-
1
-
-
0347357617
-
Protein folding and misfolding
-
Dobson CM. Protein folding and misfolding. Nature 2003;426: 884-890.
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
2
-
-
0012357343
-
The structural basis of proteinuria in man: Electron microscopic studies of renal biopsy specimens from patients with lipid nephrosis, amyloidosis, and subacute and chronic glomerulonephritis
-
Spiro D. The structural basis of proteinuria in man: electron microscopic studies of renal biopsy specimens from patients with lipid nephrosis, amyloidosis, and subacute and chronic glomerulonephritis. Am J Pathol 1959;35:47-73.
-
(1959)
Am J Pathol
, vol.35
, pp. 47-73
-
-
Spiro, D.1
-
3
-
-
0001611370
-
Electron microscopic observation on a fibrous component in amyloid of diverse origins
-
Cohen AS, Calkins E. Electron microscopic observation on a fibrous component in amyloid of diverse origins. Nature 1959;183: 1202-1203.
-
(1959)
Nature
, vol.183
, pp. 1202-1203
-
-
Cohen, A.S.1
Calkins, E.2
-
4
-
-
0019153066
-
Amyloid deposits and amyloidosis. The β-fibrilloses (first of two parts)
-
Glenner GG. Amyloid deposits and amyloidosis. The β-fibrilloses (first of two parts). N Engl J Med 1980;302:1283-1292.
-
(1980)
N Engl J Med
, vol.302
, pp. 1283-1292
-
-
Glenner, G.G.1
-
5
-
-
0018868515
-
Amyloid deposits and amyloidosis: The β-fibrilloses (second of two parts)
-
Glenner GG. Amyloid deposits and amyloidosis: the β-fibrilloses (second of two parts). N Engl J Med 1980;302:1333-1343.
-
(1980)
N Engl J Med
, vol.302
, pp. 1333-1343
-
-
Glenner, G.G.1
-
6
-
-
0347987853
-
Folding proteins in fatal ways
-
Selkoe DJ. Folding proteins in fatal ways. Nature 2003;426: 900-904.
-
(2003)
Nature
, vol.426
, pp. 900-904
-
-
Selkoe, D.J.1
-
7
-
-
0344944630
-
Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
-
Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003;81:678-699.
-
(2003)
J Mol Med
, vol.81
, pp. 678-699
-
-
Stefani, M.1
Dobson, C.M.2
-
8
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 1997;273:729-739.
-
(1997)
J Mol Biol
, vol.273
, pp. 729-739
-
-
Sunde, M.1
Serpell, L.C.2
Bartlam, M.3
Fraser, P.E.4
Pepys, M.B.5
Blake, C.C.6
-
9
-
-
0000573263
-
Configuration of polypeptide chains with favoured orientation around single bonds: Two new pleated sheets
-
Pauling L, Corey R. Configuration of polypeptide chains with favoured orientation around single bonds: two new pleated sheets. Proc Natl Acad Sci USA 1951;37:729-740.
-
(1951)
Proc Natl Acad Sci USA
, vol.37
, pp. 729-740
-
-
Pauling, L.1
Corey, R.2
-
10
-
-
0030830019
-
Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
-
Kelly JW, Colon W, Lai Z, Lashuel HA, McCulloch J, McCutchen SL, Miroy GJ, Peterson SA. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv Protein Chem 1997;50:161-181.
-
(1997)
Adv Protein Chem
, vol.50
, pp. 161-181
-
-
Kelly, J.W.1
Colon, W.2
Lai, Z.3
Lashuel, H.A.4
McCulloch, J.5
McCutchen, S.L.6
Miroy, G.J.7
Peterson, S.A.8
-
11
-
-
0004847037
-
Observations concerning the binding of thyroid hormones by human serum prealbumin
-
Ingbar SH. Observations concerning the binding of thyroid hormones by human serum prealbumin. J Clin Invest 1963;42:143-160.
-
(1963)
J Clin Invest
, vol.42
, pp. 143-160
-
-
Ingbar, S.H.1
-
12
-
-
0014961848
-
Studies on the protein-protein and protein-ligand interactions involved in retinol transport in plasma
-
Raz A, Shiratori T, Goodman DS. Studies on the protein-protein and protein-ligand interactions involved in retinol transport in plasma. J Biol Chem 1970;245:1903-1912.
-
(1970)
J Biol Chem
, vol.245
, pp. 1903-1912
-
-
Raz, A.1
Shiratori, T.2
Goodman, D.S.3
-
14
-
-
0016830196
-
Studies on thyroid hormone-binding proteins. II. Binding of thyroid hormones, retinol-binding protein, and fluorescent probes to prealbumin and effects of thyroxine on prealbumin subunit self association
-
Nilsson SF, Rask L, Peterson PA. Studies on thyroid hormone-binding proteins. II. Binding of thyroid hormones, retinol-binding protein, and fluorescent probes to prealbumin and effects of thyroxine on prealbumin subunit self association J Biol Chem 1975;250:8554-8563.
