{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T06:39:09Z","timestamp":1790663949469,"version":"4.1.0"},"reference-count":145,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,9,9]],"date-time":"2022-09-09T00:00:00Z","timestamp":1662681600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Polish National Science Center","award":["UMO-2020\/39\/B\/ST10\/01253"],"award-info":[{"award-number":["UMO-2020\/39\/B\/ST10\/01253"]}]},{"name":"Polish Ministry of Education and Science","award":["UMO-2020\/39\/B\/ST10\/01253"],"award-info":[{"award-number":["UMO-2020\/39\/B\/ST10\/01253"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Some animal organs contain mineralized tissues. These so-called hard tissues are mostly deposits of calcium salts, usually in the form of calcium phosphate or calcium carbonate. Examples of this include fish otoliths and mammalian otoconia, which are found in the inner ear, and they are an essential part of the sensory system that maintains body balance. The composition of ear stones is quite well known, but the role of individual components in the nucleation and growth of these biominerals is enigmatic. It is sure that intrinsically disordered proteins (IDPs) play an important role in this aspect. They have an impact on the shape and size of otoliths. It seems probable that IDPs, with their inherent ability to phase separate, also play a role in nucleation processes. This review discusses the major theories on the mechanisms of biomineral nucleation with a focus on the importance of protein-driven liquid\u2013liquid phase separation (LLPS). It also presents the current understanding of the role of IDPs in the formation of calcium carbonate biominerals and predicts their potential ability to drive LLPS.<\/jats:p>","DOI":"10.3390\/biom12091266","type":"journal-article","created":{"date-parts":[[2022,9,9]],"date-time":"2022-09-09T04:54:41Z","timestamp":1662699281000},"page":"1266","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["The Role of Intrinsically Disordered Proteins in Liquid\u2013Liquid Phase Separation during Calcium Carbonate Biomineralization"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2209-0919","authenticated-orcid":false,"given":"Aneta","family":"Tarczewska","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0719-5344","authenticated-orcid":false,"given":"Klaudia","family":"Bielak","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Zoglowek","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0521-2099","authenticated-orcid":false,"given":"Katarzyna","family":"So\u0142tys","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5522-2557","authenticated-orcid":false,"given":"Piotr","family":"Dobryszycki","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5874-784X","authenticated-orcid":false,"given":"Andrzej","family":"O\u017cyhar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8008-6689","authenticated-orcid":false,"given":"Miros\u0142awa","family":"R\u00f3\u017cycka","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrze\u017ce Wyspia\u0144skiego 27, 50-370 Wroclaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,9,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"7115","DOI":"10.1074\/jbc.TM118.001192","article-title":"The Molecular Language of Membraneless Organelles","volume":"294","author":"Gomes","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","article-title":"Liquid-Liquid Phase Separation in Biology","volume":"30","author":"Hyman","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.cell.2016.06.010","article-title":"Compositional Control of Phase-Separated Cellular Bodies","volume":"166","author":"Banani","year":"2016","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid Phase Condensation in Cell Physiology and Disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nphys3532","article-title":"Polymer Physics of Intracellular Phase Transitions","volume":"11","author":"Brangwynne","year":"2015","journal-title":"Nat. Phys."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.mie.2018.09.035","article-title":"Phase Separation of Intrinsically Disordered Proteins","volume":"Volume 611","author":"Posey","year":"2018","journal-title":"Methods in Enzymology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular Condensates: Organizers of Cellular Biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4666","DOI":"10.1016\/j.jmb.2018.08.003","article-title":"Who\u2019s In and Who\u2019s Out\u2014Compositional Control of Biomolecular Condensates","volume":"430","author":"Ditlev","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_9","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_10","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1016\/j.bpj.2020.09.023","article-title":"The Emergence of Phase Separation as an Organizing Principle in Bacteria","volume":"120","author":"Azaldegui","year":"2021","journal-title":"Biophys. J."