{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T19:54:23Z","timestamp":1790970863157,"version":"4.1.0"},"reference-count":79,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2021,5,6]],"date-time":"2021-05-06T00:00:00Z","timestamp":1620259200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2021,5,6]],"date-time":"2021-05-06T00:00:00Z","timestamp":1620259200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["457851\/2014-7"],"award-info":[{"award-number":["457851\/2014-7"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"crossref","award":["051\/2013"],"award-info":[{"award-number":["051\/2013"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Mol Evol"],"published-print":{"date-parts":[[2021,7]]},"DOI":"10.1007\/s00239-021-10010-8","type":"journal-article","created":{"date-parts":[[2021,5,6]],"date-time":"2021-05-06T12:02:53Z","timestamp":1620302573000},"page":"370-383","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Reenacting the Birth of a Function: Functional Divergence of HIUases and Transthyretins as Inferred by Evolutionary and Biophysical Studies"],"prefix":"10.1007","volume":"89","author":[{"given":"Lucas","family":"Carrijo de Oliveira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariana Amalia","family":"Figueiredo Costa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natan","family":"Gon\u00e7alves Pedersolli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernanda Aparecida","family":"Heleno Batista","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Carolina","family":"Migliorini Figueira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rafaela","family":"Salgado Ferreira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronaldo","family":"Alves Pinto Nagem","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laila","family":"Alves Nahum","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7121-4952","authenticated-orcid":false,"given":"Lucas","family":"Bleicher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,5,6]]},"reference":[{"key":"10010_CR1","doi-asserted-by":"publisher","first-page":"2104","DOI":"10.1093\/bioinformatics\/bti263","volume":"21","author":"F Abascal","year":"2005","unstructured":"Abascal F, Zardoya R, Posada D (2005) ProtTest: selection of best-fit models of protein evolution. Bioinformatics 21:2104\u20132105. https:\/\/doi.org\/10.1093\/bioinformatics\/bti263","journal-title":"Bioinformatics"},{"key":"10010_CR2","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams PD, Afonine PV, Bunk\u00f3czi G et al (2010) PHENIX\u202f: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr Sect D Biol Crystallogr 66:213\u2013221. https:\/\/doi.org\/10.1107\/S0907444909052925","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10010_CR3","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1111\/j.1432-1033.1997.t01-1-00401.x","volume":"246","author":"AR Aldred","year":"1997","unstructured":"Aldred AR, Prapunpoj P, Schreiber G (1997) Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3\u2019 splice site of intron 1). Eur J Biochem 246:401\u2013409. https:\/\/doi.org\/10.1111\/j.1432-1033.1997.t01-1-00401.x","journal-title":"Eur J Biochem"},{"key":"10010_CR4","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","volume":"215","author":"SF Altschul","year":"1990","unstructured":"Altschul SF, Gish W, Miller W et al (1990) Basic local alignment search tool. J Mol Biol 215:403\u2013410. https:\/\/doi.org\/10.1016\/S0022-2836(05)80360-2","journal-title":"J Mol Biol"},{"key":"10010_CR5","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gks498","author":"H Ashkenazy","year":"2012","unstructured":"Ashkenazy H, Penn O, Doron-Faigenboim A et al (2012) FastML: a web server for probabilistic reconstruction of ancestral sequences. Nucleic Acids Res. https:\/\/doi.org\/10.1093\/nar\/gks498","journal-title":"Nucleic Acids Res"},{"key":"10010_CR6","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1038\/268115a0","volume":"268","author":"CCF Blake","year":"1977","unstructured":"Blake CCF, Oatley SJ (1977) Protein\u2013DNA and protein\u2013hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor? Nature 268:115\u2013120. https:\/\/doi.org\/10.1038\/268115a0","journal-title":"Nature"},{"key":"10010_CR7","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1016\/0022-2836(71)90218-X","volume":"61","author":"CCF