-
(1975)
J Biol Chem
, vol.250
, pp. 8554-8563
-
-
Nilsson, S.F.1
Rask, L.2
Peterson, P.A.3
-
15
-
-
0029881007
-
MOLMOL: A program for display and analysis of macromolecular structures
-
Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 1996;14:51-55.
-
(1996)
J Mol Graph
, vol.14
, pp. 51-55
-
-
Koradi, R.1
Billeter, M.2
Wuthrich, K.3
-
16
-
-
0016140360
-
Structure of human plasma prealbumin at 2-5 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding
-
Blake CC, Geisow MJ, Swan ID, Rerat C, Rerat B. Structure of human plasma prealbumin at 2-5 A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding. J Mol Biol 1974;88:1-12.
-
(1974)
J Mol Biol
, vol.88
, pp. 1-12
-
-
Blake, C.C.1
Geisow, M.J.2
Swan, I.D.3
Rerat, C.4
Rerat, B.5
-
17
-
-
0017824077
-
Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
-
Blake CC, Geisow MJ, Oatley SJ, Rerat B, Rerat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 1978;121:339-356.
-
(1978)
J Mol Biol
, vol.121
, pp. 339-356
-
-
Blake, C.C.1
Geisow, M.J.2
Oatley, S.J.3
Rerat, B.4
Rerat, C.5
-
18
-
-
0025278448
-
Fibril in senile systemic amyloidosis is derived from normal transthyretin
-
Westermark P, Sletten K, Johansson B, Cornwell GG, III. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc Natl Acad Sci USA 1990;87:2843-2845.
-
(1990)
Proc Natl Acad Sci USA
, vol.87
, pp. 2843-2845
-
-
Westermark, P.1
Sletten, K.2
Johansson, B.3
Cornwell III, G.G.4
-
20
-
-
0035957104
-
Transthyretin-associated neuropathic amyloidosis. Pathogenesis and treatment
-
Hund E, Linke RP, Willig F, Grau A. Transthyretin-associated neuropathic amyloidosis. Pathogenesis and treatment. Neurology 2001;56:431-435.
-
(2001)
Neurology
, vol.56
, pp. 431-435
-
-
Hund, E.1
Linke, R.P.2
Willig, F.3
Grau, A.4
-
21
-
-
4344714361
-
Familial amyloidotic polyneuropathy. Protein aggregation in the peripheral nervous system
-
Saraiva MJ, Sousa MM, Cardoso I, Fernandes R. Familial amyloidotic polyneuropathy. Protein aggregation in the peripheral nervous system. J Mol Neurosci 2004;23:35-40.
-
(2004)
J Mol Neurosci
, vol.23
, pp. 35-40
-
-
Saraiva, M.J.1
Sousa, M.M.2
Cardoso, I.3
Fernandes, R.4
-
22
-
-
0028969996
-
Transthyretin mutations in health and disease
-
Saraiva MJ. Transthyretin mutations in health and disease. Hum Mutat 1995;5:191-196.
-
(1995)
Hum Mutat
, vol.5
, pp. 191-196
-
-
Saraiva, M.J.1
-
24
-
-
0034813793
-
Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin
-
Eneqvist T, Sauer-Eriksson AE. Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin. Amyloid 2001;8:149-168.
-
(2001)
Amyloid
, vol.8
, pp. 149-168
-
-
Eneqvist, T.1
Sauer-Eriksson, A.E.2
-
25
-
-
0035793707
-
Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution
-
Sebastiao MP, Lamzin V, Saraiva MJ, Damas AM. Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution. J Mol Biol 2001;306:733-744.
-
(2001)
J Mol Biol
, vol.306
, pp. 733-744
-
-
Sebastiao, M.P.1
Lamzin, V.2
Saraiva, M.J.3
Damas, A.M.4
-
26
-
-
0026675307
-
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
-
Colon W, Kelly JW. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992;31:8654-8660.
-
(1992)
Biochemistry
, vol.31
, pp. 8654-8660
-
-
Colon, W.1
Kelly, J.W.2
-
27
-
-
0027363264
-
Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
-
McCutchen SL, Colon W, Kelly JW. Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 1993;32:12119-12127.
-
(1993)
Biochemistry
, vol.32
, pp. 12119-12127
-
-
McCutchen, S.L.1
Colon, W.2
Kelly, J.W.3
-
28
-
-
0028839438
-
Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease
-
McCutchen SL, Lai Z, Miroy GJ, Kelly JW, Colon W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry 1995;34:13527-13536.
