サイロキシン結合プレアルブミン thyroxine binding prealbumin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/15 06:06:39」(JST)

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Transthyretin (TTR) is a serum and cerebrospinal fluid carrier of the thyroid hormone thyroxine (T4) and retinol-binding protein bound to retinol. This is how transthyretin gained its name, transports thyroxine and retinol. The liver secretes transthyretin into the blood, and the choroid plexus secretes TTR into the cerebrospinal fluid.

TTR was originally called prealbumin^[1] (or thyroxine-binding prealbumin) because it ran faster than albumin on electrophoresis gels.

Binding affinities

It functions in concert with two other thyroid hormone-binding proteins in the serum:

Protein	Binding strength	Plasma concentration
thyroxine-binding globulin (TBG)	highest	lowest
transthyretin (TTR or TBPA)	lower	higher
albumin	poorest	much higher

In cerebrospinal fluid TTR is the primary carrier of T4. TTR also acts as a carrier of retinol (vitamin A) through its association with retinol-binding protein (RBP) in the blood and the CSF. Less than 1% of TTR's T4 binding sites are occupied in blood, which is taken advantage of below to prevent TTRs dissociation, misfolding and aggregation which leads to the degeneration of post-mitotic tissue.

Numerous other small molecules are known to bind in the thyroxine binding sites, including many natural products (such as resveratrol), drugs (Tafamidis,^[2] or Vyndaqel, diflunisal,^[3]^[4]^[5] flufenamic acid),^[6] and toxins (PCB^[7]).

Structure

TTR is a 55kDa homotetramer with a dimer of dimers quaternary structure that is synthesized in the liver, choroid plexus and retinal pigment epithelium for secretion into the bloodstream, cerebrospinal fluid and the eye, respectively. Each monomer is a 127-residue polypeptide rich in beta sheet structure. Association of two monomers via their edge beta-strands forms an extended beta sandwich. Further association of two of these dimers in a face-to-face fashion produces the homotetrameric structure and creates the two thyroxine binding sites per tetramer. This dimer-dimer interface, comprising the two T4 binding sites, is the weaker dimer-dimer interface and is the one that comes apart first in the process of tetramer dissociation.^[8]

Role in disease

TTR misfolding and aggregation is known to be associated with the amyloid diseases^[9] senile systemic amyloidosis (SSA),^[10] familial amyloid polyneuropathy (FAP),^[11]^[12] and familial amyloid cardiomyopathy (FAC).^[13]

TTR tetramer dissociation is known to be rate-limiting for amyloid fibril formation.^[14]^[15]^[16] However, the monomer also must partially denature in order for TTR to be mis-assembly competent, leading to a variety of aggregate structures, including amyloid fibrils.^[17]

While wild type TTR can dissociate, misfold, and aggregate, leading to SSA, point mutations within TTR are known to destabilize the tetramer composed of mutant and wild-type TTR subunits, facilitating more facile dissociation and/or misfolding and amyloidogenesis.^[18] A replacement of valine by methionine at position 30 (TTR V30M) is the mutation most commonly associated with FAP.^[19] A position 122 replacement of valine by isoleucine (TTR V122I) is carried by 3.9% of the African-American population, and is the most common cause of FAC.^[13] SSA is estimated to affect over 25% of the population over age 80.^[10] Severity of disease varies greatly by mutation, with some mutations causing disease in the first or second decade of life, and others being more benign. Deposition of TTR amyloid is generally observed extracellularly, although TTR deposits are also clearly observed within the cardiomyocytes of the heart.

Treatment of familial TTR amyloid disease has historically relied on liver transplantation as a crude form of gene therapy.^[20] Because TTR is primarily produced in the liver, replacement of a liver containing a mutant TTR gene with a normal gene is able to reduce the mutant TTR levels in the body to < 5% of pretransplant levels. Certain mutations, however, cause CNS amyloidosis, and due to the their production by the choroid plexus, the CNS TTR amyloid diseases do not respond to gene therapy mediated by liver transplantation.

