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For: Shanmugam N, Baker MODG, Ball SR, Steain M, Pham CLL, Sunde M. Microbial functional amyloids serve diverse purposes for structure, adhesion and defence. Biophys Rev 2019;11:287-302. [PMID: 31049855 DOI: 10.1007/s12551-019-00526-1] [Cited by in Crossref: 46] [Cited by in F6Publishing: 32] [Article Influence: 15.3] [Reference Citation Analysis]
Number Citing Articles
1 Bachellier-bassi S, Mourer T, Ghalid ME, Pehaut-arnaudet G, Kauffmann B, Loquet A, Cabral V, d'Enfert C. The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans.. [DOI: 10.21203/rs.3.rs-2159129/v1] [Reference Citation Analysis]
2 Yarmola E, Ishkov IP, di Cologna NM, Menashe M, Whitener RL, Long JR, Abranches J, Hagen SJ, Brady LJ. Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms. Microbiol Spectr 2022;:e0166122. [PMID: 35950854 DOI: 10.1128/spectrum.01661-22] [Reference Citation Analysis]
3 Arad E, Jelinek R. Catalytic amyloids. Trends in Chemistry 2022. [DOI: 10.1016/j.trechm.2022.07.001] [Reference Citation Analysis]
4 Matilla-Cuenca L, Taglialegna A, Gil C, Toledo-Arana A, Lasa I, Valle J. Bacterial biofilm functionalization through Bap amyloid engineering. NPJ Biofilms Microbiomes 2022;8:62. [PMID: 35909185 DOI: 10.1038/s41522-022-00324-w] [Reference Citation Analysis]
5 Bücker R, Seuring C, Cazey C, Veith K, García-Alai M, Grünewald K, Landau M. The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils. Nat Commun 2022;13:4356. [PMID: 35896552 DOI: 10.1038/s41467-022-32039-z] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
6 Golan N, Engelberg Y, Landau M. Structural Mimicry in Microbial and Antimicrobial Amyloids. Annu Rev Biochem 2022;91:403-22. [PMID: 35729071 DOI: 10.1146/annurev-biochem-032620-105157] [Reference Citation Analysis]
7 Zhang S, Li C, Si J, Han Z, Chen D. Action Mechanisms of Effectors in Plant-Pathogen Interaction. Int J Mol Sci 2022;23:6758. [PMID: 35743201 DOI: 10.3390/ijms23126758] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 4.0] [Reference Citation Analysis]
8 Fan Q, Bibi S, Vallad GE, Goss EM, Hurlbert JC, Paret ML, Jones JB, Timilsina S. Identification of Genes in Xanthomonas euvesicatoria pv. rosa That Are Host Limiting in Tomato. Plants 2022;11:796. [DOI: 10.3390/plants11060796] [Reference Citation Analysis]
9 Navarro S, Ventura S. Computational methods to predict protein aggregation. Curr Opin Struct Biol 2022;73:102343. [PMID: 35240456 DOI: 10.1016/j.sbi.2022.102343] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 2.0] [Reference Citation Analysis]
10 Corsini PM, Wang S, Rehman S, Fenn K, Sagar A, Sirovica S, Cleaver L, Edwards-Gayle CJC, Mastroianni G, Dorgan B, Sewell LM, Lynham S, Iuga D, Franks WT, Jarvis J, Carpenter GH, Curtis MA, Bernadó P, Darbari VC, Garnett JA. Molecular and cellular insight into Escherichia coli SslE and its role during biofilm maturation. NPJ Biofilms Microbiomes 2022;8:9. [PMID: 35217675 DOI: 10.1038/s41522-022-00272-5] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
11 Bücker R, Seuring C, Cazey C, Veith K, García-alai M, Grünewald K, Landau M. The Cryo-EM Structures of two Amphibian Antimicrobial Cross-β Amyloid Fibrils.. [DOI: 10.1101/2022.01.08.475498] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
12 Heyn TR, Garamus VM, Steffen-heins A, Schwarz K, Keppler JK. Analysis of Natural and Engineered Amyloid Aggregates by Spectroscopic and Scattering Techniques. Springer Proceedings in Physics 2022. [DOI: 10.1007/978-3-030-80924-9_11] [Reference Citation Analysis]
13 Qasemi A, Rahimi F, Katouli M. Clonal groups of extended-spectrum β-lactamase and biofilm producing uropathogenic Escherichia coli in Iran. Pathog Glob Health 2021;:1-13. [PMID: 34904540 DOI: 10.1080/20477724.2021.2011578] [Reference Citation Analysis]
14 Tang Y, Zhang D, Gong X, Zheng J. A mechanistic survey of Alzheimer's disease. Biophys Chem 2021;281:106735. [PMID: 34894476 DOI: 10.1016/j.bpc.2021.106735] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
15 Islam S, Charnley M, Bindra G, Ratcliffe J, Zhou J, Mezzenga R, Hulett M, Han K, Berryman JT, Reynolds NP. Neurotoxic Amyloidogenic Peptides Identified in the Proteome of SARS-COV2: Potential Implications for Neurological Symptoms in COVID-19.. [DOI: 10.1101/2021.11.24.469537] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
