-
1
-
-
0347357617
-
Protein folding and misfolding
-
Dobson, C. M. 2003. Protein folding and misfolding. Nature. 426:884-890.
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
2
-
-
0344944630
-
Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
-
Stefani, M., and C. M. Dobson. 2003. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81:678-699.
-
(2003)
J. Mol. Med.
, vol.81
, pp. 678-699
-
-
Stefani, M.1
Dobson, C.M.2
-
3
-
-
2342569618
-
Conformational constraints for amyloid fibrillation: The importance of being unfolded
-
Uversky, V. N., and A. L. Fink. 2004. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta. 1698:131-153.
-
(2004)
Biochim. Biophys. Acta
, vol.1698
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
4
-
-
2542427690
-
Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
-
Walsh, D. M., and D. J. Selkoe. 2004. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11:213-228.
-
(2004)
Protein Pept. Lett.
, vol.11
, pp. 213-228
-
-
Walsh, D.M.1
Selkoe, D.J.2
-
5
-
-
0030801746
-
The structure of amyloid fibrils by electron microscopy and x-ray diffraction
-
Sunde, M., and C. Blake. 1997. The structure of amyloid fibrils by electron microscopy and x-ray diffraction. Adv. Protein Chem. 50:123-159.
-
(1997)
Adv. Protein Chem.
, vol.50
, pp. 123-159
-
-
Sunde, M.1
Blake, C.2
-
6
-
-
0034725535
-
The protofilament substructure of amyloid fibrils
-
Serpell, L. C., M. Sunde, M. D. Benson, G. A. Tennent, M. B. Pepys, and P. E. Fraser. 2000. The protofilament substructure of amyloid fibrils. J. Mol. Biol. 300:1033-1039.
-
(2000)
J. Mol. Biol.
, vol.300
, pp. 1033-1039
-
-
Serpell, L.C.1
Sunde, M.2
Benson, M.D.3
Tennent, G.A.4
Pepys, M.B.5
Fraser, P.E.6
-
7
-
-
0037465708
-
Insights into the amyloid folding problem from solid-state NMR
-
Tycko, R. 2003. Insights into the amyloid folding problem from solid-state NMR. Biochemistry. 42:3151-3159.
-
(2003)
Biochemistry
, vol.42
, pp. 3151-3159
-
-
Tycko, R.1
-
8
-
-
0032855483
-
Quantifying amyloid by Congo red spectral shift assay
-
Klunk, W. E., R. F. Jacob, and R. P. Mason. 1999. Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol. 309:285-305.
-
(1999)
Methods Enzymol.
, vol.309
, pp. 285-305
-
-
Klunk, W.E.1
Jacob, R.F.2
Mason, R.P.3
-
9
-
-
0032849874
-
Quantification of beta-sheet amyloid fibril structures with thioflavin T
-
LeVine 3rd, H. 1999. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:274-284.
-
(1999)
Methods Enzymol.
, vol.309
, pp. 274-284
-
-
Levine III, H.1
-
10
-
-
11144222595
-
The binding of thioflavin-T to amyloid fibrils: Localisation and implications
-
Krebs, M. R., E. H. Bromley, and A. M. Donald. 2005. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149:30-37.
-
(2005)
J. Struct. Biol.
, vol.149
, pp. 30-37
-
-
Krebs, M.R.1
Bromley, E.H.2
Donald, A.M.3
-
11
-
-
0035933721
-
Is Congo red an amyloid-specific dye?
-
Khurana, R., V. N. Uversky, L. Nielsen, and A. L. Fink. 2001. Is Congo red an amyloid-specific dye? J. Biol. Chem. 276:22715-22721.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 22715-22721
-
-
Khurana, R.1
Uversky, V.N.2
Nielsen, L.3
Fink, A.L.4
-
12
-
-
2142762962
-
Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p
-
Bousset, L., V. Redeker, P. Decottignies, S. Dubois, P. Le Marechal, and R. Melki. 2004. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry. 43:5022-5032.
-
(2004)
Biochemistry
, vol.43
, pp. 5022-5032
-
-
Bousset, L.1
Redeker, V.2
Decottignies, P.3
Dubois, S.4
Le Marechal, P.5
Melki, R.6
-
13
-
-
0345118103
-
Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: A model for misfolding in polyglutamine disease
-
Chow, M. K., H. L. Paulson, and S. P. Bottomley. 2004. Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease. J. Mol. Biol. 335:333-341.
