메뉴 건너뛰기




Volumn 6, Issue 1, 1996, Pages 11-17

Alternative conformations of amyloidogenic proteins govern their behavior

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN; LYSOZYME; PREALBUMIN; RETINOL BINDING PROTEIN;

EID: 0029981197     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80089-3     Document Type: Article
Times cited : (577)

References (44)
  • 1
    • 0028584438 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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
  • 9
    • 0026675307 scopus 로고
    • 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 scopus 로고
    • 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
  • 13
    • 0029114261 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고    scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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
  • 23
    • 0028987233 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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
  • 29
    • 0025944507 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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
  • 33
    • 0029116625 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.