P02766 (TTHY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transthyretin

Alternative name(s):
ATTR
Prealbumin
TBPA

Gene names

Name:	TTR
Synonyms:	PALB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Ref.29
Subunit structure	Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4. Ref.42 Ref.45 Ref.46 Ref.51 Ref.54 Ref.55
Subcellular location	Secreted. Cytoplasm Ref.9 Ref.29.
Tissue specificity	Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver. Ref.9 Ref.29
Domain	Each monomer has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel.
Post-translational modification	Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway. Ref.33
Involvement in disease	Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.33 Ref.36 Ref.37 Ref.40 Ref.46 Ref.47 Ref.51 Ref.53 Ref.56 Ref.66 Ref.67 Ref.69 Ref.70 Ref.71 Ref.73 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.83 Ref.84 Ref.85 Ref.86 Ref.87 Ref.88 Ref.89 Ref.90 Ref.91 Ref.93 Ref.94 Ref.95 Ref.97 Ref.98 Ref.99 Ref.100 Ref.101 Ref.102 Ref.103 Ref.104 Ref.105 Ref.108 Ref.109 Ref.110 Ref.112 Ref.113 Ref.114 Ref.115 Ref.116 Ref.117 Ref.118 Ref.119 Ref.120 Ref.121 Ref.123 Ref.124 Ref.125 Ref.126 Ref.127 Ref.128 Ref.129 Ref.130 Hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE) [MIM:145680]: A condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: A condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.96
Miscellaneous	Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils. Two binding sites for thyroxine are located in the channel. Less than 1% of plasma prealbumin molecules are normally involved in thyroxine transport. L-thyroxine binds to the transthyretin by an order of magnitude stronger than does the triiodo-L-thyronine. Thyroxine-binding globulin is the major carrier protein for thyroid hormones in man. About 40% of plasma transthyretin circulates in a tight protein-protein complex with the plasma retinol-binding protein (RBP). The formation of the complex with RBP stabilizes the binding of retinol to RBP and decreases the glomerular filtration and renal catabolism of the relatively small RBP molecule. There is evidence for 2 binding sites for RBP, one possibly being a region that includes Ile-104, located on the outer surface of the transthyretin molecule.
Sequence similarities	Belongs to the transthyretin family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Amyloid Cytoplasm Secreted
Coding sequence diversity	Polymorphism
Disease	Amyloidosis Disease mutation Neuropathy
Domain	Signal
Molecular function	Hormone Thyroid hormone
PTM	Gamma-carboxyglutamic acid Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phototransduction, visible light Traceable author statement. Source: Reactome retinoid metabolic process Traceable author statement. Source: Reactome retinol metabolic process Inferred from electronic annotation. Source: Compara transport Non-traceable author statement PubMed 10841549. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	hormone binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Chain

21 – 147

127

Transthyretin

PRO_0000035755

Regions

Region

135 – 139

5

Thyroid hormone binding

Sites

Binding site

35

1

Thyroid hormones

Binding site

74

1

Thyroid hormones

Amino acid modifications

Modified residue

62

1

4-carboxyglutamate; in a patient with Moyamoya disease Ref.32

Glycosylation

118

1

N-linked (GlcNAc...) Ref.31 Ref.33

Natural variations

Natural variant

26

1

G → S Common polymorphism. Ref.16 Ref.90 Ref.108 Ref.119 Ref.125
Corresponds to variant rs1800458 [ dbSNP | Ensembl ].

VAR_007546

Natural variant

30

1

C → R in AMYL-TTR; amyloid polyneuropathy. Ref.83

VAR_007547

Natural variant

32

1

L → P in AMYL-TTR. Ref.112 Ref.128

VAR_038959

Natural variant

33

1

M → I. Ref.128

VAR_038960

Natural variant

38

1

D → E in AMYL-TTR; amyloid polyneuropathy.

VAR_007548

Natural variant

38

1

D → G in AMYL-TTR; leptomeningeal amyloidosis; leads to unfolding and exposure of N-118 to glycosylation by STT3B and subsequent degradation by the ERAD pathway. Ref.33 Ref.99

VAR_007549

Natural variant

40

1

V → I in AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome. Ref.101 Ref.128

VAR_007550

Natural variant

43

1

S → N in AMYL-TTR. Ref.109

VAR_038961

Natural variant

44

1

P → S in AMYL-TTR; amyloid polyneuropathy. Ref.128
Corresponds to variant rs11541790 [ dbSNP | Ensembl ].

VAR_007551

Natural variant

48

1

V → M in AMYL-TTR; amyloid polyneuropathy. Ref.116

VAR_010658

Natural variant

50

1

V → A in AMYL-TTR; amyloid polyneuropathy. Ref.80 Ref.128

VAR_007552

Natural variant

50

1

V → G in AMYL-TTR. Ref.100

VAR_038962

Natural variant

50

1

V → L in AMYL-TTR; amyloid polyneuropathy. Ref.78 Ref.110

VAR_007553

Natural variant

50

1

V → M in AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation. Ref.5 Ref.6 Ref.17 Ref.18 Ref.20 Ref.36 Ref.37 Ref.46 Ref.97 Ref.120 Ref.128
Corresponds to variant rs28933979 [ dbSNP | Ensembl ].

VAR_007554

Natural variant

53

1

F → C in a patient with amyloidosis. Ref.122 Ref.125

VAR_038963

Natural variant

53

1

F → I in AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy. Ref.66 Ref.90

VAR_007555

Natural variant

53

1

F → L in AMYL-TTR; amyloid polyneuropathy. Ref.22 Ref.75 Ref.120 Ref.128

VAR_007556

Natural variant

53

1

F → V in AMYL-TTR; amyloid polyneuropathy. Ref.110 Ref.120 Ref.124 Ref.128

VAR_038964

Natural variant

54

1

R → T in AMYL-TTR. Ref.102

VAR_038965

Natural variant

55

1

K → N in AMYL-TTR; amyloid polyneuropathy. Ref.97

VAR_038966

Natural variant

56

1

A → P in AMYL-TTR; amyloid polyneuropathy. Ref.128

VAR_007557

Natural variant

58

1

D → A in AMYL-TTR. Ref.110 Ref.119

VAR_038967

Natural variant

58

1

D → V in AMYL-TTR. Ref.120 Ref.129

VAR_038968

Natural variant

61

1

W → L in AMYL-TTR. Ref.119

VAR_038969

Natural variant

62

1

E → D in AMYL-TTR. Ref.103
Corresponds to variant rs11541796 [ dbSNP | Ensembl ].

VAR_038970

Natural variant

62

1

E → G in AMYL-TTR; amyloid polyneuropathy. Ref.23 Ref.71
Corresponds to variant rs11541796 [ dbSNP | Ensembl ].

VAR_007558

Natural variant

64

1

F → S in AMYL-TTR. Ref.107 Ref.119

VAR_038971

Natural variant

65

1

A → D in AMYL-TTR; amyloid cardiomyopathy.

VAR_007559

Natural variant

65

1

A → S in AMYL-TTR. Ref.115

VAR_038972

Natural variant

65

1

A → T in AMYL-TTR; amyloid cardiomyopathy. Ref.76 Ref.128

VAR_007560

Natural variant

67

1

G → A in AMYL-TTR; amyloid polyneuropathy. Ref.89 Ref.128

VAR_007561

Natural variant

67

1

G → E in AMYL-TTR. Ref.120 Ref.125

VAR_038973

Natural variant

67

1

G → R in AMYL-TTR; amyloid polyneuropathy. Ref.77

VAR_007562

Natural variant

67

1

G → V in AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome.