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 333-341
-
-
Chow, M.K.1
Paulson, H.L.2
Bottomley, S.P.3
-
14
-
-
0037168643
-
Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
-
Lindberg, M. J., L. Tibell, and M. Oliveberg. 2002. Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proc. Natl. Acad. Sci. USA. 99:16607-16612.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 16607-16612
-
-
Lindberg, M.J.1
Tibell, L.2
Oliveberg, M.3
-
15
-
-
0036220131
-
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme
-
Canet, D., A. M. Last, P. Tito, M. Sunde, A. Spencer, D. B. Archer, C. Redfield, C. V. Robinson, and C. M. Dobson. 2002. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9:308-315.
-
(2002)
Nat. Struct. Biol.
, vol.9
, pp. 308-315
-
-
Canet, D.1
Last, A.M.2
Tito, P.3
Sunde, M.4
Spencer, A.5
Archer, D.B.6
Redfield, C.7
Robinson, C.V.8
Dobson, C.M.9
-
16
-
-
0032006678
-
The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
-
Kelly, J. W. 1998. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:101-106.
-
(1998)
Curr. Opin. Struct. Biol.
, vol.8
, pp. 101-106
-
-
Kelly, J.W.1
-
18
-
-
9144264986
-
Polyglutamine expansion in Ataxin-3 does not affect protein stability: Implications for misfolding and disease
-
Chow, M. K., A. M. Ellisdon, L. D. Cabrita, and S. P. Bottomley. 2005. Polyglutamine expansion in Ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 279:47643-47651.
-
(2005)
J. Biol. Chem.
, vol.279
, pp. 47643-47651
-
-
Chow, M.K.1
Ellisdon, A.M.2
Cabrita, L.D.3
Bottomley, S.P.4
-
19
-
-
0033777523
-
Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
-
Bouchard, M., J. Zurdo, E. J. Nettleton, C. M. Dobson, and C. V. Robinson. 2000. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9:960-967.
-
(2000)
Protein Sci.
, vol.9
, pp. 960-967
-
-
Bouchard, M.1
Zurdo, J.2
Nettleton, E.J.3
Dobson, C.M.4
Robinson, C.V.5
-
20
-
-
3342902033
-
Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
-
Pedersen, J. S., G. Christensen, and D. E. Otzen. 2004. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341:575-588.
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 575-588
-
-
Pedersen, J.S.1
Christensen, G.2
Otzen, D.E.3
-
21
-
-
1842790837
-
Aggregation of the acylphosphatase from Sulfolobus solfataricus: The folded and partially unfolded states can both be precursors for amyloid formation
-
Plakoutsi, G., N. Taddei, M. Stefani, and F. Chiti. 2004. Aggregation of the acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation. J. Biol. Chem. 279:14111-14119.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 14111-14119
-
-
Plakoutsi, G.1
Taddei, N.2
Stefani, M.3
Chiti, F.4
-
22
-
-
0037472736
-
Characterization of a novel Drosophila melanogaster acylphosphatase
-
Degl'Innocenti, D., M. Ramazzotti, R. Marzocchini, F. Chiti, G. Raugei, and G. Ramponi. 2003. Characterization of a novel Drosophila melanogaster acylphosphatase. FEBS Lett. 535:171-174.
-
(2003)
FEBS Lett.
, vol.535
, pp. 171-174
-
-
Degl'Innocenti, D.1
Ramazzotti, M.2
Marzocchini, R.3
Chiti, F.4
Raugei, G.5
Ramponi, G.6
-
23
-
-
14644399127
-
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase
-
Zuccotti, S., C. Rosano, M. Ramazzotti, D. Degl'Innocenti, M. Stefani, G. Manao, and M. Bolognesi. 2004. Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr. D Biol. Crystallogr. 60:1177-1179.
-
(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
-
24
-
-
0017123760
-
A new synthesis of benzoyl phosphate: A substrate for acyl phosphatase assay
-
Camici, G., G. Manao, G. Cappugi, and G. Ramponi. 1976. A new synthesis of benzoyl phosphate: a substrate for acyl phosphatase assay. Experientia. 32:535-536.
-
(1976)
Experientia
, vol.32
, pp. 535-536
-
-
Camici, G.1
Manao, G.2
Cappugi, G.3
Ramponi, G.4
-
25
-
-
0025301439
-
Protein secondary structure and circular dichroism: A practical guide
-
Johnson, W. C., Jr. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7:205-214.
-
(1990)
Proteins
, vol.7
, pp. 205-214
-
-
Johnson Jr., W.C.1
-
26
-
-
0013923439
-
Aromatic acyl phosphates as substrates of acyl phosphatase
-
Ramponi, G., C. Treves, and A. A. Guerritore. 1966. Aromatic acyl phosphates as substrates of acyl phosphatase. Arch. Biochem. Biophys. 115:129-135.
-
(1966)
Arch. Biochem. Biophys.
