Andrew T. Namanja, Ph.D.
Affiliations: | 2009 | University of Notre Dame, Notre Dame, IN, United States |
Area:
bio-molecular dynamicsGoogle:
"Andrew Namanja"Parents
Sign in to add mentor| Jeffrey W. Peng | grad student | 2009 | Notre Dame | |
| (Molecular basis for signal transduction in the bimodular cell-cycle enzyme Pin1.) | ||||
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Publications
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| Peng C, Namanja AT, Munoz E, et al. (2022) Efficiently driving protein-based fragment screening and lead discovery using two-dimensional NMR. Journal of Biomolecular Nmr |
| Namanja AT, Xu J, Wu H, et al. (2019) NMR-based fragment screening and lead discovery accelerated by principal component analysis. Journal of Biomolecular Nmr |
| Namanja AT, Wang J, Buettner R, et al. (2016) Allosteric Communication Across STAT3 Domains Associated with STAT3 Function and Disease-causing Mutation. Journal of Molecular Biology |
| Chen CH, Namanja AT, Chen Y. (2014) Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding. Nature Communications. 5: 4968 |
| Namanja A, Chen C, Chen Y. (2014) Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain Journal of Back and Musculoskeletal Rehabilitation |
| Namanja AT, Buettner R, Jove R, et al. (2014) Abstract 1636: NMR discovery and molecular-basis of small molecule inhibitors of STAT3 Cancer Research. 74: 1636-1636 |
| Madu IG, Namanja AT, Su Y, et al. (2013) Identification and characterization of a new chemotype of noncovalent SENP inhibitors. Acs Chemical Biology. 8: 1435-41 |
| Namanja A, Chen C, Chen Y. (2013) 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 |
| Hu W, Namanja AT, Wong S, et al. (2012) Selective editing of Val and Leu methyl groups in high molecular weight protein NMR. Journal of Biomolecular Nmr. 53: 113-24 |
| Namanja AT, Li YJ, Su Y, et al. (2012) 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 |