{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T10:05:40Z","timestamp":1790071540596,"version":"4.0.1"},"reference-count":83,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2017,6,29]],"date-time":"2017-06-29T00:00:00Z","timestamp":1498694400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Amyloids are traditionally considered pathological protein aggregates that play causative roles in neurodegenerative disease, diabetes and prionopathies. However, increasing evidence indicates that in many biological systems nonpathological amyloids are formed for functional purposes. In this review, we will specifically describe amyloids that carry out biological roles in sexual reproduction including the processes of gametogenesis, germline specification, sperm maturation and fertilization. Several of these functional amyloids are evolutionarily conserved across several taxa, including human, emphasizing the critical role amyloids perform in reproduction. Evidence will also be presented suggesting that, if altered, some functional amyloids may become pathological.<\/jats:p>","DOI":"10.3390\/biom7030046","type":"journal-article","created":{"date-parts":[[2017,6,29]],"date-time":"2017-06-29T10:40:04Z","timestamp":1498732804000},"page":"46","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["Functional Amyloids in Reproduction"],"prefix":"10.3390","volume":"7","author":[{"given":"Aveline","family":"Hewetson","sequence":"first","affiliation":[{"name":"Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hoa Quynh","family":"Do","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caitlyn","family":"Myers","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Archana","family":"Muthusubramanian","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roger Bryan","family":"Sutton","sequence":"additional","affiliation":[{"name":"Department of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin J.","family":"Wylie","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Texas Tech University, Lubbock, TX 79409, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gail A.","family":"Cornwall","sequence":"additional","affiliation":[{"name":"Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, TX 79430, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,6,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/j.cbpa.2004.09.002","article-title":"Amyloidogenic domains, prions and structural inheritance: Rudiments of early life or recent acquisition?","volume":"8","author":"Chernoff","year":"2004","journal-title":"Curr. Opin. Chem. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"11609","DOI":"10.1002\/anie.201605321","article-title":"Amyloid aggregates arise from amino acid condensations under prebiotic conditions","volume":"55","author":"Greenwald","year":"2006","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"3638","DOI":"10.1098\/rstb.2011.0084","article-title":"Translational regulation of the cell cycle: When, where, how and why?","volume":"366","author":"Kronja","year":"2011","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.cell.2015.08.060","article-title":"Regulated formation of an amyloid-like translational repressor governs gametogenesis","volume":"163","author":"Berchowitz","year":"2015","journal-title":"Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"e00117","DOI":"10.7554\/eLife.00117","article-title":"Meiosis I chromosome segregation is established through regulation of microtubule-kinetochore interactions","volume":"1","author":"Miller","year":"2012","journal-title":"eLife"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.cell.2009.02.044","article-title":"A systematic survey identifies prions and illuminates sequence features of prionogenic proteins","volume":"137","author":"Alberti","year":"2009","journal-title":"Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1126\/science.1191081","article-title":"Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits","volume":"330","author":"Halfmann","year":"2010","journal-title":"Science"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2656","DOI":"10.1038\/sj.emboj.7600738","article-title":"The DAZL family proteins are PABP-binding proteins that regulate translation in germ cells","volume":"24","author":"Collier","year":"2005","journal-title":"EMBO J."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/37987","article-title":"The mouse Dazla gene encodes a cytoplasmic protein essential for gametogenesis","volume":"389","author":"Ruggiu","year":"1997","journal-title":"Nature"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.brainres.2012.01.016","article-title":"The tip of the iceberg: RNA binding proteins with prion-like domains in neurodegenerative disease","volume":"1462","author":"King","year":"2012","journal-title":"Brain Res."},{"key":"ref_12","first-page":"2501","article-title":"Mouse oocytes differentiate through organelle enrichment from sister cyst germ cells","volume":"30","author":"Lei","year":"2016","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0070-2153(00)50008-8","article-title":"Germ plasm and molecular determinants of germ cell fate","volume":"50","author":"Houston","year":"2000","journal-title":"Curr. Top. Dev. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nrm2815","article-title":"Mechanisms guiding primordial germ cell migration: Strategies from different organisms","volume":"11","author":"Richardson","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.cell.2016.06.051","article-title":"Amyloid-like self-assembly of a cellular compartment","volume":"166","author":"Boke","year":"2016","journal-title":"Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/j.devcel.2004.05.002","article-title":"Maternal control of vertebrate development before the midblastula transition: Mutants from the zebrafish I","volume":"6","author":"Dosch","year":"2004","journal-title":"Dev. Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0092-8674(91)90137-N","article-title":"Oskar organizes the germ plasm and directs localization of the posterior determinant nanos","volume":"66","author":"Ephrussi","year":"1991","journal-title":"Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1126\/science.1172046","article-title":"Germline P granules are liquid droplets that localize by controlled dissolution\/condensation","volume":"324","author":"Brangwynne","year":"2009","journal-title":"Science"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"95","DOI":"10.4161\/spmg.1.2.16820","article-title":"Acrosome biogenesis: Revisiting old questions to yield new insights","volume":"1","author":"Berruti","year":"2011","journal-title":"Spermatogenesis"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1042\/bj2750759","article-title":"A mechanism for differential release of acrosomal enzymes during the acrosome reaction","volume":"285","author":"Hardy","year":"1991","journal-title":"Biochem. J."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.ydbio.2003.08.006","article-title":"Differential release of soluble and matrix components: Evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm","volume":"264","author":"Kim","year":"2003","journal-title":"Dev. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1126\/science.1063665","article-title":"Lack of acrosome formation in Hrb-deficient mice","volume":"294","author":"Mantchev","year":"2001","journal-title":"Science"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"6794","DOI":"10.1128\/MCB.01029-07","article-title":"Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis","volume":"27","author":"Lin","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2624","DOI":"10.1128\/MCB.00073-14","article-title":"Functional amyloids in the mouse sperm acrosome","volume":"34","author":"Guyonnet","year":"2014","journal-title":"Mol. Cell. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0092-8674(00)81223-4","article-title":"Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins","volume":"94","author":"Glover","year":"1998","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1095\/biolreprod.110.084855","article-title":"Reduced fertility in vitro in mice lacking the cystatin CRES (cystatin-related epididymal spermatogenic): Rescue by exposure of spermatozoa to dibutyryl cAMP and isobutylmethylxanthine","volume":"84","author":"Chau","year":"2011","journal-title":"Biol. Reprod."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"23289","DOI":"10.1074\/jbc.271.38.23289","article-title":"The initial molecular interaction between mouse sperm and the zona pellucida is a complex binding event","volume":"271","author":"Thaler","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"26025","DOI":"10.1074\/jbc.270.44.26025","article-title":"A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to von Willebrand factor","volume":"270","author":"Hardy","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"24863","DOI":"10.1074\/jbc.M110.123125","article-title":"Zonadhesin is essential for species specificity of sperm adhesion to the egg zona pellucida","volume":"285","author":"Tardif","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0022-2836(85)90089-0","article-title":"Mouse egg extracellular coat is a matrix of interconnected filaments possessing a structural repeat","volume":"181","author":"Greve","year":"1985","journal-title":"J. Mol. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1002\/jcp.21174","article-title":"Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions","volume":"214","author":"Litscher","year":"2008","journal-title":"J. Cell. Physiol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"34189","DOI":"10.1074\/jbc.M304026200","article-title":"Structural characterization of native mouse zona pellucida proteins using mass spectrometry","volume":"278","author":"Boja","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1146\/annurev.biochem.74.082803.133039","article-title":"Zona pellucida domain proteins","volume":"74","author":"Jovine","year":"2005","journal-title":"Annu. Rev. Biochem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/nature07599","article-title":"Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats","volume":"456","author":"Monne","year":"2008","journal-title":"Nature"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"17302","DOI":"10.1073\/pnas.0603125103","article-title":"Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs","volume":"103","author":"Aagaard","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1963","DOI":"10.1093\/molbev\/msr026","article-title":"The molecular basis of sex: Linking yeast to humans","volume":"28","author":"Swanson","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1095\/biolreprod.111.092098","article-title":"A structural view of egg coat architecture and function in fertilization","volume":"85","author":"Monne","year":"2011","journal-title":"Biol. Reprod."