In 2011, the European Medicines Agency approved Tafamidis or Vyndaqel^[2] for the amelioration of FAP. Vyndaqel kinetically stabilizes the TTR tetramer, preventing tetramer dissociation required for TTR amyloidogenesis and degradation of the autonomic nervous system^[21] and/or the peripheral nervous system and/or the heart.^[16]

TTR is also thought to have beneficial side effects, by binding to the infamous beta-amyloid protein, thereby preventing beta-amyloid's natural tendency to accumulate into the plaques associated with the early stages of Alzheimer's Disease. Preventing plaque formation is thought to enable a cell to rid itself of this otherwise toxic protein form and, thus, help prevent and maybe even treat the disease.^[22]

There is now strong genetic^[23]^[24] and pharmacologic data (see European Medicines Agency website for the Tafamidis clinical trial results) indicating that the process of amyloid fibril formation leads to the degeneration of post-mitotic tissue causing FAP and likely FAC and SSA. Evidence points to the oligomers generated in the process of amyloidogenicity leading to the observed proteotoxicity.^[25]^[26]

Transthyretin level in cerebrospinal fluid has also been found to be lower in patients with some neurobiological disorders such as schizophrenia.^[27] The reduced level of transthyretin in the CSF may indicate a lower thyroxine transport in brains of patients with schizophrenia.

Because transthyretin is made in part by the choroid plexus, it can be used as an immunohistochemical marker for choroid plexus papillomas.^{[citation needed]}

As of March 2015, there are two ongoing clinical trials undergoing recruitment in the United States and worldwide to evaluate potential treatments for TTR Amyloidosis.^[28]

Nutritional assessment

In medicine, nutritional status can be assessed by measuring the concentration of transthyretin in the blood. In theory, other transport proteins such as albumin or transferrin could be used, but transthyretin is preferred because of its shorter half-life, although this means that its concentration more closely reflects recent dietary intake rather than overall nutritional status.^[29] Transthyretin concentration has been shown to be a good indicator of whether or not a malnourished patient will develop refeeding syndrome upon commencement of refeeding, via either the enteral, parenteral or oral routes.^[30]

Protein	Half-Life (days)	Normal Levels	Malnutrition
Protein	Half-Life (days)	Normal Levels	mild	moderate	severe
Prealbumin	2-4	15.7-29.6 mg/dL	12-15	8-10	<8

Interactions

Transthyretin has been shown to interact with Perlecan.^[31]

