Molecular basis for multimerization in the activation of the epidermal growth factor receptor Y Huang, S Bharill, D Karandur, SM Peterson, M Marita, X Shi, ... elife 5, e14107, 2016 | 186 | 2016 |
Cryo-EM structure of a dimeric B-Raf: 14-3-3 complex reveals asymmetry in the active sites of B-Raf kinases Y Kondo, J Ognjenović, S Banerjee, D Karandur, A Merk, K Kulhanek, ... Science 366 (6461), 109-115, 2019 | 160 | 2019 |
An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor NH Shah, Q Wang, Q Yan, D Karandur, TA Kadlecek, IR Fallahee, ... Elife 5, e20105, 2016 | 106 | 2016 |
CRISPR-Cas12a exploits R-loop asymmetry to form double-strand breaks JC Cofsky, D Karandur, CJ Huang, IP Witte, J Kuriyan, JA Doudna Elife 9, e55143, 2020 | 95 | 2020 |
Structural insights into the regulation of Ca2+/calmodulin-dependent protein kinase II (CaMKII) M Bhattacharyya, D Karandur, J Kuriyan Cold Spring Harbor Perspectives in Biology 12 (6), a035147, 2020 | 83 | 2020 |
A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor Y Huang, J Ognjenovic, D Karandur, K Miller, A Merk, S Subramaniam, ... Elife 10, e73218, 2021 | 73 | 2021 |
Solubility and Aggregation of Gly5 in Water D Karandur, KY Wong, BM Pettitt The Journal of Physical Chemistry B 118 (32), 9565-9572, 2014 | 48 | 2014 |
Multiple interactions between an Arf/GEF complex and charged lipids determine activation kinetics on the membrane D Karandur, A Nawrotek, J Kuriyan, J Cherfils Proceedings of the National Academy of Sciences 114 (43), 11416-11421, 2017 | 47 | 2017 |
Breakage of the oligomeric CaMKII hub by the regulatory segment of the kinase D Karandur, M Bhattacharyya, Z Xia, YK Lee, S Muratcioglu, D McAffee, ... Elife 9, e57784, 2020 | 33 | 2020 |
Small local variations in B-form DNA lead to a large variety of global geometries which can accommodate most DNA-binding protein motifs A Marathe, D Karandur, M Bansal BMC structural biology 9, 1-26, 2009 | 33 | 2009 |
Intramolecular Interactions Overcome Hydration to Drive the Collapse Transition of Gly15 D Asthagiri, D Karandur, DS Tomar, BM Pettitt The Journal of Physical Chemistry B 121 (34), 8078-8084, 2017 | 32 | 2017 |
Protein collapse driven against solvation free energy without H‐bonds D Karandur, RC Harris, BM Pettitt Protein Science 25 (1), 103-110, 2016 | 28 | 2016 |
A saturation-mutagenesis analysis of the interplay between stability and activation in Ras F Hidalgo, LM Nocka, NH Shah, K Gorday, NR Latorraca, P Bandaru, ... Elife 11, e76595, 2022 | 20 | 2022 |
A structural mechanism for the generation of biased agonism in the epidermal growth factor receptor Y Huang, J Ognjenović, D Karandur, A Merk, S Subramaniam, J Kuriyan bioRxiv, 2020.12. 08.417006, 2020 | 5 | 2020 |
The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain AE van Vlimmeren, R Voleti, CA Chartier, Z Jiang, D Karandur, ... Proceedings of the National Academy of Sciences 121 (30), e2407159121, 2024 | 4 | 2024 |
The contribution of electrostatic interactions to the collapse of oligoglycine in water D Karandur, BM Pettitt Condensed matter physics 19 (2), 23802, 2016 | 3 | 2016 |
Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicity Z Jiang, AE van Vlimmeren, D Karandur, A Semmelman, NH Shah bioRxiv: the preprint server for biology, 2024 | | 2024 |
Revealing the principles of inter-and intra-domain regulation in a signaling enzyme via scanning mutagenesis Z Jiang, AE van Vlimmeren, D Karandur, A Semmelman, NH Shah bioRxiv, 2024 | | 2024 |
The pathogenic T42A mutation in SHP2 rewires interaction specificity and enhances signaling. AE van Vlimmeren, R Voleti, CA Chartier, Z Jiang, D Karandur, NH Shah Biorxiv: the Preprint Server for Biology, 2023 | | 2023 |