-
(1995)
Biochemistry
, vol.34
, pp. 13527-13536
-
-
McCutchen, S.L.1
Lai, Z.2
Miroy, G.J.3
Kelly, J.W.4
Colon, W.5
-
29
-
-
0030004644
-
The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
-
Lai Z, Colon W, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 1996;35:6470-6482.
-
(1996)
Biochemistry
, vol.35
, pp. 6470-6482
-
-
Lai, Z.1
Colon, W.2
Kelly, J.W.3
-
30
-
-
0033550075
-
The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
-
Lashuel HA, Wurth C, Woo L, Kelly JW. The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 1999;38:13560-13573.
-
(1999)
Biochemistry
, vol.38
, pp. 13560-13573
-
-
Lashuel, H.A.1
Wurth, C.2
Woo, L.3
Kelly, J.W.4
-
31
-
-
0035909981
-
The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis
-
Jiang X, Buxbaum JN, Kelly JW. The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis. Proc Natl Acad Sci USA 2001;98:14943-14948.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 14943-14948
-
-
Jiang, X.1
Buxbaum, J.N.2
Kelly, J.W.3
-
32
-
-
0036306257
-
Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin
-
Liu K, Kelly JW, Wemmer DE. Native state hydrogen exchange study of suppressor and pathogenic variants of transthyretin. J Mol Biol 2002;320:821-832.
-
(2002)
J Mol Biol
, vol.320
, pp. 821-832
-
-
Liu, K.1
Kelly, J.W.2
Wemmer, D.E.3
-
33
-
-
0023705432
-
Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
-
Roder H, Elove GA, Englander SW. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 1988;335:700-704.
-
(1988)
Nature
, vol.335
, pp. 700-704
-
-
Roder, H.1
Elove, G.A.2
Englander, S.W.3
-
34
-
-
0024331090
-
Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
-
Roder H. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol 1989;176:446-473.
-
(1989)
Methods Enzymol
, vol.176
, pp. 446-473
-
-
Roder, H.1
-
35
-
-
3242878900
-
Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins
-
Redfield C. Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins. Methods 2004;34:121-132.
-
(2004)
Methods
, vol.34
, pp. 121-132
-
-
Redfield, C.1
-
37
-
-
0034602241
-
Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies, the stable core of the individual subunits and indicates mobility at the subunit interface
-
Liu K, Cho HS, Hoyt DW, Nguyen TN, Olds P, Kelly JW, Wemmer DE. Deuterium-proton exchange on the native wild-type transthyretin tetramer identifies, the stable core of the individual subunits and indicates mobility at the subunit interface. J Mol Biol 2000;303:555-565.
-
(2000)
J Mol Biol
, vol.303
, pp. 555-565
-
-
Liu, K.1
Cho, H.S.2
Hoyt, D.W.3
Nguyen, T.N.4
Olds, P.5
Kelly, J.W.6
Wemmer, D.E.7
-
38
-
-
0033813424
-
A glimpse of a possible amyloidogenic intermediate of transthyretin
-
Liu K, Cho HS, Lashuel HA, Kelly JW, Wemmer DE. A glimpse of a possible amyloidogenic intermediate of transthyretin. Nat Struct Biol 2000;7:754-757.
-
(2000)
Nat Struct Biol
, vol.7
, pp. 754-757
-
-
Liu, K.1
Cho, H.S.2
Lashuel, H.A.3
Kelly, J.W.4
Wemmer, D.E.5
-
39
-
-
0024745055
-
Direct sequencing of the gene for Maryland/German familial amyloidotic polyneuropathy type II and genotyping by allele-specific enzymatic amplification
-
Nichols WC, Liepnieks JJ, McKusick VA, Benson MD. Direct sequencing of the gene for Maryland/German familial amyloidotic polyneuropathy type II and genotyping by allele-specific enzymatic amplification. Genomics 1989;5:535-540.
-
(1989)
Genomics
, vol.5
, pp. 535-540
-
-
Nichols, W.C.1
Liepnieks, J.J.2
McKusick, V.A.3
Benson, M.D.4
-
40
-
-
0026088357
-
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. New mutant gene (transthyretin Arg 58) in cases with hereditary polyneuropathy detected by non-isotope method of single-strand conformation polymorphism analysis. Biochem Biophys Res Commun 1991;180:380-385.
-
(1991)
Biochem Biophys Res Commun
, vol.180
, pp. 380-385
-
-
Saeki, Y.1
Ueno, S.2
Yorifuji, S.3
Sugiyama, Y.4
Ide, Y.5
Matsuzawa, Y.6
-
41
-
-
0028925450
-
A novel variant of transthyretin, 59Thr→Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family
-
Booth DR, Tan SY, Hawkins PN, Pepys MB, Frustaci A. A novel variant of transthyretin, 59Thr→Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family. Circulation 1995;91:962-967.
