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For: Harami GM, Kovács ZJ, Pancsa R, Pálinkás J, Baráth V, Tárnok K, Málnási-Csizmadia A, Kovács M. Phase separation by ssDNA binding protein controlled via protein-protein and protein-DNA interactions. Proc Natl Acad Sci U S A 2020;117:26206-17. [PMID: 33020264 DOI: 10.1073/pnas.2000761117] [Cited by in Crossref: 16] [Cited by in F6Publishing: 16] [Article Influence: 8.0] [Reference Citation Analysis]
Number Citing Articles
1 Zhou F, Wang P, Chen J, Zhu Z, Li Y, Wang S, Wu S, Sima Y, Fu T, Tan W, Zhao Z. A photochemically covalent lock stabilizes aptamer conformation and strengthens its performance for biomedicine. Nucleic Acids Res 2022:gkac703. [PMID: 35993818 DOI: 10.1093/nar/gkac703] [Reference Citation Analysis]
2 Lindström M, Chen L, Jiang S, Zhang D, Gao Y, Zheng J, Hao X, Yang X, Kabbinale A, Thoma J, Metzger LC, Zhang DY, Zhu X, Liu H, Gustafsson CM, Burmann BM, Winderickx J, Sunnerhagen P, Liu B. Lsm7 phase-separated condensates trigger stress granule formation. Nat Commun 2022;13:3701. [PMID: 35764627 DOI: 10.1038/s41467-022-31282-8] [Reference Citation Analysis]
3 Sołtys K, Tarczewska A, Bystranowska D, Sozańska N. Getting Closer to Decrypting the Phase Transitions of Bacterial Biomolecules. Biomolecules 2022;12:907. [DOI: 10.3390/biom12070907] [Reference Citation Analysis]
4 Niu J, Qiu C, Abbott NL, Gellman SH. Formation of versus Recruitment to RNA-Rich Condensates: Controlling Effects Exerted by Peptide Side Chain Identity. J Am Chem Soc 2022;144:10386-95. [PMID: 35639776 DOI: 10.1021/jacs.2c02222] [Reference Citation Analysis]
5 Chan KWY, Navi M, Kieda J, Moran T, Hammers D, Lee S, Tsai SSH. Phase transition modulation and biophysical characterization of biomolecular condensates using microfluidics. Lab Chip 2022. [PMID: 35616128 DOI: 10.1039/d2lc00037g] [Reference Citation Analysis]
6 Fefilova AS, Fonin AV, Vishnyakov IE, Kuznetsova IM, Turoverov KK. Stress-Induced Membraneless Organelles in Eukaryotes and Prokaryotes: Bird’s-Eye View. IJMS 2022;23:5010. [DOI: 10.3390/ijms23095010] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
7 Viola MG, Perdikari TM, Trebino CE, Rahmani N, Mathews KL, Pena CM, Chua XY, Xuan B, Labreck CJ, Fawzi NL, Camberg JL. An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer‐guided substrate processing by ClpXP protease. Protein Science 2022;31. [DOI: 10.1002/pro.4306] [Reference Citation Analysis]
8 Harami GM, Neuman KC. Glutamate brings out the flavor of SSB cooperativity and phase separation. J Mol Biol 2022;:167580. [PMID: 35395234 DOI: 10.1016/j.jmb.2022.167580] [Reference Citation Analysis]
9 Kozlov AG, Cheng X, Zhang H, Kyung Shinn M, Weiland E, Nguyen B, Shkel IA, Zytkiewicz E, Finkelstein IJ, Thomas Record M, Lohman TM. How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein. Journal of Molecular Biology 2022. [DOI: 10.1016/j.jmb.2022.167562] [Cited by in Crossref: 3] [Cited by in F6Publishing: 1] [Article Influence: 3.0] [Reference Citation Analysis]
10 Chu X, Sun T, Li Q, Xu Y, Zhang Z, Lai L, Pei J. Prediction of liquid-liquid phase separating proteins using machine learning. BMC Bioinformatics 2022;23:72. [PMID: 35168563 DOI: 10.1186/s12859-022-04599-w] [Cited by in Crossref: 12] [Cited by in F6Publishing: 6] [Article Influence: 12.0] [Reference Citation Analysis]