VAR_007563

Natural variant

69

1

T → A in AMYL-TTR; amyloid polyneuropathy. Ref.82 Ref.97 Ref.128

VAR_007564

Natural variant

69

1

T → I in AMYL-TTR. Ref.113 Ref.128

VAR_038974

Natural variant

70

1

S → I in AMYL-TTR; amyloid cardiomyopathy. Ref.79

VAR_007565

Natural variant

70

1

S → R in AMYL-TTR; amyloid polyneuropathy. Ref.71 Ref.97 Ref.110 Ref.130

VAR_007566

Natural variant

72

1

S → P in AMYL-TTR; amyloid polyneuropathy.

VAR_007567

Natural variant

73

1

G → E in AMYL-TTR. Ref.117

VAR_038975

Natural variant

74

1

E → G in AMYL-TTR; amyloid polyneuropathy.

VAR_007568

Natural variant

74

1

E → K in AMYL-TTR; early-onset amyloid polyneuropathy. Ref.123

VAR_038976

Natural variant

75

1

L → P in AMYL-TTR; amyloid polyneuropathy. Ref.40 Ref.56 Ref.81 Ref.95

VAR_007569

Natural variant

75

1

L → Q in AMYL-TTR. Ref.118

VAR_038977

Natural variant

78

1

L → H in AMYL-TTR; amyloid polyneuropathy. Ref.125

VAR_007570

Natural variant

78

1

L → R in AMYL-TTR; amyloid polyneuropathy. Ref.73

VAR_007571

Natural variant

79

1

T → K in AMYL-TTR; amyloid cardiomyopathy. Ref.98

VAR_007572

Natural variant

80

1

T → A in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. Ref.97 Ref.120 Ref.125 Ref.128

VAR_007573

Natural variant

81

1

E → G in AMYL-TTR. Ref.126

VAR_038978

Natural variant

81

1

E → K in AMYL-TTR; amyloid polyneuropathy. Ref.85

VAR_007574

Natural variant

84

1

F → L in AMYL-TTR; amyloid polyneuropathy. Ref.75 Ref.119 Ref.128

VAR_007575

Natural variant

88

1

I → L in AMYL-TTR; amyloid cardiomyopathy. Ref.86 Ref.128

VAR_007576

Natural variant

89

1

Y → H in AMYL-TTR; leptomeningeal amyloidosis; vitreous amyloid in some patients. Ref.121

VAR_007577

Natural variant

90

1

K → N in AMYL-TTR; amyloid polyneuropathy. Ref.84

VAR_007578

Natural variant

91

1

V → A in AMYL-TTR; amyloid polyneuropathy. Ref.87 Ref.88 Ref.128

VAR_007579

Natural variant

93

1

I → V in AMYL-TTR; amyloid polyneuropathy. Ref.105

VAR_007580

Natural variant

94

1

D → H.

VAR_007581

Natural variant

97

1

S → Y in AMYL-TTR; amyloid polyneuropathy. Ref.69 Ref.97 Ref.125 Ref.128

VAR_007582

Natural variant

98

1

Y → F in AMYL-TTR. Ref.51 Ref.56 Ref.128

VAR_038979

Natural variant

104

1

I → N in AMYL-TTR; vitrous amyloid. Ref.128

VAR_007583

Natural variant

104

1

I → S in AMYL-TTR; amyloid polyneuropathy; almost no RBP binding. Ref.67 Ref.92 Ref.128

VAR_007584

Natural variant

104

1

I → T in AMYL-TTR. Ref.128

VAR_038980

Natural variant

109

1

E → K in AMYL-TTR; amyloid polyneuropathy. Ref.114

VAR_010659

Natural variant

109

1

E → Q in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. Ref.82 Ref.97

VAR_007585

Natural variant

110

1

H → N. Ref.23 Ref.74

VAR_007586

Natural variant

111

1

A → S in AMYL-TTR; amyloid polyneuropathy. Ref.104

VAR_007587

Natural variant

114

1

V → A in a patient with amyloidosis. Ref.125 Ref.128

VAR_038981

Natural variant

117

1

A → G in AMYL-TTR; amyloid polyneuropathy. Ref.94 Ref.110 Ref.128

VAR_007588

Natural variant

117

1

A → S in AMYL-TTR. Ref.110

VAR_038982

Natural variant

121

1

G → S. Ref.106 Ref.128

VAR_007589

Natural variant

122

1

P → R.

VAR_007590

Natural variant

124

1

R → C.

VAR_007591

Natural variant

124

1

R → H. Ref.51 Ref.111

VAR_038983

Natural variant

126

1

T → N in AMYL-TTR. Ref.128

VAR_038984

Natural variant

127

1

I → M in AMYL-TTR. Ref.128

VAR_038985

Natural variant

127

1

I → V in AMYL-TTR; amyloid polyneuropathy. Ref.91 Ref.93 Ref.128

VAR_007592

Natural variant

129

1

A → T in HTDE; increased affinity for thyroxine. Ref.26 Ref.128

VAR_007593

Natural variant

131

1

L → M in AMYL-TTR. Ref.128

VAR_007594

Natural variant

134

1

Y → C in AMYL-TTR; amyloid polyneuropathy. Ref.47 Ref.53 Ref.70

VAR_007595

Natural variant

134

1

Y → H in CTS1; amyloid deposit on carpal tunnel; patients show no other abnormalities. Ref.96

VAR_007598

Natural variant

136

1

Y → S in AMYL-TTR; amyloid polyneuropathy. Ref.104

VAR_007596

Natural variant

136

1

Y → V Requires 2 nucleotide substitutions. Ref.68

VAR_007597

Natural variant

139

1

T → M in Chicago variant. Ref.46 Ref.72 Ref.119 Ref.128
Corresponds to variant rs28933981 [ dbSNP | Ensembl ].

VAR_007599

Natural variant

140

1

A → S in AMYL-TTR. Ref.120

VAR_038986

Natural variant

142

1

V → A in AMYL-TTR. Ref.108

VAR_038987

Natural variant

142

1

V → I in AMYL-TTR. Ref.19 Ref.120 Ref.128
Corresponds to variant rs28933980 [ dbSNP | Ensembl ].