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"R123","DOI":"10.1152\/ajpregu.2001.280.1.R123","article-title":"Survival of water stress in annual fish embryos: Dehydration avoidance and egg envelope amyloid fibers","volume":"280","author":"Podrabsky","year":"2001","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1002\/bip.22563","article-title":"Structural studies of \u2018aggregation-prone\u2019 peptide-analogues of teleostean egg chorion ZPB proteins","volume":"102","author":"Louros","year":"2014","journal-title":"Biopolymers"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0014-5793(00)01888-3","article-title":"Amyloids protect the silkmoth oocyte and embryo","volume":"479","author":"Iconomidou","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Egge, N., Mutusubramanian, A., and Cornwall, G.A. (2015). Amyloid properties of the mouse egg zona pellucida. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0129907"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/j.cell.2010.09.041","article-title":"Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3","volume":"143","author":"Han","year":"2010","journal-title":"Cell"},{"key":"ref_43","first-page":"2554","article-title":"Cell surface anchorage and ligand-binding domains of the Saccharomyces cerevisiae cell adhesion protein a-agglutinin, a member of the immunoglobulin superfamily","volume":"13","author":"Wojciechowicz","year":"1993","journal-title":"Mol. Cell. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1095\/biolreprod61.6.1649","article-title":"Expression of recombinant human zona pellucida protein 2 and its binding capacity to spermatozoa","volume":"61","author":"Tsubamoto","year":"1999","journal-title":"Biol. Reprod."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1083\/jcb.201404025","article-title":"A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans","volume":"205","author":"Avella","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1002\/1873-3468.12099","article-title":"A common \u201caggregation-prone\u201d interface possibly participates in the self-assembly of human zona pellucida proteins","volume":"590","author":"Louros","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Louros, N.N., Iconomidou, V.A., Giannelou, P., and Hamodrakas, S.J. (2013). Structural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: Insights into mammalian Zona Pellucida formation. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0073258"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1126\/science.1138591","article-title":"Blastocyst axis is specified independently of early cell lineage but aligns with the ZP shape","volume":"316","author":"Kurotaki","year":"2007","journal-title":"Science"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-beta spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchroton X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1016\/j.tcb.2010.06.002","article-title":"From A to Z: Apical structures and zona pellucida-domain proteins","volume":"20","author":"Plaza","year":"2010","journal-title":"Trends Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Whelly, S., Johnson, S., Powell, J., Borchardt, C., Hastert, M.C., and Cornwall, G.A. (2012). Nonpathological extracellular amyloid is present during normal epididymal sperm maturation. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0036394"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1093\/humupd\/dmn055","article-title":"New insights into epididymal biology and function","volume":"15","author":"Cornwall","year":"2009","journal-title":"Hum. Reprod. Update"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1093\/molehr\/gaw049","article-title":"Cystatin-related epididymal spermatogenic subgroup members are part of an amyloid matrix and associated with extracellular vesicles in the mouse epididymal lumen","volume":"22","author":"Whelly","year":"2016","journal-title":"Mol. Hum. Reprod."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"18318","DOI":"10.1074\/jbc.M611368200","article-title":"Fibrillogenic oligomers of human cystatin C are formed by propagated domain swapping","volume":"282","author":"Wahlbom","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2787","DOI":"10.1210\/endo.143.7.8925","article-title":"Cystatin 11: A new member of the cystatin type 2 family","volume":"143","author":"Hamil","year":"2002","journal-title":"Endocrinology"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1095\/biolreprod.102.003970","article-title":"Identification and characterization of cystatin-related epididymal spermatogenic protein in human spermatozoa: Localization in the equatorial segment","volume":"67","author":"Wassler","year":"2002","journal-title":"Biol. Reprod."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"444","DOI":"10.2164\/jandrol.110.010694","article-title":"Alterations in the testis and epididymis associated with loss of function of the cystatin-related epididymal spermatogenic (CRES) protein","volume":"32","author":"Parent","year":"2011","journal-title":"J. Androl."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Wang, L., Yuan, Q., Chen, S., Cai, H., Lu, M., Liu, Y., and Xu, C. (2012). Antimicrobial activity and molecular mechanism of the CRES protein. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0048368"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1128\/jvi.64.2.941-943.1990","article-title":"Cystatin C, a human proteinase inhibitor, blocks replication of herpes simplex virus","volume":"64","author":"Grubb","year":"1990","journal-title":"J. Virol."