-
1
-
-
0028584438
-
Amyloidosis
-
Sipe JD: Amyloidosis. Crit Rev Clin Lab Sci 1994, 31:325-354. Over the past 20 years, 16 biochemically diverse proteins have been identified as fibrilar constituents of amyloid deposits. Amyloidoses are complex disorders in which normally soluble precursors undergo pathological conformational changes and polymerize into cross-β fibrils. This review cites numerous other reviews on amyloidoses which are of interest.
-
(1994)
Crit Rev Clin Lab Sci
, vol.31
, pp. 325-354
-
-
Sipe, J.D.1
-
2
-
-
0028804827
-
Structural model for the β-amyloid fibril interstrand alignment of an antiparallel β-sheet comprising a C-terminal peptide
-
Lansbury PT, Costa PR, Griffiths JM, Simon EJ, Auger M, Halverson KJ, Kocisko DA, Hendsch ZS, Ashburn TT, Spencer RGS et al.: Structural model for the β-amyloid fibril interstrand alignment of an antiparallel β-sheet comprising a C-terminal peptide. Nature Struct Biol 1995, 2:990-998. This manuscript outlines what is currently state of the art in the use of solid state NMR to characterize the structure of amyloid.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 990-998
-
-
Lansbury, P.T.1
Costa, P.R.2
Griffiths, J.M.3
Simon, E.J.4
Auger, M.5
Halverson, K.J.6
Kocisko, D.A.7
Hendsch, Z.S.8
Ashburn, T.T.9
Spencer, R.G.S.10
-
3
-
-
0000666695
-
Rotational resonance solid state NMR elucidates a structural model of pancreatic amyloid
-
13-labeled peptide analogs of the human islet amyloid polypeptide. The intercarbon distances are consistent with a highly pleated β-sheet structure of the cross-β variety. This structural model takes us one step closer to understanding the structure of pancreatic amyloid.
-
(1995)
J Am Chem Soc
, vol.117
, pp. 3539-3546
-
-
Griffiths, J.M.1
Ashbum, T.T.2
Auger, M.3
Costa, P.R.4
Griffin, R.G.5
Lansbury, P.T.6
-
4
-
-
0029294573
-
Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein - Implication for scraple formation
-
Kazmirski SL, Alonso DOV, Cohen FE, Prusiner SB, Daggett V: Theoretical studies of sequence effects on the conformational properties of a fragment of the prion protein - implication for scraple formation. Chem Biol 1995, 2:305-315. This paper outlines the promise of molecular dynamics to elucidate the structural changes that are occurring during the conversion of the normal protein into the amyloidogenic intermediate. Prion fragment 109-122 implied in the conversion of PrP-C to PrP-Sc was studied by molecular dynamics, providing insights into the early steps in the conversion of PrP-C to PrP-Sc.
-
(1995)
Chem Biol
, vol.2
, pp. 305-315
-
-
Kazmirski, S.L.1
Alonso, D.O.V.2
Cohen, F.E.3
Prusiner, S.B.4
Daggett, V.5
-
6
-
-
0027949973
-
A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation
-
Kelly JW, Lansbury PT: A chemical approach to elucidate the mechanism of transthyretin and beta-protein amyloid fibril formation. Amyloid 1994, 1:186-205. This review demonstrates the use of a chemical approach in understanding the conformational changes occurring in TTR and the β protein which render them capable of polymerizing into amyloid. Even though there is little sequence or structural homology among the sixteen human amyloidogenic proteins, it appears that they are similar in that they all have the ability to adopt a similar amyloidogenic intermediate conformation which renders them capable of polymerizing into amyloid in vivo. Evidence in favor of this hypothesis is summarized.
-
(1994)
Amyloid
, vol.1
, pp. 186-205
-
-
Kelly, J.W.1
Lansbury, P.T.2
-
7
-
-
0015150725
-
Creation of amyloid fibrils from Bence Jones proteins in vitro
-
Glenner GG, Ein D, Eanes ED, Bladen HA, Terry W, Page DL: Creation of amyloid fibrils from Bence Jones proteins in vitro. Science 1971, 174:712-714.
