{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T17:35:58Z","timestamp":1791567358454,"version":"4.3.4"},"reference-count":86,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2004,12,1]],"date-time":"2004-12-01T00:00:00Z","timestamp":1101859200000},"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":[[2004,12]]},"DOI":"10.1016\/j.bbapap.2004.09.023","type":"journal-article","created":{"date-parts":[[2004,10,13]],"date-time":"2004-10-13T13:53:41Z","timestamp":1097675621000},"page":"1-9","source":"Crossref","is-referenced-by-count":90,"title":["Interactions amongst plasma retinol-binding protein, transthyretin and their ligands: implications in vitamin A homeostasis and transthyretin amyloidosis"],"prefix":"10.1016","volume":"1703","author":[{"given":"Pullakhandam","family":"Raghu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhattiprolu","family":"Sivakumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2004.09.023_bib1","series-title":"In Vitamin A in Health and Disease","first-page":"P1","author":"Blomhoff","year":"1994"},{"key":"10.1016\/j.bbapap.2004.09.023_bib2","first-page":"42","volume":"vol. 2","author":"Goodman","year":"1984"},{"key":"10.1016\/j.bbapap.2004.09.023_bib3","series-title":"The Retinoids, Biology, Chemistry and Medicine","author":"Sporano","year":"1994"},{"key":"10.1016\/j.bbapap.2004.09.023_bib4","series-title":"In Vitamin A in Health and Disease","first-page":"87","author":"Sivaprasadarao","year":"1994"},{"key":"10.1016\/j.bbapap.2004.09.023_bib5","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/0014-4827(92)90197-G","article-title":"Regulation of plasma retinol-binding protein secretion in human HepG2 cells","volume":"200","author":"Tosetti","year":"1992","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib6","doi-asserted-by":"crossref","first-page":"11118","DOI":"10.1021\/bi00160a023","article-title":"Interactions of retinol with binding proteins: studies with retinol-binding protein and with transthyretin","volume":"31","author":"Noy","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib7","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1074\/jbc.M008091200","article-title":"Biochemical basis for depressed serum retinol levels in transthyretin-deficient mice","volume":"276","author":"Van Bennekum","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib8","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1074\/jbc.270.2.866","article-title":"Studies on the metabolism of retinol and retinol-binding protein in transthyretin-deficient mice produced by homologous recombination","volume":"270","author":"Wei","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib9","first-page":"E485","article-title":"Transthyretin is not essential for thyroxine to reach the brain and other tissues in transthyretin-null mice","volume":"272","author":"Palha","year":"1997","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib10","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1515\/CCLM.2002.223","article-title":"Transthyretin as a thyroid hormone carrier: function revisited","volume":"40","author":"Palha","year":"2002","journal-title":"Clin. Chem. Lab. Med."},{"key":"10.1016\/j.bbapap.2004.09.023_bib11","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0959-440X(98)80016-X","article-title":"The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways","volume":"8","author":"Kelly","year":"1998","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib12","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1002\/humu.1132","article-title":"Transthyretin mutations in hyperthyroxinemia and amyloid diseases","volume":"17","author":"Saraiva","year":"2001","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbapap.2004.09.023_bib13","doi-asserted-by":"crossref","first-page":"1491","DOI":"10.1007\/PL00000791","article-title":"Transthyretin: a review from a structural perspective","volume":"58","author":"Hamilton","year":"2001","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbapap.2004.09.023_bib14","doi-asserted-by":"crossref","first-page":"26196","DOI":"10.1016\/S0021-9258(18)47178-5","article-title":"Fractional synthesis rates of retinol-binding protein, transthyretin, and a new peptide measured by stable isotope techniques in neonatal pigs","volume":"269","author":"Sivakumar","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib15","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1093\/jn\/126.5.1489","article-title":"Chronic protein deficiency differentially affects the kinetics of plasma proteins in young pigs","volume":"126","author":"Jahoor","year":"1996","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbapap.2004.09.023_bib16","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/S0167-4838(00)00150-3","article-title":"Plasma retinol-binding protein: structure and function of the prototypic lipocalin","volume":"1482","author":"Newcomer","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2004.09.023_bib17","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1126\/science.7754382","article-title":"Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein","volume":"268","author":"Monaco","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.bbapap.2004.09.023_bib18","doi-asserted-by":"crossref","first-page":"1451","DOI":"10.1002\/j.1460-2075.1984.tb01995.x","article-title":"The three-dimensional structure of retinol-binding protein","volume":"3","author":"Newcomer","year":"1984","journal-title":"EMBO J."