-
2
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332
-
(1999)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
4
-
-
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 C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA. 96:1999;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
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
Sunde M., Serpell L.C., Bartlam M., Fraser P.E., Pepys M.B., Blake C.C.F. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273:1997;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.F.6
-
7
-
-
0029981197
-
Alternative conformations of amyloidogenic proteins govern their behaviour
-
Kelly J.W. Alternative conformations of amyloidogenic proteins govern their behaviour. Curr. Opin. Struct. Biol. 6:1996;11-17
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 11-17
-
-
Kelly, J.W.1
-
8
-
-
0026101636
-
Aggregation and secondary structure of synthetic amyloid βa4 peptides of Alzheimer's disease
-
Hilbich C., Kisters-Woike B., Reed J., Masters C., Beyreuther K. Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease. J. Mol. Biol. 218:1991;149-163
-
(1991)
J. Mol. Biol.
, vol.218
, pp. 149-163
-
-
Hilbich, C.1
Kisters-Woike, B.2
Reed, J.3
Masters, C.4
Beyreuther, K.5
-
9
-
-
0027258525
-
The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
-
Jarrett J.T., Berger E.P., Lansbury P.T. Jr. The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemsitry. 32:1993;4693-4697
-
(1993)
Biochemsitry
, vol.32
, pp. 4693-4697
-
-
Jarrett, J.T.1
Berger, E.P.2
Lansbury Jr., P.T.3
-
10
-
-
0029854533
-
Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence
-
Esler W.P., Stimson E.R., Ghilardi J.R., Lu Y.A., Felix A.M., Vinters H.V., et al. Point substitution in the central hydrophobic cluster of a human beta-amyloid congener disrupts peptide folding and abolishes plaque competence. Biochemistry. 35:1996;13914-13921
-
(1996)
Biochemistry
, vol.35
, pp. 13914-13921
-
-
Esler, W.P.1
Stimson, E.R.2
Ghilardi, J.R.3
Lu, Y.A.4
Felix, A.M.5
Vinters, H.V.6
-
11
-
-
0029966282
-
Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis
-
Helms L.R., Wetzel R. Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. J. Mol. Biol. 257:1996;77-86
-
(1996)
J. Mol. Biol.
, vol.257
, pp. 77-86
-
-
Helms, L.R.1
Wetzel, R.2
-
12
-
-
0035823520
-
Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation
-
Azriel R., Gazit E. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J. Biol. Chem. 276:2001;34156-34161
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 34156-34161
-
-
Azriel, R.1
Gazit, E.2
-
13
-
-
0035847063
-
The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C)
-
Thompson A.J., Barnham K.J., Norton R.S., Barrow C.J. The Val-210-Ile pathogenic Creutzfeldt-Jakob disease mutation increases both the helical and aggregation propensities of a sequence corresponding to helix-3 of PrP(C). Biochim. Biophys. Acta. 1544:2001;242-254
-
(2001)
Biochim. Biophys. Acta
, vol.1544
, pp. 242-254
-
-
Thompson, A.J.1
Barnham, K.J.2
Norton, R.S.3
Barrow, C.J.4
-
14
-
-
0033567401
-
Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126
-
Salmona M., Malesani P., De Gioia L., Gorla S., Bruschi M., Molinari A., et al. Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126. Biochem. J. 342:1999;207-214
-
(1999)
Biochem. J.