-
(1971)
Science
, vol.174
, pp. 712-714
-
-
Glenner, G.G.1
Ein, D.2
Eanes, E.D.3
Bladen, H.A.4
Terry, W.5
Page, D.L.6
-
8
-
-
0025037933
-
Amlyoid enhancing factor-loaded macrophages in amyloid fibril formation
-
Shirihama T, Miura K, Ju S-T, Kisilevsky R, Gruys E, Cohen AS: Amlyoid enhancing factor-loaded macrophages in amyloid fibril formation. Lab Invest 1990, 62:61-68.
-
(1990)
Lab Invest
, vol.62
, pp. 61-68
-
-
Shirihama, T.1
Miura, K.2
Ju, S.-T.3
Kisilevsky, R.4
Gruys, E.5
Cohen, A.S.6
-
9
-
-
0026675307
-
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
-
Colon W, Kelly JW: Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 1992, 31:8654-8660.
-
(1992)
Biochemistry
, vol.31
, pp. 8654-8660
-
-
Colon, W.1
Kelly, J.W.2
-
10
-
-
0002254472
-
Transthyretin acid Induced denaturation is sufficient for amyloid fibril formation in vitro
-
Edited by Kelly JW, Baldwin TO. New York: Plenum
-
Colon W, Kelly JW: Transthyretin acid Induced denaturation is sufficient for amyloid fibril formation in vitro. In Applications of Enzyme Biotechnology. Edited by Kelly JW, Baldwin TO. New York: Plenum; 1991:99-108.
-
(1991)
Applications of Enzyme Biotechnology
, pp. 99-108
-
-
Colon, W.1
Kelly, J.W.2
-
11
-
-
0026760261
-
Production of the Alzheimer's amyloid beta protein by normal proteolytic processing
-
Shoji M, Golde TE, Ghiso J, Cheung TT, Estus S, Shatter LM, Cai X-D, Mckay DM, Tinter R, Frangione B, Younkin SG: Production of the Alzheimer's amyloid beta protein by normal proteolytic processing. Science 1992, 258:126-129.
-
(1992)
Science
, vol.258
, pp. 126-129
-
-
Shoji, M.1
Golde, T.E.2
Ghiso, J.3
Cheung, T.T.4
Estus, S.5
Shatter, L.M.6
Cai, X.-D.7
Mckay, D.M.8
Tinter, R.9
Frangione, B.10
Younkin, S.G.11
-
12
-
-
0026646605
-
Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids
-
Seubert P, Vigo-Pelfry C, Esch F, Lee M, Dovey H, Davis D, Sinha S, Schossmacher M, Whaley J, Swindlehurts C et al.: Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids. Nature 1992, 359:325-327.
-
(1992)
Nature
, vol.359
, pp. 325-327
-
-
Seubert, P.1
Vigo-Pelfry, C.2
Esch, F.3
Lee, M.4
Dovey, H.5
Davis, D.6
Sinha, S.7
Schossmacher, M.8
Whaley, J.9
Swindlehurts, C.10
-
13
-
-
0029114261
-
Non-Alzheimer's disease amyloidoses of the nervous system
-
Castano EM, Frangione B: Non-Alzheimer's disease amyloidoses of the nervous system. Curr Opin Neurobiol 1995, 8:279-285. Amyloidosis and prionosis are diseases that are apparently caused by protein conformational changes that make amyloidosis possible.
-
(1995)
Curr Opin Neurobiol
, vol.8
, pp. 279-285
-
-
Castano, E.M.1
Frangione, B.2
-
14
-
-
0029155934
-
Treatment of amyloidosis
-
Tan SY, Pepys MB, Hawkins PN: Treatment of amyloidosis. Am J Kidney Dis 1995, 26:267-285. This paper describes how amyloid fibril clearance has been observed in several diseases in vivo where fibril formation can be terminated or reduced.
-
(1995)
Am J Kidney Dis
, vol.26
, pp. 267-285
-
-
Tan, S.Y.1
Pepys, M.B.2
Hawkins, P.N.3
-
15
-
-
0017824077
-
Structure of prealbumin (transthyretin): Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 å
-
Blake CCF, Geisow MJ, Oatley SJ: Structure of prealbumin (transthyretin): secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J Mol Biol 1978, 121:339-356.
-
(1978)
J Mol Biol
, vol.121
, pp. 339-356
-
-
Blake, C.C.F.1
Geisow, M.J.2
Oatley, S.J.3
-
16
-
-
0027363264
-
Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
-
McCutchen S, Colon W, Kelly JW: Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry 1993, 32:12119-12127.
