-
2
-
-
0030801746
-
The structure of amyloid fibrils by electron microscopy and X-ray diffraction
-
Sunde M., and Blake C.C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Adv. Protein Chem. 50 (1997) 123-159
-
(1997)
Adv. Protein Chem.
, vol.50
, pp. 123-159
-
-
Sunde, M.1
Blake, C.C.2
-
3
-
-
3343003514
-
Techniques to study amyloid fibril formation in vitro
-
Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
-
(2004)
Methods
, vol.34
, pp. 151-160
-
-
Nilsson, M.R.1
-
4
-
-
11144222595
-
The binding of thioflavin-T to amyloid fibrils: localisation and implications
-
Krebs M.R., Bromley E.H., and Donald A.M. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149 (2005) 30-37
-
(2005)
J. Struct. Biol.
, vol.149
, pp. 30-37
-
-
Krebs, M.R.1
Bromley, E.H.2
Donald, A.M.3
-
5
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
6
-
-
57749098600
-
Amyloid formation by globular proteins under native conditions
-
Chiti F., and Dobson C.M. Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5 (2009) 15-22
-
(2009)
Nat. Chem. Biol.
, vol.5
, pp. 15-22
-
-
Chiti, F.1
Dobson, C.M.2
-
7
-
-
0036220131
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
-
Canet D., et al. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9 (2002) 308-315
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 308-315
-
-
Canet, D.1
-
8
-
-
27744607600
-
Fully metallated S134N Cu, Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution
-
Banci L., Bertini I., D'Amelio N., Gaggelli E., Libralesso E., Matecko I., Turano P., and Valentine J.S. Fully metallated S134N Cu, Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution. J. Biol. Chem. 280 (2005) 35815-35821
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 35815-35821
-
-
Banci, L.1
Bertini, I.2
D'Amelio, N.3
Gaggelli, E.4
Libralesso, E.5
Matecko, I.6
Turano, P.7
Valentine, J.S.8
-
9
-
-
15244362270
-
Amyloid-like properties of bacterial inclusion bodies
-
Carrió M., González-Montalbán N., Vera A., Villaverde A., and Ventura S. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol. 347 (2005) 1025-1037
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 1025-1037
-
-
Carrió, M.1
González-Montalbán, N.2
Vera, A.3
Villaverde, A.4
Ventura, S.5
-
10
-
-
51049095117
-
Inclusion bodies: specificity in their aggregation process and amyloid-like structure
-
Morell M., Bravo R., Espargaró A., Sisquella X., Avilés F.X., Fernàndez-Busquets X., and Ventura S. Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochim. Biophys. Acta 1783 (2008) 1815-1825
-
(2008)
Biochim. Biophys. Acta
, vol.1783
, pp. 1815-1825
-
-
Morell, M.1
Bravo, R.2
Espargaró, A.3
Sisquella, X.4
Avilés, F.X.5
Fernàndez-Busquets, X.6
Ventura, S.7
-
11
-
-
33646106328
-
Protein quality in bacterial inclusion bodies
-
Ventura S., and Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24 (2006) 179-185
-
(2006)
Trends Biotechnol.
, vol.24
, pp. 179-185
-
-
Ventura, S.1
Villaverde, A.2
-
12
-
-
50249144570
-
Bacterial inclusion bodies contain amyloid-like structure
-
Wang L., Maji S.K., Sawaya M.R., Eisenberg D., and Riek R. Bacterial inclusion bodies contain amyloid-like structure. PLoS Biol. 6 (2008) 1791-1801
-
(2008)
PLoS Biol.
, vol.6
, pp. 1791-1801
-
-
Wang, L.1
Maji, S.K.2
Sawaya, M.R.3
Eisenberg, D.4
Riek, R.5
-
13
-
-
33846176574
-
Localization of functional polypeptides in bacterial inclusion bodies
-
García-Fruitós E., Arís A., and Villaverde A. Localization of functional polypeptides in bacterial inclusion bodies. Appl. Environ. Microbiol. 73 (2007) 289-294
-
(2007)
Appl. Environ. Microbiol.
, vol.73
, pp. 289-294
-
-
García-Fruitós, E.1
Arís, A.2
Villaverde, A.3
-
14
-
-
26844569776
-
Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins
-
García-Fruitós E., González-Montalbán N., Morell M., Vera A., Ferraz R.M., Arís A., Ventura S., and Villaverde A. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb. Cell. Fact. 4 (2005) 27
-
(2005)
Microb. Cell. Fact.
, vol.4
, pp. 27
-
-
García-Fruitós, E.1
González-Montalbán, N.2
Morell, M.3
Vera, A.4
Ferraz, R.M.5
Arís, A.6
Ventura, S.7
Villaverde, A.8
-
15
-
-
0025921901
-
High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D
-
Tokatlidis K., Dhurjati P., Millet J., Béguin P., and Aubert J.P. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett. 282 (1991) 205-208
-
(1991)
FEBS Lett.