, vol.342
, pp. 207-214
-
-
Salmona, M.1
Malesani, P.2
De Gioia, L.3
Gorla, S.4
Bruschi, M.5
Molinari, A.6
-
15
-
-
0035951869
-
A hydrophobic stretch of 12 amino acid residues in the middle of synuclein is essential for filament assembly
-
Giasson B.I., Murray I.V., Trojanowski J.Q., Lee V.M. A hydrophobic stretch of 12 amino acid residues in the middle of synuclein is essential for filament assembly. J. Biol. Chem. 276:2001;2380-2386
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 2380-2386
-
-
Giasson, B.I.1
Murray, I.V.2
Trojanowski, J.Q.3
Lee, V.M.4
-
16
-
-
0036830506
-
Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
-
Li L., Von Bergen M., Mandelkow E.M., Mandelkow E. Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis. J. Biol. Chem. 277:2002;41390-41400
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 41390-41400
-
-
Li, L.1
Von Bergen, M.2
Mandelkow, E.M.3
Mandelkow, E.4
-
17
-
-
0036166319
-
Kinetic partitioning of protein folding and aggregation
-
Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G., Dobson C.M. Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9:2002;137-143
-
(2002)
Nature Struct. Biol.
, vol.9
, pp. 137-143
-
-
Chiti, F.1
Taddei, N.2
Baroni, F.3
Capanni, C.4
Stefani, M.5
Ramponi, G.6
Dobson, C.M.7
-
18
-
-
0042467550
-
Rationalization of the effects of mutations on peptide and protein aggregation rates
-
Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature. 424:2003;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
-
19
-
-
0037059063
-
De novo designed peptide-based amyloid fibrils
-
López de la Paz M., Goldie K., Zurdo J., Lacroix E., Dobson C.M., Hoenger A., Serrano L. De novo designed peptide-based amyloid fibrils. Proc. Natl Acad. Sci. USA. 99:2002;16052-16057
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 16052-16057
-
-
López De La Paz, M.1
Goldie, K.2
Zurdo, J.3
Lacroix, E.4
Dobson, C.M.5
Hoenger, A.6
Serrano, L.7
-
20
-
-
0037059069
-
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
-
Chiti F., Calamai M., Taddei N., Stefani M., Ramponi G., Dobson C.M. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl Acad. Sci. USA. 99:2002;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
-
21
-
-
0344875516
-
Amyloid fibril formation in the context of full-length protein
-
Chiba T., Hagihara Y., Higurashi T., Hasegawa K., Naiki H., Goto Y. Amyloid fibril formation in the context of full-length protein. J. Biol. Chem. 278:2003;47016-47024
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 47016-47024
-
-
Chiba, T.1
Hagihara, Y.2
Higurashi, T.3
Hasegawa, K.4
Naiki, H.5
Goto, Y.6
-
22
-
-
9044229145
-
On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants
-
Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl Acad. Sci. USA. 93:1996;1125-1129
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 1125-1129
-
-
Lomakin, A.1
Chung, D.S.2
Benedek, G.B.3
Kirschner, D.A.4
Teplow, D.B.5
-
23
-
-
0033538541
-
Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
-
Wood S.J., Wypych J., Steavenson S., Louis J.C., Citron M., Biere A.L. Alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease. J. Biol. Chem. 274:1999;19509-19512
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 19509-19512
-
-
Wood, S.J.1
Wypych, J.2
Steavenson, S.3
Louis, J.C.4
Citron, M.5
Biere, A.L.6
-
24
-
-
0035918550
-
Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
-
Nielsen L., Khurana R., Coats A., Frøkjær S., Brange J., Vyas S., Uversky V.N., Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 40:2001;6036-6046
-
(2001)
Biochemistry
, vol.40
, pp. 6036-6046
-
-
Nielsen, L.1
Khurana, R.2
Coats, A.3
Frøkjær, S.4
Brange, J.5
Vyas, S.6
Uversky, V.N.7
Fink, A.L.8
-
25
-
-
0033580679
-
Structural changes in the transition state of protein folding: An alternative interpretation of curved chevron plots
-
Otzen D.E., Kristensen O., Proctor M., Oliveberg M. Structural changes in the transition state of protein folding: an alternative interpretation of curved chevron plots. Biochemistry. 38:1999;6499-6511
-
(1999)
Biochemistry
, vol.38
, pp. 6499-6511
-
-
Otzen, D.E.1
Kristensen, O.2
Proctor, M.3
Oliveberg, M.4
-
26
-
-
0032718386
-
Salt-induced detour through compact regions of the protein folding landscape
-
Otzen D.E., Oliveberg M. Salt-induced detour through compact regions of the protein folding landscape. Proc. Natl Acad. Sci. USA. 96:1999;11746-11751
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 11746-11751
-
-
Otzen, D.E.1
Oliveberg, M.2
-
27
-
-
0036293485
-
Conformational plasticity in folding of the split β-α-β protein S6: Evidence for burst-phase disruption of the native state
-
Otzen D.E., Oliveberg M. Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state. J. Mol. Biol. 317:2002;613-627
-
(2002)