-
(1993)
Biochemistry
, vol.32
, pp. 12119-12127
-
-
McCutchen, S.1
Colon, W.2
Kelly, J.W.3
-
17
-
-
0028839438
-
Comparison of lethal and non-lethal transthyretin variants and their relationship to amyloid disease
-
McCutchen SL, Lai Z, Miroy G, Kelly JW, Colon W: Comparison of lethal and non-lethal transthyretin variants and their relationship to amyloid disease. Biochemistry 1995, 34:13527-13536. The role that TTR mutants play in amyloid disease has been probed by comparing the biophysical properties of several of the variants as a function of pH. The more destabilized the letramer, the more amyloidogenic the variant, as discerned from fibril formation in vitro and from the age of disease onset in vivo. Fluorescence studies monitoring acid denaturation reveal a fluorescence intensity plateau over the amyloid-forming pH range, implying that the amyloidogenic intermediate is being detected. Interestingly, this intermediate is not detectable in the Thr119Met variant, which is a common non-pathogenic mutation.
-
(1995)
Biochemistry
, vol.34
, pp. 13527-13536
-
-
McCutchen, S.L.1
Lai, Z.2
Miroy, G.3
Kelly, J.W.4
Colon, W.5
-
18
-
-
0343613908
-
The acid-mediated denaturation of transthyretin proceeds through an Intermediate that partitions into amyloid
-
in press
-
Lai Z, Colon W, Kelly JW: The acid-mediated denaturation of transthyretin proceeds through an Intermediate that partitions into amyloid. Biochemistry 1996, in press. As the pH is lowered from 7.5 towards 5, TTR undergoes a tetramer rearrangement followed by dissociation of the rearranged tetramer to a monomeric species that appears to be the amyloidogenic intermediate. Below pH 3.8, TTR adopts an A-state-like conformation in the presence NaCl. Neither the rearranged tetramer nor the monomeric A-state is capable of fibril formation. Single tryptophan-containing variants of TTR reveal that Trp41 is the major contributor to the fluorescence denaturation curve and is in the part of the protein that undergoes a rearrangement upon partial acid denaturation. The amyloidogenic intermediate retains both secondary and partial tertiary structure and does not have a significant hydrophobic surface exposed as discerned from minimal 1-anilino-8-naphthalene sulfonic acid (ANS) binding.
-
(1996)
Biochemistry
-
-
Lai, Z.1
Colon, W.2
Kelly, J.W.3
-
19
-
-
0028969996
-
Transthyretin mutations in health and disease
-
Saraiva MJM: Transthyretin mutations in health and disease. Hum Mutat 1995, 5:191-196. A summary of the currently known FAP mutations. This summary is important when mapped onto the known TTR structure because it provides clues as to which portions of the TTR sequence are required for FAP fibril formation. The absence of mutations in certain portions of the sequence imply that these regions are important for fibril formation. The mutation-free regions agree with the proposed amyloidogenic intermediate structure in Figure 3 of my review.
-
(1995)
Hum Mutat
, vol.5
, pp. 191-196
-
-
Saraiva, M.J.M.1
-
20
-
-
0027476367
-
The X-ray crystal structure refinements of normal human tranthyretin and the amyloidogenic Val-30-Met variant to 1.7 å resolution
-
Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L: The X-ray crystal structure refinements of normal human tranthyretin and the amyloidogenic Val-30-Met variant to 1.7 Å resolution. J Biol Chem 1993, 268:2416-2424.
-
(1993)
J Biol Chem
, vol.268
, pp. 2416-2424
-
-
Hamilton, J.A.1
Steinrauf, L.K.2
Braden, B.C.3
Liepnieks, J.4
Benson, M.D.5
Holmgren, G.6
Sandgren, O.7
Steen, L.8
-
21
-
-
0027459456
-
X-ray crystal structure of the Ala-109-Thr variant of human transthyretin which produces euthyrold hyperthyroxinemla
-
Steinrauf LK, Hamilton JA, Braden BC, Murrel JR, Benson MD: X-ray crystal structure of the Ala-109-Thr variant of human transthyretin which produces euthyrold hyperthyroxinemla. J Biol Chem 1993, 268:2425-2430.