, vol.282
, pp. 205-208
-
-
Tokatlidis, K.1
Dhurjati, P.2
Millet, J.3
Béguin, P.4
Aubert, J.P.5
-
16
-
-
34249689651
-
Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils
-
Lian H., et al. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. J. Biol. Chem. 282 (2007) 11931-11940
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 11931-11940
-
-
Lian, H.1
-
17
-
-
47049118460
-
Molecular chaperones and the assembly of the prion Ure2p in vitro
-
Savistchenko J., Krzewska J., Fay N., and Melki R. Molecular chaperones and the assembly of the prion Ure2p in vitro. J. Biol. Chem. 283 (2008) 15732-15739
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 15732-15739
-
-
Savistchenko, J.1
Krzewska, J.2
Fay, N.3
Melki, R.4
-
18
-
-
35348948549
-
Divergent genetic control of protein solubility and conformational quality in Escherichia coli
-
García-Fruitós E., Martínez-Alonso M., Gonzàlez-Montalbán N., Valli M., Mattanovich D., and Villaverde A. Divergent genetic control of protein solubility and conformational quality in Escherichia coli. J. Mol. Biol. 374 (2007) 195-205
-
(2007)
J. Mol. Biol.
, vol.374
, pp. 195-205
-
-
García-Fruitós, E.1
Martínez-Alonso, M.2
Gonzàlez-Montalbán, N.3
Valli, M.4
Mattanovich, D.5
Villaverde, A.6
-
19
-
-
0037022563
-
Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation
-
Richardson J.S., and Richardson D.C. Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA 99 (2002) 2754-2759
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 2754-2759
-
-
Richardson, J.S.1
Richardson, D.C.2
-
20
-
-
30344478570
-
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
-
Corazza A., et al. Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. Proteins 62 (2006) 64-79
-
(2006)
Proteins
, vol.62
, pp. 64-79
-
-
Corazza, A.1
-
21
-
-
15444372698
-
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii-structural insights into enzymatic catalysis, thermostability, and dimerization
-
Cheung Y.Y., Lam S.Y., Chu W.K., Allen M.D., Bycroft M., and Wong K.B. Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii-structural insights into enzymatic catalysis, thermostability, and dimerization. Biochemistry 44 (2005) 4601-4611
-
(2005)
Biochemistry
, vol.44
, pp. 4601-4611
-
-
Cheung, Y.Y.1
Lam, S.Y.2
Chu, W.K.3
Allen, M.D.4
Bycroft, M.5
Wong, K.B.6
-
22
-
-
33751002965
-
NMR solution structure of the acylphosphatase from Escherichia coli
-
Pagano K., Ramazzotti M., Viglino P., Esposito G., Degl'Innocenti D., Taddei N., and Corazza A. NMR solution structure of the acylphosphatase from Escherichia coli. J. Biomol. NMR 36 (2006) 199-204
-
(2006)
J. Biomol. NMR
, vol.36
, pp. 199-204
-
-
Pagano, K.1
Ramazzotti, M.2
Viglino, P.3
Esposito, G.4
Degl'Innocenti, D.5
Taddei, N.6
Corazza, A.7
-
23
-
-
0026522991
-
Three-dimensional structure of acylphosphatase. Refinement and structure analysis
-
Pastore A., Saudek V., Ramponi G., and Williams R.J. Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol. 224 (1992) 427-440
-
(1992)
J. Mol. Biol.
, vol.224
, pp. 427-440
-
-
Pastore, A.1
Saudek, V.2
Ramponi, G.3
Williams, R.J.4
-
24
-
-
0031568309
-
Crystal structure of common type acylphosphatase from bovine testis
-
Thunnissen M.M., Taddei N., Liguri G., Ramponi G., and Nordlund P. Crystal structure of common type acylphosphatase from bovine testis. Structure 5 (1997) 69-79
-
(1997)
Structure
, vol.5
, pp. 69-79
-
-
Thunnissen, M.M.1
Taddei, N.2
Liguri, G.3
Ramponi, G.4
Nordlund, P.5
-
25
-
-
14644399127
-
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase
-
Zuccotti S., Rosano C., Ramazzotti M., Degl'Innocenti D., Stefani M., Manao G., and Bolognesi M. Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1177-1179
-
(2004)
Acta Crystallogr. D Biol. Crystallogr.