J. Mol. Biol.
, vol.317
, pp. 613-627
-
-
Otzen, D.E.1
Oliveberg, M.2
-
28
-
-
0034730203
-
Designed protein tetramer zipped together with an Alzheimer sequence: A structural clue to amyloid assembly
-
Otzen D.E., Kristensen P., Oliveberg M. Designed protein tetramer zipped together with an Alzheimer sequence: a structural clue to amyloid assembly. Proc. Natl Acad. Sci. USA. 97:2000;9907-9912
-
(2000)
Proc. Natl Acad. Sci. USA
, vol.97
, pp. 9907-9912
-
-
Otzen, D.E.1
Kristensen, P.2
Oliveberg, M.3
-
29
-
-
0034599720
-
Mutational analysis of the propensity for amyloid formation by a globular protein
-
Chiti F., Taddei N., Bucciantini M., White P., Ramponi G., 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
-
30
-
-
0027416047
-
Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
-
Zhang S., Holmes T., Lockshin C., Rich A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc. Natl Acad. Sci. USA. 90:1993;3334-3338
-
(1993)
Proc. Natl Acad. Sci. USA
, vol.90
, pp. 3334-3338
-
-
Zhang, S.1
Holmes, T.2
Lockshin, C.3
Rich, A.4
-
31
-
-
1842845084
-
Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial
-
Caplan M.R., Schwartzfarb E.M., Zhang S., Kamm R.D., Lauffenburger D.A. Effects of systematic variation of amino acid sequence on the mechanical properties of a self-assembling, oligopeptide biomaterial. J. Biomater. Sci. Polym. Ed. 13:2002;225-236
-
(2002)
J. Biomater. Sci. Polym. Ed.
, vol.13
, pp. 225-236
-
-
Caplan, M.R.1
Schwartzfarb, E.M.2
Zhang, S.3
Kamm, R.D.4
Lauffenburger, D.A.5
-
32
-
-
0142247606
-
PH-dependent amyloid and protofibril formation by the ABri peptide of Familial British Dementia
-
Srinivasan R., Jones E.M., Liu K., Ghiso J., Marchant R.E., Zagorski M.G. pH-dependent amyloid and protofibril formation by the ABri peptide of Familial British Dementia. J. Mol. Biol. 333:2003;1003-1023
-
(2003)
J. Mol. Biol.
, vol.333
, pp. 1003-1023
-
-
Srinivasan, R.1
Jones, E.M.2
Liu, K.3
Ghiso, J.4
Marchant, R.E.5
Zagorski, M.G.6
-
33
-
-
0032855483
-
Quantifying amyloid by Congo red spectral shift assay
-
Klunk W.E., Jacob R.F., Mason R.P. Quantifying amyloid by Congo red spectral shift assay. Methods Enzymol. 309:1999;285-305
-
(1999)
Methods Enzymol.
, vol.309
, pp. 285-305
-
-
Klunk, W.E.1
Jacob, R.F.2
Mason, R.P.3
-
34
-
-
0032899322
-
Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric method
-
Klunk W.E., Jacob R.F., Mason R.P. Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotometric method. Anal. Biochem. 266:1999;66-70
-
(1999)
Anal. Biochem.