References

^ Prealbumin at the US National Library of Medicine Medical Subject Headings (MeSH)
^ ^a ^b Razavi H, Palaninathan SK, Powers ET, Wiseman RL, Purkey HE, Mohamedmohaideen NN et al. (June 2003). "Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis, evaluation, and mechanism of action". Angew. Chem. Int. Ed. Engl. 42 (24): 2758–61. doi:10.1002/anie.200351179. PMID 12820260.
^ Sekijima Y, Dendle MA, Kelly JW (December 2006). "Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis". Amyloid 13 (4): 236–49. doi:10.1080/13506120600960882. PMID 17107884.
^ Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW (January 2004). "Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis". J. Med. Chem. 47 (2): 355–74. doi:10.1021/jm030347n. PMID 14711308.
^ Vilaro M, Arsequell G, Valencia G, Ballesteros A, Barluenga J, Nieto J, Planas A, Almeida R, Saraiva MJ (2007). "Reengineering TTR amyloid inhibition properties of diflunisal". In Seldin DC, Skinner M, Berk JL, Connors LH. XIth International Symposium on Amyloidosis. Boca Raton: CRC. doi:10.1201/9781420043358.ch69. ISBN 1-4200-4281-5.
^ Baures PW, Oza VB, Peterson SA, Kelly JW (July 1999). "Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid". Bioorg. Med. Chem. 7 (7): 1339–47. doi:10.1016/S0968-0896(99)00066-8. PMID 10465408.
^ Purkey HE, Palaninathan SK, Kent KC, Smith C, Safe SH, Sacchettini JC et al. (December 2004). "Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: rationalizing rodent PCB toxicity". Chem. Biol. 11 (12): 1719–28. doi:10.1016/j.chembiol.2004.10.009. PMID 15610856.
^ Foss TR, Wiseman RL, Kelly JW (November 2005). "The pathway by which the tetrameric protein transthyretin dissociates". Biochemistry 44 (47): 15525–33. doi:10.1021/bi051608t. PMID 16300401.
^ Zeldenrust SR, Benson MD (2010). "Familial and senile amyloidosis caused by transthyretin". In Ramirez-Alvarado M, Kelly JW, Dobson C. Protein misfolding diseases: current and emerging principles and therapies. New York: Wiley. doi:10.1002/9780470572702.ch36. ISBN 0-471-79928-9.
^ ^a ^b Westermark P, Sletten K, Johansson B, Cornwell GG (April 1990). "Fibril in senile systemic amyloidosis is derived from normal transthyretin". Proc. Natl. Acad. Sci. U.S.A. 87 (7): 2843–5. doi:10.1073/pnas.87.7.2843. PMC 53787. PMID 2320592.
^ Andrade C (September 1952). "A peculiar form of peripheral neuropathy; familiar atypical generalized amyloidosis with special involvement of the peripheral nerves". Brain 75 (3): 408–27. doi:10.1093/brain/75.3.408. PMID 12978172.
^ Coelho T (October 1996). "Familial amyloid polyneuropathy: new developments in genetics and treatment". Curr. Opin. Neurol. 9 (5): 355–9. doi:10.1097/00019052-199610000-00007. PMID 8894411.
^ ^a ^b Jacobson DR, Pastore RD, Yaghoubian R, Kane I, Gallo G, Buck FS et al. (February 1997). "Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans". N. Engl. J. Med. 336 (7): 466–73. doi:10.1056/NEJM199702133360703. PMID 9017939.
^ Colon W, Kelly JW (September 1992). "Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro". Biochemistry 31 (36): 8654–60. doi:10.1021/bi00151a036. PMID 1390650.
^ Lai Z, Colón W, Kelly JW (May 1996). "The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid". Biochemistry 35 (20): 6470–82. doi:10.1021/bi952501g. PMID 8639594.
^ ^a ^b Hammarström P, Wiseman RL, Powers ET, Kelly JW (January 2003). "Prevention of transthyretin amyloid disease by changing protein misfolding energetics". Science 299 (5607): 713–6. doi:10.1126/science.1079589. PMID 12560553.
^ Jiang X, Smith CS, Petrassi HM, Hammarström P, White JT, Sacchettini JC et al. (September 2001). "An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured". Biochemistry 40 (38): 11442–52. doi:10.1021/bi011194d. PMID 11560492.
^ Sekijima Y, Wiseman RL, Matteson J, Hammarström P, Miller SR, Sawkar AR et al. (April 2005). "The biological and chemical basis for tissue-selective amyloid disease". Cell 121 (1): 73–85. doi:10.1016/j.cell.2005.01.018. PMID 15820680.
^ Saraiva MJ (1995). "Transthyretin mutations in health and disease". Hum. Mutat. 5 (3): 191–6. doi:10.1002/humu.1380050302. PMID 7599630.
^ Holmgren G, Ericzon BG, Groth CG, Steen L, Suhr O, Andersen O et al. (May 1993). "Clinical improvement and amyloid regression after liver transplantation in hereditary transthyretin amyloidosis". Lancet 341 (8853): 1113–6. doi:10.1016/0140-6736(93)93127-m. PMID 8097803.
^ Ando Y, Suhr OB (December 1998). "Autonomic dysfunction in familial amyloidotic polyneuropathy (FAP)". Amyloid 5 (4): 288–300. doi:10.3109/13506129809007303. PMID 10036588.
^ Li X, Buxbaum JN (2011). id=PMID 22112803 "Transthyretin and the brain re-visited: is neuronal synthesis of transthyretin protective in Alzheimer's disease?". Mol Neurodegener 6 (1): 79. doi:10.1186/1750-1326-6-79. PMID 22112803.
^ Coelho, T., Carvalho, M., Saraiva, M.J., Alves, I., Almeida, M.R., and Costa, P.P. (1993). A strikingly benign evolution of FAP in an individual found to be a compound heterozygote for two TTR mutations: TTR MET 30 and TTR MET 119. J Rheumatol 20, 179.
^ Hammarström P, Schneider F, Kelly JW (September 2001). "Trans-suppression of misfolding in an amyloid disease". Science 293 (5539): 2459–62. doi:10.1126/science.1062245. PMID 11577236.
^ Sousa MM, Cardoso I, Fernandes R, Guimarães A, Saraiva MJ (December 2001). "Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates". Am. J. Pathol. 159 (6): 1993–2000. PMC 1850610. PMID 11733349.
^ Reixach N, Deechongkit S, Jiang X, Kelly JW, Buxbaum JN (March 2004). "Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture". Proc. Natl. Acad. Sci. U.S.A. 101 (9): 2817–22. doi:10.1073/pnas.0400062101. PMC 365703. PMID 14981241.
^ Huang JT, Leweke FM, Oxley D, Wang L, Harris N, Koethe D et al. (November 2006). "Disease biomarkers in cerebrospinal fluid of patients with first-onset psychosis". PLoS Med. 3 (11): e428. doi:10.1371/journal.pmed.0030428. PMC 1630717. PMID 17090210.
^ Clinical trial number NCT01960348 for "APOLLO: The Study of an Investigational Drug, Patisiran (ALN-TTR02), for the Treatment of Transthyretin (TTR)-Mediated Amyloidosis" at ClinicalTrials.gov
^ Shenkin A (2006-12-01). "Serum prealbumin: Is it a marker of nutritional status or of risk of malnutrition?". Clin. Chem. 52 (12): 2177–9. doi:10.1373/clinchem.2006.077412. PMID 17138848.
^ Marik PE, Bedigian MK (1996-10-01). "Refeeding hypophosphatemia in critically ill patients in an intensive care unit. A prospective study". Arch Surg 131 (10): 1043–7. doi:10.1001/archsurg.131.10.1043. PMID 8857900.
^ Smeland S, Kolset SO, Lyon M, Norum KR, Blomhoff R (September 1997). "Binding of perlecan to transthyretin in vitro". Biochem. J. 326 (3): 829–36. PMC 1218739. PMID 9307034.

