-
1
-
-
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-R23
-
(1998)
Fold. Des.
, vol.3
-
-
Fink, A.L.1
-
2
-
-
0344944630
-
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
-
Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81 (2003) 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 Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
-
(2004)
Biochim. Biophys. Acta
, vol.1698
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
4
-
-
0842281551
-
Principles of protein folding, misfolding and aggregation
-
Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15 (2004) 3-16
-
(2004)
Semin. Cell Dev. Biol.
, vol.15
, pp. 3-16
-
-
Dobson, C.M.1
-
5
-
-
0024371647
-
Protein folding intermediates and inclusion body formation
-
Mitraki A., and King J. Protein folding intermediates and inclusion body formation. Bio/Technology 7 (1989) 690-697
-
(1989)
Bio/Technology
, vol.7
, pp. 690-697
-
-
Mitraki, A.1
King, J.2
-
6
-
-
0001882924
-
Inclusion bodies and recovery of proteins from the aggregated state
-
Georgiou G., and Bernardez-Clark E. (Eds), American Chemical Society, Washington, DC
-
Bernardez-Clark E., and Georgiou G. Inclusion bodies and recovery of proteins from the aggregated state. In: Georgiou G., and Bernardez-Clark E. (Eds). ACS Symposium Series 470, Protein Refolding (1991), American Chemical Society, Washington, DC 1-20
-
(1991)
ACS Symposium Series 470, Protein Refolding
, pp. 1-20
-
-
Bernardez-Clark, E.1
Georgiou, G.2
-
7
-
-
0039692692
-
Mechanism of inclusion body formation
-
Georgiou G., and Bernardez-Clark E. (Eds), American Chemical Society, Washington, DC
-
Mitraki A., Haase-Pettingell C., and King J. Mechanism of inclusion body formation. In: Georgiou G., and Bernardez-Clark E. (Eds). ACS Symposium Series 470, Protein Refolding (1991), American Chemical Society, Washington, DC 35-49
-
(1991)
ACS Symposium Series 470, Protein Refolding
, pp. 35-49
-
-
Mitraki, A.1
Haase-Pettingell, C.2
King, J.3
-
8
-
-
0034616258
-
Fine architecture of bacterial inclusion bodies
-
Carrió M.M., Cubarsi R., and Villaverde A. Fine architecture of bacterial inclusion bodies. FEBS Lett. 471 (2000) 7-11
-
(2000)
FEBS Lett.
, vol.471
, pp. 7-11
-
-
Carrió, M.M.1
Cubarsi, R.2
Villaverde, A.3
-
9
-
-
12844284637
-
Nondenaturing solubilization of β2 microglobulin from inclusion bodies by l-arginine
-
Umetsu M., Tsumoto K., Nitta S., Adschiri T., Ejima D., Arakawa T., and Kumagai I. Nondenaturing solubilization of β2 microglobulin from inclusion bodies by l-arginine. Biochem. Biophys. Res. Commun. 328 (2005) 189-197
-
(2005)
Biochem. Biophys. Res. Commun.