, vol.266
, pp. 66-70
-
-
Klunk, W.E.1
Jacob, R.F.2
Mason, R.P.3
-
35
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin T
-
Levine H.I. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309:1999;274-284
-
(1999)
Methods Enzymol.
, vol.309
, pp. 274-284
-
-
Levine, H.I.1
-
36
-
-
0028203301
-
Crystal structure of the ribosomal protein S6 from Thermus thermophilus
-
Lindahl M., Svensson L.A., Liljas A., Sedelnikova S.E., Eliseikina I.A., Fomenkova N.P. Crystal structure of the ribosomal protein S6 from Thermus thermophilus. EMBO J. 13:1994;1249-1254
-
(1994)
EMBO J.
, vol.13
, pp. 1249-1254
-
-
Lindahl, M.1
Svensson, L.A.2
Liljas, A.3
Sedelnikova, S.E.4
Eliseikina, I.A.5
Fomenkova, N.P.6
-
37
-
-
0014718113
-
Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
-
Tanford C. Protein denaturation. Part C. Theoretical models for the mechanism of denaturation. Advan. Protein Chem. 24:1970;1-95
-
(1970)
Advan. Protein Chem.
, vol.24
, pp. 1-95
-
-
Tanford, C.1
-
39
-
-
0029115374
-
Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
-
Engelhard M., Evans P.A. Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci. 4:1995;1553-1562
-
(1995)
Protein Sci.
, vol.4
, pp. 1553-1562
-
-
Engelhard, M.1
Evans, P.A.2
-
40
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn O.B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-229
-
(1995)
Advan. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
41
-
-
0035918550
-
Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
-
Nielsen L., Khurana R., Coats A., Frøkjær S., Brange J., Vyas S., et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 40:2001;6036-6046
-
(2001)
Biochemistry
, vol.40
, pp. 6036-6046
-
-
Nielsen, L.1
Khurana, R.2
Coats, A.3
Frøkjær, S.4
Brange, J.5
Vyas, S.6
-
42
-
-
0037066715
-
Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation
-
Souillac P.O., Uversky V.N., Millett I.S., Khurana R., Doniach S., Fink A.L. Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. J. Biol. Chem. 277:2002;12666-12679
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 12666-12679
-
-
Souillac, P.O.1
Uversky, V.N.2
Millett, I.S.3
Khurana, R.4
Doniach, S.5
Fink, A.L.6
-
43
-
-
0037058942
-
Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
-
Hammarström P., Jiang X., Hurshman A.R., Powers E.T., Kelly J.W. Sequence-dependent denaturation energetics: a major determinant in amyloid disease diversity. Proc. Natl Acad. Sci. USA. 99:2002;16427-16432
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 16427-16432
-
-
Hammarström, P.1
Jiang, X.2
Hurshman, A.R.3
Powers, E.T.4
Kelly, J.W.5
-
44
-
-
0034646397
-
The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile Pyrococcus furiosus
-
Yutani K., Takayama G., Goda S., Yamagata Y., Maki S., Namba K. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile Pyrococcus furiosus. Biochemistry. 39:2000;2769-2777
-
(2000)
Biochemistry
, vol.39
, pp. 2769-2777
-
-
Yutani, K.1
Takayama, G.2
Goda, S.3
Yamagata, Y.4
Maki, S.5
Namba, K.6
-
45
-
-
0031056829
-
Instability, unfolding and fibrillogenesis in amyloidogenic lysozyme variants
-
Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., et al. Instability, unfolding and fibrillogenesis in amyloidogenic lysozyme variants. Nature. 385:1997;787-793
-
(1997)
Nature
, vol.385
, pp. 787-793
-
-
Booth, D.R.1
Sunde, M.2
Bellotti, V.3
Robinson, C.V.4
Hutchinson, W.L.5
Fraser, P.E.6
-
46
-
-
0031585993
-
Following co-operative formation of secondary and tertiary structure in a single protein module
-
Neira J.L., Itzhaki L.S., Ladurner A.G., Davis B., de Prat Gay G., Fersht A.R. Following co-operative formation of secondary and tertiary structure in a single protein module. J. Mol. Biol. 268:1997;185-197
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 185-197
-
-
Neira, J.L.1
Itzhaki, L.S.2
Ladurner, A.G.3
Davis, B.4
De Prat Gay, G.5
Fersht, A.R.6
-
47
-
-
0034646562
-
Similarities between the spectrin SH3 domain denatured state and its folding transition state
-
Kortemme T., Kelly M.J., Kay L.E., Forman-Kay J.D., Serrano L. Similarities between the spectrin SH3 domain denatured state and its folding transition state. J. Mol. Biol. 297:2000;1217-1229
-
(2000)