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"So\u0142tys, K., Tarczewska, A., Bystranowska, D., and Soza\u0144ska, N. (2022). Getting Closer to Decrypting the Phase Transitions of Bacterial Biomolecules. Biomolecules, 12.","DOI":"10.3390\/biom12070907"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Brocca, S., Grandori, R., Longhi, S., and Uversky, V. (2020). 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., 21.","DOI":"10.3390\/ijms21239045"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1038\/s41467-020-15007-3","article-title":"Liquid-Liquid Phase Separation and Extracellular Multivalent Interactions in the Tale of Galectin-3","volume":"11","author":"Chiu","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1080\/03008200390152007","article-title":"Biomineralization: An Overview","volume":"44","author":"Boskey","year":"2003","journal-title":"Connect. Tissue Res."},{"key":"ref_15","first-page":"364","article-title":"Biomineralization--Precision of Shape, Structure and Properties Controlled by Proteins","volume":"61","author":"Poznar","year":"2015","journal-title":"Postepy Biochem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/ncomms1604","article-title":"Stable Prenucleation Mineral Clusters Are Liquid-like Ionic Polymers","volume":"2","author":"Demichelis","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.nantod.2011.10.005","article-title":"Prenucleation Clusters and Non-Classical Nucleation","volume":"6","author":"Gebauer","year":"2011","journal-title":"Nano Today"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/S0022-0248(99)00749-6","article-title":"Deposition of Calcium Carbonate Films by a Polymer-Induced Liquid-Precursor (PILP) Process","volume":"210","author":"Gower","year":"2000","journal-title":"J. Cryst. Growth"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1126\/science.1164271","article-title":"Stable Prenucleation Calcium Carbonate Clusters","volume":"332","author":"Gebauer","year":"2008","journal-title":"Science"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"834503","DOI":"10.3389\/fchem.2022.834503","article-title":"Liquid-Liquid Phase Separation in Nucleation Process of Biomineralization","volume":"10","author":"Qin","year":"2022","journal-title":"Front. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"6155","DOI":"10.1002\/anie.201915350","article-title":"Stable Prenucleation Calcium Carbonate Clusters Define Liquid\u2013Liquid Phase Separation","volume":"59","author":"Avaro","year":"2020","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.matbio.2016.01.007","article-title":"Intrinsically Disordered Proteins and Biomineralization","volume":"52\u201354","author":"Boskey","year":"2016","journal-title":"Matrix Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1073\/pnas.1017150108","article-title":"Active Liquid-like Behavior of Nucleoli Determines Their Size and Shape in Xenopus Laevis Oocytes","volume":"108","author":"Brangwynne","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1021\/acs.biochem.7b01215","article-title":"In Aqua Veritas: The Indispensable yet Mostly Ignored Role of Water in Phase Separation and Membrane-Less Organelles","volume":"57","author":"Zaslavsky","year":"2018","journal-title":"Biochemistry"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1016\/j.cub.2017.08.069","article-title":"Phase Separation in Biology","volume":"27","author":"Alberti","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2478","DOI":"10.1021\/acs.biochem.8b00008","article-title":"Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions","volume":"57","author":"Martin","year":"2018","journal-title":"Biochemistry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12964-015-0125-7","article-title":"Phase Separation in Biology; Functional Organization of a Higher Order","volume":"14","author":"Mitrea","year":"2016","journal-title":"Cell Commun. Signal."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/s41392-021-00678-1","article-title":"Liquid\u2013Liquid Phase Separation in Human Health and Diseases","volume":"6","author":"Wang","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"a034058","DOI":"10.1101\/cshperspect.a034058","article-title":"Protein Phase Separation as a Stress Survival Strategy","volume":"11","author":"Franzmann","year":"2019","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.sbi.2016.10.015","article-title":"Intrinsically Disordered Proteins in Overcrowded Milieu: Membrane-Less Organelles, Phase Separation, and Intrinsic Disorder","volume":"44","author":"Uversky","year":"2017","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1016\/j.jmb.2018.06.012","article-title":"Intrinsically Disordered Proteins: Structure, Function and Therapeutics","volume":"430","author":"Chen","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s12038-020-0010-4","article-title":"Dynamic Conformational Flexibility and Molecular Interactions of Intrinsically Disordered Proteins","volume":"45","author":"Bhattarai","year":"2020","journal-title":"J. Biosci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1146\/annurev-genet-112618-043527","article-title":"Liquid\u2013Liquid Phase Separation in Disease","volume":"53","author":"Alberti","year":"2019","journal-title":"Annu. Rev. Genet."