-
(1993)
J Biol Chem
, vol.268
, pp. 2425-2430
-
-
Steinrauf, L.K.1
Hamilton, J.A.2
Braden, B.C.3
Murrel, J.R.4
Benson, M.D.5
-
22
-
-
0027518443
-
Structure of Met-30 variant of tranthyretin and its amyloidogenic implications
-
Terry CJ, Damas AM, Oliveira P, Saraivia MJ, Alves IL, Costa PP, Matias PM, Sakaki Y, Blake CCF: Structure of Met-30 variant of tranthyretin and its amyloidogenic implications. EMBO J 1993, 12:735-741.
-
(1993)
EMBO J
, vol.12
, pp. 735-741
-
-
Terry, C.J.1
Damas, A.M.2
Oliveira, P.3
Saraivia, M.J.4
Alves, I.L.5
Costa, P.P.6
Matias, P.M.7
Sakaki, Y.8
Blake, C.C.F.9
-
23
-
-
0028987233
-
H-1 NMR of A-beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence
-
Lee JP, Stimson ER, Ghilardi JR, Mantyh PW, Lu YA, Felix AM, Llanoss W, Behbin A, Cummins M, Vancriekinge M, Timms W, Maggio JE: H-1 NMR of A-beta amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence. Biochemistry 1995, 34:5191-5200. The amyloid peptide analog 10-35 was able to form amyloid plaques between pH 5 and 9 but not below this range. This peptide was studied by NMR at submillimolar concentrations both above and below this pH range. Changes in coupling constants, chemical shifts, and NOEs indicate a pH-dependent folding transition involving a conformation which is not helical, but instead involves several turns and at least two short strands. Interestingly, a plaque-incompetent fragment consisting of residues 1-28 does not exhibit these structural transitions.
-
(1995)
Biochemistry
, vol.34
, pp. 5191-5200
-
-
Lee, J.P.1
Stimson, E.R.2
Ghilardi, J.R.3
Mantyh, P.W.4
Lu, Y.A.5
Felix, A.M.6
Llanoss, W.7
Behbin, A.8
Cummins, M.9
Vancriekinge, M.10
Timms, W.11
Maggio, J.E.12
-
24
-
-
0028265912
-
Secondary structure of amyloid β-peptide correlates with neurotoxic activity in vitro
-
Simmons LK, May PC, Tomaaselli KJ, Rydel RE, Fuson KS, Brigham EF, Wright S, Lieberburg I, Becker GW, Brems DN: Secondary structure of amyloid β-peptide correlates with neurotoxic activity in vitro. Mol Pharmacol 1994, 45:373-379. Solubilized amyloid peptide analog was maximally toxic when it adopted a β conformation under a variety of solution conditions. Importantly, A-beta can be induced to undergo a conformational change from a random coil non-toxic peptide to a β structure exhibiting toxicity.
-
(1994)
Mol Pharmacol
, vol.45
, pp. 373-379
-
-
Simmons, L.K.1
May, P.C.2
Tomaaselli, K.J.3
Rydel, R.E.4
Fuson, K.S.5
Brigham, E.F.6
Wright, S.7
Lieberburg, I.8
Becker, G.W.9
Brems, D.N.10
-
25
-
-
0028917968
-
Two conformational states of the amyloid A-beta peptide-implications for the pathogenesis of Alzheimer's disease
-
Soto C, Frangione B: Two conformational states of the amyloid A-beta peptide-implications for the pathogenesis of Alzheimer's disease. Neurosci Lett 1995, 186:115-118. The Alzheimer's peptide 1-40 that sedimented after 2 weeks of incubation has a β sheet conformation, whereas one remaining in solution exhibits a random coil/α-helical conformation.
-
(1995)
Neurosci Lett
, vol.186
, pp. 115-118
-
-
Soto, C.1
Frangione, B.2
-
26
-
-
0029034927
-
Aggregation state and neurotoxic properties of Alzheimer's beta-amyloid peptide
-
Howlett DR, Jennings KH, Lee DC, Clark MSG, Brown F, Wetzel R, Wood SJ, Camilleri P, Roberts GW: Aggregation state and neurotoxic properties of Alzheimer's beta-amyloid peptide. Neurodegeneration 1995, 4:23-32. An A-beta 1-40 fragment was incubated for up to 168 h in a time-dependent fashion and the toxicity as well as the structure was observed. The development of neurotoxicity of A-beta 1-40 is related to the structure of the peptide.