16 Rebuffat S. Ribosomally synthesized peptides, foreground players in microbial interactions: recent developments and unanswered questions. Nat Prod Rep 2021. [PMID: 34755755 DOI: 10.1039/d1np00052g] [Cited by in Crossref: 8] [Cited by in F6Publishing: 11] [Article Influence: 8.0] [Reference Citation Analysis]
17 di Cologna NM, Samaddar S, Valle CA, Vargas J, Aviles-Reyes A, Morales J, Ganguly T, Pileggi R, Brady LJ, Lemos JA, Abranches J. Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity. Appl Environ Microbiol 2021;87:e0114921. [PMID: 34406827 DOI: 10.1128/AEM.01149-21] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
18 Adam JA, Middlestead HR, Debono NE, Hirsa AH. Effects of Shear Rate and Protein Concentration on Amyloidogenesis via Interfacial Shear. J Phys Chem B 2021;125:10355-63. [PMID: 34478304 DOI: 10.1021/acs.jpcb.1c05171] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
19 Zajkowski T, Lee MD, Mondal SS, Carbajal A, Dec R, Brennock PD, Piast RW, Snyder JE, Bense NB, Dzwolak W, Jarosz DF, Rothschild LJ. The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements. Mol Biol Evol 2021;38:2088-103. [PMID: 33480998 DOI: 10.1093/molbev/msab010] [Cited by in Crossref: 6] [Cited by in F6Publishing: 7] [Article Influence: 6.0] [Reference Citation Analysis]
20 de Mojana di Cologna N, Samaddar S, Valle CA, Vargas J, Aviles-reyes A, Morales J, Ganguly T, Pileggi R, Brady LJ, Lemos JA, Abranches J. Amyloid aggregation of Streptococcus mutans Cnm influences its collagen-binding activity.. [DOI: 10.1101/2021.06.09.447825] [Reference Citation Analysis]
21 Khodaparast L, Wu G, Khodaparast L, Schmidt BZ, Rousseau F, Schymkowitz J. Bacterial Protein Homeostasis Disruption as a Therapeutic Intervention. Front Mol Biosci 2021;8:681855. [PMID: 34150852 DOI: 10.3389/fmolb.2021.681855] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
22 Zhang Y, Liu Y, Tang Y, Zhang D, He H, Wu J, Zheng J. Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection. Chem Sci 2021;12:9124-39. [PMID: 34276942 DOI: 10.1039/d1sc01133b] [Cited by in Crossref: 12] [Cited by in F6Publishing: 13] [Article Influence: 12.0] [Reference Citation Analysis]
23 Zhang Y, Tang Y, Liu Y, Zhang D, Zheng J. Design and Engineering of Amyloid Aggregation‐Prone Fragments and Their Antimicrobial Conjugates with Multi‐Target Functionality. Adv Funct Materials 2021;31:2102978. [DOI: 10.1002/adfm.202102978] [Cited by in Crossref: 8] [Cited by in F6Publishing: 9] [Article Influence: 8.0] [Reference Citation Analysis]
24 Szulc N, Gąsior-Głogowska M, Wojciechowski JW, Szefczyk M, Żak AM, Burdukiewicz M, Kotulska M. Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli. Int J Mol Sci 2021;22:5127. [PMID: 34066237 DOI: 10.3390/ijms22105127] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
25 Molina-Santiago C, de Vicente A, Romero D. Bacterial extracellular matrix as a natural source of biotechnologically multivalent materials. Comput Struct Biotechnol J 2021;19:2796-805. [PMID: 34093994 DOI: 10.1016/j.csbj.2021.05.008] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
26 Chatani E, Yuzu K, Ohhashi Y, Goto Y. Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils. Int J Mol Sci 2021;22:4349. [PMID: 33919421 DOI: 10.3390/ijms22094349] [Cited by in Crossref: 14] [Cited by in F6Publishing: 17] [Article Influence: 14.0] [Reference Citation Analysis]
27 Miryala S, Nair VG, Chandramohan S, Srinandan CS. Matrix inhibition by Salmonella excludes uropathogenic E. coli from biofilm. FEMS Microbiol Ecol 2020;97:fiaa214. [PMID: 33059364 DOI: 10.1093/femsec/fiaa214] [Reference Citation Analysis]
28 Corsini PM, Wang S, Rehman S, Fenn K, Sagar A, Sirovica S, Cleaver L, Edwards-gayle CJC, Mastroianni G, Dorgan B, Sewell LM, Lynham S, Iuga D, Franks WT, Jarvis J, Carpenter GH, Curtis MA, Bernadó P, Darbari VC, Garnett JA. Molecular and cellular insight into Escherichia coli SslE and its role during biofilm maturation.. [DOI: 10.1101/2021.02.07.430137] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
29 Tanaka S, Kahmann R. Cell wall-associated effectors of plant-colonizing fungi. Mycologia 2021;113:247-60. [PMID: 33534652 DOI: 10.1080/00275514.2020.1831293] [Cited by in Crossref: 8] [Cited by in F6Publishing: 4] [Article Influence: 8.0] [Reference Citation Analysis]