-
(1995)
Circulation
, vol.91
, pp. 962-967
-
-
Booth, D.R.1
Tan, S.Y.2
Hawkins, P.N.3
Pepys, M.B.4
Frustaci, A.5
-
42
-
-
19244367569
-
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. A basic transthyretin variant (Glu61→Lys) causes familial amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced mutation restriction analysis. Biochem Biophys Res Commun 1993;194:1090-1096.
-
(1993)
Biochem Biophys Res Commun
, vol.194
, pp. 1090-1096
-
-
Shiomi, K.1
Nakazato, M.2
Matsukura, S.3
Ohnishi, A.4
Hatanaka, H.5
Tsuji, S.6
Murai, Y.7
Kojima, M.8
Kangawa, K.9
Matsuo, H.10
-
43
-
-
20044385548
-
Dimeric transthyretin variant assembles into spherical neurotoxins
-
Matsubara K, Mizuguchi M, Igarashi K, Shinohara Y, Takeuchi M, Matsuura A, Saitoh T, Mori Y, Shinoda H, Kawano K. Dimeric transthyretin variant assembles into spherical neurotoxins. Biochemistry 2005;44:3280-3288.
-
(2005)
Biochemistry
, vol.44
, pp. 3280-3288
-
-
Matsubara, K.1
Mizuguchi, M.2
Igarashi, K.3
Shinohara, Y.4
Takeuchi, M.5
Matsuura, A.6
Saitoh, T.7
Mori, Y.8
Shinoda, H.9
Kawano, K.10
-
44
-
-
9144267702
-
Biophysical analyses of the transthyretin variants, Tyr114-His and Tyr116Ser, associated with familial amyloidotic polyneuropathy
-
Shinohara Y, Mizuguchi M, Matsubara K, Takeuchi M, Matsuura A, Aoki T, Igarashi K, Nagadome H, Terada Y, Kawano K. Biophysical analyses of the transthyretin variants, Tyr114-His and Tyr116Ser, associated with familial amyloidotic polyneuropathy. Biochemistry 2003;42:15053-15060.
-
(2003)
Biochemistry
, vol.42
, pp. 15053-15060
-
-
Shinohara, Y.1
Mizuguchi, M.2
Matsubara, K.3
Takeuchi, M.4
Matsuura, A.5
Aoki, T.6
Igarashi, K.7
Nagadome, H.8
Terada, Y.9
Kawano, K.10
-
45
-
-
0029853743
-
Quick and easy molecular weight determination with Macintosh computers and public domain image analysis software
-
Seebacher T, Bade EG. Quick and easy molecular weight determination with Macintosh computers and public domain image analysis software. Electrophoresis 1996;17:1573-1574.
-
(1996)
Electrophoresis
, vol.17
, pp. 1573-1574
-
-
Seebacher, T.1
Bade, E.G.2
-
46
-
-
0032506009
-
TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
-
Salzmann M, Pervushin K, Wider G, Senn H, Wuthrich K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc Natl Acad Sci USA 1998;95:13585-13590.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 13585-13590
-
-
Salzmann, M.1
Pervushin, K.2
Wider, G.3
Senn, H.4
Wuthrich, K.5
-
47
-
-
0033518575
-
TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
-
Salzmann M, Wider G, Pervushin K, Senn H, Wüthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J Am Chem Soc 1999;121:844-848.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 844-848
-
-
Salzmann, M.1
Wider, G.2
Pervushin, K.3
Senn, H.4
Wüthrich, K.5
-
49
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995;6:277-293.
-
(1995)
J Biomol NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
50
-
-
4644259437
-
-
Johnson BA. Using NMR. View to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 2004;278: 313-352.
-
Johnson BA. Using NMR. View to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 2004;278: 313-352.
-
-
-
-
51
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
-
Santoro MM Bolen DW. Unfolding free energy changes determined by the linear extrapolation method. I. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 1988;27:8063-8068.
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
52
-
-
0034672768
-
Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin
-
Shnyrov VL, Villar E, Zhadan GG, Sanchez-Ruiz JM, Quintas A, Saraiva MJ, Brito RM. Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin. Biophys Chem 2000;88:61-67.
-
(2000)
Biophys Chem
, vol.88
, pp. 61-67
-
-
Shnyrov, V.L.1
Villar, E.2
Zhadan, G.G.3
Sanchez-Ruiz, J.M.4
Quintas, A.5
Saraiva, M.J.6
Brito, R.M.7
-
53
-
-
0032544408
-
The crystal structure of amyloidogenic Leu55→Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils
-
Sebastiao MP, Saraiva MJ, Damas AM. The crystal structure of amyloidogenic Leu55→Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils. J Biol Chem 1998;273:24715-24722.
-
(1998)
J Biol Chem
, vol.273
, pp. 24715-24722
-
-
Sebastiao, M.P.1
Saraiva, M.J.2
Damas, A.M.3
|