-
1
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006; 75: 333-366.
-
(2006)
Annu Rev Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
2
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 2002; 416: 507-511.
-
(2002)
Nature.
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Chiti, F.3
Baroni, F.4
Formigli, L.5
Zurdo, J.6
Taddei, N.7
Ramponi, G.8
Dobson, C.M.9
Stefani, M.10
-
3
-
-
28244458451
-
Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool
-
Gazit E. Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool. FEBS J. 2005; 272: 5971-5978.
-
(2005)
FEBS J.
, vol.272
, pp. 5971-5978
-
-
Gazit, E.1
-
4
-
-
0037144424
-
Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin
-
Reches M, Porat Y, Gazit E. Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin. J Biol Chem. 2002; 277: 35475-35480.
-
(2002)
J Biol Chem.
, vol.277
, pp. 35475-35480
-
-
Reches, M.1
Porat, Y.2
Gazit, E.3
-
5
-
-
0037147221
-
Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones
-
Ben-Zvi AP, Goloubinoff P. Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones. J Biol Chem. 2002; 277: 49422-49427.
-
(2002)
J Biol Chem.
, vol.277
, pp. 49422-49427
-
-
Ben-Zvi, A.P.1
Goloubinoff, P.2
-
6
-
-
0842281551
-
Principles of protein folding, misfolding and aggregation
-
Dobson CM. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol. 2004; 15: 3-16.
-
(2004)
Semin Cell Dev Biol.
, vol.15
, pp. 3-16
-
-
Dobson, C.M.1
-
7
-
-
33846839238
-
Protein particulates: another generic form of protein aggregation?
-
Krebs MRH, Devlin GL, Donald AM. Protein particulates: another generic form of protein aggregation? Biophys J. 2007; 92: 1336-1342.
-
(2007)
Biophys J.
, vol.92
, pp. 1336-1342
-
-
Krebs, M.R.H.1
Devlin, G.L.2
Donald, A.M.3
-
8
-
-
15944405779
-
Amyloids-a functional coat for microorganisms
-
Gebbink MF, Claessen D, Bouma B, Dijkhuizen L, Wösten HA. Amyloids-a functional coat for microorganisms. Nat Rev Microbiol. 2005; 3: 333-341.
-
(2005)
Nat Rev Microbiol.
, vol.3
, pp. 333-341
-
-
Gebbink, M.F.1
Claessen, D.2
Bouma, B.3
Dijkhuizen, L.4
Wösten, H.A.5
-
9
-
-
0038612852
-
Amyloid as a natural product
-
Kelly JW, Balch EW. Amyloid as a natural product. J Cell Biol. 2003; 161: 461-462.
-
(2003)
J Cell Biol.
, vol.161
, pp. 461-462
-
-
Kelly, J.W.1
Balch, E.W.2
-
10
-
-
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
-
11
-
-
55549130444
-
Protein aggregates as depots for the release of biologically active compounds
-
Artemova NV, Kasakov AS, Bumagina ZM, Lyutova EM, Gurvits BYa. Protein aggregates as depots for the release of biologically active compounds. Biochem Biophys Res Commun. 2008; 377: 595-599.
-
(2008)
Biochem Biophys Res Commun.
, vol.377
, pp. 595-599
-
-
Artemova, N.V.1
Kasakov, A.S.2
Bumagina, Z.M.3
Lyutova, E.M.4
Gurvits, B.Y.5
-
12
-
-
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
-
13
-
-
39649101910
-
Physical and chemical perturbations induce the formation of protein aggregates with different structural features
-
Natalello A, Santarella R, Doglia SM, de Marco A. Physical and chemical perturbations induce the formation of protein aggregates with different structural features. Protein Expr Purif. 2008; 58: 356-361.
-
(2008)
Protein Expr Purif.
, vol.58
, pp. 356-361
-
-
Natalello, A.1
Santarella, R.2
Doglia, S.M.3
de Marco, A.4
-
14
-
-
34247516876
-
The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
-
Vera A, González-Montalbán N, Arís A, Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol Bioeng. 2007; 96: 1101-1106.
-
(2007)
Biotechnol Bioeng.
, vol.96
, pp. 1101-1106
-
-
Vera, A.1
González-Montalbán, N.2
Arís, A.3
Villaverde, A.4
-
15
-
-
70449716897
-
Dynamic and supramolecular organisation of α-lactalbumin/lysozyme microspheres: a microscopic study
-
Nigen M, Gaillard C, Croguennec T, Madec M-N, Bouhallab S. Dynamic and supramolecular organisation of α-lactalbumin/lysozyme microspheres: a microscopic study. Biophys Chem. 2010; 146: 30-35.
-
(2010)
Biophys Chem.