, vol.60
, pp. 1177-1179
-
-
Zuccotti, S.1
Rosano, C.2
Ramazzotti, M.3
Degl'Innocenti, D.4
Stefani, M.5
Manao, G.6
Bolognesi, M.7
-
26
-
-
1842790837
-
Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation
-
Plakoutsi G., Taddei N., Stefani M., and Chiti F. Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation. J. Biol. Chem. 279 (2004) 14111-14119
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 14111-14119
-
-
Plakoutsi, G.1
Taddei, N.2
Stefani, M.3
Chiti, F.4
-
27
-
-
33744905543
-
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus
-
Plakoutsi G., Bemporad F., Monti M., Pagnozzi D., Pucci P., and Chiti F. Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. Structure 14 (2006) 993-1001
-
(2006)
Structure
, vol.14
, pp. 993-1001
-
-
Plakoutsi, G.1
Bemporad, F.2
Monti, M.3
Pagnozzi, D.4
Pucci, P.5
Chiti, F.6
-
28
-
-
23444447864
-
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates
-
Plakoutsi G., Bemporad F., Calamai M., Taddei N., Dobson C.M., and Chiti F. Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. J. Mol. Biol. 351 (2005) 910-922
-
(2005)
J. Mol. Biol.
, vol.351
, pp. 910-922
-
-
Plakoutsi, G.1
Bemporad, F.2
Calamai, M.3
Taddei, N.4
Dobson, C.M.5
Chiti, F.6
-
29
-
-
0034681163
-
Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
-
Conway K.A., Lee S.J., Rochet J.C., Ding T.T., Williamson R.E., and Lansbury P.T.J. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc. Natl. Acad. Sci. USA 97 (2000) 571-576
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 571-576
-
-
Conway, K.A.1
Lee, S.J.2
Rochet, J.C.3
Ding, T.T.4
Williamson, R.E.5
Lansbury, P.T.J.6
-
30
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003) 486-489
-
(2003)
Science
, vol.300
, pp. 486-489
-
-
Kayed, R.1
Head, E.2
Thompson, J.L.3
McIntire, T.M.4
Milton, S.C.5
Cotman, C.W.6
Glabe, C.G.7
-
31
-
-
0035920156
-
Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
-
Quintas A., Vaz D.C., Cardoso I., Saraiva M.J., and Brito R.M. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J. Biol. Chem. 276 (2001) 27207-27213
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 27207-27213
-
-
Quintas, A.1
Vaz, D.C.2
Cardoso, I.3
Saraiva, M.J.4
Brito, R.M.5
-
32
-
-
0033520461
-
Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
-
Walsh D.M., et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274 (1999) 25945-25952
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 25945-25952
-
-
Walsh, D.M.1
-
33
-
-
54549095709
-
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state
-
Bemporad F., Vannocci T., Varela L., Azuaga A.I., and Chiti F. A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. Biochim. Biophys. Acta 1784 (2008) 1986-1996
-
(2008)
Biochim. Biophys. Acta
, vol.1784
, pp. 1986-1996
-
-
Bemporad, F.1
Vannocci, T.2
Varela, L.3
Azuaga, A.I.4
Chiti, F.5
-
34
-
-
0038442784
-
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
-
Elam J.S., et al. Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat. Struct. Biol. 10 (2003) 461-467
-
(2003)
Nat. Struct. Biol.
, vol.10
, pp. 461-467
-
-
Elam, J.S.1
-
35
-
-
1242316998
-
Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy
-
Olofsson A., Ippel J.H., Wijmenga S.S., Lundgren E., and Ohman A. Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J. Biol. Chem. 279 (2004) 5699-5707
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 5699-5707
-
-
Olofsson, A.1
Ippel, J.H.2
Wijmenga, S.S.3
Lundgren, E.4
Ohman, A.5
-
36
-
-
0036784911
-
Arrangement of subunits and ordering of beta-strands in an amyloid sheet
-
Serag A.A., Altenbach C., Gingery M., Hubbell W.L., and Yeates T.O. Arrangement of subunits and ordering of beta-strands in an amyloid sheet. Nat. Struct. Biol. 9 (2002) 734-739
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 734-739
-
-
Serag, A.A.1
Altenbach, C.2
Gingery, M.3
Hubbell, W.L.4
Yeates, T.O.5
-
37
-
-
28444464509
-
Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state
-
Soldi G., Bemporad F., Torrassa S., Relini A., Ramazzotti M., Taddei N., and Chiti F. Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. Biophys. J. 89 (2005) 4234-4244
-
(2005)
Biophys. J.
, vol.89
, pp. 4234-4244
-
-
Soldi, G.1
Bemporad, F.2
Torrassa, S.3
Relini, A.4
Ramazzotti, M.5
Taddei, N.6
Chiti, F.7
-
38
-
-
0034599720
-
Mutational analysis of the propensity for amyloid formation by a globular protein
-
Chiti F., Taddei N., Bucciantini M., White P., Ramponi G., and Dobson C.M. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19 (2000) 1441-1449
-
(2000)
EMBO J.
