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For: Goyal S, Chattopadhyay A, Kasavajhala K, Priyakumar UD. Role of Urea–Aromatic Stacking Interactions in Stabilizing the Aromatic Residues of the Protein in Urea-Induced Denatured State. J Am Chem Soc 2017;139:14931-46. [DOI: 10.1021/jacs.7b05463] [Cited by in Crossref: 33] [Cited by in F6Publishing: 27] [Article Influence: 6.6] [Reference Citation Analysis]
Number Citing Articles
1 Xu M, Jupp AR, Ong MSE, Burton KI, Chitnis SS, Stephan DW. Synthesis of Urea Derivatives from CO 2 and Silylamines. Angew Chem 2019;131:5763-7. [DOI: 10.1002/ange.201900058] [Cited by in Crossref: 12] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
2 Raghunathan S, Jaganade T, Priyakumar UD. Urea-aromatic interactions in biology. Biophys Rev 2020;12:65-84. [PMID: 32067192 DOI: 10.1007/s12551-020-00620-9] [Cited by in Crossref: 5] [Cited by in F6Publishing: 2] [Article Influence: 2.5] [Reference Citation Analysis]
3 He W, Liang D, Wang K, Lyu N, Diao H, Wu R. AromTool: predicting aromatic stacking energy using an atomic neural network model. Phys Chem Chem Phys 2021;23:16044-52. [PMID: 34286738 DOI: 10.1039/d1cp01954f] [Reference Citation Analysis]
4 Paul S, Paul S. In silico study of osmolytic effects of choline-O-sulfate on urea induced unfolding of Trp-cage mini-protein: An atomistic view from replica exchange molecular dynamics simulation. Archives of Biochemistry and Biophysics 2020;695:108484. [DOI: 10.1016/j.abb.2020.108484] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
5 Van Lommel R, Rutgeerts LAJ, De Borggraeve WM, De Proft F, Alonso M. Rationalising Supramolecular Hydrogelation of Bis‐Urea‐Based Gelators through a Multiscale Approach. ChemPlusChem 2020;85:267-76. [DOI: 10.1002/cplu.201900551] [Cited by in Crossref: 5] [Cited by in F6Publishing: 2] [Article Influence: 1.7] [Reference Citation Analysis]
6 Purkayastha A, Frontera A, Ganguly R, Misra TK. Synthesis, structures, and investigation of noncovalent interactions of 1,3-dimethyl-5-(4ʹ/3ʹ-pyridylazo)-6-aminouracil and their Ni(II) complexes. Journal of Molecular Structure 2018;1170:70-81. [DOI: 10.1016/j.molstruc.2018.05.082] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
7 Balamurugan K, Prakash M, Subramanian V. Theoretical Insights into the Role of Water Molecules in the Guanidinium-Based Protein Denaturation Process in Specific to Aromatic Amino Acids. J Phys Chem B 2019;123:2191-202. [PMID: 30672268 DOI: 10.1021/acs.jpcb.8b08968] [Cited by in Crossref: 8] [Cited by in F6Publishing: 4] [Article Influence: 2.7] [Reference Citation Analysis]
8 Kazmi M, Ibrar A, Ali HS, Ghufran M, Wadood A, Flörke U, Simpson J, Saeed A, Frontera A, Khan I. A combined experimental and theoretical analysis of the solid-state supramolecular self-assembly of N-(2,4-dichlorophenyl)-1-naphthamide: Synthesis, anticholinesterase potential and molecular docking analysis. Journal of Molecular Structure 2019;1197:458-70. [DOI: 10.1016/j.molstruc.2019.07.077] [Cited by in Crossref: 7] [Cited by in F6Publishing: 3] [Article Influence: 2.3] [Reference Citation Analysis]
9 Xu M, Jupp AR, Ong MSE, Burton KI, Chitnis SS, Stephan DW. Synthesis of Urea Derivatives from CO 2 and Silylamines. Angew Chem Int Ed 2019;58:5707-11. [DOI: 10.1002/anie.201900058] [Cited by in Crossref: 21] [Cited by in F6Publishing: 9] [Article Influence: 7.0] [Reference Citation Analysis]
10 Raghunathan S, Yadav K, Rojisha VC, Jaganade T, Prathyusha V, Bikkina S, Lourderaj U, Priyakumar UD. Transition between [R]- and [S]-stereoisomers without bond breaking. Phys Chem Chem Phys 2020;22:14983-91. [PMID: 32588839 DOI: 10.1039/d0cp02918a] [Cited by in Crossref: 5] [Article Influence: 2.5] [Reference Citation Analysis]
