-
1
-
-
16844364450
-
Protein amyloidose misfolding: Mechanisms, detection, and pathological implications
-
Jeyashekar NS, Sadana A, Vo-Dinh T. Protein amyloidose misfolding: mechanisms, detection, and pathological implications. Methods Mol Biol 2005;300:417-435.
-
(2005)
Methods Mol Biol
, vol.300
, pp. 417-435
-
-
Jeyashekar, N.S.1
Sadana, A.2
Vo-Dinh, T.3
-
2
-
-
10644225416
-
Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
-
Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta 2004;1739:5-25.
-
(2004)
Biochim Biophys Acta
, vol.1739
, pp. 5-25
-
-
Stefani, M.1
-
3
-
-
9344226144
-
Misfolded proteins and human diseases
-
Nayeem MS, Khan RH. Misfolded proteins and human diseases. Protein Pept Lett 2004;11:593-600.
-
(2004)
Protein Pept Lett
, vol.11
, pp. 593-600
-
-
Nayeem, M.S.1
Khan, R.H.2
-
4
-
-
0035961329
-
The structural basis of protein folding and its links with human disease
-
Dobson CM. The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci 2001;356:133-145.
-
(2001)
Philos Trans R Soc Lond B Biol Sci
, vol.356
, pp. 133-145
-
-
Dobson, C.M.1
-
5
-
-
0033616575
-
Designing conditions for in vitro formation of amyloid protofilaments and fibrils
-
Chiti F, Webster P, Taddei N, Clark A, Stefani M, Ramponi G, Dobson CM. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc Natl Acad Sci USA 1999;96:3590-3594.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 3590-3594
-
-
Chiti, F.1
Webster, P.2
Taddei, N.3
Clark, A.4
Stefani, M.5
Ramponi, G.6
Dobson, C.M.7
-
6
-
-
0035187228
-
Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
-
Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 2001;10:2541-2547.
-
(2001)
Protein Sci
, vol.10
, pp. 2541-2547
-
-
Chiti, F.1
Bucciantini, M.2
Capanni, C.3
Taddei, N.4
Dobson, C.M.5
Stefani, M.6
-
7
-
-
13144259646
-
Amyloid fibril formation by an SH3 domain
-
Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proc Natl Acad Sci USA 1998;95:4224-4228.
-
(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 4224-4228
-
-
Guijarro, J.I.1
Sunde, M.2
Jones, J.A.3
Campbell, I.D.4
Dobson, C.M.5
-
8
-
-
0036784667
-
A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
-
Hamada D, Dobson CM. A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci 2002;11:2417-2426.
-
(2002)
Protein Sci
, vol.11
, pp. 2417-2426
-
-
Hamada, D.1
Dobson, C.M.2
-
9
-
-
0035957696
-
Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS
-
Pertinhez TA, Bouchard M, Tomlinson EJ, Wain R, Ferguson SJ, Dobson CM, Smith LJ. Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS. FEBS Lett 2001;495:184-186.
-
(2001)
FEBS Lett
, vol.495
, pp. 184-186
-
-
Pertinhez, T.A.1
Bouchard, M.2
Tomlinson, E.J.3
Wain, R.4
Ferguson, S.J.5
Dobson, C.M.6
Smith, L.J.7
-
11
-
-
0042467550
-
Rationalization of the effects of mutations on peptide and protein aggregation rates
-
Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003;424:805-808.
-
(2003)
Nature
, vol.424
, pp. 805-808
-
-
Chiti, F.1
Stefani, M.2
Taddei, N.3
Ramponi, G.4
Dobson, C.M.5
-
12
-
-
3242785264
-
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
-
DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM, Vendruscolo M. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J Mol Biol 2004;341:1317-1326.
-
(2004)
J Mol Biol
, vol.341
, pp. 1317-1326
-
-
DuBay, K.F.1
Pawar, A.P.2
Chiti, F.3
Zurdo, J.4
Dobson, C.M.5
Vendruscolo, M.6
-
13
-
-
2342569618
-
Conformational constraints for amyloid fibrillation: The importance of being unfolded
-
Uversky VN, Fink AL. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 2004;1698:131-153.