, vol.19
, pp. 1441-1449
-
-
Chiti, F.1
Taddei, N.2
Bucciantini, M.3
White, P.4
Ramponi, G.5
Dobson, C.M.6
-
39
-
-
14644406760
-
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state
-
Marcon G., Plakoutsi G., Canale C., Relini A., Taddei N., Dobson C.M., Ramponi G., and Chiti F. Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. (2005) 347
-
(2005)
J. Mol. Biol.
, pp. 347
-
-
Marcon, G.1
Plakoutsi, G.2
Canale, C.3
Relini, A.4
Taddei, N.5
Dobson, C.M.6
Ramponi, G.7
Chiti, F.8
-
40
-
-
41549161190
-
The degree of structural protection at the edge β-strands determines the pathway of amyloid formation in globular proteins
-
Soldi G., Bemporad F., and Chiti F. The degree of structural protection at the edge β-strands determines the pathway of amyloid formation in globular proteins. J. Am. Chem. Soc. 130 (2008) 4295-4302
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 4295-4302
-
-
Soldi, G.1
Bemporad, F.2
Chiti, F.3
-
41
-
-
0037124337
-
The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro
-
Bousset L., Thomson N.H., Radford S.E., and Melki R. The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J. 21 (2002) 2903-2911
-
(2002)
EMBO J.
, vol.21
, pp. 2903-2911
-
-
Bousset, L.1
Thomson, N.H.2
Radford, S.E.3
Melki, R.4
-
42
-
-
0036789017
-
Serpinopathies and the conformational dementias
-
Lomas D.A., and Carrell R.W. Serpinopathies and the conformational dementias. Nat. Rev. Genetics 3 (2002) 759-768
-
(2002)
Nat. Rev. Genetics
, vol.3
, pp. 759-768
-
-
Lomas, D.A.1
Carrell, R.W.2
-
43
-
-
0030004644
-
The acid-mediated denaturation pathway of transhyretin yields a conformational intermediate that can self-assemble into amyloid
-
Lai Z., Colón W., and Kelly J.W. The acid-mediated denaturation pathway of transhyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35 (1996) 6470-6482
-
(1996)
Biochemistry
, vol.35
, pp. 6470-6482
-
-
Lai, Z.1
Colón, W.2
Kelly, J.W.3
-
44
-
-
33749243722
-
Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway
-
Soldi G., Plakoutsi G., Taddei N., and Chiti F. Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. J. Med. Chem. (2006) 6057-6064
-
(2006)
J. Med. Chem.
, pp. 6057-6064
-
-
Soldi, G.1
Plakoutsi, G.2
Taddei, N.3
Chiti, F.4
-
45
-
-
28244502156
-
Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses
-
Johnson S.M., Wiseman R.L., Sekijima Y., Green N.S., Adamski-Werner S.L., and Kelly J.W. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc. Chem. Res. 38 (2005) 911-921
-
(2005)
Acc. Chem. Res.
, vol.38
, pp. 911-921
-
-
Johnson, S.M.1
Wiseman, R.L.2
Sekijima, Y.3
Green, N.S.4
Adamski-Werner, S.L.5
Kelly, J.W.6
-
46
-
-
0033777523
-
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
-
Bouchard M., Zurdo J., Nettleton E.J., Dobson C.M., and Robinson C.V. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9 (2000) 1960-1967
-
(2000)
Protein Sci.
, vol.9
, pp. 1960-1967
-
-
Bouchard, M.1
Zurdo, J.2
Nettleton, E.J.3
Dobson, C.M.4
Robinson, C.V.5
-
47
-
-
33746365408
-
Identification of the core structure of lysozyme amyloid fibrils by proteolysis
-
Frare E., Mossuto M.F., Polverino de Laureto P., Dumoulin M., Dobson C.M., and Fontana A. Identification of the core structure of lysozyme amyloid fibrils by proteolysis. J. Mol. Biol. 361 (2006) 551-561
-
(2006)
J. Mol. Biol.
, vol.361
, pp. 551-561
-
-
Frare, E.1
Mossuto, M.F.2
Polverino de Laureto, P.3
Dumoulin, M.4
Dobson, C.M.5
Fontana, A.6
-
48
-
-
9144228981
-
Lithostathine quadruple-helical filaments form proteinase K-resistant deposits in Creutzfeldt-Jakob disease
-
Laurine E., et al. Lithostathine quadruple-helical filaments form proteinase K-resistant deposits in Creutzfeldt-Jakob disease. J. Biol. Chem. 278 (2003) 51770-51778
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 51770-51778
-
-
Laurine, E.1
|