Blake","year":"1971","unstructured":"Blake CCF, Swan IDA, Rerat C et al (1971) An X-ray study of the subunit structure of prealbumin. J Mol Biol 61:217\u2013224. https:\/\/doi.org\/10.1016\/0022-2836(71)90218-X","journal-title":"J Mol Biol"},{"key":"10010_CR8","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/0022-2836(74)90291-5","volume":"88","author":"CC Blake","year":"1974","unstructured":"Blake CC, Geisow MJ, Swan ID et al (1974) Structure of human plasma prealbumin at 2\u20135 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol 88:1\u201312. https:\/\/doi.org\/10.1016\/0022-2836(74)90291-5","journal-title":"J Mol Biol"},{"key":"10010_CR9","doi-asserted-by":"publisher","first-page":"1721","DOI":"10.1016\/j.neurobiolaging.2007.04.007","volume":"29","author":"J Brouillette","year":"2008","unstructured":"Brouillette J, Quirion R (2008) Transthyretin: a key gene involved in the maintenance of memory capacities during aging. Neurobiol Aging 29:1721\u20131732. https:\/\/doi.org\/10.1016\/j.neurobiolaging.2007.04.007","journal-title":"Neurobiol Aging"},{"key":"10010_CR10","doi-asserted-by":"publisher","first-page":"1972","DOI":"10.1093\/bioinformatics\/btp348","volume":"25","author":"S Capella-Guti\u00e9rrez","year":"2009","unstructured":"Capella-Guti\u00e9rrez S, Silla-Mart\u00ednez JM, Gabald\u00f3n T (2009) trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses. Bioinformatics 25:1972\u20131973. https:\/\/doi.org\/10.1093\/bioinformatics\/btp348","journal-title":"Bioinformatics"},{"key":"10010_CR11","doi-asserted-by":"publisher","first-page":"504","DOI":"10.1016\/j.jmb.2011.04.022","volume":"409","author":"L Cendron","year":"2011","unstructured":"Cendron L, Ramazzina I, Percudani R et al (2011) Probing the evolution of hydroxyisourate hydrolase into transthyretin through active-site redesign. J Mol Biol 409:504\u2013512. https:\/\/doi.org\/10.1016\/j.jmb.2011.04.022","journal-title":"J Mol Biol"},{"key":"10010_CR12","doi-asserted-by":"publisher","first-page":"534","DOI":"10.1046\/j.1432-1327.1999.00076.x","volume":"259","author":"L Chang","year":"1999","unstructured":"Chang L, Munro SLA, Richardson SJ, Schreiber G (1999) Evolution of thyroid hormone binding by transthyretins in birds and mammals. Eur J Biochem 259:534\u2013542. https:\/\/doi.org\/10.1046\/j.1432-1327.1999.00076.x","journal-title":"Eur J Biochem"},{"key":"10010_CR13","doi-asserted-by":"publisher","first-page":"1164","DOI":"10.1093\/bioinformatics\/btr088","volume":"27","author":"D Darriba","year":"2011","unstructured":"Darriba D, Taboada GL, Doallo R, Posada D (2011) ProtTest 3: fast selection of best-fit models of protein evolution. Bioinformatics 27:1164\u20131165. https:\/\/doi.org\/10.1093\/bioinformatics\/btr088","journal-title":"Bioinformatics"},{"key":"10010_CR14","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1107\/S0907444999016352","volume":"56","author":"Z Dauter","year":"2000","unstructured":"Dauter Z, Dauter M, Rajashankar KR (2000) Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr D Biol Crystallogr 56:232\u2013237","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10010_CR15","doi-asserted-by":"publisher","first-page":"31731","DOI":"10.1074\/jbc.M110.157206","volume":"285","author":"LC De Palmieri","year":"2010","unstructured":"De Palmieri LC, Lima LMTR, Freire JBB et al (2010a) Novel Zn2+-binding sites in human transthyretin: Implications for amyloidogenesis and retinol-binding protein recognition. J Biol Chem 285:31731\u201331741. https:\/\/doi.org\/10.1074\/jbc.M110.157206","journal-title":"J Biol Chem"},{"key":"10010_CR16","unstructured":"DeLano WL (2007) PyMOL: An Open-Source Molecular Graphics Tool"},{"key":"10010_CR17","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","volume":"60","author":"P Emsley","year":"2004","unstructured":"Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr Sect D Biol Crystallogr 60:2126\u20132132. https:\/\/doi.org\/10.1107\/S0907444904019158","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10010_CR18","doi-asserted-by":"publisher","first-page":"518","DOI":"10.1046\/j.1432-1033.2003.03408.x","volume":"270","author":"T Eneqvist","year":"2003","unstructured":"Eneqvist T, Lundberg E, Nilsson L et al (2003) The transthyretin-related protein family. Eur J