-
(2004)
Biochim Biophys Acta
, vol.1698
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
14
-
-
0036669903
-
Examining the structure of the mature amyloid fibril
-
Makin OS, Serpell LC. Examining the structure of the mature amyloid fibril. Biochem Soc Trans 2002;30:521-525.
-
(2002)
Biochem Soc Trans
, vol.30
, pp. 521-525
-
-
Makin, O.S.1
Serpell, L.C.2
-
15
-
-
0036052739
-
Ideas of order for amyloid fibril structure
-
Wetzel R. Ideas of order for amyloid fibril structure. Structure 2002;10:1031-1036.
-
(2002)
Structure
, vol.10
, pp. 1031-1036
-
-
Wetzel, R.1
-
16
-
-
20444440728
-
Structure of the cross-β spine of amyloid-like fibrils
-
Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Reikel C, Grothe R, Eisenberg D. Structure of the cross-β spine of amyloid-like fibrils. Nature 2005;435:747-749.
-
(2005)
Nature
, vol.435
, pp. 747-749
-
-
Nelson, R.1
Sawaya, M.R.2
Balbirnie, M.3
Madsen, A.O.4
Reikel, C.5
Grothe, R.6
Eisenberg, D.7
-
17
-
-
34249290108
-
Atomic structures of amyloid cross-β spines reveal varied steric zippers
-
Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJW, McFarlane HT, Madsen AØ, Reikel C, Eisenberg D. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 2007;447:453-457.
-
(2007)
Nature
, vol.447
, pp. 453-457
-
-
Sawaya, M.R.1
Sambashivan, S.2
Nelson, R.3
Ivanova, M.I.4
Sievers, S.A.5
Apostol, M.I.6
Thompson, M.J.7
Balbirnie, M.8
Wiltzius, J.J.W.9
McFarlane, H.T.10
Madsen, A.11
Reikel, C.12
Eisenberg, D.13
-
18
-
-
4143097041
-
Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
-
Pallares I, Vendrell J, Aviles FX, Ventura S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. J Mol Biol 2004;342:321-331.
-
(2004)
J Mol Biol
, vol.342
, pp. 321-331
-
-
Pallares, I.1
Vendrell, J.2
Aviles, F.X.3
Ventura, S.4
-
19
-
-
4143148674
-
Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme
-
Vernaglia BA, Huang J, Clark ED. Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme. Biomacromolecules 2004;5:1362-1370.
-
(2004)
Biomacromolecules
, vol.5
, pp. 1362-1370
-
-
Vernaglia, B.A.1
Huang, J.2
Clark, E.D.3
-
20
-
-
0038532258
-
Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
-
Kim YS, Randolph TW, Manning MC, Stevens FJ, Carpenter JF. Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J Biol Chem 2003;278:10842-10850.
-
(2003)
J Biol Chem
, vol.278
, pp. 10842-10850
-
-
Kim, Y.S.1
Randolph, T.W.2
Manning, M.C.3
Stevens, F.J.4
Carpenter, J.F.5
-
21
-
-
0035920156
-
Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
-
Quintas A, Vaz DC, Carsoso I, Saraiva MJ, Brito RM. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 2001;276:27207-27213.
-
(2001)
J Biol Chem
, vol.276
, pp. 27207-27213
-
-
Quintas, A.1
Vaz, D.C.2
Carsoso, I.3
Saraiva, M.J.4
Brito, R.M.5
-
22
-
-
0035957228
-
Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
-
Khurana R, Gillespie JR, Talapatra A, Minert LJ, Ionescu-Zanetti C, Millett I, Fink AL. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 2001;40:3525-3535.
-
(2001)
Biochemistry
, vol.40
, pp. 3525-3535
-
-
Khurana, R.1
Gillespie, J.R.2
Talapatra, A.3
Minert, L.J.4
Ionescu-Zanetti, C.5
Millett, I.6
Fink, A.L.7
-
23
-
-
0032555738
-
Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
-
Nettleton EJ, Sunde M, Lai Z, Kelly JW, Dobson CM, Robinson CV. Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J Mol Biol 1998;281:553-564.