30 Valette N, Renou J, Boutilliat A, Fernández-González AJ, Gautier V, Silar P, Guyeux C, Charr JC, Cuenot S, Rose C, Gelhaye E, Morel-Rouhier M. OSIP1 is a self-assembling DUF3129 protein required to protect fungal cells from toxins and stressors. Environ Microbiol 2021;23:1594-607. [PMID: 33393164 DOI: 10.1111/1462-2920.15381] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
31 Kukharenko OY, Terzova VO, Zubova GV. Protein aggregates carry non-genetic memory in bacteria after stresses. Biopolym Cell 2020;36:409-422. [DOI: 10.7124/bc.000a3f] [Reference Citation Analysis]
32 Shanmugam N, Baker MODG, Sanz-Hernandez M, Sierecki E, Gambin Y, Steain M, Pham CLL, Sunde M. Herpes simplex virus encoded ICP6 protein forms functional amyloid assemblies with necroptosis-associated host proteins. Biophys Chem 2021;269:106524. [PMID: 33348174 DOI: 10.1016/j.bpc.2020.106524] [Cited by in Crossref: 13] [Cited by in F6Publishing: 9] [Article Influence: 6.5] [Reference Citation Analysis]
33 Morris DL, Johnson S, Bleck CK, Lee D, Tjandra N. Humanin selectively prevents the activation of pro-apoptotic protein BID by sequestering it into fibers. Journal of Biological Chemistry 2020;295:18226-38. [DOI: 10.1074/jbc.ra120.013023] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 4.5] [Reference Citation Analysis]
34 Kosolapova AO, Antonets KS, Belousov MV, Nizhnikov AA. Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions. Int J Mol Sci 2020;21:E7240. [PMID: 33008049 DOI: 10.3390/ijms21197240] [Cited by in Crossref: 7] [Cited by in F6Publishing: 9] [Article Influence: 3.5] [Reference Citation Analysis]
35 Beg AZ, Khan AU. Motifs and interface amino acid-mediated regulation of amyloid biogenesis in microbes to humans: potential targets for intervention. Biophys Rev 2020;12:1249-56. [PMID: 32930961 DOI: 10.1007/s12551-020-00759-5] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
36 Kaur A, New EJ, Sunde M. Strategies for the Molecular Imaging of Amyloid and the Value of a Multimodal Approach. ACS Sens 2020;5:2268-82. [PMID: 32627533 DOI: 10.1021/acssensors.0c01101] [Cited by in Crossref: 13] [Cited by in F6Publishing: 13] [Article Influence: 6.5] [Reference Citation Analysis]
37 Ulamec SM, Radford SE. Spot the Difference: Function versus Toxicity in Amyloid Fibrils. Trends in Biochemical Sciences 2020;45:635-6. [DOI: 10.1016/j.tibs.2020.04.007] [Cited by in Crossref: 10] [Cited by in F6Publishing: 10] [Article Influence: 5.0] [Reference Citation Analysis]
38 Zajkowski T, Lee MD, Mondal SS, Carbajal A, Dec R, Brennock PD, Piast RW, Snyder JE, Bense NB, Dzwolak W, Jarosz DF, Rothschild LJ. The hunt for ancient prions: Archaeal prion-like domains form amyloids and substitute for yeast prion domains.. [DOI: 10.1101/2020.07.20.212902] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]
39 Miryala S, Chandramohan S, Srinandan CS. Competitive exclusion of uropathogenic E. coli biofilm by Salmonella through matrix inhibition.. [DOI: 10.1101/2020.01.18.911263] [Reference Citation Analysis]
40 Ball SR, Kwan AH, Sunde M. Hydrophobin Rodlets on the Fungal Cell Wall. In: Latgé J, editor. The Fungal Cell Wall. Cham: Springer International Publishing; 2020. pp. 29-51. [DOI: 10.1007/82_2019_186] [Cited by in Crossref: 9] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
41 Li Y, Rebuffat S. The manifold roles of microbial ribosomal peptide-based natural products in physiology and ecology. J Biol Chem 2020;295:34-54. [PMID: 31784450 DOI: 10.1074/jbc.REV119.006545] [Cited by in Crossref: 41] [Cited by in F6Publishing: 42] [Article Influence: 13.7] [Reference Citation Analysis]
42 Hall D. 2019-A year in Biophysical Reviews. Biophys Rev 2019;11:833-9. [PMID: 31741173 DOI: 10.1007/s12551-019-00607-1] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
43 Battle AR, Norton RS, Böcking T, Noji H, Kim KK, Nagayama K. Editorial: Special issue of Biophysical Reviews dedicated to the joint 10th Asian Biophysics Association Symposium and 42nd Australian Society for Biophysics Meeting, Melbourne, Australia, December 2-6, 2018. Biophys Rev 2019;11:245-7. [PMID: 31115863 DOI: 10.1007/s12551-019-00553-y] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 1.3] [Reference Citation Analysis]