VAR_007600

Natural variant

144

1

N → S in AMYL-TTR. Ref.127

VAR_038988

Experimental info

Mutagenesis

107

1

F → M: Loss of tetramerization; when associated with M-130. Ref.45

Mutagenesis

130

1

L → M: Loss of tetramerization; when associated with M-107. Ref.45

Sequence conflict

41

1

R → P in AAA98771. Ref.3

Sequence conflict

147

1

E → D in CAG33189. Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Turn

23 – 26

4

Beta strand

32 – 38

7

Turn

39 – 42

4

Beta strand

49 – 55

7

Beta strand

57 – 59

3

Beta strand

61 – 68

8

Beta strand

73 – 75

3

Beta strand

77 – 80

4

Turn

81 – 83

3

Beta strand

86 – 93

8

Helix

95 – 101

7

Beta strand

107 – 118

12

Beta strand

119 – 121

3

Beta strand

124 – 132

9

Beta strand

135 – 143

9

Sequences

	Sequence		Length	Mass (Da)
	P02766 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: 3A6AEBCBBA56BC44	FASTA	147	15,887
	10 20 30 40 50 60 MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT 70 80 90 100 110 120 WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS 130 140 GPRRYTIAAL LSPYSYSTTA VVTNPKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of cDNA for human prealbumin." Mita S., Maeda S., Shimada K., Araki S. Biochem. Biophys. Res. Commun. 124:558-564(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Localization of the human prealbumin gene to chromosome 18." Wallace M.R., Naylor S.L., Kluve-Beckerman B., Long G.L., McDonald L., Shows T.B., Benson M.D. Biochem. Biophys. Res. Commun. 129:753-758(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of the chromosomal gene for human serum prealbumin." Sasaki H., Yoshioka N., Takagi Y., Sakaki Y. Gene 37:191-197(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Structure of the human prealbumin gene." Tsuzuki T., Mita S., Maeda S., Araki S., Shimada K. J. Biol. Chem. 260:12224-12227(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Analyses of prealbumin mRNAs in individuals with familial amyloidotic polyneuropathy." Mita S., Maeda S., Shimada K., Araki S. J. Biochem. 100:1215-1222(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AMYL-TTR MET-50.
[6]	"Structure and expression of the mutant prealbumin gene associated with familial amyloidotic polyneuropathy." Maeda S., Mita S., Araki S., Shimada K. Mol. Biol. Med. 3:329-338(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMYL-TTR MET-50. Tissue: Liver.
[7]	"The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis." Christmanson L., Betsholtz C., Gustavsson A., Johansson B., Sletten K., Westermark P. FEBS Lett. 281:177-180(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-28. Tissue: Liver.
[8]	"Transthyretin (prealbumin) gene in human primary hepatic cancer." Gu J.R., Jiang H.Q., He L.P., Li D.Z., Zhou X.M., Dai W.L., Qian L.F., Chen Y.Q., Schweinfest C., Papas T. Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 34:1312-1318(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[9]	"Transthyretin localization in cultured and native human retinal pigment epithelium." Getz R.K., Kennedy B.G., Mangini N.J. Exp. Eye Res. 68:629-636(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Retina.
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Corpus callosum.
[11]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[13]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[15]	"The amino acid sequence of human plasma prealbumin." Kanda Y., Goodman D.S., Canfield R.E., Morgan F.J. J. Biol. Chem. 249:6796-6805(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147.
[16]	"Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin." Pras M., Prelli F., Franklin E.C., Frangione B. Proc. Natl. Acad. Sci. U.S.A. 80:539-542(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 21-147, VARIANT SER-26.
[17]	"Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type)." Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S. Biochem. Biophys. Res. Commun. 116:880-888(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[18]	"Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin." Dwulet F.E., Benson M.D. Proc. Natl. Acad. Sci. U.S.A. 81:694-698(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[19]	"Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin." Cornwell G.G. III, Sletten K., Johansson B., Westermark P. Biochem. Biophys. Res. Commun. 154:648-653(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR ILE-142.
[20]	"Characterization of a transthyretin-related amyloid fibril protein from cerebral amyloid angiopathy in type I familial amyloid polyneuropathy." Kametani F., Ikeda S., Yanagisawa N., Ishi T., Hanyu N. J. Neurol. Sci. 108:178-183(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[21]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41. Tissue: Platelet.
[22]	"A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy." Harding J., Skare J., Skinner M. Biochim. Biophys. Acta 1097:183-186(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR LEU-53.
[23]	"Two transthyretin mutations (Glu42Gly, His90Asn) in an Italian family with amyloidosis." Skare J.C., Jones L.A., Myles N., Kane K., Milunsky A., Cohen A.S., Skinner M. Clin. Genet. 45:281-284(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR GLY-62, VARIANT ASN-110.
[24]	"Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat." Soprano D.R., Herbert J., Soprano K.J., Schon E.A., Goodman D.S. J. Biol. Chem. 260:11793-11798(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
[25]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 42-68; 101-123 AND 125-146, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[26]	"A point mutation in transthyretin increases affinity for thyroxine and produces euthyroid hyperthyroxinemia." Moses A.C., Rosen H.N., Moller D.E., Tsuzaki S., Haddow J.E., Lawlor J., Liepnieks J.J., Nichols W.C., Benson M.D. J. Clin. Invest. 86:2025-2033(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, VARIANT HTDE THR-129.
[27]	"Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis." Gustavsson A., Jahr H., Tobiassen R., Jacobson D.R., Sletten K., Westermark P. Lab. Invest. 73:703-708(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[28]	"Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?" Blake C.C.F., Oatley S.J. Nature 268:115-120(1977) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING SITES FOR THYROID HORMONES.
[29]	"Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S. Weir Mitchell award." Herbert J., Wilcox J.N., Pham K.T., Fremeau R.T. Jr., Zeviani M., Dwork A., Soprano D.R., Makover A., Goodman D.S., Zimmerman E.A., Roberts J.L., Schon E.A. Neurology 36:900-911(1986) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[30]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Plasma.
[31]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118, MASS SPECTROMETRY. Tissue: Plasma.
[32]	"Detection of a gamma-carboxy-glutamate as novel post-translational modification of human transthyretin." Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T. Protein Pept. Lett. 15:43-46(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GAMMA-CARBOXYGLUTAMATION AT GLU-62, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[33]	"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms." Ruiz-Canada C., Kelleher D.J., Gilmore R. Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-118, CHARACTERIZATION OF VARIANT AMYL-TTR GLY-38.
[34]	"Structure of human plasma prealbumin at 2.5-A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding." Blake C.C.F., Geisow M.J., Swan I.D.A., Rerat C., Rerat B. J. Mol. Biol. 88:1-12(1974) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[35]	"Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A." Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C. J. Mol. Biol. 121:339-356(1978) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[36]	"Structure of Met30 variant of transthyretin and its amyloidogenic implications." Terry C.J., Damas A.M., Oliveira P., Saraiva M.J.M., Alves I.L., Costa P.P., Matias P.M., Sakaki Y., Blake C.C.F. EMBO J. 12:735-741(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
[37]	"The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution." Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D., Holmgren G., Sandgren O., Steen L. J. Biol. Chem. 268:2416-2424(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
[38]	"Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein." Monaco H.L., Rizzi M., Coda A. Science 268:1039-1041(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
