{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,23]],"date-time":"2026-01-23T14:40:16Z","timestamp":1769179216190,"version":"3.49.0"},"reference-count":46,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2008,3,1]],"date-time":"2008-03-01T00:00:00Z","timestamp":1204329600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2008,3]]},"DOI":"10.1016\/j.bbapap.2007.11.014","type":"journal-article","created":{"date-parts":[[2007,12,4]],"date-time":"2007-12-04T14:20:26Z","timestamp":1196778026000},"page":"512-517","source":"Crossref","is-referenced-by-count":21,"title":["Iodination of salicylic acid improves its binding to transthyretin"],"prefix":"10.1016","volume":"1784","author":[{"given":"Lu\u00eds","family":"Gales","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Ros\u00e1rio","family":"Almeida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gemma","family":"Arsequell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gregorio","family":"Valencia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Jo\u00e3o","family":"Saraiva","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana Margarida","family":"Damas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2007.11.014_bib1","first-page":"1039\u20131041","article-title":"Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein","author":"Monaco","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.bbapap.2007.11.014_bib2","doi-asserted-by":"crossref","first-page":"8554\u20138563","DOI":"10.1016\/S0021-9258(19)40795-3","article-title":"Studies on thyroid hormone-binding proteins. II. Binding of thyroid hormones, retinol-binding protein, and fluorescent probes to prealbumin and effects of thyroxine on prealbumin subunit self association","volume":"250","author":"Nilsson","year":"1975","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib3","doi-asserted-by":"crossref","first-page":"758\u2013765","DOI":"10.1107\/S0907444996003046","article-title":"Structures of human transthyretin complexed with thyroxine at 2.0\u00a0A resolution and 3\u2032,5\u2032-dinitro-N-acetyl-l-thyronine at 2.2\u00a0A resolution","volume":"52","author":"Wojtczak","year":"1996","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib4","doi-asserted-by":"crossref","first-page":"339\u2013356","DOI":"10.1016\/0022-2836(78)90368-6","article-title":"Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8\u00a0A","volume":"121","author":"Blake","year":"1978","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib5","doi-asserted-by":"crossref","first-page":"107\u2013110","DOI":"10.1111\/j.1399-0012.1994.tb00955.x","article-title":"Orthotopic liver transplantation for familial amyloidotic polyneuropathy","volume":"8","author":"Lewis","year":"1994","journal-title":"Clin. Transplant."},{"key":"10.1016\/j.bbapap.2007.11.014_bib6","first-page":"587\u2013596","article-title":"Small transthyretin (TTR) ligands as possible therapeutic agents in TTR amyloidoses","volume":"4","author":"Almeida","year":"2005","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bbapap.2007.11.014_bib7","doi-asserted-by":"crossref","first-page":"1389\u20131401","DOI":"10.1016\/S0968-0896(98)00130-8","article-title":"Discovering transthyretin amyloid fibril inhibitors by limited screening","volume":"6","author":"Baures","year":"1998","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib8","doi-asserted-by":"crossref","first-page":"14545","DOI":"10.1073\/pnas.0501609102","article-title":"Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis","volume":"102","author":"Green","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.11.014_bib9","doi-asserted-by":"crossref","first-page":"1861\u20131869","DOI":"10.1016\/j.bcp.2005.09.012","article-title":"The binding of xanthone derivatives to transthyretin","volume":"70","author":"Maia","year":"2005","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib10","doi-asserted-by":"crossref","first-page":"355\u2013374","DOI":"10.1021\/jm030347n","article-title":"Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis","volume":"47","author":"Adamski-Werner","year":"2004","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib11","doi-asserted-by":"crossref","first-page":"351\u2013356","DOI":"10.1042\/BJ20040011","article-title":"Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative","volume":"381","author":"Almeida","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2007.11.014_bib12","doi-asserted-by":"crossref","first-page":"615\u2013621","DOI":"10.1042\/BJ20042035","article-title":"Human transthyretin in complex with iododiflunisal: structural features associated with a potent amyloid inhibitor","volume":"388","author":"Gales","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2007.11.014_bib13","first-page":"312\u2013321","article-title":"Rational design of potent human transthyretin amyloid disease