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"11541","DOI":"10.1021\/acs.jpcb.0c07598","article-title":"The Dynamism of Intrinsically Disordered Proteins: Binding-Induced Folding, Amyloid Formation, and Phase Separation","volume":"124","author":"Mukhopadhyay","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"5850","DOI":"10.1074\/jbc.AC120.013166","article-title":"Zinc Promotes Liquid-Liquid Phase Separation of Tau Protein","volume":"295","author":"Singh","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1111\/j.1471-4159.2008.05339.x","article-title":"A Novel Calcium-Binding Protein Is Associated with Tau Proteins in Tauopathy","volume":"106","author":"Vega","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"573","DOI":"10.2174\/0929866511320050011","article-title":"Functional and Structural Analysis of the Conserved EFhd2 Protein","volume":"20","author":"Vaquer","year":"2013","journal-title":"Protein Pept. Lett."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1111\/jnc.12155","article-title":"EFhd2 Is a Novel Amyloid Protein Associated with Pathological Tau in Alzheimer\u2019s Disease","volume":"125","author":"Orange","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"845","DOI":"10.3389\/fnins.2019.00845","article-title":"EFhd2 Affects Tau Liquid-Liquid Phase Separation","volume":"13","author":"Vega","year":"2019","journal-title":"Front. Neurosci."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Wi\u0119ch, A., Tarczewska, A., O\u017cyhar, A., and Or\u0142owski, M. (2021). Metal Ions Induce Liquid Condensate Formation by the F Domain of Aedes Aegypti Ecdysteroid Receptor. New Perspectives of Nuclear Receptor Studies. Cells, 10.","DOI":"10.3390\/cells10030571"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.cell.2018.06.006","article-title":"A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins","volume":"174","author":"Wang","year":"2018","journal-title":"Cell"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.cell.2018.12.035","article-title":"Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates","volume":"176","author":"Alberti","year":"2019","journal-title":"Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e64004","DOI":"10.7554\/eLife.64004","article-title":"Charge-Driven Condensation of RNA and Proteins Suggests Broad Role of Phase Separation in Cytoplasmic Environments","volume":"10","author":"Dutagaci","year":"2021","journal-title":"Elife"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Mayfield, J.E., Pollak, A.J., Worby, C.A., Xu, J.C., Tandon, V., Newton, A.C., and Dixon, J.E. (2021). Ca2+-Dependent Liquid-Liquid Phase Separation Underlies Intracellular Ca2+ Stores. bioRxiv.","DOI":"10.1101\/2021.07.06.451223"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Wojtas, M., Dobryszycki, P., and O\u017cyhar, A. (2012). Intrinsically Disordered Proteins in Biomineralization, Advanced Topics in Biomineralization, IntechOpen.","DOI":"10.5772\/31121"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2368","DOI":"10.1016\/j.biomaterials.2007.01.029","article-title":"Protein Mapping of Calcium Carbonate Biominerals by Immunogold","volume":"28","author":"Press","year":"2007","journal-title":"Biomaterials"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"157","DOI":"10.2138\/rmg.2005.59.7","article-title":"The Organic-Mineral Interface in Biominerals","volume":"59","author":"Gilbert","year":"2005","journal-title":"Rev. Mineral. Geochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.bone.2012.05.009","article-title":"Structural Disorder in Proteins Brings Order to Crystal Growth in Biomineralization","volume":"51","author":"Kalmar","year":"2012","journal-title":"Bone"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1111\/febs.14715","article-title":"The Inner Ear Proteome of Fish","volume":"286","author":"Thomas","year":"2019","journal-title":"FEBS J."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6877","DOI":"10.1096\/fj.201802268R","article-title":"In Vivo and in Vitro Analysis of Starmaker Activity in Zebrafish Otolith Biomineralization","volume":"33","author":"Kalka","year":"2019","journal-title":"FASEB J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1126\/science.1116994","article-title":"Rigid Biological Systems as Models for Synthetic Composites","volume":"310","author":"George","year":"2005","journal-title":"Science"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"5808","DOI":"10.1021\/acs.cgd.0c00413","article-title":"Fish Otolith Matrix Macromolecule-64 (OMM-64) and Its Role in Calcium Carbonate Biomineralization","volume":"20","author":"Poznar","year":"2020","journal-title":"Cryst. Growth Des."