[39]	"Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation." Schormann N., Murrell J.R., Benson M.D. Amyloid 5:175-187(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
[40]	"The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils." Sebastiao M.P., Saraiva M.J., Damas A.M. J. Biol. Chem. 273:24715-24722(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PRO-75.
[41]	"Inhibiting transthyretin conformational changes that lead to amyloid fibril formation." Peterson S.A., Klabunde T., Lashuel H.A., Purkey H., Sacchettini J.C., Kelly J.W. Proc. Natl. Acad. Sci. U.S.A. 95:12956-12960(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[42]	"The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP." Naylor H.M., Newcomer M.E. Biochemistry 38:2647-2653(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP4, SUBUNIT.
[43]	"A comparative analysis of 23 structures of the amyloidogenic protein transthyretin." Hoernberg A., Eneqvist T., Olofsson A., Lundgren E., Sauer-Eriksson A.E. J. Mol. Biol. 302:649-669(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147.
[44]	"Rational design of potent human transthyretin amyloid disease inhibitors." Klabunde T., Petrassi H.M., Oza V.B., Raman P., Kelly J.W., Sacchettini J.C. Nat. Struct. Biol. 7:312-321(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[45]	"An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured." Jiang X., Smith C.S., Petrassi H.M., Hammarstroem P., White J.T., Sacchettini J.C., Kelly J.W. Biochemistry 40:11442-11452(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-147, MUTAGENESIS OF PHE-107 AND LEU-130, MASS SPECTROMETRY, FORMATION OF AMYLOID FIBERS AT ACIDIC PH, SUBUNIT.
[46]	"Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution." Sebastiao M.P., Lamzin V., Saraiva M.J., Damas A.M. J. Mol. Biol. 306:733-744(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 30-144 OF VARIANT AMYL-TTR MET-50 AND VARIANT CHICAGO MET-139 IN COMPLEX WITH L-THYROXINE, SUBUNIT.
[47]	"Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro." Eneqvist T., Olofsson A., Ando Y., Miyakawa T., Katsuragi S., Jass J., Lundgren E., Sauer-Eriksson A.E. Biochemistry 41:13143-13151(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134.
[48]	"Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis, evaluation, and mechanism of action." Razavi H., Palaninathan S.K., Powers E.T., Wiseman R.L., Purkey H.E., Mohamedmohaideen N.N., Deechongkit S., Chiang K.P., Dendle M.T.A., Sacchettini J.C., Kelly J.W. Angew. Chem. Int. Ed. 42:2758-2761(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147IN COMPLEX WITH AMYLOIDOGENESIS INHIBITORS.
[49]	"Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization." Green N.S., Palaninathan S.K., Sacchettini J.C., Kelly J.W. J. Am. Chem. Soc. 125:13404-13414(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 21-147 IN COMPLEX WITH AMYLOIDOGENESIS INHIBITORS, FIBRIL FORMATION.
[50]	"Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis." Adamski-Werner S.L., Palaninathan S.K., Sacchettini J.C., Kelly J.W. J. Med. Chem. 47:355-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147 IN COMPLEX WITH DIFLUNISAL ANALOGS, INHIBITION OF AMYLOID FORMATION.
[51]	"X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis." Neto-Silva R.M., Macedo-Ribeiro S., Pereira P.J.B., Coll M., Saraiva M.J., Damas A.M. Acta Crystallogr. D 61:333-339(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PHE-98 AND VARIANT HIS-124, SUBUNIT.
[52]	"The effect of iodide and chloride on transthyretin structure and stability." Hoernberg A., Hultdin U.W., Olofsson A., Sauer-Eriksson A.E. Biochemistry 44:9290-9299(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEXES WITH CHLORIDE AND IODIDE IONS.
[53]	"Cys114-linked dimers of transthyretin are compatible with amyloid formation." Karlsson A., Olofsson A., Eneqvist T., Sauer-Eriksson A.E. Biochemistry 44:13063-13070(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134.
[54]	"Kinetic stabilization of an oligomeric protein by a single ligand binding event." Wiseman R.L., Johnson S.M., Kelker M.S., Foss T., Wilson I.A., Kelly J.W. J. Am. Chem. Soc. 127:5540-5551(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-147 IN COMPLEX WITH THYROID HORMONE ANALOG, SUBUNIT.
[55]	"Kinetic stabilization of the native state by protein engineering: implications for inhibition of transthyretin amyloidogenesis." Foss T.R., Kelker M.S., Wiseman R.L., Wilson I.A., Kelly J.W. J. Mol. Biol. 347:841-854(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 31-147, SUBUNIT.
[56]	"The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin." Morais-de-Sa E., Neto-Silva R.M., Pereira P.J.B., Saraiva M.J., Damas A.M. Acta Crystallogr. D 62:512-519(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND VARIANTS AMYL-TTR PRO-75 AND PHE-98.
[57]	"Structural basis for the protective role of sulfite against transthyretin amyloid formation." Gales L., Saraiva M.J., Damas A.M. Biochim. Biophys. Acta 1774:59-64(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-147.
[58]	"Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin." Pasquato N., Berni R., Folli C., Alfieri B., Cendron L., Zanotti G. J. Mol. Biol. 366:711-719(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147.
[59]	"Iodination of salicylic acid improves its binding to transthyretin." Gales L., Almeida M.R., Arsequell G., Valencia G., Saraiva M.J., Damas A.M. Biochim. Biophys. Acta 1784:512-517(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 IN COMPLEX WITH 3,5-DIIODOSALICYLIC ACID, THYROXINE BINDING.
[60]	"Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein." Zanotti G., Folli C., Cendron L., Alfieri B., Nishida S.K., Gliubich F., Pasquato N., Negro A., Berni R. FEBS J. 275:5841-5854(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 21-147 IN COMPLEX WITH RBP4.
[61]	"Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors." Johnson S.M., Connelly S., Wilson I.A., Kelly J.W. J. Med. Chem. 51:260-270(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147 IN COMPLEX WITH 2-ARYLBENZOXAZOLE-BASED TRANSTHYRETIN AMYLOIDOGENESIS INHIBITORS.
[62]	"Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies." Johnson S.M., Connelly S., Wilson I.A., Kelly J.W. J. Med. Chem. 51:6348-6358(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-147 IN COMPLEX WITH BISARYL AMYLOIDOGENESIS INHIBITORS.
[63]	"Structural insight into pH-induced conformational changes within the native human transthyretin tetramer." Palaninathan S.K., Mohamedmohaideen N.N., Snee W.C., Kelly J.W., Sacchettini J.C. J. Mol. Biol. 382:1157-1167(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 21-147 AT PH 3.5 AND 4.5.
[64]	"Crystal structure of the F87M/L110M mutant of human transthyretin at pH 4.6 soaked." Mycobacterium tuberculosis structural genomics consortium (TB) Submitted (JUL-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-147.
[65]	"Transthyretin mutations in health and disease." Saraiva M.J.M. Hum. Mutat. 5:191-196(1995) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[66]	"Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin." Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S. Biochem. Biophys. Res. Commun. 123:921-928(1984) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ILE-53.
[67]	"Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis." Wallace M.R., Dwulet F.E., Conneally P.M., Benson M.D. J. Clin. Invest. 78:6-12(1986) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR SER-104.
[68]	"Identification and characterization of a human transthyretin variant." Strahler J.R., Rosenblum B.B., Hanash S.M. Biochem. Biophys. Res. Commun. 148:471-477(1987) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-136.
[69]	"Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis." Wallace M.R., Dwulet F.E., Williams E.C., Conneally P.M., Benson M.D. J. Clin. Invest. 81:189-193(1988) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR TYR-97.
[70]	"A novel variant of transthyretin (Tyr114 to Cys) deduced from the nucleotide sequences of gene fragments from familial amyloidotic polyneuropathy in Japanese sibling cases." Ueno S., Uemichi T., Yorifuji S., Tarui S. Biochem. Biophys. Res. Commun. 169:143-147(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR CYS-134.
[71]	"Two novel variants of transthyretin identified in Japanese cases with familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and transthyretin (Ser50 to Arg)." Ueno S., Uemichi T., Takahashi N., Soga F., Yorifuji S., Tarui S. Biochem. Biophys. Res. Commun. 169:1117-1121(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR GLY-62 AND ARG-70.