, vol.328
, pp. 189-197
-
-
Umetsu, M.1
Tsumoto, K.2
Nitta, S.3
Adschiri, T.4
Ejima, D.5
Arakawa, T.6
Kumagai, I.7
-
10
-
-
0035961329
-
The structural basis of protein folding and its links with human disease
-
Dobson C.M. The structural basis of protein folding and its links with human disease. Phil. Trans. R. Soc. Lond. B 356 (2001) 133-145
-
(2001)
Phil. Trans. R. Soc. Lond. B
, vol.356
, pp. 133-145
-
-
Dobson, C.M.1
-
11
-
-
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 C.M., and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416 (2002) 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
-
12
-
-
0032855484
-
Kinetic analysis of amyloid fibril formation
-
Methods Enzymol. Wetzel R. (Ed), Academic Press, London
-
Naiki H., and Gejyo F. Kinetic analysis of amyloid fibril formation. In: Wetzel R. (Ed). Methods Enzymol. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999), Academic Press, London 305-318
-
(1999)
Amyloid, Prions, and Other Protein Aggregates
, vol.309
, pp. 305-318
-
-
Naiki, H.1
Gejyo, F.2
-
13
-
-
0035918550
-
Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
-
Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., and 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
Frokjaer, S.4
Brange, J.5
Vyas, S.6
Uversky, V.N.7
Fink, A.L.8
-
14
-
-
0015268596
-
Infrared spectroscopy of human amyloid fibrils and immunoglobulin proteins
-
Termine J.D., Eanes E.D., Ein D., and Glenner G.G. Infrared spectroscopy of human amyloid fibrils and immunoglobulin proteins. Biopolymers 11 (1972) 1103-1113
-
(1972)
Biopolymers
, vol.11
, pp. 1103-1113
-
-
Termine, J.D.1
Eanes, E.D.2
Ein, D.3
Glenner, G.G.4
-
15
-
-
0026693596
-
In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information
-
Lansbury P.T. In pursuit of the molecular structure of amyloid plaque: new technology provides unexpected and critical information. Biochemistry 31 (1992) 6865-6870
-
(1992)
Biochemistry
, vol.31
, pp. 6865-6870
-
-
Lansbury, P.T.1
-
16
-
-
0346057932
-
Increasing the amphiphilicity of an amyloidogenic peptide changes the β-sheet structure in the fibrils from antiparallel to parallel
-
Gordon D.J., Balbach J.J., Tycko R., and Meredith S.C. Increasing the amphiphilicity of an amyloidogenic peptide changes the β-sheet structure in the fibrils from antiparallel to parallel. Biophys. J. 86 (2004) 428-434
-
(2004)
Biophys. J.
, vol.86
, pp. 428-434
-
-
Gordon, D.J.1
Balbach, J.J.2
Tycko, R.3
Meredith, S.C.4
-
17
-
-
0002693020
-
Physical basis of the stability of the folded conformations of proteins
-
Creighton T.E. (Ed), W. H. Freeman and Company, New York
-
Privalov P.L. Physical basis of the stability of the folded conformations of proteins. In: Creighton T.E. (Ed). Protein Folding (1992), W. H. Freeman and Company, New York 83-126
-
(1992)
Protein Folding
, pp. 83-126
-
-
Privalov, P.L.1
-
18
-
-
0002733477
-
Stabilization of protein structure by solvents
-
Creighton T.E. (Ed), Oxford University Press, Oxford
-
Timasheff S.N., and Arakawa T. Stabilization of protein structure by solvents. In: Creighton T.E. (Ed). Protein Structure (1997), Oxford University Press, Oxford 348-364
-
(1997)
Protein Structure
, pp. 348-364
-
-
Timasheff, S.N.1
Arakawa, T.2
-
20
-
-
73649177752
-
Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
-
Goldberger R.F., Epstein C.J., and Anfinsen C.B. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238 (1963) 628-635
-
(1963)
J. Biol. Chem.
, vol.238
, pp. 628-635
-
-
Goldberger, R.F.1
Epstein, C.J.2
Anfinsen, C.B.3
-
21
-
-
0024337857
-
Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins
-
Freedman R.B. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57 (1989) 1069-1072
-
(1989)
Cell
, vol.57
, pp. 1069-1072
-
-
Freedman, R.B.1
-
22
-
-
0027270735
-
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
-
Weissman J.S., and Kim P.S. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365 (1993) 185-188
-
(1993)
Nature
, vol.365
, pp. 185-188
-
-
Weissman, J.S.1
Kim, P.S.2
-
23
-
-
0027959156
-
Protein disulphide isomerase: building bridges in protein folding
-
Freedman R.B., Hirst T.R., and Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19 (1994) 331-336
-
(1994)
Trends Biochem. Sci.