External links

GeneReviews/NIH/NCBI/UW entry on Familial Transthyretin Amyloidosis

UpToDate Contents

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1. 甲状腺機能正常型高サイロキシン血症および低サイロキシン血症 euthyroid hyperthyroxinemia and hypothyroxinemia
2. 非甲状腺疾患における甲状腺機能 thyroid function in nonthyroidal illness
3. 甲状腺ホルモンの合成および生理 thyroid hormone synthesis and physiology
4. 甲状腺機能の臨床検査評価 laboratory assessment of thyroid function

English Journal

Relationship between relative interdialytic weight gain and serum leptin levels, nutrition, and inflammation in chronic hemodialysis patients.

Ahbap E1, Sakaci T, Kara E, Sahutoglu T, Koc Y, Basturk T, Sevinc M, Akgol C, Kayalar AO, Ucar ZA, Bayraktar F, Unsal A.
Clinical nephrology.Clin Nephrol.2015 Mar;83(3):154-60.
INTRODUCTION: Excessive relative interdialytic weight gain (RIDWG, %) is an important risk factor for long-term adverse cardiovascular outcomes in chronic hemodialysis (HD) patients. On the other hand, it may also be an index of good appetite and nutritional status. We aimed to assess the relationsh
PMID 25685870

Elevated serum leptin levels are associated with good nutritional status in non-obese chronic hemodialysis patients.

