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For: Bianchi G, Longhi S, Grandori R, Brocca S. Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. Int J Mol Sci. 2020;21. [PMID: 32867340 DOI: 10.3390/ijms21176208] [Cited by in Crossref: 31] [Cited by in F6Publishing: 34] [Article Influence: 15.5] [Reference Citation Analysis]
Number Citing Articles
1 Pesce G, Brocca S, Grandori R, Longhi S, Uversky VN. Droplets of life: role of phase separation in virus replication and compartmentalization. Droplets of Life 2023. [DOI: 10.1016/b978-0-12-823967-4.00019-1] [Reference Citation Analysis]
2 Amankwaa B, Schoborg T, Labrador M. Drosophila insulator proteins exhibit in vivo liquid-liquid phase separation properties. Life Sci Alliance 2022;5:e202201536. [PMID: 35853678 DOI: 10.26508/lsa.202201536] [Reference Citation Analysis]
3 Baidya L, Reddy G. pH Induced Switch in the Conformational Ensemble of Intrinsically Disordered Protein Prothymosin-α and Its Implications for Amyloid Fibril Formation. J Phys Chem Lett 2022;:9589-98. [PMID: 36206480 DOI: 10.1021/acs.jpclett.2c01972] [Reference Citation Analysis]
4 Gonçalves-kulik M, Mier P, Kastano K, Cortés J, Bernadó P, Schmid F, Andrade-navarro MA. Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered. Biomolecules 2022;12:1098. [DOI: 10.3390/biom12081098] [Cited by in Crossref: 2] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
5 Wei W, Bai L, Yan B, Meng W, Wang H, Zhai J, Si F, Zheng C. When liquid-liquid phase separation meets viral infections. Front Immunol 2022;13:985622. [DOI: 10.3389/fimmu.2022.985622] [Reference Citation Analysis]
6 Maity H, Baidya L, Reddy G. Salt-Induced Transitions in the Conformational Ensembles of Intrinsically Disordered Proteins. J Phys Chem B 2022. [PMID: 35944496 DOI: 10.1021/acs.jpcb.2c03476] [Reference Citation Analysis]
7 Dang L, Cao X, Zhang T, Sun Y, Tian S, Gong T, Xiong H, Cao P, Li Y, Yu S, Yang L, Zhang L, Liu T, Zhang K, Liang J, Chen Y. Nuclear Condensation of CDYL Links Histone Crotonylation and Cystogenesis in Autosomal Dominant Polycystic Kidney Disease. J Am Soc Nephrol 2022:ASN. [PMID: 35918147 DOI: 10.1681/ASN.2021111425] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
8 Li H, Ernst C, Kolonko-Adamska M, Greb-Markiewicz B, Man J, Parissi V, Ng BW. Phase separation in viral infections. Trends Microbiol 2022:S0966-842X(22)00161-5. [PMID: 35902318 DOI: 10.1016/j.tim.2022.06.005] [Reference Citation Analysis]
9 Devarajan DS, Rekhi S, Nikoubashman A, Kim YC, Howard MP, Mittal J. Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins.. [DOI: 10.1101/2022.07.04.498718] [Reference Citation Analysis]
10 Choi Y, Lee Y, Lin Y, Heo Y, Lee Y, Song K. The Multivalent Polyampholyte Domain of Nst1, a P-Body-Associated Saccharomyces cerevisiae Protein, Provides a Platform for Interacting with P-Body Components. IJMS 2022;23:7380. [DOI: 10.3390/ijms23137380] [Reference Citation Analysis]
11 Badaczewska-dawid AE, Uversky VN, Potoyan DA. BIAPSS: A Comprehensive Physicochemical Analyzer of Proteins Undergoing Liquid–Liquid Phase Separation. IJMS 2022;23:6204. [DOI: 10.3390/ijms23116204] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
12 Bigman LS, Iwahara J, Levy Y. Negatively Charged Disordered Regions are Prevalent and Functionally Important Across Proteomes. J Mol Biol 2022;434:167660. [PMID: 35659505 DOI: 10.1016/j.jmb.2022.167660] [Cited by in Crossref: 3] [Cited by in F6Publishing: 5] [Article Influence: 3.0] [Reference Citation Analysis]
13 Anwar MA, Haseeb M, Choi S, Kwong-pyo K. P176S polymorphism in Maspin rewires electrostatic interaction that alters Maspin functionality.. [DOI: 10.1101/2022.05.31.494110] [Reference Citation Analysis]
14 Amankwaa B, Schoborg T, Labrador M. Drosophila insulator proteins exhibit in-vivo liquid-liquid phase separation properties.. [DOI: 10.1101/2022.05.27.493687] [Reference Citation Analysis]
15 Ubbiali D, Fratini M, Piersimoni L, Ihling CH, Kipping M, Heilmann I, Iacobucci C, Sinz A. First direct observation of ‘elongated’ conformational states in α-synuclein upon liquid-liquid phase separation.. [DOI: 10.1101/2022.04.20.488894] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
16 Chae MK, Lee NK, Jung Y, Johner A, Joanny JF. Partially Globular Conformations from Random Charge Sequences. ACS Macro Lett 2022;11:382-6. [PMID: 35575372 DOI: 10.1021/acsmacrolett.1c00655] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
17 Maity H, Baidya L, Reddy G. Salt Induced Transitions in the Conformational Ensembles of Intrinsically Disordered Proteins.. [DOI: 10.1101/2022.02.16.480648] [Reference Citation Analysis]