11 Bianco PR. OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block. Front Mol Biosci 2022;9:784451. [DOI: 10.3389/fmolb.2022.784451] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
12 Zhang C, Zhao W, Duvall SW, Kowallis KA, Childers WS. Regulation of the activity of bacterial histidine kinase PleC by the scaffolding protein PodJ. Journal of Biological Chemistry 2022. [DOI: 10.1016/j.jbc.2022.101683] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 2.0] [Reference Citation Analysis]
13 Shen Z, Tang CM, Liu GY. Towards a better understanding of antimicrobial resistance dissemination: what can be learnt from studying model conjugative plasmids? Mil Med Res 2022;9:3. [PMID: 35012680 DOI: 10.1186/s40779-021-00362-z] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
14 Babl L, Giacomelli G, Ramm B, Gelmroth AK, Bramkamp M, Schwille P. CTP-controlled liquid-liquid phase separation of ParB. J Mol Biol 2021;434:167401. [PMID: 34902429 DOI: 10.1016/j.jmb.2021.167401] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
15 Cohan MC, Shinn MK, Lalmansingh JM, Pappu RV. Uncovering Non-random Binary Patterns Within Sequences of Intrinsically Disordered Proteins. J Mol Biol 2021;434:167373. [PMID: 34863777 DOI: 10.1016/j.jmb.2021.167373] [Cited by in Crossref: 11] [Cited by in F6Publishing: 4] [Article Influence: 11.0] [Reference Citation Analysis]
16 Gao Z, Zhang W, Chang R, Zhang S, Yang G, Zhao G. Liquid-Liquid Phase Separation: Unraveling the Enigma of Biomolecular Condensates in Microbial Cells. Front Microbiol 2021;12:751880. [PMID: 34759902 DOI: 10.3389/fmicb.2021.751880] [Reference Citation Analysis]
17 Kumar M, Michael S, Alvarado-Valverde J, Mészáros B, Sámano-Sánchez H, Zeke A, Dobson L, Lazar T, Örd M, Nagpal A, Farahi N, Käser M, Kraleti R, Davey NE, Pancsa R, Chemes LB, Gibson TJ. The Eukaryotic Linear Motif resource: 2022 release. Nucleic Acids Res 2021:gkab975. [PMID: 34718738 DOI: 10.1093/nar/gkab975] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
18 Paiz EA, Allen JH, Correia JJ, Fitzkee NC, Hough LE, Whitten ST. Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins. J Biol Chem 2021;297:101343. [PMID: 34710373 DOI: 10.1016/j.jbc.2021.101343] [Reference Citation Analysis]
19 Donaldson LW. Molecular Modeling the Proteins from the exo-xis Region of Lambda and Shigatoxigenic Bacteriophages. Antibiotics (Basel) 2021;10:1282. [PMID: 34827220 DOI: 10.3390/antibiotics10111282] [Reference Citation Analysis]
20 Bhowmik D, Du M, Tian Y, Ma S, Wu J, Chen Z, Yin Q, Zhu F. Cooperative DNA binding mediated by KicGAS/ORF52 oligomerization allows inhibition of DNA-induced phase separation and activation of cGAS. Nucleic Acids Res 2021:gkab689. [PMID: 34387695 DOI: 10.1093/nar/gkab689] [Reference Citation Analysis]
21 Wang W, Li K, Yang Z, Hou Q, Zhao WW, Sun Q. RNase H1C collaborates with ssDNA binding proteins WHY1/3 and recombinase RecA1 to fulfill the DNA damage repair in Arabidopsis chloroplasts. Nucleic Acids Res 2021;49:6771-87. [PMID: 34133716 DOI: 10.1093/nar/gkab479] [Cited by in Crossref: 1] [Cited by in F6Publishing: 7] [Article Influence: 1.0] [Reference Citation Analysis]