, vol.146
, pp. 30-35
-
-
Nigen, M.1
Gaillard, C.2
Croguennec, T.3
Madec, M.-N.4
Bouhallab, S.5
-
16
-
-
0030712099
-
Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins
-
Trivedi VD, Raman B, Rao CM, Ramakrishna T. Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins. FEBS Lett. 1997; 418: 363-366.
-
(1997)
FEBS Lett.
, vol.418
, pp. 363-366
-
-
Trivedi, V.D.1
Raman, B.2
Rao, C.M.3
Ramakrishna, T.4
-
17
-
-
0344442884
-
Prevention of thermal inactivation and aggregation of lysozyme by polyamines
-
Kudou M, Shiraki K, Fujiwara S, Imanaka T, Takagi M. Prevention of thermal inactivation and aggregation of lysozyme by polyamines. Eur J Biochem. 2003; 270: 4547-4554.
-
(2003)
Eur J Biochem.
, vol.270
, pp. 4547-4554
-
-
Kudou, M.1
Shiraki, K.2
Fujiwara, S.3
Imanaka, T.4
Takagi, M.5
-
18
-
-
29544443508
-
Interaction of polyanions with basic proteins: influence of complexing polyanions on the thermoaggregation of oligomeric enzymes
-
Shalova IN, Asryants RA, Sholukh MV, Saso L, Kurganov BI, Muronetz VI, Izumrudov VA. Interaction of polyanions with basic proteins: influence of complexing polyanions on the thermoaggregation of oligomeric enzymes. Macromol Biosci. 2005; 5: 1184-1192.
-
(2005)
Macromol Biosci.
, vol.5
, pp. 1184-1192
-
-
Shalova, I.N.1
Asryants, R.A.2
Sholukh, M.V.3
Saso, L.4
Kurganov, B.I.5
Muronetz, V.I.6
Izumrudov, V.A.7
-
19
-
-
0037474250
-
Cellular polyamines promote the aggregation of α-synuclein
-
Antony T, Hoyer W, Cherny D, Heim G, Jovin TM, Subramaniam V. Cellular polyamines promote the aggregation of α-synuclein. J Biol Chem. 2003; 278: 3235-3240.
-
(2003)
J Biol Chem.
, vol.278
, pp. 3235-3240
-
-
Antony, T.1
Hoyer, W.2
Cherny, D.3
Heim, G.4
Jovin, T.M.5
Subramaniam, V.6
-
20
-
-
0142180141
-
Glycation induces formation of amyloid cross-β structure in albumin
-
Bouma B, Kroon-Batenburg LMJ, Wu Y-P, Brunjes B, Posthuma G, Kranenburg O, Groot PG, Voest EE, Gebbink MFBG. Glycation induces formation of amyloid cross-β structure in albumin. J Biol Chem. 2003; 278: 41810-41819.
-
(2003)
J Biol Chem.
, vol.278
, pp. 41810-41819
-
-
Bouma, B.1
Kroon-Batenburg, L.M.J.2
Wu, Y.-P.3
Brunjes, B.4
Posthuma, G.5
Kranenburg, O.6
Groot, P.G.7
Voest, E.E.8
Gebbink, M.F.B.G.9
-
21
-
-
53049097848
-
Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins
-
Chakraborty A, Basak S. Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins. J Photochem Photobiol. 2008; 93: 36-43.
-
(2008)
J Photochem Photobiol.
, vol.93
, pp. 36-43
-
-
Chakraborty, A.1
Basak, S.2
-
22
-
-
0035941201
-
Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein
-
Uversky VN, Li J, Fink AL. Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein. J Biol Chem. 2001; 276: 44284-44296.
-
(2001)
J Biol Chem.
, vol.276
, pp. 44284-44296
-
-
Uversky, V.N.1
Li, J.2
Fink, A.L.3
-
23
-
-
0035085736
-
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation
-
Chiti F, Taddei N, Stefani M, Dobson CM, Ramponi G. Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci. 2001; 10: 879-886.
-
(2001)
Protein Sci.
, vol.10
, pp. 879-886
-
-
Chiti, F.1
Taddei, N.2
Stefani, M.3
Dobson, C.M.4
Ramponi, G.5
-
24
-
-
5444228298
-
Role of arginine in protein refolding, solubilization, and purification
-
Tsumoto K, Umetsu M, Kumagai I, Ejima D, Philo JS, Arakawa T. Role of arginine in protein refolding, solubilization, and purification. Biotechnol Prog. 2004; 20: 1301-1308.
-
(2004)
Biotechnol Prog.