inhibitors","volume":"7","author":"Klabunde","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib14","doi-asserted-by":"crossref","first-page":"53483","DOI":"10.1074\/jbc.M408053200","article-title":"The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors","volume":"279","author":"Morais-de-Sa","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib15","doi-asserted-by":"crossref","first-page":"183\u2013188","DOI":"10.1007\/s100480050081","article-title":"Potential treatment of transthyretin-type amyloidoses by sulfite","volume":"2","author":"Altland","year":"1999","journal-title":"Neurogenetics"},{"key":"10.1016\/j.bbapap.2007.11.014_bib16","doi-asserted-by":"crossref","first-page":"61\u201367","DOI":"10.1007\/s10048-003-0160-1","article-title":"Sulfite and base for the treatment of familial amyloidotic polyneuropathy: two additive approaches to stabilize the conformation of human amyloidogenic transthyretin","volume":"5","author":"Altland","year":"2004","journal-title":"Neurogenetics"},{"key":"10.1016\/j.bbapap.2007.11.014_bib17","first-page":"59\u201364","article-title":"Structural basis for the protective role of sulfite against transthyretin amyloid formation","volume":"1774","author":"Gales","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2007.11.014_bib18","doi-asserted-by":"crossref","first-page":"2754\u20132759","DOI":"10.1073\/pnas.052706099","article-title":"Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation","volume":"99","author":"Richardson","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.11.014_bib19","doi-asserted-by":"crossref","first-page":"11654","DOI":"10.1074\/jbc.M210798200","article-title":"X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization","volume":"278","author":"Gales","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib20","doi-asserted-by":"crossref","first-page":"24715","DOI":"10.1074\/jbc.273.38.24715","article-title":"The crystal structure of amyloidogenic Leu55 \u2192 Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils","volume":"273","author":"Sebastiao","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.11.014_bib21","doi-asserted-by":"crossref","first-page":"734\u2013739","DOI":"10.1038\/nsb838","article-title":"Arrangement of subunits and ordering of beta-strands in an amyloid sheet","volume":"9","author":"Serag","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib22","doi-asserted-by":"crossref","first-page":"2959\u20132963","DOI":"10.1073\/pnas.92.7.2959","article-title":"Interaction of the anthracycline 4\u2032-iodo-4\u2032-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis","volume":"92","author":"Merlini","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.11.014_bib23","doi-asserted-by":"crossref","first-page":"1919\u20131925","DOI":"10.1016\/S0002-9440(10)65065-1","article-title":"4\u2032-Iodo-4\u2032-deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid","volume":"156","author":"Palha","year":"2000","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib24","doi-asserted-by":"crossref","first-page":"273\u2013279","DOI":"10.1042\/0264-6021:3510273","article-title":"The molecular interaction of 4\u2032-iodo-4\u2032-deoxydoxorubicin with Leu-55Pro transthyretin \u2018amyloid-like\u2019 oligomer leading to disaggregation","volume":"351","author":"Sebastiao","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2007.11.014_bib25","doi-asserted-by":"crossref","first-page":"803\u2013809","DOI":"10.1096\/fj.02-0764com","article-title":"4\u2032-iodo-4\u2032-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters","volume":"17","author":"Cardoso","year":"2003","journal-title":"Faseb J."},{"key":"10.1016\/j.bbapap.2007.11.014_bib26","doi-asserted-by":"crossref","first-page":"404\u2013407","DOI":"10.1016\/S0014-5793(00)02380-2","article-title":"Anti-amyloidogenic activity of tetracyclines: studies in vitro","volume":"487","author":"Forloni","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2007.11.014_bib27","doi-asserted-by":"crossref","first-page":"1309\u20131322","DOI":"10.1006\/jmbi.2000.3840","article-title":"Tetracycline affects abnormal properties of synthetic PrP peptides and PrP(Sc) in vitro","volume":"300","author":"Tagliavini","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib28","doi-asserted-by":"crossref","first-page":"1297\u20131299","DOI":"10.1096\/fj.00-0676fje","article-title":"Inhibition of Alzheimer's disease beta-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapy","volume":"15","author":"De Felice","year":"2001","journal-title":"Faseb J."