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Saurav Mallik (Robb), Ph.D
Saurav Mallik (Robb), Ph.D
Postdoctoral Fellow, The Weizmann Institute of Science
Verified email at weizmann.ac.il - Homepage
Title
Cited by
Cited by
Year
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
732021
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
392020
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
242018
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
162022
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
162013
Assembly constraints drive co-evolution among ribosomal constituents
S Mallik, H Akashi, S Kundu
Nucleic acids research 43 (11), 5352-5363, 2015
152015
Determining the interaction status and evolutionary fate of duplicated homomeric proteins
S Mallik, DS Tawfik
PLoS Computational Biology 16 (8), e1008145, 2020
132020
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
122016
Co-evolutionary constraints of globular proteins correlate with their folding rates
S Mallik, S Kundu
FEBS Letters, 2015
122015
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
102017
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
102015
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
82014
Genome-scale molecular principles of mRNA half-life regulation in yeast
S Basu, S Mallik, S Hait, S Kundu
The FEBS journal, 2020
62020
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
52017
The lipid-RNA world
S Mallik, S Kundu
arXiv preprint arXiv:1211.0413, 2012
52012
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
42018
Transiently disordered tails accelerate folding of globular proteins
S Mallik, T Ray, S Kundu
FEBS letters 591 (14), 2180-2191, 2017
32017
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
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Articles 1–19