, vol.19
, pp. 331-336
-
-
Freedman, R.B.1
Hirst, T.R.2
Tuite, M.F.3
-
24
-
-
0031826990
-
Molecular evolution of the domain structures of protein disulfide isomerases
-
Kanai S., Toh H., Hayano T., and Kikuchi M. Molecular evolution of the domain structures of protein disulfide isomerases. J. Mol. Evol. 47 (1998) 200-210
-
(1998)
J. Mol. Evol.
, vol.47
, pp. 200-210
-
-
Kanai, S.1
Toh, H.2
Hayano, T.3
Kikuchi, M.4
-
25
-
-
0344288101
-
Protein disulfide isomerase
-
Fink A.L., and Goto Y. (Eds), Marcel Dekker, Inc., New York
-
Walker K.W., and Gilbert H.F. Protein disulfide isomerase. In: Fink A.L., and Goto Y. (Eds). Molecular Chaperones in the Life Cycle of Proteins (1998), Marcel Dekker, Inc., New York 331-359
-
(1998)
Molecular Chaperones in the Life Cycle of Proteins
, pp. 331-359
-
-
Walker, K.W.1
Gilbert, H.F.2
-
27
-
-
1042266634
-
Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding
-
Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., Kimura I., Tsujimoto T., and Kikuchi M. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. J. Biol. Chem. 279 (2004) 4604-4611
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 4604-4611
-
-
Horibe, T.1
Gomi, M.2
Iguchi, D.3
Ito, H.4
Kitamura, Y.5
Masuoka, T.6
Kimura, I.7
Tsujimoto, T.8
Kikuchi, M.9
-
28
-
-
0028321726
-
Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
-
Puig A., and Gilbert H.F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269 (1994) 7764-7771
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 7764-7771
-
-
Puig, A.1
Gilbert, H.F.2
-
29
-
-
0032924105
-
Chaperone-mediated protein folding
-
Fink A.L. Chaperone-mediated protein folding. Physiol. Rev. 79 (1999) 425-449
-
(1999)
Physiol. Rev.
, vol.79
, pp. 425-449
-
-
Fink, A.L.1
-
30
-
-
0032939206
-
Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
-
Zai A., Rudd M.A., Scribner A.W., and Loscalzo J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J. Clin. Invest. 103 (1999) 393-399
-
(1999)
J. Clin. Invest.
, vol.103
, pp. 393-399
-
-
Zai, A.1
Rudd, M.A.2
Scribner, A.W.3
Loscalzo, J.4
-
31
-
-
4544381890
-
Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption
-
Root P., Sliskovic I., and Mutus B. Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption. Biochem. J. 382 (2004) 575-580
-
(2004)
Biochem. J.
, vol.382
, pp. 575-580
-
-
Root, P.1
Sliskovic, I.2
Mutus, B.3
-
32
-
-
1442348240
-
Use of 2,3-diaminonaphthalene for studying denitrosation activity of protein disulfide isomerase
-
Raturi A., and Mutus B. Use of 2,3-diaminonaphthalene for studying denitrosation activity of protein disulfide isomerase. Anal. Biochem. 326 (2004) 281-283
-
(2004)
Anal. Biochem.
, vol.326
, pp. 281-283
-
-
Raturi, A.1
Mutus, B.2
-
33
-
-
36849067495
-
Modified procedure for rapid purification of protein disulphide-isomerase from bovine liver
-
Lambert N., and Freedman R.B. Modified procedure for rapid purification of protein disulphide-isomerase from bovine liver. Biochem. Soc. Trans. 10 (1982) 113-114
-
(1982)
Biochem. Soc. Trans.
, vol.10
, pp. 113-114
-
-
Lambert, N.1
Freedman, R.B.2
-
34
-
-
0020787176
-
Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure
-
Lambert N., and Freedman R.B. Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure. Biochem. J. 213 (1983) 225-234
-
(1983)
Biochem. J.