11 Akkoca Palabıyık B, Batyrow M, Erucar I. Computational investigations of Bio-MOF membranes for uremic toxin separation. Separation and Purification Technology 2022;281:119852. [DOI: 10.1016/j.seppur.2021.119852] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
12 Alodia N, Jaganade T, Priyakumar UD. Quantum mechanical investigation of the nature of nucleobase-urea stacking interaction, a crucial driving force in RNA unfolding in aqueous urea. J Chem Sci 2018;130. [DOI: 10.1007/s12039-018-1563-8] [Cited by in Crossref: 2] [Article Influence: 0.5] [Reference Citation Analysis]
13 Pal S, Roy R, Paul S. Potential of a Natural Deep Eutectic Solvent, Glyceline, in the Thermal Stability of the Trp-Cage Mini-protein. J Phys Chem B 2020;124:7598-610. [DOI: 10.1021/acs.jpcb.0c03501] [Cited by in Crossref: 6] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
14 Bootsma AN, Wheeler SE. Stacking Interactions of Heterocyclic Drug Fragments with Protein Amide Backbones. ChemMedChem 2018;13:835-41. [PMID: 29451739 DOI: 10.1002/cmdc.201700721] [Cited by in Crossref: 13] [Cited by in F6Publishing: 10] [Article Influence: 3.3] [Reference Citation Analysis]
15 Jaganade T, Chattopadhyay A, Raghunathan S, Priyakumar UD. Urea-water solvation of protein side chain models. Journal of Molecular Liquids 2020;311:113191. [DOI: 10.1016/j.molliq.2020.113191] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
16 Sarkar S, Ghosh S, Chakrabarti R. Ammonium based stabilizers effectively counteract urea-induced denaturation in a small protein: insights from molecular dynamics simulations. RSC Adv 2017;7:52888-906. [DOI: 10.1039/c7ra10712a] [Cited by in Crossref: 11] [Article Influence: 2.2] [Reference Citation Analysis]
17 Chattopadhyay A, Zheng M, Waller MP, Priyakumar UD. A Probabilistic Framework for Constructing Temporal Relations in Replica Exchange Molecular Trajectories. J Chem Theory Comput 2018;14:3365-80. [PMID: 29791153 DOI: 10.1021/acs.jctc.7b01245] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
18 Shaikh SR, Gawade RL, Kumar D, Kotmale A, Gonnade RG, Stürzer T. Crystal Engineering for Intramolecular π–π Stacking: Effect of Sequential Substitution of F on Molecular Geometry in Conformationally Flexible Sulfonamides. Crystal Growth & Design 2019;19:5665-78. [DOI: 10.1021/acs.cgd.9b00667] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
19 Jangizehi A, Ahmadi M, Seiffert S. Emergence, evidence, and effect of junction clustering in supramolecular polymer materials. Mater Adv 2021;2:1425-53. [DOI: 10.1039/d0ma00795a] [Cited by in Crossref: 4] [Cited by in F6Publishing: 2] [Article Influence: 4.0] [Reference Citation Analysis]
20 Oprzeska-Zingrebe EA, Smiatek J. Preferential Binding of Urea to Single-Stranded DNA Structures: A Molecular Dynamics Study. Biophys J 2018;114:1551-62. [PMID: 29642026 DOI: 10.1016/j.bpj.2018.02.013] [Cited by in Crossref: 21] [Cited by in F6Publishing: 20] [Article Influence: 7.0] [Reference Citation Analysis]
21 Pathak Y, Mehta S, Priyakumar UD. Learning Atomic Interactions through Solvation Free Energy Prediction Using Graph Neural Networks. J Chem Inf Model 2021;61:689-98. [PMID: 33546556 DOI: 10.1021/acs.jcim.0c01413] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
22 Sarkar S, Ramanathan N, Sruthi P, Sundararajan K. Computational and experimental evidence of N–H…π and cooperative πN…π∗ interactions in pyrrole…benzene and pyrrole…ethylene heterodimers at low temperatures. Journal of Molecular Structure 2020;1209:127983. [DOI: 10.1016/j.molstruc.2020.127983] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
23 Dasari S, Mallik BS. Solubility and solvation free energy of a cardiovascular drug, LASSBio-294, in ionic liquids: A computational study. Journal of Molecular Liquids 2020;301:112449. [DOI: 10.1016/j.molliq.2020.112449] [Cited by in Crossref: 9] [Cited by in F6Publishing: 3] [Article Influence: 4.5] [Reference Citation Analysis]