J. Mol. Biol.
, vol.297
, pp. 1217-1229
-
-
Kortemme, T.1
Kelly, M.J.2
Kay, L.E.3
Forman-Kay, J.D.4
Serrano, L.5
-
48
-
-
0030874395
-
GdmCl-induced denaturation and refolding of transthyretin exhibits marked hysteresis: Equilibria with high kinetic barriers
-
Lai Z., McCulloch J., Kelly J.W. GdmCl-induced denaturation and refolding of transthyretin exhibits marked hysteresis: equilibria with high kinetic barriers. Biochemistry. 36:1997;10230-10239
-
(1997)
Biochemistry
, vol.36
, pp. 10230-10239
-
-
Lai, Z.1
McCulloch, J.2
Kelly, J.W.3
-
49
-
-
0030474922
-
The structure, stability and folding process of amyloidogenic mutant human lysozyme
-
Funahashi J., Takano K., Ogasahara K., Yamagata Y., Uutani K. The structure, stability and folding process of amyloidogenic mutant human lysozyme. J. Biochem. 120:1996;1216-1223
-
(1996)
J. Biochem.
, vol.120
, pp. 1216-1223
-
-
Funahashi, J.1
Takano, K.2
Ogasahara, K.3
Yamagata, Y.4
Uutani, K.5
-
50
-
-
0033603336
-
Formation of fibrous aggregates from a non-native intermediate: The isolated P22 tailspike beta-helix domain
-
Schuler B., Rachel R., Seckler R. Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain. J. Biol. Chem. 274:1999;18589-18596
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 18589-18596
-
-
Schuler, B.1
Rachel, R.2
Seckler, R.3
-
51
-
-
0033538015
-
Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
-
Kayed R., Bernhagen J., Greenfield N., Sweimeh K., Brunner H., Voelter W., Kapurniota A. Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. J. Mol. Biol. 287:1999;781-796
-
(1999)
J. Mol. Biol.
, vol.287
, pp. 781-796
-
-
Kayed, R.1
Bernhagen, J.2
Greenfield, N.3
Sweimeh, K.4
Brunner, H.5
Voelter, W.6
Kapurniota, A.7
-
52
-
-
0032497910
-
Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C
-
Gerhartz B., Ekiel I., Abrahamson M. Two stable unfolding intermediates of the disease-causing L68Q variant of human cystatin C. Biochemistry. 37:1998;17309-17317
-
(1998)
Biochemistry
, vol.37
, pp. 17309-17317
-
-
Gerhartz, B.1
Ekiel, I.2
Abrahamson, M.3
-
53
-
-
0031932169
-
Protein aggregation: Folding aggregates, inclusion bodies and amyloid
-
Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 3:1998;R9-R29
-
(1998)
Fold. Des.
, vol.3
-
-
Fink, A.L.1
-
54
-
-
0023375497
-
Three film genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae
-
Klemm P., Christiansen G. Three film genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae. Mol. Gen. Genet. 208:1987;439-445
-
(1987)
Mol. Gen. Genet.
, vol.208
, pp. 439-445
-
-
Klemm, P.1
Christiansen, G.2
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