[72]	"Biochemical and clinical characterization of prealbuminCHICAGO: an apparently benign variant of serum prealbumin (transthyretin) discovered with high-resolution two-dimensional electrophoresis." Harrison H.H., Gordon E.D., Nichols W.C., Benson M.D. Am. J. Med. Genet. 39:442-452(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CHICAGO MET-139.
[73]	"New mutant gene (transthyretin Arg 58) in cases with hereditary polyneuropathy detected by non-isotope method of single-strand conformation polymorphism analysis." Saeki Y., Ueno S., Yorifuji S., Sugiyama Y., Ide Y., Matsuzawa Y. Biochem. Biophys. Res. Commun. 180:380-385(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ARG-78.
[74]	"A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90." Skare J.C., Milunsky J.M., Milunsky A., Skare I.B., Cohen A.S., Skinner M. Clin. Genet. 39:6-12(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASN-110.
[75]	"Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two novel point mutations." Li S., Minnerath S., Li K., Dyck P.J., Sommer S.S. Neurology 41:893-898(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR LEU-53 AND LEU-84.
[76]	"A new transthyretin mutation associated with amyloid cardiomyopathy." Saraiva M.J.M., Almeida M.R., Sherman W., Gawinowicz M., Costa P., Costa P.P., Goodman D.S. Am. J. Hum. Genet. 50:1027-1030(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR THR-65.
[77]	"A novel transthyretin mutation associated with familial amyloidotic polyneuropathy." Murakami T., Maeda S., Yi S., Ikegawa S., Kawashima E., Onodera S., Shimada K., Araki S. Biochem. Biophys. Res. Commun. 182:520-526(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ARG-67.
[78]	"A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy." Murakami T., Atsumi T., Maeda S., Tanase S., Ishikawa K., Mita S., Kumamoto T., Araki S., Ando M. Biochem. Biophys. Res. Commun. 187:397-403(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LEU-50.
[79]	"Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac amyloidosis." Nishi H., Kimura A., Harada H., Hayashi Y., Nakamura M., Sasazuki T. Biochem. Biophys. Res. Commun. 187:460-466(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ILE-70.
[80]	"Familial amyloidotic polyneuropathy: a new transthyretin position 30 mutation (alanine for valine) in a family of German descent." Jones L.A., Skare J.C., Cohen A.S., Harding J.A., Milunsky A., Skinner M. Clin. Genet. 41:70-73(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ALA-50.
[81]	"Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement." Jacobson D.R., McFarlin D.E., Kane I., Buxbaum J.N. Hum. Genet. 89:353-356(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR PRO-75.
[82]	"Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian kindreds with hereditary amyloidosis." Almeida M.R., Ferlini A., Forabosco A., Gawinowicz M.A., Costa P.P., Salvi F., Plasmati R., Tassinari C.A., Altland K., Saraiva M.J. Hum. Mutat. 1:211-215(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR ALA-69 AND GLN-109.
[83]	"A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy." Uemichi T., Murrel J.R., Zeldenrust S., Benson M.D. J. Med. Genet. 29:888-891(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ARG-30.
[84]	"Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome and a new transthyretin mutation, asparagine 70." Izumoto S., Younger D., Hays A.P., Martone R.L., Smith R.T., Herbert J. Neurology 42:2094-2102(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ASN-90.
[85]	"A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced mutation restriction analysis." Shiomi K., Nakazato M., Matsukura S., Ohnishi A., Hatanaka H., Tsuji S., Murai Y., Kojima M., Kangawa K., Matsuo H. Biochem. Biophys. Res. Commun. 194:1090-1096(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LYS-81.
[86]	"Cardiac amyloidosis: a review and report of a new transthyretin (prealbumin) variant." Hesse A., Altland K., Linke R.P., Almeida M.R., Saraiva M.J.M., Steinmetz A., Maisch B. Br. Heart J. 70:111-115(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LEU-88.
[87]	"Transthyretin Ala-71: a new transthyretin variant in a Spanish family with familial amyloidotic polyneuropathy." Almeida M.R., Lopez-Andreu F., Munar-Ques M., Costa P.P., Saraiva M.J. Hum. Mutat. 2:420-421(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ALA-91.
[88]	"A transthyretin variant (alanine 71) associated with familial amyloidotic polyneuropathy in a French family." Benson M.D. II, Turpin J.C., Lucotte G., Zeldenrust S., Lechevalier B., Benson M.D. J. Med. Genet. 30:120-122(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ALA-91.
[89]	"Gly47Ala: a new transthyretin gene mutation in hereditary amyloidosis TTR-related." Ferlini A., Salvi F., Patrosso C., Fini S., Vezzoni P., Forbasco A. J. Rheumatol. 20:187-187(1993) Cited for: VARIANT AMYL-TTR ALA-67.
[90]	"A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli patient 'SKO' with familial amyloidotic polyneuropathy." Jacobson D.R., Buxbaum J.N. Hum. Mutat. 3:254-260(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-26, VARIANT AMYL-TTR ILE-53.
[91]	"Transthyretin VAL107, a new variant associated with familial cardiac and neuropathic amyloidosis." Jacobson D., Gertz M.A., Buxbaum J.N. Hum. Mutat. 3:399-401(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR VAL-127.
[92]	"The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein." Berni R., Malpeli G., Folli C., Murrell J.R., Liepnieks J.J., Benson M.D. J. Biol. Chem. 269:23395-23398(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-104, RBP BINDING STUDIES.
[93]	"Amyloid polyneuropathy in two German-American families: a new transthyretin variant (Val 107)." Uemichi T., Gertz M.A., Benson M.D. J. Med. Genet. 31:416-417(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR VAL-127.
[94]	"Familial amyloidotic polyneuropathy with late-onset and well-preserved autonomic function: a Japanese kindred with novel mutant transthyretin (Ala97 to Gly)." Yasuda T., Sobue G., Doyu M., Nakazato M., Shiomi K., Yanagi T., Mitsuma T. J. Neurol. Sci. 121:97-102(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLY-117.
[95]	"Familial amyloid polyneuropathy in Taiwan: identification of transthyretin variant (Leu55-->Pro)." Yamamoto K., Hsu S.P., Yoshida K., Ikeda S., Nakazato M., Shiomi K., Cheng S.Y., Furihata K., Ueno I., Yanagisawa N. Muscle Nerve 17:637-641(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR PRO-75.
[96]	"Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114 variant." Murakami T., Tachibana S., Endo Y., Kawai R., Hara M., Tanase S., Ando M. Neurology 44:315-318(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CTS1 HIS-134.
[97]	"Transthyretin gene analysis in European patients with suspected familial amyloid polyneuropathy." Reilly M.M., Adams D., Booth D.R., Davis M.B., Said G., Laubriat-Bianchin M., Pepys M.B., Thomas P.K., Harding A.E. Brain 118:849-856(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND GLN-109.
[98]	"A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family." Booth D.R., Tan S.Y., Hawkins P.N., Pepys M.B., Frustaci A. Circulation 91:962-967(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LYS-79.
[99]	"Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD 18G)." Vidal R., Garzuly F., Budka H., Lalowski M., Linke R.P., Brittig F., Frangione B., Wisniewski T. Am. J. Pathol. 148:361-366(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLY-38.
[100]	"Transthyretin amyloidosis: a new mutation associated with dementia." Petersen R.B., Goren H., Cohen M., Richardson S.L., Tresser N., Lynn A., Gali M., Estes M., Gambetti P. Ann. Neurol. 41:307-313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLY-50.
[101]	"Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis." Jacobson D.R., Pan T., Kyle R.A., Buxbaum J.N. Hum. Mutat. 9:83-85(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ILE-40.
[102]	"Novel transthyretin missense mutation (Thr34) in an Italian family with hereditary amyloidosis." Patrosso M.C., Salvi F., De Grandis D., Vezzoni P., Jacobson D.R., Ferlini A. Am. J. Med. Genet. 77:135-138(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR THR-54.
[103]	"A novel variant of transthyretin (Glu42Asp) associated with sporadic late-onset cardiac amyloidosis." Dupuy O., Bletry O., Blanc A.S., Droz D., Viemont M., Delpech M., Grateau G. Amyloid 5:285-287(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ASP-62.