Biochem 270:518\u2013532","journal-title":"Eur J Biochem"},{"key":"10010_CR19","doi-asserted-by":"publisher","first-page":"26411","DOI":"10.1074\/jbc.M313553200","volume":"279","author":"T Eneqvist","year":"2004","unstructured":"Eneqvist T, Lundberg E, Karlsson A et al (2004) High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine. J Biol Chem 279:26411\u201326416. https:\/\/doi.org\/10.1074\/jbc.M313553200","journal-title":"J Biol Chem"},{"key":"10010_CR20","doi-asserted-by":"publisher","first-page":"282","DOI":"10.1021\/bi00673a014","volume":"14","author":"RN Ferguson","year":"1975","unstructured":"Ferguson RN, Edelhoch H, Saroff HA et al (1975) Negative cooperativity in the binding of thyroxine to human serum prealbumin. Biochemistry 14:282\u2013289. https:\/\/doi.org\/10.1021\/bi00673a014","journal-title":"Biochemistry"},{"key":"10010_CR21","doi-asserted-by":"publisher","first-page":"1739","DOI":"10.1021\/jm0306430","volume":"47","author":"RA Friesner","year":"2004","unstructured":"Friesner RA, Banks JL, Murphy RB et al (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47:1739\u20131749. https:\/\/doi.org\/10.1021\/jm0306430","journal-title":"J Med Chem"},{"key":"10010_CR22","doi-asserted-by":"publisher","first-page":"3784","DOI":"10.1093\/nar\/gkg563","volume":"31","author":"E Gasteiger","year":"2003","unstructured":"Gasteiger E, Gattiker A, Hoogland C et al (2003) ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31:3784\u20133788. https:\/\/doi.org\/10.1093\/nar\/gkg563","journal-title":"Nucleic Acids Res"},{"key":"10010_CR23","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1107\/S0909049508034870","volume":"16","author":"BG Guimar\u00e3es","year":"2009","unstructured":"Guimar\u00e3es BG, Sanfelici L, Neuenschwander RT et al (2009) The MX2 macromolecular crystallography beamline: a wiggler X-ray source at the LNLS. J Synchrotron Radiat 16:69\u201375. https:\/\/doi.org\/10.1107\/S0909049508034870","journal-title":"J Synchrotron Radiat"},{"key":"10010_CR24","doi-asserted-by":"publisher","first-page":"415","DOI":"10.1210\/jcem-37-3-415","volume":"37","author":"GA Hagen","year":"1973","unstructured":"Hagen GA, Elliott WJ (1973) Transport of thyroid hormones in serum and cerebrospinal fluid. J Clin Endocrinol Metab 37:415\u2013422. https:\/\/doi.org\/10.1210\/jcem-37-3-415","journal-title":"J Clin Endocrinol Metab"},{"key":"10010_CR25","doi-asserted-by":"publisher","first-page":"5367","DOI":"10.1111\/j.1742-4658.2009.07246.x","volume":"276","author":"SC Hennebry","year":"2009","unstructured":"Hennebry SC (2009) Evolutionary changes to transthyretin: structure and function of a transthyretin-like ancestral protein. FEBS J 276:5367\u20135379. https:\/\/doi.org\/10.1111\/j.1742-4658.2009.07246.x","journal-title":"FEBS J"},{"key":"10010_CR26","doi-asserted-by":"publisher","first-page":"1389","DOI":"10.1016\/j.jmb.2006.04.057","volume":"359","author":"SC Hennebry","year":"2006","unstructured":"Hennebry SC, Law RHP, Richardson SJ et al (2006a) The crystal structure of the transthyretin-like protein from Salmonella dublin, a prokaryote 5-hydroxyisourate hydrolase. J Mol Biol 359:1389\u20131399. https:\/\/doi.org\/10.1016\/j.jmb.2006.04.057","journal-title":"J Mol Biol"},{"key":"10010_CR27","doi-asserted-by":"publisher","first-page":"1024","DOI":"10.1002\/prot.21033","volume":"64","author":"SC Hennebry","year":"2006","unstructured":"Hennebry SC, Wright HM, Likic VA, Richardson SJ (2006b) Structural and functional evolution of transthyretin and transthyretin-like proteins. Proteins Struct Funct Bioinforma 64:1024\u20131045. https:\/\/doi.org\/10.1002\/prot.21033","journal-title":"Proteins Struct Funct Bioinforma"},{"key":"10010_CR28","doi-asserted-by":"publisher","first-page":"2966","DOI":"10.1073\/pnas.1019605109","volume":"109","author":"R Huang","year":"2012","unstructured":"Huang R, Hippauf F, Rohrbeck D et al (2012) Enzyme functional evolution through improved catalysis of ancestrally nonpreferred substrates. Proc Natl Acad Sci USA 109:2966\u20132971. https:\/\/doi.org\/10.1073\/pnas.1019605109","journal-title":"Proc Natl Acad Sci USA"},{"key":"10010_CR29","doi-asserted-by":"publisher","first-page":"1690","DOI":"10.1016\/j.str.2013.06.020","volume":"21","author":"A Ingles-Prieto","year":"2013","unstructured":"Ingles-Prieto A, Ibarra-Molero