| HDX-MS: an analytical tool to capture protein motion in action D Narang, C Lento, D J. Wilson Biomedicines 8 (7), 224, 2020 | 50 | 2020 |
| Direct observation of the intrinsic backbone torsional mobility of disordered proteins N Jain, D Narang, K Bhasne, V Dalal, S Arya, M Bhattacharya, ... Biophysical journal 111 (4), 768-774, 2016 | 36 | 2016 |
| Characterization of an acid inducible lipase Rv3203 from Mycobacterium tuberculosis H37Rv G Singh, S Arya, D Narang, D Jadeja, G Singh, UD Gupta, K Singh, J Kaur Molecular biology reports 41, 285-296, 2014 | 31 | 2014 |
| Molecular Characterization of Oxidative Stress-Inducible LipD of Mycobacterium tuberculosis H37Rv G Singh, S Arya, A Kumar, D Narang, J Kaur Current microbiology 68, 387-396, 2014 | 28 | 2014 |
| Protein footprinting, conformational dynamics, and core interface-adjacent neutralization “hotspots” in the SARS-CoV-2 spike protein receptor binding domain/human ACE2 interaction D Narang, DA James, MT Balmer, DJ Wilson Journal of the American Society for Mass Spectrometry 32 (7), 1593-1600, 2021 | 23 | 2021 |
| Nanoscale fluorescence imaging of single amyloid fibrils V Dalal, M Bhattacharya, D Narang, PK Sharma, S Mukhopadhyay The Journal of Physical Chemistry Letters 3 (13), 1783-1787, 2012 | 19 | 2012 |
| RelA-Containing nfκb dimers have strikingly different DNA-Binding cavities in the absence of DNA D Narang, W Chen, CG Ricci, EA Komives Journal of molecular biology 430 (10), 1510-1520, 2018 | 15 | 2018 |
| An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA HER Baughman, D Narang, W Chen, ACV Suárez, J Lee, MJ Bachochin, ... Journal of Biological Chemistry 298 (9), 2022 | 11 | 2022 |
| Prediction of the presence of a seventh ankyrin repeat in IκBε from homology modeling combined with hydrogen–deuterium exchange mass spectrometry (HDX‐MS) KM Ramsey, D Narang, EA Komives Protein Science 27 (9), 1624-1635, 2018 | 7 | 2018 |
| Site-specific fluorescence depolarization kinetics distinguishes the amyloid folds responsible for distinct yeast prion strains D Narang, HM Swasthi, S Mahapatra, S Mukhopadhyay The Journal of Physical Chemistry B 121 (36), 8447-8453, 2017 | 7 | 2017 |
| Dynamics and dimension of an amyloidogenic disordered state of human β2-microglobulin D Narang, PK Sharma, S Mukhopadhyay European Biophysics Journal 42, 767-776, 2013 | 7 | 2013 |
| Stepwise unfolding of human β2-microglobulin into a disordered amyloidogenic precursor at low pH D Narang, A Singh, S Mukhopadhyay European Biophysics Journal 46, 65-76, 2017 | 6 | 2017 |
| Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pH D Narang, A Singh, HM Swasthi, S Mukhopadhyay The Journal of Physical Chemistry B 120 (32), 7815-7823, 2016 | 6 | 2016 |
| NF-κB Interaction with Nucleosomes J Zeng, D Narang, EA Komives | | |