, vol.213
, pp. 225-234
-
-
Lambert, N.1
Freedman, R.B.2
-
35
-
-
0025331418
-
Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
-
Lundström J., and Holmgren A. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J. Biol. Chem. 265 (1990) 9114-9120
-
(1990)
J. Biol. Chem.
, vol.265
, pp. 9114-9120
-
-
Lundström, J.1
Holmgren, A.2
-
36
-
-
0020787907
-
Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction
-
Lambert N., and Freedman R.B. Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction. Biochem. J. 213 (1983) 235-243
-
(1983)
Biochem. J.
, vol.213
, pp. 235-243
-
-
Lambert, N.1
Freedman, R.B.2
-
37
-
-
0024509805
-
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T
-
Naiki H., Higuchi K., Hosokawa M., and Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T. Anal. Biochem. 177 (1989) 244-249
-
(1989)
Anal. Biochem.
, vol.177
, pp. 244-249
-
-
Naiki, H.1
Higuchi, K.2
Hosokawa, M.3
Takeda, T.4
-
38
-
-
0032849874
-
Quantification of β-sheet amyloid fibril structures with thioflavin T
-
Methods Enzymol. Wetzel R. (Ed), Academic Press, London
-
Levine III H. Quantification of β-sheet amyloid fibril structures with thioflavin T. In: Wetzel R. (Ed). Methods Enzymol. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999), Academic Press, London 274-284
-
(1999)
Amyloid, Prions, and Other Protein Aggregates
, vol.309
, pp. 274-284
-
-
Levine III, H.1
-
39
-
-
0024352110
-
Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
-
Klunk W.E., Pettegrew J.W., and Abraham D.J. Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37 (1989) 1273-1281
-
(1989)
J. Histochem. Cytochem.
, vol.37
, pp. 1273-1281
-
-
Klunk, W.E.1
Pettegrew, J.W.2
Abraham, D.J.3
-
40
-
-
0024363054
-
Two simple methods for quantifying low-affinity dye-substrate binding
-
Klunk W.E., Pettegrew J.W., and Abraham D.J. Two simple methods for quantifying low-affinity dye-substrate binding. J. Histochem. Cytochem. 37 (1989) 1293-1297
-
(1989)
J. Histochem. Cytochem.
, vol.37
, pp. 1293-1297
-
-
Klunk, W.E.1
Pettegrew, J.W.2
Abraham, D.J.3
-
41
-
-
0032855483
-
Quantifying amyloid by Congo red spectral shift assay
-
Methods Enzymol. Wetzel R. (Ed), Academic Press, London
-
Klunk W.E., Jacob R.F., and Mason R.P. Quantifying amyloid by Congo red spectral shift assay. In: Wetzel R. (Ed). Methods Enzymol. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999), Academic Press, London 285-305
-
(1999)
Amyloid, Prions, and Other Protein Aggregates
, vol.309
, pp. 285-305
-
-
Klunk, W.E.1
Jacob, R.F.2
Mason, R.P.3
-
42
-
-
0032855076
-
Staining methods for identification of amyloid in tissue
-
Methods Enzymol. Wetzel R. (Ed), Academic Press, London
-
Westermark G.T., Johnson K.H., and Westermark P. Staining methods for identification of amyloid in tissue. In: Wetzel R. (Ed). Methods Enzymol. Amyloid, Prions, and Other Protein Aggregates vol. 309 (1999), Academic Press, London 3-25
-
(1999)
Amyloid, Prions, and Other Protein Aggregates
, vol.309
, pp. 3-25
-
-
Westermark, G.T.1
Johnson, K.H.2
Westermark, P.3
-
43
-
-
0022691315
-
Examination of the secondary structure of proteins by deconvolved FTIR spectra
-
Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
-
(1986)
Biopolymers
, vol.25
, pp. 469-487
-
-
Byler, D.M.1
Susi, H.2
-
44
-
-
0023837785
-
New insight into protein secondary structure from resolution-enhanced infrared spectra
-
Surewicz W.K., and Mantsch H.H. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952 (1988) 115-130
-
(1988)
Biochim. Biophys. Acta
, vol.952
, pp. 115-130
-
-
Surewicz, W.K.1
Mantsch, H.H.2
-
45
-
-
0000316288
-
Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins
-
Jackson M., Haris P.I., and Chapman D. Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins. J. Mol. Struct. 214 (1989) 329-355
-
(1989)