Kara E, Ahbap E, Sahutoglu T, Sakaci T, Basturk T, Koc Y, Sevinc M, Akgol C, Ucar ZA, Kayalar AO, Bayraktar F, Unsal A.
Clinical nephrology.Clin Nephrol.2015 Mar;83(3):147-53. doi: 10.5414/CN108409.
OBJECTIVE: Leptin is a hormone and a proinflammatory cytokine secreted from adipocytes, which functions to suppress appetite in healthy persons. Serum leptin levels are significantly elevated in patients with end-stage renal disease (ESRD) primarily due to decreased clearance by the kidneys The cons
PMID 25600857

Optimized human factor IX expression cassettes for hepatic-directed gene therapy of hemophilia B.

Zhang R1, Wang Q, Zhang L, Chen S.
Frontiers of medicine.Front Med.2015 Mar;9(1):90-9. doi: 10.1007/s11684-015-0390-2. Epub 2015 Feb 7.
Gene therapy provides a potential cure for hemophilia B, and significant progress has been achieved in liver-directed gene transfer mediated by adeno-associated viral vectors. Recent clinical trials involving the use of a self-complementary adeno-associated virus serotype 8-human codon-optimized fac
PMID 25663062

Japanese Journal

Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis.

IRWIN S. W.
Mol. Microbiol. 8, 1125-1133, 1993
NAID 30014458717

Plasma Thyroxine-Binding Proteins and Thyroid Hormone Levels in Primate Species: Is Callithricidae Thyroid Hormone Resistant

SEO HISAO,ANDO MICHIYASU,YAMAUCHI KAZUYUKI,MATSUI NOBUO,TAKENAKA OSAMU
Endocrinologia Japonica 36(5), 665-673, 1989
… From the electrophoretic analysis, it was shown that thyroxinebinding proteins similar to human thyroxine-binding globulin (TBG) and thyroxine-binding prealbumin (TBPA) were present in catarrhini and prosimiae species, but not in platyrrhini (callithricidae and cebidae). …
NAID 130000952694

Related Pictures

TBPA-5.08-10 What does TBPA mean? It stands for thyroid ms180cm | TBPA TBPA en chine TbpA (silver) grabs transferrin (gold TBPA Car Meet #2 (GTA Online) 17/05/14 Home / Disney Tinkerbell Backpack (TBPA) tbpa_2016_005_handover_001