B, Delgado-Delgado A et al (2013) Conservation of protein structure over four billion years. Structure 21:1690\u20131697. https:\/\/doi.org\/10.1016\/j.str.2013.06.020","journal-title":"Structure"},{"key":"10010_CR30","doi-asserted-by":"publisher","first-page":"9790","DOI":"10.1073\/pnas.0600523103","volume":"103","author":"D-K Jung","year":"2006","unstructured":"Jung D-K, Lee Y, Park SG et al (2006) Structural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family. Proc Natl Acad Sci USA 103:9790\u20139795. https:\/\/doi.org\/10.1073\/pnas.0600523103","journal-title":"Proc Natl Acad Sci USA"},{"key":"10010_CR31","doi-asserted-by":"publisher","first-page":"3586","DOI":"10.1093\/bioinformatics\/bty386","volume":"34","author":"A Jurcik","year":"2018","unstructured":"Jurcik A, Bednar D, Byska J et al (2018) CAVER Analyst 2.0: analysis and visualization of channels and tunnels in protein structures and molecular dynamics trajectories. Bioinformatics 34:3586\u20133588. https:\/\/doi.org\/10.1093\/bioinformatics\/bty386","journal-title":"Bioinformatics"},{"key":"10010_CR32","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1172\/jci101335","volume":"21","author":"EA Kabat","year":"1942","unstructured":"Kabat EA, Moore DH, Landow H (1942) An electrophoretic study of the protein components in cerebrospinal fluid and their relationship to the serum proteins 1. J Clin Investig 21:571\u2013577. https:\/\/doi.org\/10.1172\/jci101335","journal-title":"J Clin Investig"},{"key":"10010_CR33","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"W Kabsch","year":"2010","unstructured":"Kabsch W (2010) XDS. Acta Crystallogr Sect D Biol Crystallogr 66:125\u2013132. https:\/\/doi.org\/10.1107\/S0907444909047337","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10010_CR34","doi-asserted-by":"publisher","first-page":"2025","DOI":"10.1172\/JCI105889","volume":"47","author":"M Kanai","year":"1968","unstructured":"Kanai M, Raz A, Goodman DS (1968) Retinol-binding protein: the transport protein for vitamin A in human plasma. J Clin Investig 47:2025\u20132044. https:\/\/doi.org\/10.1172\/JCI105889","journal-title":"J Clin Investig"},{"key":"10010_CR35","doi-asserted-by":"publisher","first-page":"74","DOI":"10.1016\/j.mce.2018.02.012","volume":"474","author":"K Kasai","year":"2018","unstructured":"Kasai K, Nishiyama N, Yamauchi K (2018) Molecular and thyroid hormone binding properties of lamprey transthyretins: the role of an N-terminal histidine-rich segment in hormone binding with high affinity. Mol Cell Endocrinol 474:74\u201388. https:\/\/doi.org\/10.1016\/j.mce.2018.02.012","journal-title":"Mol Cell Endocrinol"},{"key":"10010_CR36","doi-asserted-by":"publisher","first-page":"1359","DOI":"10.1093\/molbev\/msq022","volume":"27","author":"AC Keebaugh","year":"2010","unstructured":"Keebaugh AC, Thomas JW (2010) The evolutionary fate of the genes encoding the purine catabolic enzymes in hominoids, birds, and reptiles. Mol Biol Evol 27:1359\u20131369. https:\/\/doi.org\/10.1093\/molbev\/msq022","journal-title":"Mol Biol Evol"},{"key":"10010_CR37","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1016\/j.beem.2007.04.001","volume":"21","author":"J K\u00f6hrle","year":"2007","unstructured":"K\u00f6hrle J (2007) Thyroid hormone transporters in health and disease: advances in thyroid hormone deiodination. Best Pract Res Clin Endocrinol Metab 21:173\u2013191. https:\/\/doi.org\/10.1016\/j.beem.2007.04.001","journal-title":"Best Pract Res Clin Endocrinol Metab"},{"key":"10010_CR38","doi-asserted-by":"publisher","first-page":"3763","DOI":"10.1073\/pnas.1320393111","volume":"111","author":"JT Kratzer","year":"2014","unstructured":"Kratzer JT, Lanaspa MA, Murphy MN et al (2014) Evolutionary history and metabolic insights of ancient mammalian uricases. Proc Natl Acad Sci USA 111:3763\u20133768. https:\/\/doi.org\/10.1073\/pnas.1320393111","journal-title":"Proc Natl Acad Sci USA"},{"key":"10010_CR39","doi-asserted-by":"publisher","first-page":"190","DOI":"10.2306\/scienceasia1513-1874.2016.42.190","volume":"42","author":"L Leelawatwattana","year":"2016","unstructured":"Leelawatwattana L, Praphanphoj V, Prapunpoj P (2016) Proteolytic activity of Crocodylus porosus transthyretin protease and role of the terminal polypeptide sequences. ScienceAsia 