Tamjeed Saleh, Ph.D.
Affiliations: | 2012 | Graduate School - New Brunswick | Rutgers University, New Brunswick, New Brunswick, NJ, United States |
Area:
BiochemistryGoogle:
"Tamjeed Saleh"Mean distance: (not calculated yet)
Parents
Sign in to add mentorCharalampos G. Kalodimos | grad student | 2012 | Rutgers, New Brunswick | |
(Structural analysis of adaptor protein CrkL and the role of CypA in Bcr-Abl mediated signaling.) |
BETA: Related publications
See more...
Publications
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
Clay MC, Saleh T, Kamatham S, et al. (2021) Progress toward automated methyl assignments for methyl-TROSY applications. Structure (London, England : 1993) |
Xie T, Saleh T, Rossi P, et al. (2021) Imatinib can act as an Allosteric Activator of Abl Kinase. Journal of Molecular Biology. 434: 167349 |
Xie T, Saleh T, Rossi P, et al. (2020) Conformational states dynamically populated by a kinase determine its function. Science (New York, N.Y.) |
Davra V, Saleh T, Geng K, et al. (2020) Cyclophilin A inhibitor Debio-025 targets Crk, reduces metastasis, and induces tumor immunogenicity in breast cancer. Molecular Cancer Research : McR |
Saleh T. (2018) An Allosteric Mechanism of Abl Kinase Activation and Catalysis Biophysical Journal. 114 |
Xie T, Saleh T, Kalodimos CG. (2018) Gleevec Can Act as an Allosteric Activator of ABL Kinase Biophysical Journal. 114: 229a |
Xia Y, Rossi P, Subrahmanian MV, et al. (2017) Enhancing the sensitivity of multidimensional NMR experiments by using triply-compensated π pulses. Journal of Biomolecular Nmr |
Monneau YR, Rossi P, Bhaumik A, et al. (2017) Automatic methyl assignment in large proteins by the MAGIC algorithm. Journal of Biomolecular Nmr |
Saleh T, Rossi P, Kalodimos CG. (2017) Atomic view of the energy landscape in the allosteric regulation of Abl kinase. Nature Structural & Molecular Biology |
Saleh T, Kalodimos CG. (2017) Enzymes at work are enzymes in motion. Science (New York, N.Y.). 355: 247-248 |