, vol.115
, pp. 129-135
-
-
Ramponi, G.1
Treves, C.2
Guerritore, A.A.3
-
27
-
-
0023697408
-
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl alpha-chymotrypsin using different denaturants
-
Santoro, M. M., and D. W. Bolen. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyl-methanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry. 27:8063-8068.
-
(1988)
Biochemistry
, vol.27
, pp. 8063-8068
-
-
Santoro, M.M.1
Bolen, D.W.2
-
28
-
-
0026345750
-
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
-
Jackson, S. E., and A. R. Fersht. 1991. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry. 30:10428-10435.
-
(1991)
Biochemistry
, vol.30
, pp. 10428-10435
-
-
Jackson, S.E.1
Fersht, A.R.2
-
29
-
-
0028063528
-
Determination of protein tertiary structure class from circular dichroism spectra
-
Venyaminov, S. Yu., and K. S. Vassilenko. 1994. Determination of protein tertiary structure class from circular dichroism spectra. Anal. Biochem. 222:176-184.
-
(1994)
Anal. Biochem.
, vol.222
, pp. 176-184
-
-
Yu, V.S.1
Vassilenko, K.S.2
-
30
-
-
11144353842
-
Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
-
Relini, A., C. Canale, S. Torrassa, R. Rolandi, A. Gliozzi, C. Rosano, M. Bolognesi, G. Plakoutsi, M. Bucciantini, F. Chiti, and M. Stefani. 2004. Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J. Mol. Biol. 338:943-957.
-
(2004)
J. Mol. Biol.
, vol.338
, pp. 943-957
-
-
Relini, A.1
Canale, C.2
Torrassa, S.3
Rolandi, R.4
Gliozzi, A.5
Rosano, C.6
Bolognesi, M.7
Plakoutsi, G.8
Bucciantini, M.9
Chiti, F.10
Stefani, M.11
-
31
-
-
0013800421
-
The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
-
Stryer, L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13:482-495.
-
(1965)
J. Mol. Biol.
, vol.13
, pp. 482-495
-
-
Stryer, L.1
-
32
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn, O. B. 1995. Molten globule and protein folding. Adv. Protein Chem. 47:83-229.
-
(1995)
Adv. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
33
-
-
0031972919
-
1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
-
Matulis, D., and R. Lovrien. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74:422-429.
-
(1998)
Biophys. J.
, vol.74
, pp. 422-429
-
-
Matulis, D.1
Lovrien, R.2
-
34
-
-
0030814166
-
Insights into acylphosphatase structure and catalytic mechanism
-
Stefani, M., N. Taddei, and G. Ramponi. 1997. Insights into acylphosphatase structure and catalytic mechanism. Cell. Mol. Life Sci. 53:141-151.
-
(1997)
Cell. Mol. Life Sci.
, vol.53
, pp. 141-151
-
-
Stefani, M.1
Taddei, N.2
Ramponi, G.3
-
35
-
-
0033988167
-
Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol
-
Hamada, D., F. Chili, J. I. Guijarro, M. Kataoka, N. Taddei, and C. M. Dobson. 2000. Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nat. Struct. Biol. 7:58-61.
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 58-61
-
-
Hamada, D.1
Chili, F.2
Guijarro, J.I.3
Kataoka, M.4
Taddei, N.5
Dobson, C.M.6
-
36
-
-
0025698613
-
Transient folding intermediates characterized by protein engineering
-
Matouschek, A., J. T. Kellis, Jr., L. Serrano, M. Bycroft, and A. R. Fersht. 1990. Transient folding intermediates characterized by protein engineering. Nature. 346:440-445.
-
(1990)
Nature
, vol.346
, pp. 440-445
-
-
Matouschek, A.1
Kellis Jr., J.T.2
Serrano, L.3
Bycroft, M.4
Fersht, A.R.5
-
37
-
-
14644406760
-
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state
-
Marcon, G., G. Plakoutsi, C. Canale, A. Relini, N. Taddei, C. M. Dobson, G. Ramponi, and F. Chiti. 2005. Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. J. Mol. Biol. 347:323-335.
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 323-335
-
-
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
-
38
-
-
3242785264
-
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
-
DuBay, K. F., A. P. Pawar, F. Chiti, J. Zurdo, C. M. Dobson, and M. Vendruscolo. 2004. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J. Mol. Biol. 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
-
39
-
-
0037059069
-
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
-
Chiti, F., M. Calamai, N. Taddei, M. Stefani, G. Ramponi, and C. M. Dobson. 2002. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA. 99:16419-16426.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 16419-16426
-
-
Chiti, F.1
Calamai, M.2
Taddei, N.3
Stefani, M.4
Ramponi, G.5
Dobson, C.M.6
-
40
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
41
-
-
0033814617
-
Protein engineering as a strategy to avoid formation of amyloid fibrils
-
Villegas, V., J. Zurdo, V. V. Filimonov, F. X. Aviles, C. M. Dobson, and L. Serrano. 2000. Protein engineering as a strategy to avoid formation of amyloid fibrils. Protein Sci. 9:1700-1708.