},{"key":"ref_61","first-page":"1371","article-title":"Cystatin and cystatin-derived peptides have antibacterial activity against the pathogen Porphyromonas gingivalis","volume":"379","author":"Blankenvoorde","year":"1998","journal-title":"Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"340ra72","DOI":"10.1126\/scitranslmed.aaf1059","article-title":"Amyloid-\u03b2 peptide protects against microbial infection in mouse and worm models of Alzheimer\u2019s disease","volume":"8","author":"Kumar","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/j.bbrc.2016.08.052","article-title":"Functional characterization of \u03b1-synuclein protein with antimicrobial activity","volume":"478","author":"Park","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1021\/mp200419b","article-title":"Antimicrobial properties of amyloid peptides","volume":"9","author":"Kagan","year":"2012","journal-title":"Mol. Pharm."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1146\/annurev.micro.60.080805.142106","article-title":"Curli biogenesis and function","volume":"60","author":"Barnhart","year":"2006","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1016\/j.cell.2007.10.014","article-title":"Semen-derived amyloid fibrils drastically enhance HIV infection","volume":"131","author":"Adermann","year":"2007","journal-title":"Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.chom.2011.10.010","article-title":"Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection","volume":"10","author":"Roan","year":"2011","journal-title":"Cell Host Microbe"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1128\/AAC.02464-12","article-title":"Semen-derived enhancer of viral infection (SEVI) binds bacteria, enhances bacterial phagocytosis by macrophages, and can protect against vaginal infection by a sexually transmitted bacterial pathogen","volume":"57","author":"Easterhoff","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Fowler, D.M., Koulov, A.V., Alory-Jost, C., Marks, M.S., Balch, W.E., and Kelly, J.W. (2006). Functional amyloid formation within mammalian tissue. PLoS Biol., 4.","DOI":"10.1371\/journal.pbio.0040006"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1073\/pnas.97.2.571","article-title":"Acceleration of oligomerization, not fibrillization, is a shared property of both \u03b1-synuclein mutations linked to early-onset Parkinson\u2019s disease: Implications for pathogenesis and therapy","volume":"97","author":"Conway","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1074\/jbc.M609269200","article-title":"Visualization of aggregation of the Rnq1 prion domain and cross-seeding interactions with Sup35NM","volume":"282","author":"Vitrenko","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"11842","DOI":"10.1074\/jbc.M111.314336","article-title":"Seminal plasma accelerates semen-derived enhancer viral infection (SEV1) fibril formation by the prostatic acid phosphatase (PAP 248\u2013286) peptide","volume":"287","author":"Olsen","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"38265","DOI":"10.1038\/srep38265","article-title":"Identification and structural characterization of the N-terminal amyloid core of Orb2 isoform A","volume":"6","author":"Cervantes","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"13731","DOI":"10.1073\/pnas.0906509106","article-title":"The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis","volume":"106","author":"McGlinchey","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_76","unstructured":"Do, Q.-H., Hewetson, A., Cornwall, G.A., and Wylie, B.J. Structural characterization of a functional amyloid along its unique amyloidogenic pathway, Manuscript in preparation."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/nsmb.2503","article-title":"Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEB","volume":"20","author":"Raveendra","year":"2013","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.sbi.2014.12.001","article-title":"The structure of fibrils from \u201cmisfolded\u201d proteins","volume":"30","author":"Meier","year":"2015","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_79","unstructured":"Hewetson, A., Cornwall, G.A., and Sutton, R.B. X-ray crystal structure of cystatin-related epididymal spermatogenic (CRES) to 1.8 \u00c5, Manuscript in preparation."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1073\/pnas.1610371113","article-title":"Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson\u2019s disease","volume":"113","author":"Horvath","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"e5","DOI":"10.7717\/peerj.5","article-title":"Bacterial curli protein promotes the conversion of PAP248\u2013286 into amyloid SEV1: Cross-seeding of dissimilar amyloid sequences","volume":"1","author":"Hartman","year":"2013","journal-title":"PeerJ"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1046\/j.1471-4159.2001.00256.x","article-title":"Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type","volume":"77","author":"Calero","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"7718","DOI":"10.1074\/jbc.M113.515759","article-title":"Fertility defects in mice expressing the L68Q variant of human cystatin C: A role for amyloid in male infertility","volume":"289","author":"Whelly","year":"2014","journal-title":"J. Biol. Chem."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/7\/3\/46\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:40:50Z","timestamp":1760208050000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/7\/3\/46"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,6,29]]},"references-count":83,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2017,9]]}},"alternative-id":["biom7030046"],"URL":"https:\/\/doi.org\/10.3390\/biom7030046","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,6,29]]}}}