24 Mayol E, Campillo M, Cordomí A, Olivella M. Inter-residue interactions in alpha-helical transmembrane proteins. Bioinformatics 2019;35:2578-84. [PMID: 30566615 DOI: 10.1093/bioinformatics/bty978] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
25 Zheng H, Zheng YC, Cui Y, Zhu JJ, Zhong JY. Study on effects of co-solvents on the structure of DhaA by molecular dynamics simulation. J Biomol Struct Dyn 2021;39:5999-6007. [PMID: 32696722 DOI: 10.1080/07391102.2020.1796801] [Reference Citation Analysis]
26 Jaganade T, Chattopadhyay A, Pazhayam NM, Priyakumar UD. Energetic, Structural and Dynamic Properties of Nucleobase-Urea Interactions that Aid in Urea Assisted RNA Unfolding. Sci Rep 2019;9:8805. [PMID: 31217494 DOI: 10.1038/s41598-019-45010-8] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
27 Ghosh AK, Brindisi M. Urea Derivatives in Modern Drug Discovery and Medicinal Chemistry. J Med Chem 2020;63:2751-88. [PMID: 31789518 DOI: 10.1021/acs.jmedchem.9b01541] [Cited by in Crossref: 41] [Cited by in F6Publishing: 23] [Article Influence: 13.7] [Reference Citation Analysis]
28 Yıldız T, Erucar I. Revealing the performance of bio-MOFs for adsorption-based uremic toxin separation using molecular simulations. Chemical Engineering Journal 2022;431:134263. [DOI: 10.1016/j.cej.2021.134263] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 2.0] [Reference Citation Analysis]
29 Biswas B, Muttathukattil AN, Reddy G, Singh PC. Contrasting Effects of Guanidinium Chloride and Urea on the Activity and Unfolding of Lysozyme. ACS Omega 2018;3:14119-26. [PMID: 31458105 DOI: 10.1021/acsomega.8b01911] [Cited by in Crossref: 14] [Cited by in F6Publishing: 10] [Article Influence: 3.5] [Reference Citation Analysis]
30 Ribeiro SS, Castro TG, Gomes CM, Marcos JC. Hofmeister effects on protein stability are dependent on the nature of the unfolded state. Phys Chem Chem Phys 2021;23:25210-25. [PMID: 34730580 DOI: 10.1039/d1cp02477a] [Reference Citation Analysis]
31 Lv L, Han X, Wu X, Li C. Peeling and Mesoscale Dissociation of Silk Fibers for Hybridization of Electrothermic Fibrous Composites. ACS Sustainable Chem Eng 2020;8:248-55. [DOI: 10.1021/acssuschemeng.9b05261] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 1.3] [Reference Citation Analysis]
32 Millard S, Fothergill JW, Anderson Z, Brown EC, King MD, Colson AC. Supramolecular Interactions of Group VI Metal Carbonyl Complexes: The Facilitating Role of 1,3-Bis( p -isocyanophenyl)urea. Inorg Chem 2019;58:8130-9. [DOI: 10.1021/acs.inorgchem.9b00917] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 0.7] [Reference Citation Analysis]
33 Dasari S, Mallik BS. Conformational Free-Energy Landscapes of Alanine Dipeptide in Hydrated Ionic Liquids from Enhanced Sampling Methods. J Phys Chem B 2020;124:6728-37. [PMID: 32666802 DOI: 10.1021/acs.jpcb.0c05629] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
34 Li HZ, Shao XX, Shou LL, Li N, Liu YL, Xu ZG, Guo ZY. Unusual orthologs shed new light on the binding mechanism of ghrelin to its receptor GHSR1a. Arch Biochem Biophys 2021;704:108872. [PMID: 33857472 DOI: 10.1016/j.abb.2021.108872] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
35 Xing H, Rodger A, Comer J, Picco AS, Huck-Iriart C, Ezell EL, Conda-Sheridan M. Urea-Modified Self-Assembling Peptide Amphiphiles That Form Well-Defined Nanostructures and Hydrogels for Biomedical Applications. ACS Appl Bio Mater 2022. [PMID: 35653507 DOI: 10.1021/acsabm.2c00158] [Reference Citation Analysis]
36 Masutani K, Yamamori Y, Kim K, Matubayasi N. Free-energy analysis of the hydration and cosolvent effects on the β-sheet aggregation through all-atom molecular dynamics simulation. J Chem Phys 2019;150:145101. [DOI: 10.1063/1.5088395] [Cited by in Crossref: 7] [Cited by in F6Publishing: 4] [Article Influence: 2.3] [Reference Citation Analysis]