[104]	"New transthyretin variants Ser 91 and Ser 116 associated with familial amyloidotic polyneuropathy." Misrahi A.M., Plante V., Lalu T., Serre I., Adams D., Lacroix D.C., Said G. Hum. Mutat. 12:71-71(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR SER-111 AND SER-136.
[105]	"Transthyretin Ile73Val is associated with familial amyloidotic polyneuropathy in a Bangladeshi family." Booth D.R., Gillmore J.D., Persey M.R., Booth S.E., Cafferty K.D., Tennent G.A., Madhoo S., Cochrane S.W., Whitehead T.C., Pasvol G., Hawkins P.N. Hum. Mutat. 12:135-135(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR VAL-93.
[106]	"A new nonamyloid transthyretin variant, G101S, detected by electrospray ionization/mass spectrometry." Kishikawa M., Nakanishi T., Miyazaki A., Hatanaka M., Shimizu A., Tamoto S., Ohsawa N., Hayashi H., Kanai M. Hum. Mutat. 12:363-363(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-121, MASS SPECTROMETRY.
[107]	"Transthyretin amyloidosis (serine 44) with headache, hearing loss, and peripheral neuropathy." Klein C.J., Nakumura M., Jacobson D.R., Lacy M.Q., Benson M.D., Petersen R.C. Neurology 51:1462-1464(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-64.
[108]	"A new amyloidogenic transthyretin variant (Val122Ala) found in a compound heterozygous patient." Theberge R., Connors L., Skare J., Skinner M., Falk R.H., Costello C.E. Amyloid 6:54-58(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ALA-142, VARIANT SER-26, MASS SPECTROMETRY.
[109]	"A new transthyretin variant (Ser23Asn) associated with familial amyloidosis in a Portuguese patient." Connors L.H., Theberge R., Skare J., Costello C.E., Falk R.H., Skinner M. Amyloid 6:114-118(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ASN-43, MASS SPECTROMETRY.
[110]	"Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum variant transthyretin in the diagnosis of familial amyloid polyneuropathy." Tachibana N., Tokuda T., Yoshida K., Taketomi T., Nakazato M., Li Y.F., Masuda Y., Ikeda S. Amyloid 6:282-288(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117, MASS SPECTROMETRY.
[111]	"A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with high serum transthyretin (TTR) and retinol binding protein (RBP) levels." Terazaki H., Ando Y., Misumi S., Nakamura M., Ando E., Matsunaga N., Shoji S., Okuyama M., Ideta H., Nakagawa K., Ishizaki T., Ando M., Saraiva M.J. Biochem. Biophys. Res. Commun. 264:365-370(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-124, MASS SPECTROMETRY.
[112]	"Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis." Brett M., Persey M.R., Reilly M.M., Revesz T., Booth D.R., Booth S.E., Hawkins P.N., Pepys M.B., Morgan-Hughes J.A. Brain 122:183-190(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR PRO-32.
[113]	"Identification of a new transthyretin variant (Ile49) in familial amyloidotic polyneuropathy using electrospray ionization mass spectrometry and nonisotopic RNase cleavage assay." Nakamura M., Yamashita T., Ando Y., Hamidi Asl K., Tashima K., Ohlsson P., Kususe Y., Benson M.D. Hum. Hered. 49:186-189(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ILE-69, MASS SPECTROMETRY.
[114]	"A novel variant of transthyretin (Glu89Lys) associated with familial amyloidotic polyneuropathy." Nakamura M., Hamidi Asl K., Benson M.D. Amyloid 7:46-50(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LYS-109.
[115]	"Heart failure caused by a novel amyloidogenic mutation of the transthyretin gene: ATTR Ala45Ser." Janunger T., Anan I., Holmgren G., Lovheim O., Ohlsson P.I., Suhr O.B., Tashima K. Amyloid 7:137-140(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR SER-65, MASS SPECTROMETRY.
[116]	"New transthyretin mutation V28M in a Portuguese kindred with amyloid polyneuropathy." de Carvalho M., Moreira P., Evangelista T., Ducla-Soares J.L., Bento M., Fernandes R., Saraiva M.J. Muscle Nerve 23:1016-1021(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR MET-48.
[117]	"Recurrent subarachnoid hemorrhage associated with a new transthyretin variant (Gly53Glu)." Ellie E., Camou F., Vital A., Rummens C., Grateau G., Delpech M., Valleix S. Neurology 57:135-137(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLU-73.
[118]	"A new transthyretin variant Leu55Gln in a patient with systemic amyloidosis." Yazaki M., Varga J., Dyck P.J., Benson M.D. Amyloid 9:268-271(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLN-75.
[119]	"Characterization of transthyretin variants in familial transthyretin amyloidosis by mass spectrometric peptide mapping and DNA sequence analysis." Lim A., Prokaeva T., McComb M.E., O'Connor P.B., Theberge R., Connors L.H., Skinner M., Costello C.E. Anal. Chem. 74:741-751(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-26 AND MET-139, VARIANTS AMYL-TTR ALA-58; LEU-61; SER-64 AND LEU-84, MASS SPECTROMETRY.
[120]	"Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis." Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A., Gillmore J.D., Pepys M.B., Hawkins P.N. N. Engl. J. Med. 346:1786-1791(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140 AND ILE-142.
[121]	"Oculoleptomeningeal amyloidosis in a large kindred with a new transthyretin variant Tyr69His." Blevins G., Macaulay R., Harder S., Fladeland D., Yamashita T., Yazaki M., Hamidi Asl K., Benson M.D., Donat J.R. Neurology 60:1625-1630(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR HIS-89.
[122]	"Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosis." Lim A., Prokaeva T., McComb M.E., Connors L.H., Skinner M., Costello C.E. Protein Sci. 12:1775-1785(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CYS-53, MASS SPECTROMETRY.
[123]	"A severe form of amyloidotic polyneuropathy in a Costa Rican family with a rare transthyretin mutation (Glu54Lys)." Busse A., Sanchez M.A., Monterroso V., Alvarado M.V., Leon P. Am. J. Med. Genet. A 128:190-194(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR LYS-74.
[124]	"An unusual transthyretin gene missense mutation (TTR Phe33Val) linked to familial amyloidotic polyneuropathy." Frigerio R., Fabrizi G.M., Ferrarini M., Cavallaro T., Brighina L., Santoro P., Agostoni E., Cavaletti G., Rizzuto N., Ferrarese C. Amyloid 11:121-124(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR VAL-53.
[125]	"Identification of transthyretin variants by sequential proteomic and genomic analysis." Bergen H.R. III, Zeldenrust S.R., Butz M.L., Snow D.S., Dyck P.J., Dyck P.J.B., Klein C.J., O'Brien J.F., Thibodeau S.N., Muddiman D.C. Clin. Chem. 50:1544-1552(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL-TTR GLU-67; HIS-78; ALA-80 AND TYR-97, MASS SPECTROMETRY.
[126]	"A new transthyretin variant (Glu61Gly) associated with cardiomyopathy." Rosenzweig M., Skinner M., Prokaeva T., Theberge R., Costello C., Drachman B.M., Connors L.H. Amyloid 14:65-71(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR GLY-81.
[127]	"A novel type of familial transthyretin amyloidosis, ATTR Asn124Ser, with co-localization of kappa light chains." Bergstroem J., Patrosso M.C., Colussi G., Salvadore M., Penco S., Lando G., Marocchi A., Ueda A., Nakamura M., Ando Y. Amyloid 14:141-145(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR SER-144.
[128]	"Genetic microheterogeneity of human transthyretin detected by IEF." Altland K., Benson M.D., Costello C.E., Ferlini A., Hazenberg B.P.C., Hund E., Kristen A.V., Linke R.P., Merlini G., Salvi F., Saraiva M.J., Singer R., Skinner M., Winter P. Electrophoresis 28:2053-2064(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53; VAL-53; PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84; LEU-88; ALA-91; TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114; GLY-117; ASN-126; MET-127; VAL-127; MET-131 AND ILE-142, VARIANTS ILE-33; SER-121 AND THR-129, VARIANT CHICAGO MET-139.
[129]	"Familial amyloidosis in a large Spanish kindred resulting from a D38V mutation in the transthyretin gene." Augustin S., Llige D., Andreu A., Gonzalez A., Genesca J. Eur. J. Clin. Invest. 37:673-678(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR VAL-58.
[130]	"Delayed diagnosis of transthyretin amyloidosis with a novel mutation (c.210T>A) in the transthyretin gene." Dekmezian M.S., Tschen J.A., Cho-Vega J.H. J. Am. Acad. Dermatol. 68:E49-E51(2013) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMYL-TTR ARG-70.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Transthyretin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

