On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life ME Rebeaud, S Mallik, P Goloubinoff, DS Tawfik Proceedings of the National Academy of Sciences 118 (21), 2021 | 73 | 2021 |
Finding the generalized molecular principles of protein thermal stability S Hait, S Mallik, S Basu, S Kundu Proteins: Structure, Function, and Bioinformatics 88 (6), 788-808, 2020 | 39 | 2020 |
Topology and oligomerization of mono-and oligomeric proteins regulate their half-lives in the cell S Mallik, S Kundu Structure 26 (6), 869-878. e3, 2018 | 24 | 2018 |
How gene duplication diversifies the landscape of protein oligomeric state and function S Mallik, DS Tawfik, ED Levy Current opinion in genetics & development 76, 101966, 2022 | 16 | 2022 |
A comparison of structural and evolutionary attributes of Escherichia coli and Thermus thermophilus small ribosomal subunits: signatures of thermal adaptation S Mallik, S Kundu PloS one 8 (8), e69898, 2013 | 16 | 2013 |
Assembly constraints drive co-evolution among ribosomal constituents S Mallik, H Akashi, S Kundu Nucleic acids research 43 (11), 5352-5363, 2015 | 15 | 2015 |
Determining the interaction status and evolutionary fate of duplicated homomeric proteins S Mallik, DS Tawfik PLoS Computational Biology 16 (8), e1008145, 2020 | 13 | 2020 |
Predicting protein folding rate change upon point mutation using residue‐level coevolutionary information S Mallik, S Das, S Kundu Proteins: Structure, Function, and Bioinformatics 84 (1), 3-8, 2016 | 12 | 2016 |
Co-evolutionary constraints of globular proteins correlate with their folding rates S Mallik, S Kundu FEBS Letters, 2015 | 12 | 2015 |
Coevolutionary constraints in the sequence‐space of macromolecular complexes reflect their self‐assembly pathways S Mallik, S Kundu Proteins: Structure, Function, and Bioinformatics 85 (7), 1183-1189, 2017 | 10 | 2017 |
Molecular interactions within the halophilic, thermophilic, and mesophilic prokaryotic ribosomal complexes: clues to environmental adaptation S Mallik, S Kundu Journal of Biomolecular Structure and Dynamics 33 (3), 639-656, 2015 | 10 | 2015 |
Compensatory mutations occur within the electrostatic interaction range of deleterious mutations in protein structure A Bhattacherjee, S Mallik, S Kundu Journal of Molecular Evolution, 1-3, 2014 | 8 | 2014 |
Genome-scale molecular principles of mRNA half-life regulation in yeast S Basu, S Mallik, S Hait, S Kundu The FEBS journal, 2020 | 6 | 2020 |
Modular organization of residue-level contacts shapes the selection pressure on individual amino acid sites of ribosomal proteins S Mallik, S Kundu Genome Biology and Evolution 9 (4), 916-931, 2017 | 5 | 2017 |
The lipid-RNA world S Mallik, S Kundu arXiv preprint arXiv:1211.0413, 2012 | 5 | 2012 |
Translational regulation of ribosomal protein S15 drives characteristic patterns of protein‐mRNA epistasis S Mallik, S Basu, S Hait, S Kundu Proteins: Structure, Function, and Bioinformatics 86 (8), 827-832, 2018 | 4 | 2018 |
Transiently disordered tails accelerate folding of globular proteins S Mallik, T Ray, S Kundu FEBS letters 591 (14), 2180-2191, 2017 | 3 | 2017 |
Structural determinants of co-translational protein complex assembly S Malik, J Venezian, A Lobov, M Heidenreich, H Garcia-Seisdedos, ... bioRxiv, 2024.01. 20.576408, 2024 | | 2024 |
Mutational biases contribute to the neutral complexification of protein interaction networks following gene duplication AF Cisneros, L Nielly-Thibault, S Mallik, ED Levy, CR Landry | | 2023 |