-
(2000)
Protein Sci.
, vol.9
, pp. 1700-1708
-
-
Villegas, V.1
Zurdo, J.2
Filimonov, V.V.3
Aviles, F.X.4
Dobson, C.M.5
Serrano, L.6
-
42
-
-
0034612254
-
The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state
-
Ferrao-Gonzales, A. D., S. O. Souto, J. L. Silva, and D. Foguel. 2000. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc. Natl. Acad. Sci. USA. 97:6445-6450.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 6445-6450
-
-
Ferrao-Gonzales, A.D.1
Souto, S.O.2
Silva, J.L.3
Foguel, D.4
-
43
-
-
0034254241
-
Partially unfolded states of β(2)-microglobulin and amyloid formation in vitro
-
McParland, V. J., N. M. Kad, A. P. Kalverda, A. Brown, P. Kirwin-Jones, M. G. Hunter, M. Sunde, and S. E. Radford. 2000. Partially unfolded states of β(2)-microglobulin and amyloid formation in vitro. Biochemistry. 39:8735-8746.
-
(2000)
Biochemistry
, vol.39
, pp. 8735-8746
-
-
McParland, V.J.1
Kad, N.M.2
Kalverda, A.P.3
Brown, A.4
Kirwin-Jones, P.5
Hunter, M.G.6
Sunde, M.7
Radford, S.E.8
-
44
-
-
0034599720
-
Mutational analysis of the propensity for amyloid formation by a globular protein
-
Chiti, R, N. Taddei, M. Bucciantini, P. White, G. Ramponi, and C. M. Dobson. 2000. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19:1441-1449.
-
(2000)
EMBO J.
, vol.19
, pp. 1441-1449
-
-
Chiti, R.1
Taddei, N.2
Bucciantini, M.3
White, P.4
Ramponi, G.5
Dobson, C.M.6
-
45
-
-
0033020141
-
Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
-
Raffen, R., L. J. Dieckman, M. Szpunar, C. Wunschl, P. R. Pokkuluri, P. Dave, P. Wilkins Stevens, X. Cai, M. Schiffer, and F. J. Stevens. 1999. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains. Protein Sci. 8:509-517.
-
(1999)
Protein Sci.
, vol.8
, pp. 509-517
-
-
Raffen, R.1
Dieckman, L.J.2
Szpunar, M.3
Wunschl, C.4
Pokkuluri, P.R.5
Dave, P.6
Wilkins Stevens, P.7
Cai, X.8
Schiffer, M.9
Stevens, F.J.10
-
46
-
-
0037058942
-
Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
-
Hammarstrom, P., X. Jiang, A. R. Hurshman, E. T. Powers, and J. W. Kelly. 2002. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proc. Natl. Acad. Sci. USA. 99:16427-16432.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 16427-16432
-
-
Hammarstrom, P.1
Jiang, X.2
Hurshman, A.R.3
Powers, E.T.4
Kelly, J.W.5
-
47
-
-
0034255027
-
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
-
Ramirez-Alvarado, M., J. S. Merkel, and L. Regan. 2000. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. USA. 97:8979-8984.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 8979-8984
-
-
Ramirez-Alvarado, M.1
Merkel, J.S.2
Regan, L.3
-
48
-
-
15444373859
-
Investigating the effects of mutations on protein aggregation in the cell
-
Calloni, G., S. Zoffoli, M. Stefani, C. M. Dobson, and F. Chiti. 2005. Investigating the effects of mutations on protein aggregation in the cell. J. Biol. Chem. 280:10607-10613.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 10607-10613
-
-
Calloni, G.1
Zoffoli, S.2
Stefani, M.3
Dobson, C.M.4
Chiti, F.5
-
49
-
-
0346500469
-
The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process
-
Monti, M., B. L. Garolla di Bard, G. Calloni, F. Chiti, A. Amoresano, G. Ramponi, and P. Pucci. 2004. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J. Mol. Biol. 336:253-262.
-
(2004)
J. Mol. Biol.
, vol.336
, pp. 253-262
-
-
Monti, M.1
Garolla Di Bard, B.L.2
Calloni, G.3
Chiti, F.4
Amoresano, A.5
Ramponi, G.6
Pucci, P.7
-
50
-
-
0037022563
-
Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
-
Richardson, J. S., and D. C. Richardson. 2002. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA. 99:2754-2759.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 2754-2759
-
-
Richardson, J.S.1
Richardson, D.C.2
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