K02091 mRNA. Translation: AAA60011.1.
M10605 mRNA. Translation: AAA60012.1.
M11518 Genomic DNA. Translation: AAA98771.1.
M11844 Genomic DNA. Translation: AAA60013.1.
X59498 mRNA. Translation: CAA42087.1.
D00096 mRNA. Translation: BAA00059.1.
M15517, M15515, M15516 Genomic DNA. Translation: AAA60018.1.
U19780 mRNA. Translation: AAA73473.1.
AF162690 mRNA. Translation: AAD45014.1.
AK312051 mRNA. Translation: BAG34987.1.
BT007189 mRNA. Translation: AAP35853.1.
CR456908 mRNA. Translation: CAG33189.1.
CH471088 Genomic DNA. Translation: EAX01264.1.
BC005310 mRNA. Translation: AAH05310.1.
BC020791 mRNA. Translation: AAH20791.1.
S63185 Genomic DNA. Translation: AAD14937.2.
S72385 Genomic DNA. Translation: AAD14098.1.
M11714 mRNA. Translation: AAA61181.1.
M63285 Genomic DNA. Translation: AAA36784.1.

IPI

IPI00022432.

PIR

VBHU. A91532.

RefSeq

NP_000362.1. NM_000371.3.

UniGene

Hs.427202.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BM7	X-ray	2.00	A/B	21-147	[»]
1BMZ	X-ray	2.00	A/B	21-147	[»]
1BZ8	X-ray	2.00	A/B	21-141	[»]
1BZD	X-ray	1.90	A/B	21-147	[»]
1BZE	X-ray	1.80	A/B	21-147	[»]
1DVQ	X-ray	2.00	A/B	21-144	[»]
1DVS	X-ray	2.00	A/B	21-144	[»]
1DVT	X-ray	1.90	A/B	21-144	[»]
1DVU	X-ray	1.90	A/B	21-144	[»]
1DVX	X-ray	2.00	A/B	21-144	[»]
1DVY	X-ray	1.90	A/B	21-144	[»]
1DVZ	X-ray	1.90	A/B	21-144	[»]
1E3F	X-ray	1.90	A/B	21-145	[»]
1E4H	X-ray	1.80	A/B	21-147	[»]
1E5A	X-ray	1.80	A/B	21-147	[»]
1ETA	X-ray	1.70	1/2	21-147	[»]
1ETB	X-ray	1.70	1/2	21-147	[»]
1F41	X-ray	1.30	A/B	21-147	[»]
1F64	model	-	A	21-147	[»]
1F86	X-ray	1.10	A/B	30-144	[»]
1FH2	X-ray	1.80	A/B	21-147	[»]
1FHN	X-ray	1.75	A/B	21-147	[»]
1G1O	X-ray	2.30	A/B/C/D	21-147	[»]
1GKO	X-ray	2.10	A/B/C/D	21-147	[»]
1ICT	X-ray	3.00	A/B/C/D/E/F/G/H	21-147	[»]
1III	X-ray	2.00	A/B	21-147	[»]
1IIK	X-ray	2.00	A/B	21-147	[»]
1IJN	X-ray	1.70	A/B	21-147	[»]
1QAB	X-ray	3.20	A/B/C/D	21-147	[»]
1QWH	X-ray	1.36	A/B	31-147	[»]
1RLB	X-ray	3.10	A/B/C/D	21-147	[»]
1SOK	X-ray	1.60	A/B	21-147	[»]
1SOQ	X-ray	2.10	A/B/C/D	21-147	[»]
1THA	X-ray	2.00	A/B	21-147	[»]
1THC	X-ray	2.30	A/B	21-147	[»]
1TLM	X-ray	1.90	A/B	21-147	[»]
1TSH	X-ray	1.70	A/B	21-147	[»]
1TT6	X-ray	1.80	A/B	21-147	[»]
1TTA	X-ray	1.70	A/B	21-147	[»]
1TTB	X-ray	1.70	A/B	21-147	[»]
1TTC	X-ray	1.70	A/B	21-147	[»]
1TTR	X-ray	1.90	A/B	21-147	[»]
1TYR	X-ray	1.80	A/B	21-147	[»]
1TZ8	X-ray	1.85	A/B/C/D	21-147	[»]
1U21	X-ray	1.69	A/B	21-147	[»]
1X7S	X-ray	1.55	A/B	21-147	[»]
1X7T	X-ray	1.60	A/B	21-147	[»]
1Y1D	X-ray	1.70	A/B	21-147	[»]
1Z7J	X-ray	2.20	A/B	21-147	[»]
1ZCR	X-ray	1.80	A/B	21-147	[»]
1ZD6	X-ray	1.90	A/B	21-147	[»]
2B14	X-ray	2.00	A/B	21-147	[»]
2B15	X-ray	1.70	A/B	21-147	[»]
2B16	X-ray	1.75	A/B	21-147	[»]
2B77	X-ray	1.70	A/B	21-147	[»]
2B9A	X-ray	1.54	A/B	21-147	[»]
2F7I	X-ray	1.60	A/B	21-147	[»]
2F8I	X-ray	1.54	A/B	21-147	[»]
2FBR	X-ray	1.46	A/B	21-147	[»]
2FLM	X-ray	1.65	A/B	21-147	[»]
2G3X	X-ray	1.58	A/B	21-147	[»]
2G3Z	X-ray	1.90	A/B	21-147	[»]
2G4E	X-ray	2.17	A/B	21-147	[»]
2G4G	X-ray	1.85	A/B	21-147	[»]
2G5U	X-ray	1.80	A/B	21-147	[»]
2G9K	X-ray	1.85	A/B	21-147	[»]
2GAB	X-ray	1.85	A/B	21-147	[»]
2H4E	X-ray	1.45	A/B	21-147	[»]
2NOY	X-ray	1.80	A/B	21-147	[»]
2PAB	X-ray	1.80	A/B	21-147	[»]
2QEL	X-ray	2.29	A/B/C/D	21-147	[»]
2QGB	X-ray	1.40	A/B	21-147	[»]
2QGC	X-ray	1.30	A/B	21-147	[»]
2QGD	X-ray	1.50	A/B	21-147	[»]
2QGE	X-ray	1.45	A/B	21-147	[»]
2ROX	X-ray	2.00	A/B	21-147	[»]
2ROY	X-ray	2.20	A/B	21-147	[»]
2TRH	X-ray	1.90	A/B	21-147	[»]
2TRY	X-ray	2.00	A/B	21-147	[»]
2WQA	X-ray	2.85	A/B/C/D	21-147	[»]
3A4D	X-ray	2.00	A/B	21-147	[»]
3A4E	X-ray	1.70	A/B	21-147	[»]
3A4F	X-ray	1.99	A/B	21-147	[»]
3B56	X-ray	1.55	A/B	21-147	[»]
3BSZ	X-ray	3.38	A/B/C/D	21-147	[»]
3BT0	X-ray	1.59	A/B	21-147	[»]
3CBR	X-ray	1.70	A/B	21-147	[»]
3CFM	X-ray	1.60	A/B	30-147	[»]
3CFN	X-ray	1.87	A/B	30-147	[»]
3CFQ	X-ray	2.09	A/B	30-147	[»]
3CFT	X-ray	1.87	A/B	30-147	[»]
3CN0	X-ray	1.52	A/B	21-147	[»]
3CN1	X-ray	1.52	A/B	21-147	[»]
3CN2	X-ray	1.52	A/B	21-147	[»]
3CN3	X-ray	1.80	A/B	21-147	[»]
3CN4	X-ray	1.40	A/B	21-147	[»]
3CXF	X-ray	2.30	A/B	21-147	[»]
3D2T	X-ray	1.85	A/B	21-147	[»]
3D7P	X-ray	1.72	A/B	21-147	[»]
3DGD	X-ray	1.38	A/B/C/D	21-147	[»]
3DID	X-ray	1.78	A/B/C/D	21-147	[»]
3DJR	X-ray	2.02	A/B	21-147	[»]
3DJS	X-ray	1.80	A/B	21-147	[»]
3DJT	X-ray	2.30	A/B	21-147	[»]
3DJZ	X-ray	1.82	A/B	21-147	[»]
3DK0	X-ray	1.87	A/B	21-147	[»]
3DK2	X-ray	2.35	A/B	21-147	[»]
3DO4	X-ray	2.40	A/B/C/D/E/F/G/H	21-147	[»]
3ESN	X-ray	1.35	A/B	21-147	[»]
3ESO	X-ray	1.31	A/B	21-147	[»]
3ESP	X-ray	1.31	A/B	21-147	[»]
3FC8	X-ray	1.85	A/B	21-144	[»]
3FCB	X-ray	1.80	A/B	21-144	[»]
3GLZ	X-ray	1.78	A/B	21-147	[»]
3GPS	X-ray	1.78	A/B/C/D	21-147	[»]
3GRB	X-ray	1.75	A/B/C/D	21-147	[»]
3GRG	X-ray	1.90	A/B/C/D	21-147	[»]
3GS0	X-ray	1.85	A/B	21-147	[»]
3GS4	X-ray	1.78	A/B	21-147	[»]
3GS7	X-ray	1.80	A/B	21-147	[»]
3HJ0	X-ray	1.34	A/B	21-147	[»]
3I9A	X-ray	1.65	A/B	21-147	[»]
3I9I	X-ray	1.80	A/B	30-145	[»]
3I9P	X-ray	1.90	A/B	30-145	[»]
3IMR	X-ray	1.70	A/B	21-147	[»]
3IMS	X-ray	1.40	A/B	21-147	[»]
3IMT	X-ray	1.40	A/B	21-147	[»]
3IMU	X-ray	1.40	A/B	21-147	[»]
3IMV	X-ray	1.47	A/B	21-147	[»]
3IMW	X-ray	1.31	A/B	21-147	[»]
3IPB	X-ray	1.90	A/B	21-147	[»]
3IPE	X-ray	1.40	A/B	21-147	[»]
3KGS	X-ray	1.80	A/B	21-147	[»]
3KGT	X-ray	1.95	A/B	21-147	[»]
3KGU	X-ray	1.85	A/B	21-147	[»]
3M1O	X-ray	1.20	A/B	21-147	[»]
3NEE	X-ray	1.55	A/B	30-145	[»]
3NEO	X-ray	2.00	A/B	30-145	[»]
3NES	X-ray	1.75	A/B	30-145	[»]
3NEX	X-ray	1.70	A/B	30-145	[»]
3NG5	X-ray	1.70	A/B	21-147	[»]
3OZK	X-ray	1.90	A/B	21-147	[»]
3OZL	X-ray	1.90	A/B	21-147	[»]
3P3R	X-ray	1.25	A/B	21-147	[»]
3P3S	X-ray	1.60	A/B	21-147	[»]
3P3T	X-ray	1.45	A/B	21-147	[»]
3P3U	X-ray	1.50	A/B	21-147	[»]
3SSG	X-ray	2.00	A	21-147	[»]
3TCT	X-ray	1.30	A/B	21-147	[»]
3TFB	X-ray	2.03	A/B	30-145	[»]
3U2I	X-ray	1.70	A/B	32-147	[»]
3U2J	neutron diffraction	2.00	A/B	32-147	[»]
3W3B	X-ray	1.90	A/B	21-147	[»]
4ABQ	X-ray	1.70	A/B	21-144	[»]
4ABU	X-ray	1.86	A/B	21-144	[»]
4ABV	X-ray	1.80	A/B	21-144	[»]
4ABW	X-ray	1.70	A/B	21-144	[»]
4AC2	X-ray	1.81	A/B	21-144	[»]
4AC4	X-ray	1.80	A/B	21-147	[»]
4ACT	X-ray	1.80	A/B	21-147	[»]
4ANK	X-ray	1.70	A/B	1-147	[»]
4DER	X-ray	1.90	A/B	30-145	[»]
4DES	X-ray	1.75	A/B	30-145	[»]
4DET	X-ray	2.05	A/B	30-145	[»]
4DEU	X-ray	1.60	A/B	30-145	[»]
4DEW	X-ray	1.90	A/B	1-147	[»]
4FI6	X-ray	1.46	A/B	21-147	[»]
4FI7	X-ray	1.40	A/B	21-147	[»]
4FI8	X-ray	1.22	A/B	21-147	[»]
4IIZ	X-ray	2.10	A/B	21-147	[»]
4IK6	X-ray	2.00	A/B	21-147	[»]
4IK7	X-ray	2.10	A/B	21-147	[»]
4IKI	X-ray	2.00	A/B	21-147	[»]
4IKJ	X-ray	2.10	A/B	21-147	[»]
4IKK	X-ray	1.90	A/B	21-147	[»]
4IKL	X-ray	1.90	A/B	21-147	[»]
5TTR	X-ray	2.70	A/B/C/D/E/F/G/H	21-147	[»]

