메뉴 건너뛰기




Volumn 9, Issue 2, 2000, Pages 417-420

Cleaved antitrypsin polymers at atomic resolution

Author keywords

Conformational disease; Polymerization; X ray crystallography; antitrypsin deficiency

Indexed keywords

ALPHA 1 ANTITRYPSIN; POLYMER;

EID: 0034000728     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.2.417     Document Type: Article
Times cited : (81)

References (26)
  • 1
    • 0023838532 scopus 로고
    • Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease
    • Abraham CR, Selkoe DJ, Potter H. 1988. Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 52:487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 3
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW, Lomas DA. 1997. Conformational disease. Lancet 350:134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (Collaborative Computing Project Number 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 5
    • 0032065494 scopus 로고    scopus 로고
    • Lung polymers in Z alpha1-antitrypsin deficiency-related emphysema
    • Elliott PR, Bilton D, Lomas DA. 1998. Lung polymers in Z alpha1-antitrypsin deficiency-related emphysema. Am J Respir Cell Mol Biol 18:670-674.
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 670-674
    • Elliott, P.R.1    Bilton, D.2    Lomas, D.A.3
  • 8
    • 0028935156 scopus 로고
    • The putative role of alpha-1-antitrypsin in the disaggregation of amyloid lambda fibrils
    • Eriksson S, Janciauskiene S, Merlini G. 1995. The putative role of alpha-1-antitrypsin in the disaggregation of amyloid lambda fibrils. J Intern Med 237:143-149.
    • (1995) J Intern Med , vol.237 , pp. 143-149
    • Eriksson, S.1    Janciauskiene, S.2    Merlini, G.3
  • 9
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to Molscript version 1.4, including reading and contouring of electron density maps
    • Esnouf RM. 1999. Further additions to Molscript version 1.4, including reading and contouring of electron density maps. Acta Crystallogr D55:938-940.
    • (1999) Acta Crystallogr , vol.D55 , pp. 938-940
    • Esnouf, R.M.1
  • 10
    • 0027182969 scopus 로고
    • Effects of mutations in the hinge region of serpins
    • Hopkins PC, Carrell RW, Stone SR. 1993. Effects of mutations in the hinge region of serpins. Biochemistry 32:7650-7657.
    • (1993) Biochemistry , vol.32 , pp. 7650-7657
    • Hopkins, P.C.1    Carrell, R.W.2    Stone, S.R.3
  • 11
    • 0028879762 scopus 로고
    • The contribution of the conserved hinge region residues of alpha1-antitrypsin to its reaction with elastase
    • Hopkins PC, Stone SR. 1995. The contribution of the conserved hinge region residues of alpha1-antitrypsin to its reaction with elastase. Biochemistry 34:15872-15879.
    • (1995) Biochemistry , vol.34 , pp. 15872-15879
    • Hopkins, P.C.1    Stone, S.R.2
  • 12
    • 0029248222 scopus 로고
    • In vitro amyloid fibril formation from alpha 1-antitrypsin
    • Janciauskiene S, Carlemalm E, Eriksson S. 1995. In vitro amyloid fibril formation from alpha 1-antitrypsin. Biol Chem 376:103-109.
    • (1995) Biol Chem , vol.376 , pp. 103-109
    • Janciauskiene, S.1    Carlemalm, E.2    Eriksson, S.3
  • 13
    • 0032561313 scopus 로고    scopus 로고
    • Alzheimer's peptide A beta 1-42 binds to two beta sheets of antichymotrypsin and transforms it from inhibitor to substrate
    • Janciauskiene S, Rubin H, Lukacs CM, Wright HT. 1998. Alzheimer's peptide A beta 1-42 binds to two beta sheets of antichymotrypsin and transforms it from inhibitor to substrate. J Biol Chem 273:28360-28364.
    • (1998) J Biol Chem , vol.273 , pp. 28360-28364
    • Janciauskiene, S.1    Rubin, H.2    Lukacs, C.M.3    Wright, H.T.4
  • 14
    • 0000243829 scopus 로고
    • PROCHECH: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECH: A program to check the stereochemical quality of protein structures. J Appl Crstallogr 26:283-291.
    • (1993) J Appl Crstallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 15
    • 0027177515 scopus 로고
    • The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the Kunitz inhibitors
    • Le Bonniec BF, Guinto ER, MacGillivray RT, Stone SR, Esmon CT. 1993. The role of thrombin's Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the Kunitz inhibitors. J Biol Chem 268:19055-19061.
    • (1993) J Biol Chem , vol.268 , pp. 19055-19061
    • Le Bonniec, B.F.1    Guinto, E.R.2    MacGillivray, R.T.3    Stone, S.R.4    Esmon, C.T.5
  • 16
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H, Tokuoka R, Deisenhofer J, Huber R. 1984. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 177:531-557.
    • (1984) J Mol Biol , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 18
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW. 1992. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 357:605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 19
    • 0027295822 scopus 로고
    • Alpha 1-antitrypsin Siiyama (Ser53 → Phe). Further evidence for intracellular loop-sheet polymerization
    • Lomas DA, Finch JT, Seyama K, Nukiwa T, Carrell RW. 1993. Alpha 1-antitrypsin Siiyama (Ser53 → Phe). Further evidence for intracellular loop-sheet polymerization. J Biol Chem 268:15333-15335.
    • (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
  • 20
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis
    • Mast AE, Enghild JJ, Salvesen G. 1992. Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis. Biochemistry 31:2720-2728.
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 21
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262:10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 22
    • 0020670626 scopus 로고
    • Alpha 1-antitrypsin and reactive systemic amyloidosis
    • Maury CP, Teppo AM, Froseth B, Wegelius O. 1983. Alpha 1-antitrypsin and reactive systemic amyloidosis. Clin Sci 64:453-454.
    • (1983) Clin Sci , vol.64 , pp. 453-454
    • Maury, C.P.1    Teppo, A.M.2    Froseth, B.3    Wegelius, O.4
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A50:157-163.
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. 1967. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Comm 27:157-162.
    • (1967) Biochem Biophys Res Comm , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 26
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein PE, Carrell RW. 1995. What do dysfunctional serpins tell us about molecular mobility and disease? Nat Struct Biol 2:96-113.
    • (1995) Nat Struct Biol , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.