},{"key":"10.1016\/j.bbapap.2004.09.023_bib19","doi-asserted-by":"crossref","first-page":"10728","DOI":"10.1016\/S0021-9258(18)82046-4","article-title":"Crystal structure of liganded and unliganded forms of bovine plasma retinol-binding protein","volume":"268","author":"Zanotti","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib20","doi-asserted-by":"crossref","first-page":"29613","DOI":"10.1016\/S0021-9258(18)43925-7","article-title":"Crystallographic studies on complexes between retinoids and plasma retinol-binding protein","volume":"269","author":"Zanotti","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib21","doi-asserted-by":"crossref","first-page":"6308","DOI":"10.1016\/S0021-9258(19)43449-2","article-title":"Conformational changes following interaction between retinol isomers and human retinol-binding protein and between the retinol-binding protein and prealbumin","volume":"248","author":"Heller","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib22","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0005-2795(72)90218-8","article-title":"Circular dichroic studies of human plasma retinol-binding protein and prealbumin","volume":"271","author":"Gotto","year":"1972","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2004.09.023_bib23","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0014-5793(93)81272-2","article-title":"Mechanism of pH-induced release of retinol from retinol-binding protein","volume":"317","author":"Ptitsyn","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2004.09.023_bib24","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/0005-2736(87)90122-2","article-title":"Studies of the spontaneous transfer of retinol from the retinol:retinol-binding protein complex to unilamellar liposomes","volume":"901","author":"Fex","year":"1987","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2004.09.023_bib25","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1006\/excr.1996.0010","article-title":"Retinol-binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells","volume":"222","author":"Bellovini","year":"1996","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib26","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1074\/jbc.273.6.3336","article-title":"The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor","volume":"273","author":"Sundaram","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib27","first-page":"1031","article-title":"Membrane receptors for retinol-binding protein in cultured human retinal pigment epithelium","volume":"27","author":"Pfeffer","year":"1986","journal-title":"Invest. Ophthalmol. Visual Sci."},{"key":"10.1016\/j.bbapap.2004.09.023_bib28","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1093\/emboj\/18.17.4633","article-title":"Impaired retinal function and vitamin A availability in mice lacking retinol-binding protein","volume":"18","author":"Quadro","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.bbapap.2004.09.023_bib29","doi-asserted-by":"crossref","first-page":"15360","DOI":"10.1021\/bi0268551","article-title":"Retinol-binding protein-deficient mice: biochemical basis for impaired vision","volume":"41","author":"Vogel","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib30","first-page":"258","article-title":"A case of human vitamin A deficiency caused by an inherited defect in retinol-binding protein without clinical symptoms except night blindness","volume":"57","author":"Wolf","year":"1999","journal-title":"Nutr. Rev."},{"key":"10.1016\/j.bbapap.2004.09.023_bib31","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1161\/01.RES.0000069030.30886.8F","article-title":"Increased fibronectin deposition in embryonic hearts of retinol-binding protein-null mice","volume":"92","author":"Wendler","year":"2003","journal-title":"Circ. Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib32","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/S0899-9007(97)00192-5","article-title":"Vitamin A homeostasis and diabetes mellitus","volume":"13","author":"Basu","year":"1997","journal-title":"Nutrition"},{"key":"10.1016\/j.bbapap.2004.09.023_bib33","doi-asserted-by":"crossref","first-page":"1958","DOI":"10.1093\/jn\/130.8.1958","article-title":"The metabolic availability of vitamin A is decreased at the onset of diabetes in BB rats","volume":"130","author":"Lu","year":"2000","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbapap.2004.09.023_bib34","doi-asserted-by":"crossref","first-page":"339","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 A","volume":"121","author":"Blake","year":"1978","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib35","doi-asserted-by":"crossref","first-page":"867","DOI":"10.18388\/abp.2001_3852","article-title":"Structural basis of negative cooperativity in transthyretin","volume":"48","author":"Neumann","year":"2001","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib36","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-2836(74)90291-5","article-title":"Structure of human plasma prealbumin at 2\u20135 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding","volume":"88","author":"Blake","year":"1974","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib37","doi-asserted-by":"crossref","first-page":"11453","DOI":"10.1021\/bi010673+","article-title":"Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope induced unfolding dichotomy","volume":"40","author":"Hammarstrom","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib38","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/74082","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.2004.09.023_bib39","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1089\/thy.2000.10.141","article-title":"The thyroxine-binding proteins","volume":"10","author":"Schussler","year":"2000","journal-title":"Thyroid"},{"key":"10.1016\/j.bbapap.2004.09.023_bib40","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1021\/bi00173a029","article-title":"Synthesis and secretion of retinol-binding protein and transthyretin by cultured retinal pigment epithelium","volume":"33","author":"Ong","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib41","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1515\/CCLM.2002.210","article-title":"The evolution of transthyretin synthesis in the choroids plexus","volume":"40","author":"Schreiber","year":"2002","journal-title":"Clin. Chem. Lab. Med."},{"key":"10.1016\/j.bbapap.2004.09.023_bib42","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/0014-5793(95)00095-Q","article-title":"A yellow component associated with human transthyretin has properties like a pterin derivative, 7,8-dihydropterin-6-carboxaldehyde","volume":"360","author":"Ernstrom","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbapap.2004.09.023_bib43","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/S0022-2275(20)32074-5","article-title":"Transthyretin in high density lipoproteins: association with apolipoprotein A-I","volume":"41","author":"Sousa","year":"2000","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib44","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1006\/excr.1996.0010","article-title":"Retinol-binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells","volume":"222","author":"Bellovini","year":"1996","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib45","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/S0021-9258(18)62529-3","article-title":"Studies on the interaction between prealbumin, retinol-binding protein, and vitamin A","volume":"246","author":"Peterson","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib46","doi-asserted-by":"crossref","first-page":"4698","DOI":"10.1016\/S0021-9258(19)43720-4","article-title":"The interaction of human plasma retinol-binding protein and prealbumin","volume":"248","author":"Van Jaarsveld","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib47","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/S0022-2275(20)39396-2","article-title":"Extraction and recombination studies of the interaction of retinol with human plasma retinol-binding protein","volume":"13","author":"Goodman","year":"1972","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bbapap.2004.09.023_bib48","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1016\/S0021-9258(18)63184-9","article-title":"Studies on the protein\u2013protein and protein\u2013ligand interactions involved in retinol transport in plasma","volume":"245","author":"Raz","year":"1970","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib49","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0005-2795(72)90218-8","article-title":"Circular dichroic studies of human plasma retinal binding protein and prealbumin","volume":"271","author":"Gotto","year":"1972","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2004.09.023_bib50","first-page":"77","article-title":"Potein turnover studies using stable isotope tracer techniques","volume":"26","author":"Sivakumar","year":"1999","journal-title":"Proc. Nutr. Soc. India"},{"key":"10.1016\/j.bbapap.2004.09.023_bib51","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1042\/BA20020100","article-title":"A new method for purification of human plasma retinol-binding protein and transthyretin","volume":"38","author":"Raghu","year":"2003","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib52","doi-asserted-by":"crossref","first-page":"2647","DOI":"10.1021\/bi982291i","article-title":"The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP","volume":"38","author":"Naylor","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib53","doi-asserted-by":"crossref","first-page":"13949","DOI":"10.1074\/jbc.M006779200","article-title":"Unique