-
(1995)
Neurodegeneration
, vol.4
, pp. 23-32
-
-
Howlett, D.R.1
Jennings, K.H.2
Lee, D.C.3
Clark, M.S.G.4
Brown, F.5
Wetzel, R.6
Wood, S.J.7
Camilleri, P.8
Roberts, G.W.9
-
27
-
-
0028305304
-
A role for destabilizing amino acid replacements in light chain amyloidosis
-
Hurle MR, Helms LR, Li L, Chan W, Wetzel R: A role for destabilizing amino acid replacements in light chain amyloidosis. Proc Natl Acad Sci USA 1994, 91:5446-5450. The data are consistent with a mechanism for disease progress in which the VL domain of the light chain, either before or after proteolytic cleavage from the light chain constant domain, unfolds due to mutations, leading to an amyloidogenic conformational intermediate which can self-assemble into amyloid.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 5446-5450
-
-
Hurle, M.R.1
Helms, L.R.2
Li, L.3
Chan, W.4
Wetzel, R.5
-
28
-
-
0027506498
-
Human lysozyme gene mutations cause hereditary systemic amyloidosis
-
Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CCF, Terry CJ et al: Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 1993, 362:553-557.
-
(1993)
Nature
, vol.362
, pp. 553-557
-
-
Pepys, M.B.1
Hawkins, P.N.2
Booth, D.R.3
Vigushin, D.M.4
Tennent, G.A.5
Soutar, A.K.6
Totty, N.7
Nguyen, O.8
Blake, C.C.F.9
Terry, C.J.10
-
29
-
-
0025944507
-
Secondary structural analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
-
Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS: Secondary structural analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991, 30:7672-7680.
-
(1991)
Biochemistry
, vol.30
, pp. 7672-7680
-
-
Caughey, B.W.1
Dong, A.2
Bhat, K.S.3
Ernst, D.4
Hayes, S.F.5
Caughey, W.S.6
-
30
-
-
0029110883
-
The chemistry of the scrapie infection - Implications of the ICE 9 metaphor
-
Lansbury PT: The chemistry of the scrapie infection - implications of the ICE 9 metaphor. Chem Biol 1995, 2:1-5. A model for reproduction of the prion protein, involving a nucleated polymerization explaining the conformational changes in the conversion of PrP-C to PrP-Sc.
-
(1995)
Chem Biol
, vol.2
, pp. 1-5
-
-
Lansbury, P.T.1
-
31
-
-
0027975260
-
Predisposition of prion protein homozygotes to Creutzfeldt-Jakob Disease can be explained by a nucleation-dependent polymerization mechanism
-
Come JH, Lansbury PT Jr: Predisposition of prion protein homozygotes to Creutzfeldt-Jakob Disease can be explained by a nucleation-dependent polymerization mechanism. J Am Chem Soc 1994, 116:4109-4110. The hypothesis that PrP-Sc is an aggregate in which an alternative conformation of PrP is stabilized by intermolecular interactions is probed by peptidic fragments of PrP 118-133, which form amyloid via a nucleation-dependent phenomenon. Peptides reflecting the homozygous situation formed amyloid much faster than did mixtures of peptides, implying that nucleation was difficult in heterozygotes.
-
(1994)
J Am Chem Soc
, vol.116
, pp. 4109-4110
-
-
Come, J.H.1
Lansbury P.T., Jr.2
-
32
-
-
0027332116
-
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
-
Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhom I, Huang Z, Fletterick RJ, Cohen FE: Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993, 90:10962-10966.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 10962-10966
-
-
Pan, K.M.1
Baldwin, M.2
Nguyen, J.3
Gasset, M.4
Serban, A.5
Groth, D.6
Mehlhom, I.7
Huang, Z.8
Fletterick, R.J.9
Cohen, F.E.10
-
33
-
-
0029116625
-
Conformational transitions in peptides containing two putative α-helices of the prion protein
-
Zhang H, Kaneko K, Nguyen JT, Livshits TL, Baldwin ML, Cohen FE, James TL, Prusiner SB: Conformational transitions in peptides containing two putative α-helices of the prion protein. J Mol Biol 1995, 250:514-526. Peptide fragments corresponding to the fragments 90-145 and 109-141 adopt a helical structure in aqueous-organic solvents. On the other hand, solutions of high salt concentration allow conversion to an associated rodshaped β-sheet structure, analogous to the helix→sheet conversion which appears to operate in the PrP-soluble to PrP-scrapie transition.