42:190\u2013200. https:\/\/doi.org\/10.2306\/scienceasia1513-1874.2016.42.190","journal-title":"ScienceAsia"},{"key":"10010_CR40","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1042\/BJ20111690","volume":"443","author":"MA Liz","year":"2012","unstructured":"Liz MA, Leite SC, Juliano L et al (2012) Transthyretin is a metallopeptidase with an inducible active site. Biochem J 443:769\u2013778. https:\/\/doi.org\/10.1042\/BJ20111690","journal-title":"Biochem J"},{"key":"10010_CR41","doi-asserted-by":"publisher","first-page":"2890","DOI":"10.1210\/endo-126-6-2890","volume":"126","author":"W Lueprasitsakul","year":"1990","unstructured":"Lueprasitsakul W, Alex S, Fang SL et al (1990) Flavonoid administration immediately displaces thyroxine (T4) from serum transthyretin, increases serum free t4and decreases serum thyrotropin in the rat. Endocrinology 126:2890\u20132895. https:\/\/doi.org\/10.1210\/endo-126-6-2890","journal-title":"Endocrinology"},{"key":"10010_CR42","doi-asserted-by":"publisher","first-page":"712","DOI":"10.1016\/j.bbrc.2009.07.094","volume":"387","author":"C Matiollo","year":"2009","unstructured":"Matiollo C, Vernal J, Ecco G et al (2009) A transthyretin-related protein is functionally expressed in Herbaspirillum seropedicae. Biochem Biophys Res Commun 387:712\u2013716. https:\/\/doi.org\/10.1016\/j.bbrc.2009.07.094","journal-title":"Biochem Biophys Res Commun"},{"key":"10010_CR43","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1007\/978-3-642-00646-3_8","volume-title":"Recent advances in transthyretin evolution, structure and biological functions","author":"HL Monaco","year":"2009","unstructured":"Monaco HL (2009) The transthyretin\u2014retinol-binding protein complex. Recent advances in transthyretin evolution, structure and biological functions. Springer, Berlin, pp 123\u2013142"},{"key":"10010_CR44","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1126\/science.7754382","volume":"268","author":"HL Monaco","year":"1995","unstructured":"Monaco HL, Rizzi M, Coda A (1995) Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein. Science 268:1039\u20131041. https:\/\/doi.org\/10.1126\/science.7754382","journal-title":"Science"},{"key":"10010_CR45","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.mce.2008.06.010","volume":"295","author":"I Morgado","year":"2008","unstructured":"Morgado I, Melo EP, Lundberg E et al (2008) Hormone affinity and fibril formation of piscine transthyretin: the role of the N-terminal. Mol Cell Endocrinol 295:48\u201358. https:\/\/doi.org\/10.1016\/j.mce.2008.06.010","journal-title":"Mol Cell Endocrinol"},{"key":"10010_CR46","doi-asserted-by":"publisher","first-page":"1720","DOI":"10.1002\/1873-3468.12637","volume":"591","author":"JM Morrow","year":"2017","unstructured":"Morrow JM, Castiglione GM, Dungan SZ et al (2017) An experimental comparison of human and bovine rhodopsin provides insight into the molecular basis of retinal disease. FEBS Lett 591:1720\u20131731","journal-title":"FEBS Lett"},{"key":"10010_CR47","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1016\/S0076-6879(03)74005-1","volume":"374","author":"RAP Nagem","year":"2003","unstructured":"Nagem RAP, Polikarpov I, Dauter Z (2003) Phasing on rapidly soaked ions. Methods Enzymol 374:120\u2013137. https:\/\/doi.org\/10.1016\/S0076-6879(03)74005-1","journal-title":"Methods Enzymol"},{"key":"10010_CR48","doi-asserted-by":"publisher","first-page":"867","DOI":"10.18388\/abp.2001_3852","volume":"48","author":"P Neumann","year":"2001","unstructured":"Neumann P, Cody V, Wojtczak A (2001) Structural basis of negative cooperativity in transthyretin. Acta Biochim Pol 48:867\u2013875","journal-title":"Acta Biochim Pol"},{"key":"10010_CR49","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1096\/fj.05-4106fje","volume":"20","author":"AF Nunes","year":"2006","unstructured":"Nunes AF, Saraiva MJ, Sousa MM (2006) Transthyretin knockouts are a new mouse model for increased neuropeptide Y. FASEB J 20:166\u2013168. https:\/\/doi.org\/10.1096\/fj.05-4106fje","journal-title":"FASEB J"},{"key":"10010_CR50","doi-asserted-by":"publisher","first-page":"9","DOI":"10.3891\/acta.chem.scand.17s-0009","volume":"17 supl.","author":"L Pauling","year":"1963","unstructured":"Pauling L, Zuckerkandl E, Henriksen T, L\u00f6vstad R (1963) Chemical paleogenetics. Molecular \u201cRestoration Studies\u201d of extinct forms of life. Acta Chem Scand 17 supl.:9\u201316. https:\/\/doi.org\/10.3891\/acta.chem.scand.17s-0009","journal-title":"Acta Chem Scand"},{"key":"10010_CR51","doi-asserted-by":"publisher","first-page":"592","DOI":"10.1038\/nsmb.2020","volume":"18","author":"R Perez-Jimenez","year":"2011","unstructured":"Perez-Jimenez R, Ingl\u00e9s-Prieto A, Zhao Z-M et al (2011) Single-molecule paleoenzymology probes the chemistry of resurrected enzymes. Nat Struct Mol Biol 18:592\u2013596. https:\/\/doi.org\/10.1038\/nsmb.2020","journal-title":"Nat Struct Mol Biol"},{"key":"10010_CR52","doi-asserted-by":"publisher","first-page":"5149","DOI":"10.1039\/c1ob05433c","volume":"9","author":"S Pipolo","year":"2011","unstructured":"Pipolo S, Percudani R, Cammi R (2011) Absolute stereochemistry and preferred conformations of urate degradation intermediates from computed and experimental circular dichroism spectra. Org Biomol Chem 9:5149\u20135155. https:\/\/doi.org\/10.1039\/c1ob05433c","journal-title":"Org Biomol Chem"},{"key":"10010_CR53","doi-asserted-by":"publisher","first-page":"5330","DOI":"10.1111\/j.1742-4658.2009.07243.x","volume":"276","author":"P Prapunpoj","year":"2009","unstructured":"Prapunpoj P, Leelawatwattana L (2009) Evolutionary changes to transthyretin: structure-function relationships. FEBS J 276:5330\u20135341. https:\/\/doi.org\/10.1111\/j.1742-4658.2009.07243.x","journal-title":"FEBS J"},{"key":"10010_CR54","doi-asserted-by":"publisher","first-page":"R2026","DOI":"10.1152\/ajpregu.2000.279.6.R2026","volume":"279","author":"P Prapunpoj","year":"2000","unstructured":"Prapunpoj P, Yamauchi K, Nishiyama N et al (2000) Evolution of structure, ontogeny of gene expression, and function of Xenopus laevis transthyretin. Am J Physiol Regul Integr Comp Physiol 279:R2026\u2013R2041. https:\/\/doi.org\/10.1152\/ajpregu.2000.279.6.R2026","journal-title":"Am J Physiol Regul Integr Comp Physiol"},{"key":"10010_CR55","doi-asserted-by":"publisher","first-page":"4013","DOI":"10.1111\/j.1742-4658.2006.05404.x","volume":"273","author":"P Prapunpoj","year":"2006","unstructured":"Prapunpoj P, Leelawatwatana L, Schreiber G, Richardson SJ (2006) Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3. FEBS J 273:4013\u20134023. https:\/\/doi.org\/10.1111\/j.1742-4658.2006.05404.x","journal-title":"FEBS J"},{"key":"10010_CR56","doi-asserted-by":"publisher","first-page":"144","DOI":"10.1038\/nchembio768","volume":"2","author":"I Ramazzina","year":"2006","unstructured":"Ramazzina I, Folli C, Secchi A et al (2006) Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat Chem Biol 2:144\u2013148. https:\/\/doi.org\/10.1038\/nchembio768","journal-title":"Nat Chem Biol"},{"key":"10010_CR57","doi-asserted-by":"publisher","first-page":"12847","DOI":"10.1038\/ncomms12847","volume":"7","author":"RN Randall","year":"2016","unstructured":"Randall RN, Radford CE, Roof KA et al (2016) An experimental phylogeny to benchmark ancestral sequence reconstruction. Nat Commun 7:12847. https:\/\/doi.org\/10.1038\/ncomms12847","journal-title":"Nat Commun"},{"key":"10010_CR58","doi-asserted-by":"publisher","first-page":"3335","DOI":"10.1210\/jcem.81.9.8784093","volume":"81","author":"S Refetoff","year":"1996","unstructured":"Refetoff S, Marinov VS, Tunca H et al (1996) A new family with hyperthyroxinemia caused by transthyretin Val109 misdiagnosed as thyrotoxicosis and resistance to thyroid hormone\u2013a clinical research center study. J Clin Endocrinol Metab 81:3335\u20133340. https:\/\/doi.org\/10.1210\/jcem.81.9.8784093","journal-title":"J Clin Endocrinol Metab"},{"key":"10010_CR59","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1111\/j.1600-0404.1988.tb03687.x","volume":"78","author":"H Riis\u00f8en","year":"1988","unstructured":"Riis\u00f8en H (1988) Reduced prealbumin (transthyretin) in CSF of severely demented patients with Alzheimer\u2019s disease. Acta Neurol Scand 78:455\u2013459. https:\/\/doi.org\/10.1111\/j.1600-0404.1988.tb03687.x","journal-title":"Acta Neurol Scand"},{"key":"10010_CR60","doi-asserted-by":"publisher","first-page":"2899","DOI":"10.1021\/ja311630a","volume":"135","author":"VA Risso","year":"2013","unstructured":"Risso VA, Gavira JA, Mejia-Carmona DF et al (2013) Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian \u03b2-lactamases. J Am Chem Soc 135:2899\u20132902. https:\/\/doi.org\/10.1021\/ja311630a","journal-title":"J Am Chem Soc"},{"key":"10010_CR61","doi-asserted-by":"publisher","first-page":"866","DOI":"10.1038\/nrm2805","volume":"10","author":"PA Romero","year":"2009","unstructured":"Romero PA, Arnold FH (2009) Exploring protein fitness landscapes by directed evolution. Nat Rev Mol Cell Biol 10:866\u2013876. https:\/\/doi.org\/10.1038\/nrm2805","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10010_CR62","doi-asserted-by":"publisher","first-page":"1572","DOI":"10.1093\/bioinformatics\/btg180","volume":"19","author":"F Ronquist","year":"2003","unstructured":"Ronquist F, Huelsenbeck JP (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572\u20131574. https:\/\/doi.org\/10.1093\/bioinformatics\/btg180","journal-title":"Bioinformatics"},{"key":"10010_CR63","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1002\/humu.1132","volume":"17","author":"MJM Saraiva","year":"2001","unstructured":"Saraiva MJM (2001) Transthyretin mutations in hyperthyroxinemia and amyloid diseases. Hum Mutat 17:493\u2013503. https:\/\/doi.org\/10.1002\/humu.1132","journal-title":"Hum Mutat"},{"key":"10010_CR64","unstructured":"Schr\u00f6dinger L (2010) The PyMOL Molecular Graphics System, Version~1.3r1"},{"key":"10010_CR65","doi-asserted-by":"publisher","first-page":"3293","DOI":"10.1128\/JB.183.11.3293-3302.2001","volume":"183","author":"AC Schultz","year":"2001","unstructured":"Schultz AC, Nygaard P, Saxild HH (2001) Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J Bacteriol 183:3293\u20133302. https:\/\/doi.org\/10.1128\/JB.183.11.3293-3302.2001","journal-title":"J Bacteriol"},{"key":"10010_CR66","doi-asserted-by":"publisher","first-page":"8368","DOI":"10.1073\/pnas.91.18.8368","volume":"91","author":"AL Schwarzman","year":"1994","unstructured":"Schwarzman AL, Gregori L, Vitek MP et al (1994) Transthyretin sequesters amyloid beta protein and prevents amyloid formation. Proc Natl Acad Sci 91:8368\u20138372. https:\/\/doi.org\/10.1073\/pnas.91.18.8368","journal-title":"Proc Natl Acad Sci"},{"key":"10010_CR67","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1016\/S0021-9258(18)72655-0","volume":"143","author":"FB Seibert","year":"1942","unstructured":"Seibert FB, Nelson JW (1942) Electrophoretic study of the blood protein response in tuberculosis. J Biol Chem 143:29\u201338","journal-title":"J Biol Chem"},{"key":"10010_CR68","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/0304-4165(94)90099-X","volume":"1199","author":"TJ Smith","year":"1994","unstructured":"Smith TJ, Davis FB, Deziel MR et al (1994) Retinoic acid inhibition of thyroxine binding to human transthyretin. Biochim Biophys Acta Gen Subj 1199:76\u201380. https:\/\/doi.org\/10.1016\/0304-4165(94)90099-X","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10010_CR69","doi-asserted-by":"publisher","first-page":"1052","DOI":"10.1046\/j.1471-4159.2003.02309.x","volume":"88","author":"JC Sousa","year":"2004","unstructured":"Sousa JC, Grandela C, Fern\u00e1ndez-Ruiz J et al (2004) Transthyretin is involved in depression-like behaviour and exploratory activity. J Neurochem 88:1052\u20131058. https:\/\/doi.org\/10.1046\/j.1471-4159.2003.02309.x","journal-title":"J Neurochem"},{"key":"10010_CR70","doi-asserted-by":"publisher","first-page":"16625","DOI":"10.1073\/pnas.1010390107","volume":"107","author":"WS Stevenson","year":"2010","unstructured":"Stevenson WS, Hyland CD, Zhang J-G et al (2010) Deficiency of 5-hydroxyisourate hydrolase causes hepatomegaly and hepatocellular carcinoma in mice. Proc Natl Acad Sci USA 107:16625\u201316630. https:\/\/doi.org\/10.1073\/pnas.1010390107","journal-title":"Proc Natl Acad Sci USA"},{"key":"10010_CR71","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1038\/nrg1324","volume":"5","author":"JW Thornton","year":"2004","unstructured":"Thornton JW (2004) Resurrecting ancient genes: experimental analysis of extinct molecules. Nat Rev Genet 5:366\u2013375","journal-title":"Nat Rev Genet"},{"key":"10010_CR72","doi-asserted-by":"publisher","first-page":"108610","DOI":"10.1016\/j.cbpc.2019.108610","volume":"226","author":"AJ Tola","year":"2019","unstructured":"Tola AJ, Leelawatwattana L, Prapunpoj P (2019) The catalytic kinetics of chicken transthyretin towards human