J. Mol. Struct.
, vol.214
, pp. 329-355
-
-
Jackson, M.1
Haris, P.I.2
Chapman, D.3
-
46
-
-
0023008334
-
Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
-
Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-367
-
(1986)
Adv. Protein Chem.
, vol.38
, pp. 181-367
-
-
Krimm, S.1
Bandekar, J.2
-
47
-
-
36449001245
-
Model calculations on the amide-I infrared bands of globular proteins
-
Torii H., and Tasumi M. Model calculations on the amide-I infrared bands of globular proteins. J. Chem. Phys. 96 (1992) 3379-3387
-
(1992)
J. Chem. Phys.
, vol.96
, pp. 3379-3387
-
-
Torii, H.1
Tasumi, M.2
-
48
-
-
0036880493
-
What vibrations tell us about proteins
-
Barth A., and Zscherp C. What vibrations tell us about proteins. Quart. Rev. Biophys. 35 (2002) 369-430
-
(2002)
Quart. Rev. Biophys.
, vol.35
, pp. 369-430
-
-
Barth, A.1
Zscherp, C.2
-
49
-
-
0035815664
-
Evidence for a partially folded intermediate in α-synuclein fibril formation
-
Uversky V.N., Li J., and Fink A.L. Evidence for a partially folded intermediate in α-synuclein fibril formation. J. Biol. Chem. 276 (2001) 10737-10744
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 10737-10744
-
-
Uversky, V.N.1
Li, J.2
Fink, A.L.3
-
51
-
-
0014346532
-
Histochemical observations on amyloid with reference to polarization microscopy
-
Delellis R.A., Glenner G.G., and Ram J.S. Histochemical observations on amyloid with reference to polarization microscopy. J. Histochem. Cytochem. 16 (1968) 663-665
-
(1968)
J. Histochem. Cytochem.
, vol.16
, pp. 663-665
-
-
Delellis, R.A.1
Glenner, G.G.2
Ram, J.S.3
-
52
-
-
0035158241
-
Studies of the structure of insulin fibrils by fourier transform infrared (FTIR) spectroscopy and electron microscopy
-
Nielsen L., Frokjaer S., Carpenter J.F., and Brange J. Studies of the structure of insulin fibrils by fourier transform infrared (FTIR) spectroscopy and electron microscopy. J. Pharm. Sci. 90 (2001) 29-37
-
(2001)
J. Pharm. Sci.
, vol.90
, pp. 29-37
-
-
Nielsen, L.1
Frokjaer, S.2
Carpenter, J.F.3
Brange, J.4
-
53
-
-
1242271236
-
Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
-
Militello V., Casarino C., Emanuele A., Giostra A., Pullara F., and Leone M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 107 (2004) 175-187
-
(2004)
Biophys. Chem.
, vol.107
, pp. 175-187
-
-
Militello, V.1
Casarino, C.2
Emanuele, A.3
Giostra, A.4
Pullara, F.5
Leone, M.6
-
54
-
-
9344243513
-
FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
-
Zandomeneghi G., Krebs M.R.H., Mccammon M.G., and Fändrich M. FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13 (2004) 3314-3321
-
(2004)
Protein Sci.