★リンクテーブル★

リンク元	「トランスサイレチン」「サイロキシン結合プレアルブミン」
関連記事	「TBP」「TB」

「トランスサイレチン」

Transthyretin
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1BM7, 1BMZ, 1BZ8, 1BZD, 1BZE, 1DVQ, 1DVS, 1DVT, 1DVU, 1DVX, 1DVY, 1DVZ, 1E3F, 1E4H, 1E5A, 1ETA, 1ETB, 1F41, 1F64, 1F86, 1FH2, 1FHN, 1G1O, 1GKO, 1ICT, 1III, 1IIK, 1IJN, 1QAB, 1QWH, 1RLB, 1SOK, 1SOQ, 1THA, 1THC, 1TLM, 1TSH, 1TT6, 1TTA, 1TTB, 1TTC, 1TTR, 1TYR, 1TZ8, 1U21, 1X7S, 1X7T, 1Y1D, 1Z7J, 1ZCR, 1ZD6, 2B14, 2B15, 2B16, 2B77, 2B9A, 2F7I, 2F8I, 2FBR, 2FLM, 2G3X, 2G3Z, 2G4E, 2G4G, 2G5U, 2G9K, 2GAB, 2H4E, 2M5N, 2NOY, 2PAB, 2QEL, 2QGB, 2QGC, 2QGD, 2QGE, 2ROX, 2ROY, 2TRH, 2TRY, 2WQA, 3A4D, 3A4E, 3A4F, 3B56, 3BSZ, 3BT0, 3CBR, 3CFM, 3CFN, 3CFQ, 3CFT, 3CN0, 3CN1, 3CN2, 3CN3, 3CN4, 3CXF, 3D2T, 3D7P, 3DGD, 3DID, 3DJR, 3DJS, 3DJT, 3DJZ, 3DK0, 3DK2, 3DO4, 3ESN, 3ESO, 3ESP, 3FC8, 3FCB, 3GLZ, 3GPS, 3GRB, 3GRG, 3GS0, 3GS4, 3GS7, 3HJ0, 3I9A, 3I9I, 3I9P, 3IMR, 3IMS, 3IMT, 3IMU, 3IMV, 3IMW, 3IPB, 3IPE, 3KGS, 3KGT, 3KGU, 3M1O, 3NEE, 3NEO, 3NES, 3NEX, 3NG5, 3OZK, 3OZL, 3P3R, 3P3S, 3P3T, 3P3U, 3SSG, 3TCT, 3TFB, 3U2I, 3U2J, 3W3B, 4ABQ, 4ABU, 4ABV, 4ABW, 4AC2, 4AC4, 4ACT, 4ANK, 4DER, 4DES, 4DET, 4DEU, 4DEW, 4FI6, 4FI7, 4FI8, 4HIQ, 4HIS, 4HJS, 4HJT, 4HJU, 4I85, 4I87, 4I89, 4IIZ, 4IK6, 4IK7, 4IKI, 4IKJ, 4IKK, 4IKL, 4KY2, 4L1S, 4L1T, 4MAS, 4MRB, 4MRC, 4N85, 4N86, 4N87, 5TTR
Identifiers
Symbols	TTR ; CTS; CTS1; HEL111; HsT2651; PALB; TBPA
External IDs	OMIM: 176300 MGI: 98865 HomoloGene: 317 ChEMBL: 3194 GeneCards: TTR Gene
Gene ontology
Molecular function	• hormone activity; • protein binding; • hormone binding; • identical protein binding; • protein heterodimerization activity;
Cellular component	• extracellular region; • extracellular space; • cytoplasm; • protein complex; • extracellular vesicular exosome;
Biological process	• retinoid metabolic process; • transport; • phototransduction, visible light; • extracellular matrix organization; • retinol metabolic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: transthyretin, TTR
同: プレアルブミン, prealbumin、thyroxine-binding prealbumin TBPA

蛋白分画でAlb分画に分けられる
トランスサイレチンの分解産物はangiostatic factorのvasculostatinと呼ばれる

臨床関連

「サイロキシン結合プレアルブミン」

　　[★] thyroxine-binding prealbumin TBPA

「TBP」

　　[★]

同: TATA-binding protein

同: TATA-binding protein

関: See TATA binding protein

「TB」

　　[★]

[1] Prealbumin at the US National Library of Medicine Medical Subject Headings (MeSH)

[pmid12820260-2] Razavi H, Palaninathan SK, Powers ET, Wiseman RL, Purkey HE, Mohamedmohaideen NN et al. (June 2003). "Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis, evaluation, and mechanism of action". Angew. Chem. Int. Ed. Engl. 42 (24): 2758–61. doi:10.1002/anie.200351179. PMID 12820260.

[pmid17107884-3] Sekijima Y, Dendle MA, Kelly JW (December 2006). "Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis". Amyloid 13 (4): 236–49. doi:10.1080/13506120600960882. PMID 17107884.

[pmid14711308-4] Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW (January 2004). "Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis". J. Med. Chem. 47 (2): 355–74. doi:10.1021/jm030347n. PMID 14711308.