-
(1998)
J Mol Biol
, vol.281
, pp. 553-564
-
-
Nettleton, E.J.1
Sunde, M.2
Lai, Z.3
Kelly, J.W.4
Dobson, C.M.5
Robinson, C.V.6
-
24
-
-
0036228167
-
Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
-
Dima RI, Thirumalai D. Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics. Protein Sci 2002;11:1036-1049.
-
(2002)
Protein Sci
, vol.11
, pp. 1036-1049
-
-
Dima, R.I.1
Thirumalai, D.2
-
25
-
-
0346500469
-
-
Monti M, Leij Garolla di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G, Pucci P. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J Mol Biol 2004;336:253-262.
-
Monti M, Leij Garolla di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G, Pucci P. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J Mol Biol 2004;336:253-262.
-
-
-
-
26
-
-
26844498710
-
Sequence determinants of protein aggregation: Tools to increase protein solubility
-
Ventura S. Sequence determinants of protein aggregation: tools to increase protein solubility. Microb Cell Fact 2005;4:11.
-
(2005)
Microb Cell Fact
, vol.4
, pp. 11
-
-
Ventura, S.1
-
28
-
-
0036308719
-
Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: An unbiased search for the sequence determinants of Aβ amyloidogenesis
-
Wurth C, Guimard NK, Hecht MH. Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis. J Mol Biol 2002;319:1279-1290.
-
(2002)
J Mol Biol
, vol.319
, pp. 1279-1290
-
-
Wurth, C.1
Guimard, N.K.2
Hecht, M.H.3
-
29
-
-
0037117485
-
Mechanism of inactivation on prion coversion of the Saccharomyces cerevisiae Ure2 protein
-
Baxa U, Speransky V, Steven AC, Wickner RB. Mechanism of inactivation on prion coversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci USA 2002;99:5253-5260.
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5253-5260
-
-
Baxa, U.1
Speransky, V.2
Steven, A.C.3
Wickner, R.B.4
-
30
-
-
0030712145
-
Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
-
Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 1997;89:811-819.
-
(1997)
Cell
, vol.89
, pp. 811-819
-
-
Glover, J.R.1
Kowal, A.S.2
Schirmer, E.C.3
Patino, M.M.4
Liu, J.J.5
Lindquist, S.6
-
31
-
-
0032883765
-
Yeast prion [psi+] and its determinant
-
Serio TR, Cashikar AG, Moslehi JJ, Kowal AS, Lindquist SL. Yeast prion [psi+] and its determinant. Sup35p Methods Enzymol 1999;309:649-673.
-
(1999)
Sup35p Methods Enzymol
, vol.309
, pp. 649-673
-
-
Serio, T.R.1
Cashikar, A.G.2
Moslehi, J.J.3
Kowal, A.S.4
Lindquist, S.L.5
-
32
-
-
0034723391
-
Creating a protein-based element of inheritance
-
Li L, Lindquist SL. Creating a protein-based element of inheritance. Science 2000;287:661-664.
-
(2000)
Science
, vol.287
, pp. 661-664
-
-
Li, L.1
Lindquist, S.L.2
-
33
-
-
34447649216
-
Crystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIII
-
Lin H, Huai Q, Huang M, Furie B, Furie BC. Crystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIII. J Mol Biol 2007;371:717-724.
-
(2007)
J Mol Biol
, vol.371
, pp. 717-724
-
-
Lin, H.1
Huai, Q.2
Huang, M.3
Furie, B.4
Furie, B.C.5
-
34
-
-
0029655338
-
Evidence for two prions in yeast: [URE3] and [PSI]
-
Wickner RB, Masison DC. Evidence for two prions in yeast: [URE3] and [PSI]. Curr Top Microbiol Immunol 1996;207:147-160.
-
(1996)
Curr Top Microbiol Immunol
, vol.207
, pp. 147-160
-
-
Wickner, R.B.1
Masison, D.C.2
-
35
-
-
0036366021
-
Prions of yeast as epigenetic phonomena: High protein "copy number" inducing protein "silencing
-
Wickner RB, Edskes HK, Roberts BT, Pierce M, Baxa U. Prions of yeast as epigenetic phonomena: high protein "copy number" inducing protein "silencing." Adv Genet 2002;46:485-525.