18 Li L, Casalini T, Arosio P, Salvalaglio M. Modeling the Structure and Interactions of Intrinsically Disordered Peptides with Multiple Replica, Metadynamics-Based Sampling Methods and Force-Field Combinations. J Chem Theory Comput 2022. [PMID: 35174713 DOI: 10.1021/acs.jctc.1c00889] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
19 Montepietra D, Cecconi C, Brancolini G. Combining enhanced sampling and deep learning dimensionality reduction for the study of the heat shock protein B8 and its pathological mutant K141E. RSC Adv 2022;12:31996-32011. [DOI: 10.1039/d2ra04913a] [Reference Citation Analysis]
20 Jeilani M, Billington K, Sunter JD, Dean S, Wheeler RJ. Nucleolar targeting in an early-branching eukaryote suggests a general physicochemical mechanism for ribosome protein sorting.. [DOI: 10.1101/2021.12.20.473284] [Reference Citation Analysis]
21 Wohl S, Jakubowski M, Zheng W. Salt-Dependent Conformational Changes of Intrinsically Disordered Proteins. J Phys Chem Lett 2021;12:6684-91. [PMID: 34259536 DOI: 10.1021/acs.jpclett.1c01607] [Cited by in Crossref: 10] [Cited by in F6Publishing: 11] [Article Influence: 10.0] [Reference Citation Analysis]
22 Shapiro DM, Ney M, Eghtesadi SA, Chilkoti A. Protein Phase Separation Arising from Intrinsic Disorder: First-Principles to Bespoke Applications. J Phys Chem B 2021;125:6740-59. [PMID: 34143622 DOI: 10.1021/acs.jpcb.1c01146] [Cited by in Crossref: 13] [Cited by in F6Publishing: 14] [Article Influence: 13.0] [Reference Citation Analysis]
23 Suetake I, Nakazawa S, Sato K, Mutoh R, Mishima Y, Kawakami T, Takei T, Watanabe M, Sakai N, Fujiwara T, Takui T, Miyata M, Shinohara A, Hojo H, Arata T. Structural dynamics of the chromo-shadow domain and chromodomain of HP1 bound to histone H3K9 methylated peptide, as measured by site-directed spin-labeling EPR spectroscopy. Biochem Biophys Res Commun 2021;567:42-8. [PMID: 34139556 DOI: 10.1016/j.bbrc.2021.06.010] [Reference Citation Analysis]
24 Vodnala M, Choi EB, Fong YW. Low complexity domains, condensates, and stem cell pluripotency. World J Stem Cells 2021; 13(5): 416-438 [PMID: 34136073 DOI: 10.4252/wjsc.v13.i5.416] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
25 Wessén J, Pal T, Das S, Lin YH, Chan HS. A Simple Explicit-Solvent Model of Polyampholyte Phase Behaviors and Its Ramifications for Dielectric Effects in Biomolecular Condensates. J Phys Chem B 2021;125:4337-58. [PMID: 33890467 DOI: 10.1021/acs.jpcb.1c00954] [Cited by in Crossref: 16] [Cited by in F6Publishing: 19] [Article Influence: 16.0] [Reference Citation Analysis]
26 Lee N, Jung Y, Johner A, Joanny J. Globular Polyampholytes: Structure and Translocation. Macromolecules 2021;54:2394-411. [DOI: 10.1021/acs.macromol.0c02413] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
27 Manica G, Ghenea S, Munteanu CVA, Martin EC, Butnaru C, Surleac M, Chiritoiu GN, Alexandru PR, Petrescu AJ, Petrescu SM. EDEM3 Domains Cooperate to Perform Its Overall Cell Functioning. Int J Mol Sci 2021;22:2172. [PMID: 33671632 DOI: 10.3390/ijms22042172] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
28 Badaczewska-dawid AE, Potoyan DA. BIAPSS - BioInformatic Analysis of liquid-liquid Phase-Separating protein Sequences.. [DOI: 10.1101/2021.02.11.430806] [Reference Citation Analysis]
29 Adegoke SC, Tahergorabi R. Utilization of seafood-processing by-products for the development of value-added food products. Valorization of Agri-Food Wastes and By-Products 2021. [DOI: 10.1016/b978-0-12-824044-1.00012-x] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
30 Santofimia-Castaño P, Rizzuti B, Pey AL, Fárez-Vidal ME, Iovanna JL, Neira JL. Intrinsically disordered protein NUPR1 binds to the armadillo-repeat domain of Plakophilin 1. Int J Biol Macromol 2021;170:549-60. [PMID: 33385445 DOI: 10.1016/j.ijbiomac.2020.12.193] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
31 Brocca S, Grandori R, Longhi S, Uversky V. Liquid-Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus-Host Interactions. Int J Mol Sci 2020;21:E9045. [PMID: 33260713 DOI: 10.3390/ijms21239045] [Cited by in Crossref: 42] [Cited by in F6Publishing: 48] [Article Influence: 21.0] [Reference Citation Analysis]
32 Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S. Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. Sci Rep 2020;10:19574. [PMID: 33177626 DOI: 10.1038/s41598-020-76522-3] [Cited by in Crossref: 9] [Cited by in F6Publishing: 10] [Article Influence: 4.5] [Reference Citation Analysis]
33 Kastano K, Erdős G, Mier P, Alanis-Lobato G, Promponas VJ, Dosztányi Z, Andrade-Navarro MA. Evolutionary Study of Disorder in Protein Sequences. Biomolecules 2020;10:E1413. [PMID: 33036302 DOI: 10.3390/biom10101413] [Cited by in Crossref: 10] [Cited by in F6Publishing: 12] [Article Influence: 5.0] [Reference Citation Analysis]