22 Shamilov R, Robinson VL, Aneskievich BJ. Seeing Keratinocyte Proteins through the Looking Glass of Intrinsic Disorder. Int J Mol Sci 2021;22:7912. [PMID: 34360678 DOI: 10.3390/ijms22157912] [Reference Citation Analysis]
23 Bianco PR. The mechanism of action of the SSB interactome reveals it is the first OB-fold family of genome guardians in prokaryotes. Protein Sci 2021;30:1757-75. [PMID: 34089559 DOI: 10.1002/pro.4140] [Cited by in F6Publishing: 5] [Reference Citation Analysis]
24 Ujaoney AK, Padwal MK, Basu B. An in vivo Interaction Network of DNA-Repair Proteins: A Snapshot at Double Strand Break Repair in Deinococcus radiodurans. J Proteome Res 2021;20:3242-55. [PMID: 33929844 DOI: 10.1021/acs.jproteome.1c00078] [Reference Citation Analysis]
25 Ismail H, Liu X, Yang F, Li J, Zahid A, Dou Z, Liu X, Yao X. Mechanisms and regulation underlying membraneless organelle plasticity control. J Mol Cell Biol 2021;13:239-58. [PMID: 33914074 DOI: 10.1093/jmcb/mjab028] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
26 Marnef A, Legube G. R-loops as Janus-faced modulators of DNA repair. Nat Cell Biol 2021;23:305-13. [PMID: 33837288 DOI: 10.1038/s41556-021-00663-4] [Cited by in Crossref: 14] [Cited by in F6Publishing: 31] [Article Influence: 14.0] [Reference Citation Analysis]
27 Feric M, Misteli T. Phase separation in genome organization across evolution. Trends Cell Biol 2021;31:671-85. [PMID: 33771451 DOI: 10.1016/j.tcb.2021.03.001] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 8.0] [Reference Citation Analysis]
28 Farahi N, Lazar T, Wodak SJ, Tompa P, Pancsa R. Integration of Data from Liquid-Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers. Int J Mol Sci 2021;22:3017. [PMID: 33809541 DOI: 10.3390/ijms22063017] [Cited by in Crossref: 7] [Cited by in F6Publishing: 4] [Article Influence: 7.0] [Reference Citation Analysis]
29 Stracy M, Schweizer J, Sherratt DJ, Kapanidis AN, Uphoff S, Lesterlin C. Transient non-specific DNA binding dominates the target search of bacterial DNA-binding proteins. Mol Cell 2021;81:1499-1514.e6. [PMID: 33621478 DOI: 10.1016/j.molcel.2021.01.039] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
30 King JT, Shakya A. Phase separation of DNA: From past to present. Biophys J 2021;120:1139-49. [PMID: 33582138 DOI: 10.1016/j.bpj.2021.01.033] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
31 Alshareedah I, Thurston GM, Banerjee PR. Quantifying viscosity and surface tension of multicomponent protein-nucleic acid condensates. Biophys J 2021;120:1161-9. [PMID: 33453268 DOI: 10.1016/j.bpj.2021.01.005] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 9.0] [Reference Citation Analysis]
32 Yuan Z, Zhang D, Yu F, Ma Y, Liu Y, Li X, Wang H. Precise sequencing of single protected-DNA fragment molecules for profiling of protein distribution and assembly on DNA. Chem Sci 2021;12:2039-49. [PMID: 34163966 DOI: 10.1039/d0sc01742f] [Reference Citation Analysis]
33 Azaldegui CA, Vecchiarelli AG, Biteen JS. The emergence of phase separation as an organizing principle in bacteria. Biophys J 2021;120:1123-38. [PMID: 33186556 DOI: 10.1016/j.bpj.2020.09.023] [Cited by in Crossref: 15] [Cited by in F6Publishing: 15] [Article Influence: 7.5] [Reference Citation Analysis]