, vol.20
, pp. 1301-1308
-
-
Tsumoto, K.1
Umetsu, M.2
Kumagai, I.3
Ejima, D.4
Philo, J.S.5
Arakawa, T.6
-
25
-
-
20044370990
-
Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo
-
Yang F, Lim GP, Begum AN, Ubeda OJ, Simmons MR, Ambegaokar SS, Chen P, Kayed R, Glabe CG, Frautschy SA, Cole GM. Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem. 2005; 280: 5892-5901.
-
(2005)
J Biol Chem.
, vol.280
, pp. 5892-5901
-
-
Yang, F.1
Lim, G.P.2
Begum, A.N.3
Ubeda, O.J.4
Simmons, M.R.5
Ambegaokar, S.S.6
Chen, P.7
Kayed, R.8
Glabe, C.G.9
Frautschy, S.A.10
Cole, G.M.11
-
26
-
-
67650477387
-
Elucidating the mechanism of lipid membrane-induced IAPP fibrillogenesis and its inhibition by the red wine compound resveratrol: a synchrotron X-ray reflectivity study
-
Evers F, Jeworrek C, Tiemeyer S, Weise K, Sellin D, Paulus M, Struth B, Tolan M, Winter R. Elucidating the mechanism of lipid membrane-induced IAPP fibrillogenesis and its inhibition by the red wine compound resveratrol: a synchrotron X-ray reflectivity study. J Am Chem Soc. 2009; 131: 9516-9521.
-
(2009)
J Am Chem Soc.
, vol.131
, pp. 9516-9521
-
-
Evers, F.1
Jeworrek, C.2
Tiemeyer, S.3
Weise, K.4
Sellin, D.5
Paulus, M.6
Struth, B.7
Tolan, M.8
Winter, R.9
-
27
-
-
29344455729
-
Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein
-
Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, Dobson CM, Wilson MR, Carver JA. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. Biochemistry. 2005; 44: 17027-17036.
-
(2005)
Biochemistry.
, vol.44
, pp. 17027-17036
-
-
Thorn, D.C.1
Meehan, S.2
Sunde, M.3
Rekas, A.4
Gras, S.L.5
MacPhee, C.E.6
Dobson, C.M.7
Wilson, M.R.8
Carver, J.A.9
-
28
-
-
54749122331
-
Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: nanomolar affinity inhibition of insulin aggregation by an IAPP mimic
-
Velkova A, Tatarek-Nossol M, Andreetto E, Kapurniotu A. Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: nanomolar affinity inhibition of insulin aggregation by an IAPP mimic. Angew Chem Int Ed. 2008; 47: 7114-7118.
-
(2008)
Angew Chem Int Ed.
, vol.47
, pp. 7114-7118
-
-
Velkova, A.1
Tatarek-Nossol, M.2
Andreetto, E.3
Kapurniotu, A.4
-
29
-
-
66149143156
-
The osmolyte betaine promotes protein misfolding and disruption of protein aggregates
-
Natalello A, Liu J, Ami D, Doglia SM, de Marco A. The osmolyte betaine promotes protein misfolding and disruption of protein aggregates. Proteins. 2009; 75: 509-517.
-
(2009)
Proteins.
, vol.75
, pp. 509-517
-
-
Natalello, A.1
Liu, J.2
Ami, D.3
Doglia, S.M.4
de Marco, A.5
-
30
-
-
0030059690
-
The molten globule state of α-lactalbumin
-
Kuwajima K. The molten globule state of α-lactalbumin. FASEB J. 1996; 10: 102-109.
-
(1996)
FASEB J.
, vol.10
, pp. 102-109
-
-
Kuwajima, K.1
-
31
-
-
0034711229
-
Crystal structure of apo- and holo-bovine α-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interaction
-
Christina ED, Brew K, Acharya KR. Crystal structure of apo- and holo-bovine α-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interaction. J Biol Chem. 2000; 275: 37021-37029.
-
(2000)
J Biol Chem.
, vol.275
, pp. 37021-37029
-
-
Christina, E.D.1
Brew, K.2
Acharya, K.R.3
-
33
-
-
0036704245
-
Aggregate formation and the structure of the aggregates of disulfide-reduced proteins
-
Takase K, Higashi T, Omura T. Aggregate formation and the structure of the aggregates of disulfide-reduced proteins. J Protein Chem. 2002; 21: 427-433.
-
(2002)
J Protein Chem.
, vol.21
, pp. 427-433
-
-
Takase, K.1
Higashi, T.2
Omura, T.3
-
34
-
-
0032939419
-
Molecular dynamics simulation of α-lactalbumin and calcium binding c-type lysozyme
-
Iyer LK, Qasba PK. Molecular dynamics simulation of α-lactalbumin and calcium binding c-type lysozyme. Protein Eng. 1999; 12: 129-139.
-
(1999)
Protein Eng.