biochemical nature of carp retinol-binding protein. N-linked glycosylation and uncleavable NH2-terminal signal peptide","volume":"276","author":"Bellovini","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib54","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/S0899-9007(99)00009-X","article-title":"The stressful condition as a nutritionally dependent adaptive dichotomy","volume":"15","author":"Ingenbleek","year":"1999","journal-title":"Nutrition"},{"key":"10.1016\/j.bbapap.2004.09.023_bib55","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1515\/CCLM.2002.222","article-title":"Significance of transthyretin in protein metabolism","volume":"40","author":"Ingenbleek","year":"2002","journal-title":"Clin. Chem. Lab. Med."},{"key":"10.1016\/j.bbapap.2004.09.023_bib56","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0959-440X(99)90003-9","article-title":"Folding and binding: problems with proteins","volume":"10","author":"Rochet","year":"2000","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib57","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1006\/jsbi.2000.4221","article-title":"Review: history of the amyloid fibril","volume":"130","author":"Sipe","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib58","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/S0092-8674(00)80143-9","article-title":"For protein misassembly, it's the \u201cI\u201d decade","volume":"86","author":"Wetzel","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.bbapap.2004.09.023_bib59","doi-asserted-by":"crossref","first-page":"73","DOI":"10.3109\/07853898909149187","article-title":"The deposition of amyloid proteins in the aging mammalian brain: implications for Alzheimer's disease","volume":"21","author":"Selkoe","year":"1989","journal-title":"Ann. Med."},{"key":"10.1016\/j.bbapap.2004.09.023_bib60","doi-asserted-by":"crossref","first-page":"8654","DOI":"10.1021\/bi00151a036","article-title":"Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro","volume":"31","author":"Colon","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib61","doi-asserted-by":"crossref","first-page":"6470","DOI":"10.1021\/bi952501g","article-title":"The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid","volume":"35","author":"Lai","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib62","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1038\/78980","article-title":"A glimpse of a possible amyloidogenic intermediate of transthyretin","volume":"7","author":"Liu","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib63","doi-asserted-by":"crossref","first-page":"17851","DOI":"10.1021\/bi981876+","article-title":"Characterization of the transthyretin acid denaturation pathways by analytical ultra centrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation","volume":"37","author":"Lashuel","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib64","doi-asserted-by":"crossref","first-page":"14943","DOI":"10.1073\/pnas.261419998","article-title":"The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis","volume":"98","author":"Jiang","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2004.09.023_bib65","doi-asserted-by":"crossref","first-page":"733","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.2004.09.023_bib66","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0301-4622(00)00199-X","article-title":"Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin","volume":"88","author":"Shnyrov","year":"2000","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib67","doi-asserted-by":"crossref","first-page":"5699","DOI":"10.1074\/jbc.M310605200","article-title":"Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy","volume":"279","author":"Olofsson","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib68","doi-asserted-by":"crossref","first-page":"27207","DOI":"10.1074\/jbc.M101024200","article-title":"Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants","volume":"276","author":"Quintas","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2004.09.023_bib69","doi-asserted-by":"crossref","first-page":"257","DOI":"10.3109\/13506120108993822","article-title":"Serum transthyretin monomer in patients with familial amyloid polyneuropathy","volume":"8","author":"Sekijima","year":"2001","journal-title":"Amyloid"},{"key":"10.1016\/j.bbapap.2004.09.023_bib70","doi-asserted-by":"crossref","first-page":"12956","DOI":"10.1073\/pnas.95.22.12956","article-title":"Inhibiting transthyretin conformational changes that lead to amyloid fibril formation","volume":"95","author":"Peterson","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2004.09.023_bib71","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1006\/abbi.2002.2779","article-title":"2,4-Dinitrophenols inhibits transthyretin amyloid fibril formation through tetramer