas.1019382108 |
0.593 |
|
2010 |
Namanja AT, Wang XJ, Xu B, Mercedes-Camacho AY, Wilson BD, Wilson KA, Etzkorn FA, Peng JW. Toward flexibility-activity relationships by NMR spectroscopy: dynamics of Pin1 ligands. Journal of the American Chemical Society. 132: 5607-9. PMID 20356313 DOI: 10.1021/Ja9096779 |
0.561 |
|
2009 |
Peng JW, Wilson BD, Namanja AT. Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance. Journal of Biomolecular Nmr. 45: 171-83. PMID 19639385 DOI: 10.1007/S10858-009-9349-4 |
0.579 |
|
2007 |
Namanja AT, Peng T, Zintsmaster JS, Elson AC, Shakour MG, Peng JW. Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1. Structure (London, England : 1993). 15: 313-27. PMID 17355867 DOI: 10.1016/J.Str.2007.01.014 |
0.568 |
|
2007 |
Peng T, Zintsmaster JS, Namanja AT, Peng JW. Sequence-specific dynamics modulate recognition specificity in WW domains. Nature Structural & Molecular Biology. 14: 325-31. PMID 17334375 DOI: 10.1038/Nsmb1207 |
0.574 |
|
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