-
(1995)
J Mol Biol
, vol.250
, pp. 514-526
-
-
Zhang, H.1
Kaneko, K.2
Nguyen, J.T.3
Livshits, T.L.4
Baldwin, M.L.5
Cohen, F.E.6
James, T.L.7
Prusiner, S.B.8
-
34
-
-
0028925377
-
Prion protein peptides Induce α-helix to beta sheet conformational transitions
-
Nguyen J, Baldwin MA, Cohen FE, Prusiner SB: Prion protein peptides Induce α-helix to beta sheet conformational transitions. Biochemistry 1995, 34:4186-4192. Peptides corresponding to the regions of putative secondary structure in the cellular prion protein were studied as models for the conformational transition governing the conversion to PrP-scrapie. PrP 109-122 adopts a sheet structure in aqueous buffers and converts PrP 104-122, which is helical, into a sheet conformation apparently approximating the PrP-C to PrP-Sc conversion occurring in vivo.
-
(1995)
Biochemistry
, vol.34
, pp. 4186-4192
-
-
Nguyen, J.1
Baldwin, M.A.2
Cohen, F.E.3
Prusiner, S.B.4
-
35
-
-
0028120343
-
Scrapie amyloid prion protein has the conformational characteristics of an aggregated molten globule folding Intermediate
-
Safar J, Roller PP, Gajdusek DC, Gibbs CJ Jr: Scrapie amyloid prion protein has the conformational characteristics of an aggregated molten globule folding Intermediate. Biochemistry 1994, 33:8375-8383. At low concentrations of guanidinium hydrochloride, the scrapie protein PrP 27-30 dissociates into a compact intermediate with substantial secondary structure and a partially native tertiary structure. The results suggest that PrP 27-30 associates through a compact metastable hydrophobic intermediate with non-native tertiary and secondary structure.
-
(1994)
Biochemistry
, vol.33
, pp. 8375-8383
-
-
Safar, J.1
Roller, P.P.2
Gajdusek, D.C.3
Gibbs C.J., Jr.4
-
36
-
-
0027363495
-
Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
-
Safar J, Roller PP, Gajdusek DC, Gibbs CJ Jr: Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci 1993, 2:2206-2216.
-
(1993)
Protein Sci
, vol.2
, pp. 2206-2216
-
-
Safar, J.1
Roller, P.P.2
Gajdusek, D.C.3
Gibbs C.J., Jr.4
-
37
-
-
0028782010
-
Spectroscopic charaterization of conformational differences between PrPC and PrP-Sc: An alpha-helix to beta-sheet transition
-
Baldwin MA, Pan KM, Nguyen J, Huang Z, Groth D, Serban A, Gasset M, Mehlhorn I, Fletterick RJ, Cohen FE: Spectroscopic charaterization of conformational differences between PrPC and PrP-Sc: an alpha-helix to beta-sheet transition. Philos Trans R Soc Lond Biol 1995, 343:435-441. Spectroscopic methods reveal a major conformational difference between PrP-C and PrP-Sc: PrP-C is rich in a helices whereas PrP-Sc has a high β sheet content. Thus, the formation of PrP-Sc from PrP-C involves a conformational change from a helix to β sheet.
-
(1995)
Philos Trans R Soc Lond Biol
, vol.343
, pp. 435-441
-
-
Baldwin, M.A.1
Pan, K.M.2
Nguyen, J.3
Huang, Z.4
Groth, D.5
Serban, A.6
Gasset, M.7
Mehlhorn, I.8
Fletterick, R.J.9
Cohen, F.E.10
-
38
-
-
0029066886
-
Species specificity in the cell free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier
-
Kocisko DA, Priola SA, Raymond GJ, Chesebro B, Lansbury PT Jr, Caughey B: Species specificity in the cell free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier. Proc Natl Acad Sci USA 1995, 9:3923-3927. Mouse PrP-C and hamster PrP-C can be converted into PrP-Sc with mouse and hamster PrP-Sc respectively. Hamster PrP-C can also be converted into a protease-resistant prion-like form with mouse PrP-C, but little activity was observed in the reciprocal reaction. These results and others imply that the different structures of the mouse and hamster prion may explain the species barriers.