, vol.13
, pp. 3314-3321
-
-
Zandomeneghi, G.1
Krebs, M.R.H.2
Mccammon, M.G.3
Fändrich, M.4
-
55
-
-
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
-
56
-
-
0036231272
-
Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
-
Meersman F., Smeller L., and Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82 (2002) 2635-2644
-
(2002)
Biophys. J.
, vol.82
, pp. 2635-2644
-
-
Meersman, F.1
Smeller, L.2
Heremans, K.3
-
57
-
-
0032102197
-
Purification of a 58-kDa protein (ER58) from monkey liver microsomes and comparison with protein-disulfide isomerase
-
Bonfils C. Purification of a 58-kDa protein (ER58) from monkey liver microsomes and comparison with protein-disulfide isomerase. Eur. J. Biochem. 254 (1998) 420-427
-
(1998)
Eur. J. Biochem.
, vol.254
, pp. 420-427
-
-
Bonfils, C.1
-
58
-
-
0027480757
-
The structure and mechanism of formation of human calcitonin fibrils
-
Arvinte T., Cudd A., and Drake A.F. The structure and mechanism of formation of human calcitonin fibrils. J. Biol. Chem. 268 (1993) 6415-6422
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 6415-6422
-
-
Arvinte, T.1
Cudd, A.2
Drake, A.F.3
-
59
-
-
0039696212
-
Protein disulfide isomerase and the complications of protein folding
-
Guzman N.A. (Ed), Marcel Dekker, New York
-
Gilbert H.F. Protein disulfide isomerase and the complications of protein folding. In: Guzman N.A. (Ed). Prolyl Hydroxylase, Protein Disulfide Isomerase, and Other Structurally Related Proteins (1998), Marcel Dekker, New York 341-367
-
(1998)
Prolyl Hydroxylase, Protein Disulfide Isomerase, and Other Structurally Related Proteins
, pp. 341-367
-
-
Gilbert, H.F.1
-
60
-
-
0027195933
-
Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
-
Jarrett J.T., and Lansbury P.T. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 73 (1993) 1055-1058
-
(1993)
Cell
, vol.73
, pp. 1055-1058
-
-
Jarrett, J.T.1
Lansbury, P.T.2
-
61
-
-
0030908095
-
Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truth and physiological consequences of the time-dependent solubility of amyloid proteins
-
Harper J.D., and Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truth and physiological consequences of the time-dependent solubility of amyloid proteins. Ann. Rev. Biochem. 66 (1997) 385-407
-
(1997)
Ann. Rev. Biochem.
, vol.66
, pp. 385-407
-
-
Harper, J.D.1
Lansbury, P.T.2
-
62
-
-
0016369152
-
Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease
-
Hofrichter J., Ross P.D., and Eaton W.A. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Proc. Nat. Acad. Sci. 71 (1974) 4864-4868
-
(1974)
Proc. Nat. Acad. Sci.
, vol.71
, pp. 4864-4868
-
-
Hofrichter, J.1
Ross, P.D.2
Eaton, W.A.3
-
63
-
-
11144222595
-
The binding of thioflavin-T to amyloid fibrils: localisation and implications
-
Krebs M.R.H., Bromley E.H.C., 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.H.1
Bromley, E.H.C.2
Donald, A.M.3
-
64
-
-
0036836665
-
Proteins of the PDI family: unpredicted non-ER locations and functions
-
Turano C., Coppari S., Altieri F., and Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J. Cell. Physiol. 193 (2002) 154-163
-
(2002)
J. Cell. Physiol.
, vol.193
, pp. 154-163
-
-
Turano, C.1
Coppari, S.2
Altieri, F.3
Ferraro, A.4
-
65
-
-
30344444015
-
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active site
-
Tian G., Xiang S., Noiva R., Lennarz J., and Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active site. Cell 124 (2006) 61-73
-
(2006)
Cell
, vol.124
, pp. 61-73
-
-
Tian, G.1
Xiang, S.2
Noiva, R.3
Lennarz, J.4
Schindelin, H.5
|