-
(2002)
Adv Genet
, vol.46
, pp. 485-525
-
-
Wickner, R.B.1
Edskes, H.K.2
Roberts, B.T.3
Pierce, M.4
Baxa, U.5
-
36
-
-
0034160086
-
Protein-only inheritance in yeast: Something to get [PSI+]-ched about
-
Serio TR, Lindquist SL. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol 2001;10:98-105.
-
(2001)
Trends Cell Biol
, vol.10
, pp. 98-105
-
-
Serio, T.R.1
Lindquist, S.L.2
-
37
-
-
0034943645
-
The yeast prion [PSI+]: Molecule insights and functional consequences
-
Serio TR, Lindquist SL. The yeast prion [PSI+]: molecule insights and functional consequences. Adv Protein Chem 2001;57:335-366.
-
(2001)
Adv Protein Chem
, vol.57
, pp. 335-366
-
-
Serio, T.R.1
Lindquist, S.L.2
-
38
-
-
9644287905
-
The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms
-
Bai M, Zhou J-M, Perrett S. The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 2004;279:50025-50030.
-
(2004)
J Biol Chem
, vol.279
, pp. 50025-50030
-
-
Bai, M.1
Zhou, J.-M.2
Perrett, S.3
-
39
-
-
0037124337
-
The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro
-
Bousset L, Thomson NH, Radford SE, Melki R. The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro. EMBO J 2002;21:2903-2911.
-
(2002)
EMBO J
, vol.21
, pp. 2903-2911
-
-
Bousset, L.1
Thomson, N.H.2
Radford, S.E.3
Melki, R.4
-
40
-
-
0033587677
-
Medin: An integral fragment of aotic smooth muscle cell-produced lactadherin forms the most common human amyloid
-
Häggqvist B, Näslund J, Sletten K, Westermark GT, Mucchiano G, Tjernberg LO, Nordstedt C, Engstr̂m U, Westermark P. Medin: an integral fragment of aotic smooth muscle cell-produced lactadherin forms the most common human amyloid. Proc Natl Acad Sci USA 1999;96:8669-8674.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 8669-8674
-
-
Häggqvist, B.1
Näslund, J.2
Sletten, K.3
Westermark, G.T.4
Mucchiano, G.5
Tjernberg, L.O.6
Nordstedt, C.7
Engstr̂m, U.8
Westermark, P.9
-
41
-
-
0026551594
-
Senile aortic amyloid. Evidence for two distinct forms of localized deposits
-
Mucchiano G, Cornwell GG, III, Westermark P. Senile aortic amyloid. Evidence for two distinct forms of localized deposits. Am J Pathol 1992;140:871-877.
-
(1992)
Am J Pathol
, vol.140
, pp. 871-877
-
-
Mucchiano, G.1
Cornwell III, G.G.2
Westermark, P.3
-
42
-
-
0037592927
-
Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
-
Ban T, Hamada D, Hasegawa K, Naiki H, Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 2003;278:16462-16465.
-
(2003)
J Biol Chem
, vol.278
, pp. 16462-16465
-
-
Ban, T.1
Hamada, D.2
Hasegawa, K.3
Naiki, H.4
Goto, Y.5
-
43
-
-
0025005940
-
Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
-
Goormaghtigh E, Cabiaux V, Ruysschaert JM. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur J Biochem 1990;193:409-420.
-
(1990)
Eur J Biochem
, vol.193
, pp. 409-420
-
-
Goormaghtigh, E.1
Cabiaux, V.2
Ruysschaert, J.M.3
-
44
-
-
0029586689
-
Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
-
Ogawa H, Inouye S, Tsuji FI, Yasuda K, Umesono K. Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc Natl Acad Sci USA 1995;92:11899-11903.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 11899-11903
-
-
Ogawa, H.1
Inouye, S.2
Tsuji, F.I.3
Yasuda, K.4
Umesono, K.5
-
45
-
-
1642563960
-
Engineering amyloidogenicity towards the development of nanofibrillar materials
-
Hamada D, Yanagihara I, Tsumoto K. Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends Biotechnol 2004;22:93-97.
-
(2004)
Trends Biotechnol
, vol.22
, pp. 93-97
-
-
Hamada, D.1
Yanagihara, I.2
Tsumoto, K.3
|