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1038\/nmat4631","article-title":"Tuning Hardness in Calcite by Incorporation of Amino Acids","volume":"15","author":"Kim","year":"2016","journal-title":"Nat. Mater."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"3032","DOI":"10.1021\/acs.biochem.8b00207","article-title":"Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization","volume":"57","author":"Jain","year":"2018","journal-title":"Biochemistry"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Evans, J.S. (2020). Glycosylation: A \u201cLast Word\u201d in the Protein-Mediated Biomineralization Process. Crystals, 10.","DOI":"10.3390\/cryst10090818"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"34","DOI":"10.3109\/03008207.2013.867336","article-title":"The Role of Acidic Phosphoproteins in Biomineralization","volume":"55","author":"Alvares","year":"2014","journal-title":"Connect. Tissue Res."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1021\/cg200905f","article-title":"Phosphorylation of Intrinsically Disordered Starmaker Protein Increases Its Ability To Control the Formation of Calcium Carbonate Crystals","volume":"12","author":"Wojtas","year":"2012","journal-title":"Cryst. Growth Des."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1126\/science.1217817","article-title":"Secreted Kinase Phosphorylates Extracellular Proteins That Regulate Biomineralization","volume":"336","author":"Tagliabracci","year":"2012","journal-title":"Science"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"3563","DOI":"10.1038\/s41598-018-21797-w","article-title":"Fam20C Participates in the Shell Formation in the Pearl Oyster, Pinctada Fucata","volume":"8","author":"Du","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1021\/acs.biochem.5b01186","article-title":"Insect Cell Glycosylation and Its Impact on the Functionality of a Recombinant Intracrystalline Nacre Protein, AP24","volume":"55","author":"Chang","year":"2016","journal-title":"Biochemistry"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"4410","DOI":"10.1021\/acs.biochem.6b00619","article-title":"A Model Sea Urchin Spicule Matrix Protein Self-Associates To Form Mineral-Modifying Protein Hydrogels","volume":"55","author":"Jain","year":"2016","journal-title":"Biochemistry"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.febslet.2008.01.026","article-title":"In Vitro Regulation of CaCO3 Crystal Polymorphism by the Highly Acidic Molluscan Shell Protein Aspein","volume":"582","author":"Takeuchi","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/j.bbrc.2004.06.072","article-title":"Structure and Expression of an Unusually Acidic Matrix Protein of Pearl Oyster Shells","volume":"320","author":"Tsukamoto","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s00239-012-9514-3","article-title":"A Comparative Study of the Shell Matrix Protein Aspein in Pterioid Bivalves","volume":"75","author":"Isowa","year":"2012","journal-title":"J. Mol. Evol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/j.peptides.2006.12.005","article-title":"Significance of the N- and C-Terminal Regions of CAP-1, a Cuticle Calcification-Associated Peptide from the Exoskeleton of the Crayfish, for Calcification","volume":"28","author":"Inoue","year":"2007","journal-title":"Peptides"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1039\/C4OB01796J","article-title":"Biomineralization-Inspired Synthesis of Functional Organic\/Inorganic Hybrid Materials: Organic Molecular Control of Self-Organization of Hybrids","volume":"13","author":"Arakaki","year":"2015","journal-title":"Org. Biomol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1016\/j.cub.2013.05.007","article-title":"Cloning and Characterization of Four Novel Coral Acid-Rich Proteins That Precipitate Carbonates In Vitro","volume":"23","author":"Mass","year":"2013","journal-title":"Curr. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"107431","DOI":"10.1016\/j.jsb.2019.107431","article-title":"Coral Acid Rich Protein Selects Vaterite Polymorph in Vitro","volume":"209","author":"Laipnik","year":"2020","journal-title":"J. Struct. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"253","DOI":"10.2108\/zsj.19.253","article-title":"Biomineralization of the Spicules of Sea Urchin Embryos","volume":"19","author":"Wilt","year":"2002","journal-title":"Zoolog. Sci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/s00427-002-0261-0","article-title":"Identification and Developmental Expression of New Biomineralization Proteins in the Sea Urchin Strongylocentrotus Purpuratus","volume":"212","author":"Illies","year":"2002","journal-title":"Dev. Genes Evol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1071\/MF04267","article-title":"Why Otoliths? Insights from Inner Ear Physiology and Fisheries Biology","volume":"56","author":"Popper","year":"2005","journal-title":"Mar. Freshw. Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1098\/rstb.1984.0038","article-title":"Some Properties of Otoconia","volume":"304","author":"Ross","year":"1984","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1002\/dvdy.24195","article-title":"Mechanisms of Otoconia and Otolith Development","volume":"244","author":"Lundberg","year":"2015","journal-title":"Dev. Dyn."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1080\/23308249.2019.1627285","article-title":"Otolith Biochemistry\u2014A Review","volume":"27","author":"Thomas","year":"2019","journal-title":"Rev. Fish. Sci. Aquac."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.crpv.2004.07.013","article-title":"Endolymph Chemistry and Otolith Growth in Fish","volume":"3","author":"Payan","year":"2004","journal-title":"Comptes Rendus Palevol"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3133","DOI":"10.1007\/s00405-013-2784-6","article-title":"Detection of Human Utricular Otoconia Degeneration in Vital Specimen and Implications for Benign Paroxysmal Positional Vertigo","volume":"271","author":"Walther","year":"2014","journal-title":"Eur. Arch. Oto-Rhino-Laryngol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1007\/s10162-008-0137-8","article-title":"Sparc Protein Is Required for Normal Growth of Zebrafish Otoliths","volume":"9","author":"Kang","year":"2008","journal-title":"J. Assoc. Res. Otolaryngol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/j.mod.2005.03.002","article-title":"Otolith Matrix Proteins OMP-1 and Otolin-1 Are Necessary for Normal Otolith Growth and Their Correct Anchoring onto the Sensory Maculae","volume":"122","author":"Murayama","year":"2005","journal-title":"Mech. Dev."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.1111\/j.1742-4658.2008.06400.x","article-title":"Identification of a Novel Matrix Protein Contained in a Protein Aggregate Associated with Collagen in Fish Otoliths","volume":"275","author":"Tohse","year":"2008","journal-title":"FEBS J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1016\/j.bbapap.2017.08.019","article-title":"Structural Properties of the Intrinsically Disordered, Multiple Calcium Ion-Binding Otolith Matrix Macromolecule-64 (OMM-64)","volume":"1865","author":"Poznar","year":"2017","journal-title":"Biochim. Biophys. Acta-Proteins Proteom."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"R\u00f3\u017cycka, M., Wojtas, M., Jak\u00f3b, M., Stigloher, C., Grzeszkowiak, M., Mazur, M., and O\u017cyhar, A. (2014). Intrinsically Disordered and Pliable Starmaker-Like Protein from Medaka (Oryzias Latipes) Controls the Formation of Calcium Carbonate Crystals. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0114308"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1002\/dneu.20587","article-title":"Otoc1: A Novel Otoconin-90 Ortholog Required for Otolith Mineralization in Zebrafish","volume":"68","author":"Petko","year":"2008","journal-title":"Dev. Neurobiol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1126\/science.1088443","article-title":"Control of Crystal Size and Lattice Formation by Starmaker in Otolith Biomineralization","volume":"302","author":"Sollner","year":"2003","journal-title":"Science"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"12740","DOI":"10.1002\/chem.201902157","article-title":"Lattice Shrinkage by Incorporation of Recombinant Starmaker-Like Protein within Bioinspired Calcium Carbonate Crystals","volume":"25","author":"Coronado","year":"2019","journal-title":"Chemistry"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1046\/j.0014-2956.2001.02701.x","article-title":"Fish Otolith Contains a Unique Structural Protein, Otolin-1","volume":"269","author":"Murayama","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/s00418-003-0605-5","article-title":"Immunohistochemical Localization of Two Otolith Matrix Proteins in the Otolith and Inner Ear of the Rainbow Trout, Oncorhynchus Mykiss: Comparative Aspects between the Adult Inner Ear and Embryonic Otocysts","volume":"121","author":"Murayama","year":"2004","journal-title":"Histochem. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.heares.2012.07.003","article-title":"Immunogold TEM of Otoconin 90 and Otolin-Relevance to Mineralization of Otoconia, and Pathogenesis of Benign Positional Vertigo","volume":"292","author":"Andrade","year":"2012","journal-title":"Hear. Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1126\/science.7863331","article-title":"Molecular Cloning and Characterization of an Inner Ear-Specific Structural Protein","volume":"267","author":"Davis","year":"1995","journal-title":"Science"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1111\/febs.14308","article-title":"Effect of Calcium Ions on Structure and Stability of the C1q-like Domain of Otolin-1 from Human and Zebrafish","volume":"284","author":"Dobryszycki","year":"2017","journal-title":"FEBS J."