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Volumn 293, Issue 3, 1999, Pages 449-455

A 2.6 Å structure of a serpin polymer and implications for conformational disease

Author keywords

Amyloid; Polymer; Serpin; Structure; 1 antitrypsin

Indexed keywords

ALPHA 1 ANTITRYPSIN; AMYLOID; SERINE PROTEINASE INHIBITOR; PEPTIDE FRAGMENT; POLYMER; RECOMBINANT PROTEIN;

EID: 0032589794     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3184     Document Type: Article
Times cited : (120)

References (32)
  • 1
    • 0023838532 scopus 로고
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell. 52:1988;487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 2
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon D., Anderson W. F. A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6:1988;219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.1    Anderson, W.F.2
  • 3
  • 5
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R. W., Lomas D. A. Conformational disease. Lancet. 350:1997;134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 6
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive-loop conformations by proteolytic cleavage
    • Chang W. S., Wardell M. R., Lomas D. A., Carrell R. W. Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314:1996;647-653.
    • (1996) Biochem. J. , vol.314 , pp. 647-653
    • Chang, W.S.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 7
    • 0031033206 scopus 로고    scopus 로고
    • Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins
    • Chang W. S., Whisstock J., Hopkins P. C., Lesk A. M., Carrell R. W., Wardell M. R. Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins. Protein Sci. 6:1997;89-98.
    • (1997) Protein Sci. , vol.6 , pp. 89-98
    • Chang, W.S.1    Whisstock, J.2    Hopkins, P.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 11
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J. D., Lansbury P. T. J. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.J.2
  • 12
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang J. S., Brünger A. T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243:1994;100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 13
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 14
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
    • Lansbury P. T. J. Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease. Proc. Natl Acad. Sci. USA. 96:1999;3342-3344.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury, P.T.J.1
  • 16
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177:1984;531-557.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 18
    • 0027295822 scopus 로고
    • 1-Antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization
    • 1-Antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization. J. Biol. Chem. 268:1993;15333-15335.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15333-15335
    • Lomas, D.A.1    Finch, J.T.2    Seyama, K.3    Nukiwa, T.4    Carrell, R.W.5
  • 19
    • 0028173205 scopus 로고
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments
    • 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer β-protein into filaments. Nature. 372:1994;92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer, H.B.J.3    Das, S.4    Potter, H.5
  • 22
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee D. E. A visual protein crystallographic software system for X11/XView. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 23
    • 0028057108 scopus 로고
    • Raster3d version-2.0 - A program for photorealistic molecular graphics
    • Merritt E. A., Murphy M. E. P. Raster3d version-2.0 - a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 25
    • 84920325457 scopus 로고
    • AMoRe - an automated package for molecular replacement
    • Navaza J. AMoRe - an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu N. S., Read R. J. Improved structure refinement through maximum likelihood. Acta Crystallog. sect. A. 52:1996;659-668.
    • (1996) Acta Crystallog. Sect. a , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 28
    • 0030768649 scopus 로고    scopus 로고
    • Model phases: Probabilities and bias
    • Read R. J. Model phases: probabilities and bias. Methods Enzymol. 277:1997;110-128.
    • (1997) Methods Enzymol. , vol.277 , pp. 110-128
    • Read, R.J.1
  • 30
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein P. E., Carrell R. W. What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2:1995;96-113.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 32
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • Xue Y., Bjorquist P., Inghardt T., Linschoten M., Musil D., Sjolin L., Deinum J. Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure. 6:1998;627-636.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Bjorquist, P.2    Inghardt, T.3    Linschoten, M.4    Musil, D.5    Sjolin, L.6    Deinum, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.