stabilization","volume":"400","author":"Raghu","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2004.09.023_bib72","doi-asserted-by":"crossref","first-page":"15051","DOI":"10.1073\/pnas.93.26.15051","article-title":"Inhibiting transthyretin amyloid fibril formation via protein stabilization","volume":"93","author":"Miroy","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2004.09.023_bib73","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0002-9440(10)63123-9","article-title":"Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met","volume":"164","author":"Takaoka","year":"2004","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib74","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/bi030077a","article-title":"Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions","volume":"42","author":"Zhang","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2004.09.023_bib75","doi-asserted-by":"crossref","first-page":"61","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":"2003","journal-title":"Neurogenetics"},{"key":"10.1016\/j.bbapap.2004.09.023_bib76","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1159\/000116264","article-title":"Serum prealbumin and retinol-binding protein concentrations in Japanese-type familial amyloid polyneuropathy","volume":"28","author":"Shoji","year":"1988","journal-title":"Eur. Neurol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib77","doi-asserted-by":"crossref","first-page":"13019","DOI":"10.1073\/pnas.241406698","article-title":"Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro","volume":"98","author":"White","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2004.09.023_bib78","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1042\/0264-6021:3510273","article-title":"The molecular interaction of 4\u2032-iodo-4\u2032-deoxydoxorubicin with Leu-55Pro transthyretin 'amyloid-like' oligomer leading to disaggregation","volume":"351","author":"Sebastiao","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2004.09.023_bib79","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S0006-291X(02)00465-5","article-title":"Only amyloidogenic intermediates of transthyretin induce apoptosis","volume":"294","author":"Andersson","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2004.09.023_bib80","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1016\/S0002-9440(10)63050-7","article-title":"Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates","volume":"159","author":"Sousa","year":"2001","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.bbapap.2004.09.023_bib81","doi-asserted-by":"crossref","first-page":"803","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.2004.09.023_bib82","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1097\/01.TP.0000092307.98347.CB","article-title":"Ten years of international experience with liver transplantation for familial amyloidotic polyneuropathy: results from the Familial Amyloidotic Polyneuropathy World Transplant Registry","volume":"77","author":"Herlenius","year":"2004","journal-title":"Transplantation"},{"key":"10.1016\/j.bbapap.2004.09.023_bib83","doi-asserted-by":"crossref","first-page":"247","DOI":"10.3109\/13506120209114101","article-title":"Presence of variant transthyretin in aqueous humor of a patient with familial amyloidotic polyneuropathy after liver transplantation","volume":"9","author":"Haraoka","year":"2002","journal-title":"Amyloid"},{"key":"10.1016\/j.bbapap.2004.09.023_bib84","first-page":"146","article-title":"Interaction of transthyretin with amyloid beta-protein: binding and inhibition of amyloid formation","volume":"199","author":"Schwarzman","year":"1996","journal-title":"Ciba Found. Symp."},{"key":"10.1016\/j.bbapap.2004.09.023_bib85","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1523\/JNEUROSCI.20-04-01318.2000","article-title":"Nicotine enhances the biosynthesis and secretion of transthyretin from the choroids plexus in rats: implications for beta-amyloid formation","volume":"20","author":"Li","year":"2000","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbapap.2004.09.023_bib86","doi-asserted-by":"crossref","first-page":"1580","DOI":"10.1073\/pnas.0337683100","article-title":"Short-term administration of omega 3 fatty acids from fish oil results in increased transthyretin transcription in old rat hippocampus","volume":"100","author":"Puskas","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963904002651?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963904002651?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,26]],"date-time":"2021-06-26T10:40:05Z","timestamp":1624704005000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963904002651"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,12]]},"references-count":86,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2004,12]]}},"alternative-id":["S1570963904002651"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2004.09.023","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2004,12]]}}}