ProteinModelPortal

P02766.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1083N.

IntAct

P02766. 19 interactions.

MINT

MINT-1374623.

STRING

9606.ENSP00000237014.

PTM databases

PhosphoSite

P02766.

Polymorphism databases

DMDM

136464.

2D gel databases

DOSAC-COBS-2DPAGE

P02766.

REPRODUCTION-2DPAGE

P02766.

SWISS-2DPAGE

P02766.

UCD-2DPAGE

P02766.

Proteomic databases

PaxDb

P02766.

PeptideAtlas

P02766.

PRIDE

P02766.

Protocols and materials databases

DNASU

7276.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000237014; ENSP00000237014; ENSG00000118271.

GeneID

7276.

KEGG

hsa:7276.

UCSC

uc002kwx.4. human.

Organism-specific databases

CTD

7276.

GeneCards

GC18P029194.

HGNC

HGNC:12405. TTR.

HPA

CAB002517.
HPA002550.

MIM

105210. phenotype.
115430. phenotype.
145680. phenotype.
176300. gene.

neXtProt

NX_P02766.

Orphanet

85447. Familial amyloid polyneuropathy.
85451. Transthyretin-related familial amyloid cardiomyopathy.

PharmGKB

PA37069.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG321124.

HOGENOM

HOG000251776.

HOVERGEN

HBG000285.

InParanoid

P02766.

OrthoDB

EOG4B5P6N.

PhylomeDB

P02766.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

P02766.

Bgee

P02766.

CleanEx

HS_TTR.

Genevestigator

P02766.

GermOnline

ENSG00000118271. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.180. 1 hit.

InterPro

IPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]

Pfam

PF00576. Transthyretin. 1 hit.
[Graphical view]

PRINTS

PR00189. TRNSTHYRETIN.

SMART

SM00095. TR_THY. 1 hit.
[Graphical view]

SUPFAM

SSF49472. Transthyretin. 1 hit.

PROSITE

PS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02766.

ChEMBL

CHEMBL3194.

ChiTaRS

TTR. human.

DrugBank

DB00586. Diclofenac.
DB00255. Diethylstilbestrol.
DB00861. Diflunisal.
DB01093. Dimethyl sulfoxide.
DB00451. Levothyroxine.
DB00279. Liothyronine.

EvolutionaryTrace

P02766.

GenomeRNAi

7276.

NextBio

28455.

PMAP-CutDB

P02766.

SOURCE

Search...

Entry information

Entry name

TTHY_HUMAN

Accession

Primary (citable) accession number: P02766
Secondary accession number(s): Q549C7 , Q6IB96, Q9UBZ6, Q9UCM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 20, 1987
Last modified:	May 29, 2013
This is version 172 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.