},{"key":"10.1016\/j.bbapap.2007.11.014_bib29","doi-asserted-by":"crossref","first-page":"758\u2013765","DOI":"10.1107\/S0907444996003046","article-title":"Structures of human transthyretin complexed with thyroxine at 2.0\u00a0A resolution and 3\u2032,5\u2032-dinitro-N-acetyl-l-thyronine at 2.2\u00a0A resolution","volume":"52","author":"Wojtczak","year":"1996","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib30","doi-asserted-by":"crossref","first-page":"1141\u20131147","DOI":"10.1210\/jcem-68-6-1141","article-title":"Drug competition for thyroxine binding to transthyretin (prealbumin): comparison with effects on thyroxine-binding globulin","volume":"68","author":"Munro","year":"1989","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.bbapap.2007.11.014_bib31","doi-asserted-by":"crossref","first-page":"359\u2013364","DOI":"10.1089\/thy.1999.9.359","article-title":"Salsalate and salicylate binding to and their displacement of thyroxine from thyroxine-binding globulin, transthyrin, and albumin","volume":"9","author":"Wang","year":"1999","journal-title":"Thyroid"},{"key":"10.1016\/j.bbapap.2007.11.014_bib32","doi-asserted-by":"crossref","first-page":"53\u201358","DOI":"10.1093\/jn\/53.1.53","article-title":"Nutritional availability of iodine from several insoluble iodine compounds","volume":"53","author":"Mittler","year":"1954","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib33","first-page":"189\u2013200","article-title":"Transthyretin (prealbumin) in familial amyloidotic polyneuropathy: genetic and functional aspects","volume":"48","author":"Saraiva","year":"1988","journal-title":"Advances in Neurology"},{"key":"10.1016\/j.bbapap.2007.11.014_bib34","doi-asserted-by":"crossref","first-page":"309\u2013315","DOI":"10.1007\/BF02820508","article-title":"Thyroxine binding to transthyretin Met 119. Comparative studies of different heterozygotic carriers and structural analysis","volume":"6","author":"Almeida","year":"1997","journal-title":"Endocrine"},{"key":"10.1016\/j.bbapap.2007.11.014_bib35","doi-asserted-by":"crossref","first-page":"2415\u20132421","DOI":"10.1021\/bi00223a017","article-title":"Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP)","volume":"30","author":"Furuya","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.11.014_bib36","series-title":"Crystallographic Computing vol. 5: from Chemistry to Biology","article-title":"Molecular data processing","author":"Leslie","year":"1992"},{"key":"10.1016\/j.bbapap.2007.11.014_bib37","first-page":"760\u2013763","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib38","doi-asserted-by":"crossref","first-page":"458\u2013464","DOI":"10.1107\/S0907444905001617","article-title":"Likelihood-enhanced fast translation functions","volume":"61","author":"McCoy","year":"2005","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib39","doi-asserted-by":"crossref","first-page":"733\u2013744","DOI":"10.1006\/jmbi.2000.4415","article-title":"Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution","volume":"306","author":"Sebastiao","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib40","doi-asserted-by":"crossref","first-page":"606\u2013611","DOI":"10.1016\/S0959-440X(98)80152-8","article-title":"Recent developments for the efficient crystallographic refinement of macromolecular structures","volume":"8","author":"Brunger","year":"1998","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib41","series-title":"TurboFRODO, Silicon Graphics Geometry, Partner Directory","author":"Roussel","year":"1991"},{"key":"10.1016\/j.bbapap.2007.11.014_bib42","doi-asserted-by":"crossref","first-page":"1355\u20131363","DOI":"10.1107\/S0907444904011679","article-title":"PRODRG: a tool for high-throughput crystallography of protein\u2013ligand complexes","volume":"60","author":"Schuttelkopf","year":"2004","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib43","doi-asserted-by":"crossref","first-page":"240\u2013255","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib44","doi-asserted-by":"crossref","first-page":"649\u2013669","DOI":"10.1006\/jmbi.2000.4078","article-title":"A comparative analysis of 23 structures of the amyloidogenic protein transthyretin","volume":"302","author":"Hornberg","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2007.11.014_bib45","doi-asserted-by":"crossref","first-page":"1085\u20131095","DOI":"10.1107\/S0907444900008568","article-title":"Structure of human transthyretin complexed with bromophenols: a new mode of binding","volume":"56","author":"Ghosh","year":"2000","journal-title":"Acta Crystallogr., D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2007.11.014_bib46","doi-asserted-by":"crossref","first-page":"9290\u20139299","DOI":"10.1021\/bi050249z","article-title":"The effect of iodide and chloride on transthyretin structure and stability","volume":"44","author":"Hornberg","year":"2005","journal-title":"Biochemistry"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963907002877?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963907002877?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,1,23]],"date-time":"2025-01-23T06:14:03Z","timestamp":1737612843000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963907002877"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2008,3]]},"references-count":46,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2008,3]]}},"alternative-id":["S1570963907002877"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2007.11.014","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2008,3]]}}}