-
(1995)
Proc Natl Acad Sci USA
, vol.9
, pp. 3923-3927
-
-
Kocisko, D.A.1
Priola, S.A.2
Raymond, G.J.3
Chesebro, B.4
Lansbury P.T., Jr.5
Caughey, B.6
-
39
-
-
0028997297
-
Non-genetic propagation of strain-specific properties of scrapie prion protein
-
Bessen RA, Kocisko DA, Raymond GJ, Nandan S, Lansbury PT, Caughey B: Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 1995, 375:698-700. One of the requirements for the protein-only model of prion disease is that the inheritance of strain differences must be mediated by stable variations in PrP-scrapie structure. Different PrP-scrapie strains were able to convert PrP-soluble into the strain of the prion used as a template, as discerned from their different susceptibility to proteinase K. Strain-specific infectivity experiments are underway.
-
(1995)
Nature
, vol.375
, pp. 698-700
-
-
Bessen, R.A.1
Kocisko, D.A.2
Raymond, G.J.3
Nandan, S.4
Lansbury, P.T.5
Caughey, B.6
-
40
-
-
0027956109
-
Cell-free formation of protease-resistant prion protein
-
Kocisko DA, Come JH, Priola SA, Cheseboro B, Raymond GJ, Lansbury PT, Caughey B: Cell-free formation of protease-resistant prion protein. Nature 1994, 370:471-474. The conversion of PrP-soluble into PrP-scrapie by a PrP-scrapie particle suggests that this conversion employs an interaction between PrP-soluble and PrP-scrapie and involves a conformational change in the former.
-
(1994)
Nature
, vol.370
, pp. 471-474
-
-
Kocisko, D.A.1
Come, J.H.2
Priola, S.A.3
Cheseboro, B.4
Raymond, G.J.5
Lansbury, P.T.6
Caughey, B.7
-
41
-
-
0027945627
-
Conformational changes in the serpins and the mechanism of α-1 antichymotrypsin deficiency
-
Carrell RW, Whisstock J, Lomas DA: Conformational changes in the serpins and the mechanism of α-1 antichymotrypsin deficiency. Amer J Respir Crit Care Med 1994, 150:171-175. Like other members of the serine protease family of inhibitors, α-1 antichymotrypsin has its reactive center situated in a loop. This loop can adopt a variety of conformations including ones where the loop becomes part of an existing β sheet extending the sheet by one strand. The loop can also insert into another sheet intermolecularly, creating a dimeric sheet structure which causes polymerization to occur within the hepatocyte of the common 2. mutant of antichymotrypsin, leading to liver damage.
-
(1994)
Amer J Respir Crit Care Med
, vol.150
, pp. 171-175
-
-
Carrell, R.W.1
Whisstock, J.2
Lomas, D.A.3
-
42
-
-
0029011597
-
Defective protein folding as a cause of disease
-
Sifers RN: Defective protein folding as a cause of disease. Nature Struct Biol 1995, 2:355-357. A concise review on the conformational changes leading to disease in the case of antichymotrypsin.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 355-357
-
-
Sifers, R.N.1
-
43
-
-
0026597011
-
β-sheet rearrangements, serpins and beyond
-
Banzon JA, Kelly JW: β-sheet rearrangements, serpins and beyond. Protein Eng 1992, 5:113-115.
-
(1992)
Protein Eng
, vol.5
, pp. 113-115
-
-
Banzon, J.A.1
Kelly, J.W.2
-
44
-
-
0027999955
-
Thromboembolic disease due to thermolablle conformational changes of antithrombin Rouen-VI
-
Bruce D, Perry DJ, Borg J-Y, Carrell RW, Wardell MR: Thromboembolic disease due to thermolablle conformational changes of antithrombin Rouen-VI. J Clin Invest 1994, 94:2265-2274. A new variant of antithrombin was shown to have normal activity which decreased at 4°C due to a loop→strand conformational change that leads to polymerization.
-
(1994)
J Clin Invest
, vol.94
, pp. 2265-2274
-
-
Bruce, D.1
Perry, D.J.2
Borg, J.-Y.3
Carrell, R.W.4
Wardell, M.R.5
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