[isbn1-4200-4281-5-5] Vilaro M, Arsequell G, Valencia G, Ballesteros A, Barluenga J, Nieto J, Planas A, Almeida R, Saraiva MJ (2007). "Reengineering TTR amyloid inhibition properties of diflunisal". In Seldin DC, Skinner M, Berk JL, Connors LH. XIth International Symposium on Amyloidosis. Boca Raton: CRC. doi:10.1201/9781420043358.ch69. ISBN 1-4200-4281-5.

[pmid10465408-6] Baures PW, Oza VB, Peterson SA, Kelly JW (July 1999). "Synthesis and evaluation of inhibitors of transthyretin amyloid formation based on the non-steroidal anti-inflammatory drug, flufenamic acid". Bioorg. Med. Chem. 7 (7): 1339–47. doi:10.1016/S0968-0896(99)00066-8. PMID 10465408.

[pmid15610856-7] Purkey HE, Palaninathan SK, Kent KC, Smith C, Safe SH, Sacchettini JC et al. (December 2004). "Hydroxylated polychlorinated biphenyls selectively bind transthyretin in blood and inhibit amyloidogenesis: rationalizing rodent PCB toxicity". Chem. Biol. 11 (12): 1719–28. doi:10.1016/j.chembiol.2004.10.009. PMID 15610856.

[pmid16300401-8] Foss TR, Wiseman RL, Kelly JW (November 2005). "The pathway by which the tetrameric protein transthyretin dissociates". Biochemistry 44 (47): 15525–33. doi:10.1021/bi051608t. PMID 16300401.

[isbn0-471-79928-9-9] Zeldenrust SR, Benson MD (2010). "Familial and senile amyloidosis caused by transthyretin". In Ramirez-Alvarado M, Kelly JW, Dobson C. Protein misfolding diseases: current and emerging principles and therapies. New York: Wiley. doi:10.1002/9780470572702.ch36. ISBN 0-471-79928-9.

[pmid2320592-10] Westermark P, Sletten K, Johansson B, Cornwell GG (April 1990). "Fibril in senile systemic amyloidosis is derived from normal transthyretin". Proc. Natl. Acad. Sci. U.S.A. 87 (7): 2843–5. doi:10.1073/pnas.87.7.2843. PMC 53787. PMID 2320592.

[pmid12978172-11] Andrade C (September 1952). "A peculiar form of peripheral neuropathy; familiar atypical generalized amyloidosis with special involvement of the peripheral nerves". Brain 75 (3): 408–27. doi:10.1093/brain/75.3.408. PMID 12978172.

[pmid8894411-12] Coelho T (October 1996). "Familial amyloid polyneuropathy: new developments in genetics and treatment". Curr. Opin. Neurol. 9 (5): 355–9. doi:10.1097/00019052-199610000-00007. PMID 8894411.

[pmid9017939-13] Jacobson DR, Pastore RD, Yaghoubian R, Kane I, Gallo G, Buck FS et al. (February 1997). "Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans". N. Engl. J. Med. 336 (7): 466–73. doi:10.1056/NEJM199702133360703. PMID 9017939.

[pmid1390650-14] Colon W, Kelly JW (September 1992). "Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro". Biochemistry 31 (36): 8654–60. doi:10.1021/bi00151a036. PMID 1390650.

[pmid8639594-15] Lai Z, Colón W, Kelly JW (May 1996). "The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid". Biochemistry 35 (20): 6470–82. doi:10.1021/bi952501g. PMID 8639594.

[pmid12560553-16] Hammarström P, Wiseman RL, Powers ET, Kelly JW (January 2003). "Prevention of transthyretin amyloid disease by changing protein misfolding energetics". Science 299 (5607): 713–6. doi:10.1126/science.1079589. PMID 12560553.

[pmid11560492-17] Jiang X, Smith CS, Petrassi HM, Hammarström P, White JT, Sacchettini JC et al. (September 2001). "An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured". Biochemistry 40 (38): 11442–52. doi:10.1021/bi011194d. PMID 11560492.

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