A\u03b21\u201342. Comp Biochem Physiol Part C Toxicol Pharmacol 226:108610. https:\/\/doi.org\/10.1016\/j.cbpc.2019.108610","journal-title":"Comp Biochem Physiol Part C Toxicol Pharmacol"},{"key":"10010_CR73","doi-asserted-by":"publisher","first-page":"2699","DOI":"10.1093\/nar\/gky092","volume":"46","author":"UniProt Consortium T","year":"2018","unstructured":"UniProt Consortium T (2018) UniProt: the universal protein knowledgebase. Nucleic Acids Res 46:2699\u20132699. https:\/\/doi.org\/10.1093\/nar\/gky092","journal-title":"Nucleic Acids Res"},{"key":"10010_CR74","doi-asserted-by":"publisher","first-page":"1692","DOI":"10.1093\/nar\/gkl091","volume":"34","author":"IM Wallace","year":"2006","unstructured":"Wallace IM, O\u2019Sullivan O, Higgins DG, Notredame C (2006) M-Coffee: combining multiple sequence alignment methods with T-Coffee. Nucleic Acids Res 34:1692\u20131699. https:\/\/doi.org\/10.1093\/nar\/gkl091","journal-title":"Nucleic Acids Res"},{"key":"10010_CR75","doi-asserted-by":"publisher","first-page":"882","DOI":"10.1126\/science.aaa1823","volume":"347","author":"C Wilson","year":"2015","unstructured":"Wilson C, Agafonov RV, Hoemberger M et al (2015) Kinase dynamics. Using ancient protein kinases to unravel a modern cancer drug\u2019s mechanism. Science 347:882\u2013886. https:\/\/doi.org\/10.1126\/science.aaa1823","journal-title":"Science"},{"key":"10010_CR76","doi-asserted-by":"publisher","first-page":"457","DOI":"10.1007\/s00239-018-9858-4","volume":"86","author":"K Yamauchi","year":"2018","unstructured":"Yamauchi K, Kasai K (2018) Sequential molecular events of functional trade-offs in 5-hydroxyisourate hydrolase before and after gene duplication led to the evolution of transthyretin during chordate diversification. J Mol Evol 86:457\u2013469. https:\/\/doi.org\/10.1007\/s00239-018-9858-4","journal-title":"J Mol Evol"},{"key":"10010_CR77","doi-asserted-by":"publisher","first-page":"2254","DOI":"10.1210\/endo.132.5.8477670","volume":"132","author":"K Yamauchi","year":"1993","unstructured":"Yamauchi K, Kasahara T, Hayashi H, Horiuchi R (1993) Purification and characterization of a 3, 5, 3\u2032-l- triiodothyronine-specific binding protein from bullfrog tadpole plasma: a homolog of mammalian transthyretin. Endocrinology 132:2254\u20132261. https:\/\/doi.org\/10.1210\/endo.132.5.8477670","journal-title":"Endocrinology"},{"key":"10010_CR78","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jmb.2006.07.079","volume":"363","author":"G Zanotti","year":"2006","unstructured":"Zanotti G, Cendron L, Ramazzina I et al (2006) Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. J Mol Biol 363:1\u20139. https:\/\/doi.org\/10.1016\/j.jmb.2006.07.079","journal-title":"J Mol Biol"},{"key":"10010_CR79","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1007\/978-3-642-00646-3_6","volume-title":"Recent advances in transthyretin evolution, structure and biological functions","author":"G Zanotti","year":"2009","unstructured":"Zanotti G, Ramazzina I, Cendron L et al (2009) Vertebrate 5-hydroxyisourate hydrolase identification, function, structure, and evolutionary relationship with transthyretin. Recent advances in transthyretin evolution, structure and biological functions. Springer, Berlin, pp 95\u2013108"}],"container-title":["Journal of Molecular Evolution"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00239-021-10010-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00239-021-10010-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00239-021-10010-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,6,16]],"date-time":"2021-06-16T11:05:44Z","timestamp":1623841544000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00239-021-10010-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,5,6]]},"references-count":79,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2021,7]]}},"alternative-id":["10010"],"URL":"https:\/\/doi.org\/10.1007\/s00239-021-10010-8","relation":{},"ISSN":["0022-2844","1432-1432"],"issn-type":[{"value":"0022-2844","type":"print"},{"value":"1432-1432","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,5,6]]},"assertion":[{"value":"10 November 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 April 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 May 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}