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1016\/j.ijbiomac.2022.04.088","article-title":"N\u2032-Terminal- and Ca2+-Induced Stabilization of High-Order Oligomers of Full-Length Danio Rerio and Homo Sapiens Otolin-1","volume":"209","author":"Bielak","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Moreland, K.T., Hong, M., Lu, W., Rowley, C.W., Ornitz, D.M., De Yoreo, J.J., and Thalmann, R. (2014). In Vitro Calcite Crystal Morphology Is Modulated by Otoconial Proteins Otolin-1 and Otoconin-90. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0095333"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/s00239-013-9539-2","article-title":"The Dentin Matrix Acidic Phosphoprotein 1 (DMP1) in the Light of Mammalian Evolution","volume":"76","author":"Silvent","year":"2013","journal-title":"J. Mol. Evol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1002\/dvdy.22405","article-title":"Expression, Functional, and Structural Analysis of Proteins Critical for Otoconia Development","volume":"239","author":"Xu","year":"2010","journal-title":"Dev. Dyn."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"34700","DOI":"10.1074\/jbc.M305315200","article-title":"Evidence for the Proteolytic Processing of Dentin Matrix Protein 1: Identification and characterization of processed fragments and cleavage sites","volume":"278","author":"Qin","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"6147","DOI":"10.1096\/fj.201901999R","article-title":"Functional Derivatives of Human Dentin Matrix Protein 1 Modulate Morphology of Calcium Carbonate Crystals","volume":"34","author":"Szewczuk","year":"2020","journal-title":"FASEB J."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"57","DOI":"10.2113\/0540057","article-title":"Principles of Crystal Nucleation and Growth","volume":"54","author":"Vekilov","year":"2003","journal-title":"Rev. Mineral. Geochem."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Debenedetti, P.G. (1996). Metastable Liquids, Princeton University Press.","DOI":"10.1515\/9780691213941"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"441","DOI":"10.2475\/ajs.s3-16.96.441","article-title":"On the Equilibrium of Heterogeneous Substances","volume":"s3\u201316","author":"Gibbs","year":"1878","journal-title":"Am. J. Sci."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1002\/andp.19354160806","article-title":"Kinetische Behandlung Der Keimbildung in \u00dcbers\u00e4ttigten D\u00e4mpfen","volume":"416","author":"Becker","year":"1935","journal-title":"Ann. Phys."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1515\/zpch-1927-12513","article-title":"Keimbildungsgeschwindigkeit in \u00dcbers\u00e4ttigten D\u00e4mpfen","volume":"125U","author":"Farkas","year":"1927","journal-title":"Z. Phys. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1515\/zpch-1926-11927","article-title":"Keimbildung in \u00dcbers\u00e4ttigten Gebilden","volume":"119U","author":"Volmer","year":"1926","journal-title":"Z. Phys. Chem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1002\/crat.200310070","article-title":"Review: Nucleation in Solutions Revisited","volume":"38","author":"Kashchiev","year":"2003","journal-title":"Cryst. Res. Technol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"969","DOI":"10.2475\/09.2018.05","article-title":"On classical and non-classical views on nucleation","volume":"318","author":"Gebauer","year":"2018","journal-title":"Am. J. Sci."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1126\/science.1230915","article-title":"Microscopic Evidence for Liquid-Liquid Separation in Supersaturated CaCO3 Solutions","volume":"341","author":"Wallace","year":"2013","journal-title":"Science"},{"key":"ref_105","unstructured":"Koishi, A. (2017). Carbonate Mineral Nucleation Pathways, Universit\u00e9 Grenoble Alpes."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"8388","DOI":"10.1039\/c3ce40803e","article-title":"\u201cLiquid-like\u201d Biomineralization Protein Assemblies: A Key to the Regulation of Non-Classical Nucleation","volume":"15","author":"Evans","year":"2013","journal-title":"CrystEngComm"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1126\/science.1167221","article-title":"Materials Science. Now You See Them","volume":"322","author":"Meldrum","year":"2008","journal-title":"Science"},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Gebauer, D. (2018). How Can Additives Control the Early Stages of Mineralisation?. Minerals, 8.","DOI":"10.3390\/min8050179"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1039\/c2fd20080e","article-title":"A Metastable Liquid Precursor Phase of Calcium Carbonate and Its Interactions with Polyaspartate","volume":"159","author":"Bewernitz","year":"2012","journal-title":"Faraday Discuss."