, vol.12
, pp. 129-139
-
-
Iyer, L.K.1
Qasba, P.K.2
-
35
-
-
0025811817
-
Lysozyme and α-lactalbumin: structure, function, and interrelationships
-
McKenzie HA, White FHJ. Lysozyme and α-lactalbumin: structure, function, and interrelationships. Adv Protein Chem. 1991; 41: 173-315.
-
(1991)
Adv Protein Chem.
, vol.41
, pp. 173-315
-
-
McKenzie, H.A.1
White, F.H.J.2
-
36
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin T
-
LeVine H. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999; 309: 274-284.
-
(1999)
Methods Enzymol.
, vol.309
, pp. 274-284
-
-
LeVine, H.1
-
37
-
-
0024509805
-
Fluorimetric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
-
Naiki H, Higuchi K, Hosokawa M, Takeda T. Fluorimetric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal Biochem. 1989; 177: 244-249.
-
(1989)
Anal Biochem.
, vol.177
, pp. 244-249
-
-
Naiki, H.1
Higuchi, K.2
Hosokawa, M.3
Takeda, T.4
-
38
-
-
72749101127
-
Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin
-
Bumagina ZM, Gurvits BYa, Artemova NV, Muranov KO, Yudin IK, Kurganov BI. Mechanism of suppression of dithiothreitol-induced aggregation of bovine α-lactalbumin by α-crystallin. Biophys Chem. 2010; 146: 108-117.
-
(2010)
Biophys Chem.
, vol.146
, pp. 108-117
-
-
Bumagina, Z.M.1
Gurvits, BY.2
Artemova, N.V.3
Muranov, K.O.4
Yudin, I.K.5
Kurganov, B.I.6
-
39
-
-
0026483279
-
Alpha-crystallin can function as a molecular chaperone
-
Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992; 89: 10449-10453.
-
(1992)
Proc Natl Acad Sci USA.
, vol.89
, pp. 10449-10453
-
-
Horwitz, J.1
-
40
-
-
0028801832
-
Role of hydrophobic and hydrophilic forces in peptide-protein interaction: new advances
-
Cserhaty T, Szogy M. Role of hydrophobic and hydrophilic forces in peptide-protein interaction: new advances. Peptides. 1995; 16: 165-173.
-
(1995)
Peptides.
, vol.16
, pp. 165-173
-
-
Cserhaty, T.1
Szogy, M.2
-
41
-
-
0034087948
-
Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity
-
Bhatia R, Lin H, Lal R. Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity. FASEB J. 2000; 14: 1233-1243.
-
(2000)
FASEB J.
, vol.14
, pp. 1233-1243
-
-
Bhatia, R.1
Lin, H.2
Lal, R.3
-
42
-
-
33645504776
-
Nano neuro knitting: peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision
-
Ellis-Behnke RG, Liang Y-X, You S-W, Tay DKC, Zhang S, So K-F, Schneider GE. Nano neuro knitting: peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision. Proc Natl Acad Sci USA. 2006; 103: 5054-5059.
-
(2006)
Proc Natl Acad Sci USA.
, vol.103
, pp. 5054-5059
-
-
Ellis-Behnke, R.G.1
Liang, Y.-X.2
You, S.-W.3
Tay, D.K.C.4
Zhang, S.5
So, K.-F.6
Schneider, G.E.7
-
43
-
-
33645510751
-
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase
-
Bemporad F, Taddei N, Stefani M, Chiti F. Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase. Protein Sci. 2006; 15: 862-870.
-
(2006)
Protein Sci.
, vol.15
, pp. 862-870
-
-
Bemporad, F.1
Taddei, N.2
Stefani, M.3
Chiti, F.4
-
44
-
-
12244285938
-
Molecular basis for amyloid fibril formation and stability
-
Makin OS, Atkins E, Sikorski P, Johansson J, Serpell LC. Molecular basis for amyloid fibril formation and stability. Proc Natl Acad Sci USA. 2005; 102: 315-320.
-
(2005)
Proc Natl Acad Sci USA.
, vol.102
, pp. 315-320
-
-
Makin, O.S.1
Atkins, E.2
Sikorski, P.3
Johansson, J.4
Serpell, L.C.5
-
45
-
-
0842307662
-
Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed 13C solid-state NMR spectroscopy
-
Naito A, Kamihira M, Inoue R, Saito H. Structural diversity of amyloid fibril formed in human calcitonin as revealed by site-directed 13C solid-state NMR spectroscopy. Magn Reson Chem. 2004; 42: 247-257.
-
(2004)
Magn Reson Chem.
, vol.42
, pp. 247-257
-
-
Naito, A.1
Kamihira, M.2
Inoue, R.3
Saito, H.4
|