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1021\/cr800443h","article-title":"Biomimetic Model Systems for Investigating the Amorphous Precursor Pathway and Its Role in Biomineralization","volume":"108","author":"Gower","year":"2008","journal-title":"Chem. Rev."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1021\/acs.langmuir.6b03974","article-title":"Gel-Like Calcium Carbonate Precursors Observed by in Situ AFM","volume":"33","author":"Wolf","year":"2017","journal-title":"Langmuir"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1126\/science.1169434","article-title":"The Initial Stages of Template-Controlled CaCO3 Formation Revealed by Cryo-TEM","volume":"323","author":"Pouget","year":"2009","journal-title":"Science"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1002\/adma.200300381","article-title":"Taking Advantage of Disorder: Amorphous Calcium Carbonate and Its Roles in Biomineralization","volume":"15","author":"Addadi","year":"2003","journal-title":"Adv. Mater."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1007\/s11706-009-0036-x","article-title":"Overview of the Amorphous Precursor Phase Strategy in Biomineralization","volume":"3","author":"Weiner","year":"2009","journal-title":"Front. Mater. Sci. China"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"16438","DOI":"10.1073\/pnas.1009959107","article-title":"Transformation and Crystallization Energetics of Synthetic and Biogenic Amorphous Calcium Carbonate","volume":"107","author":"Radha","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"12096","DOI":"10.1073\/pnas.0404778101","article-title":"Energetic Clues to Pathways to Biomineralization: Precursors, Clusters, and Nanoparticles","volume":"101","author":"Alexandra","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"44703","DOI":"10.1063\/1.3530288","article-title":"Sampling the Structure of Calcium Carbonate Nanoparticles with Metadynamics","volume":"134","author":"Quigley","year":"2011","journal-title":"J. Chem. Phys."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"11680","DOI":"10.1021\/jp902606x","article-title":"A Molecular Dynamics Study of the Early Stages of Calcium Carbonate Growth","volume":"113","author":"Tribello","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1002\/jcc.21939","article-title":"Application of Molecular Dynamics Simulations in Molecular Property Prediction II: Diffusion Coefficient","volume":"32","author":"Wang","year":"2011","journal-title":"J. Comput. Chem."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"2348","DOI":"10.1039\/C3CS60451A","article-title":"Pre-Nucleation Clusters as Solute Precursors in Crystallisation","volume":"43","author":"Gebauer","year":"2014","journal-title":"Chem. Soc. Rev."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1002\/adma.200306565","article-title":"Amorphous Calcium Carbonate: Synthesis and Potential Intermediate in Biomineralization","volume":"16","author":"Faatz","year":"2004","journal-title":"Adv. Mater."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"12342","DOI":"10.1021\/ja800984y","article-title":"Early Homogenous Amorphous Precursor Stages of Calcium Carbonate and Subsequent Crystal Growth in Levitated Droplets","volume":"130","author":"Wolf","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.gca.2012.10.044","article-title":"In Situ Observations of Liquid-Liquid Phase Separation in Aqueous MgSO4 Solutions: Geological and Geochemical Implications","volume":"103","author":"Wang","year":"2013","journal-title":"Geochim. Cosmochim. Acta"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.gca.2016.03.001","article-title":"In Situ Observations of Liquid\u2013Liquid Phase Separation in Aqueous ZnSO4 Solutions at Temperatures up to 400 \u00b0C: Implications for Zn2+\u2013SO42\u2212 Association and Evolution of Submarine Hydrothermal Fluids","volume":"181","author":"Wang","year":"2016","journal-title":"Geochim. Cosmochim. Acta"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1126\/science.1173793","article-title":"An Acidic Matrix Protein, Pif, Is a Key Macromolecule for Nacre Formation","volume":"325","author":"Suzuki","year":"2009","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"3182","DOI":"10.1093\/bioinformatics\/bts604","article-title":"Aragonite-Associated Biomineralization Proteins Are Disordered and Contain Interactive Motifs","volume":"28","author":"Evans","year":"2012","journal-title":"Bioinformatics"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"e1700765","DOI":"10.1126\/sciadv.1700765","article-title":"Control of Nacre Biomineralization by Pif80 in Pearl Oyster","volume":"3","author":"Bahn","year":"2017","journal-title":"Sci. Adv."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Farahi, N., Lazar, T., Wodak, S.J., Tompa, P., and Pancsa, R. (2021). Integration of Data from Liquid-Liquid Phase Separation Databases Highlights Concentration and Dosage Sensitivity of LLPS Drivers. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22063017"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.molcel.2015.08.018","article-title":"Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins","volume":"60","author":"Lin","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1038\/381056a0","article-title":"Control of crystal phase switching and orientation by soluble mollusc-shell proteins","volume":"381","author":"Belcher","year":"1996","journal-title":"Nature"},{"key":"ref_131","first-page":"273","article-title":"Unusually Acidic Proteins in Biomineralization","volume":"Volume 1","author":"Behrens","year":"2007","journal-title":"Handbook of Biomineralization"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"20200859","DOI":"10.1098\/rsif.2020.0859","article-title":"The Spatial Network of Skeletal Proteins in a Stony Coral","volume":"18","author":"Mummadisetti","year":"2021","journal-title":"J. R. Soc. Interface"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"4670","DOI":"10.1021\/cr0782729","article-title":"Phosphorylated Proteins and Control over Apatite Nucleation, Crystal Growth, and Inhibition","volume":"108","author":"George","year":"2008","journal-title":"Chem. Rev."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/S0968-0004(98)01246-8","article-title":"Evolving Views of Protein Glycosylation","volume":"23","author":"Drickamer","year":"1998","journal-title":"Trends Biochem. Sci."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.bpj.2016.11.3200","article-title":"CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins","volume":"112","author":"Holehouse","year":"2017","journal-title":"Biophys. J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"bbaa408","DOI":"10.1093\/bib\/bbaa408","article-title":"Computational Resources for Identifying and Describing Proteins Driving Liquid\u2013Liquid Phase Separation","volume":"22","author":"Pancsa","year":"2021","journal-title":"Brief. Bioinform."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"167201","DOI":"10.1016\/j.jmb.2021.167201","article-title":"Sequence Determinants of the Aggregation of Proteins Within Condensates Generated by Liquid-Liquid Phase Separation","volume":"434","author":"Vendruscolo","year":"2022","journal-title":"J. Mol. Biol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"33254","DOI":"10.1073\/pnas.2007670117","article-title":"Widespread Occurrence of the Droplet State of Proteins in the Human Proteome","volume":"117","author":"Hardenberg","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1093\/nar\/gkac386","article-title":"FuzDrop on AlphaFold: Visualizing the Sequence-Dependent Propensity of Liquid\u2013Liquid Phase Separation and Aggregation of Proteins","volume":"50","author":"Hatos","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"e31486","DOI":"10.7554\/eLife.31486","article-title":"Pi-Pi Contacts Are an Overlooked Protein Feature Relevant to Phase Separation","volume":"7","author":"Vernon","year":"2018","journal-title":"Elife"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1016\/j.bbapap.2009.07.010","article-title":"The Rod-Shaped Conformation of Starmaker","volume":"1794","author":"Michnik","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Horvath, A., Miskei, M., Ambrus, V., Vendruscolo, M., and Fuxreiter, M. (2020). Sequence-Based Prediction of Protein Binding Mode Landscapes. PLoS Comput. Biol., 16.","DOI":"10.1371\/journal.pcbi.1007864"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Chen, Y., Feng, Y., Deveaux, J.G., Masoud, M.A., Chandra, F.S., Chen, H., Zhang, D., and Feng, L. (2019). Biomineralization Forming Process and Bio-Inspired Nanomaterials for Biomedical Application: A Review. Minerals, 9.","DOI":"10.3390\/min9020068"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"3261","DOI":"10.1016\/j.gca.2003.12.018","article-title":"Strontium Incorporation into Calcite Generated by Bacterial Ureolysis","volume":"68","author":"Fujita","year":"2004","journal-title":"Geochim. Cosmochim. Acta"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"jeb206961","DOI":"10.1242\/jeb.206961","article-title":"Molecular Mechanisms of Biomineralization in Marine Invertebrates","volume":"223","author":"Clark","year":"2020","journal-title":"J. Exp. Biol."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/12\/9\/1266\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:28:02Z","timestamp":1760142482000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/12\/9\/1266"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9,9]]},"references-count":145,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["biom12091266"],"URL":"https:\/\/doi.org\/10.3390\/biom12091266","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,9,9]]}}}