메뉴 건너뛰기




Volumn 39, Issue 5-6, 2002, Pages 273-288

Idiotypic mimicry of a catalytic antibody active site

Author keywords

Acetylcholinesterase; Anti idiotypic; Catalytic antibody; Cholinesterase; Peripheral anionic site

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; BENZYLSULFONYL FLUORIDE; BUTYRYLTHIOCHOLINE; CATALYTIC ANTIBODY; CHOLINESTERASE; EDROPHONIUM; FASCICULIN; IDIOTYPIC ANTIBODY; IMMUNOGLOBULIN; ISO OMPA; MONOCLONAL ANTIBODY; PYRIDOSTIGMINE; TETRAMETHYLAMMONIUM;

EID: 0036772365     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(02)00113-X     Document Type: Article
Times cited : (8)

References (41)
  • 2
    • 0031820915 scopus 로고    scopus 로고
    • Electrotactins: A class of adhesion proteins with conserved electrostatic and structural motifs
    • Botti S.A., Felder C.E., Sussman J.L., Silman I. Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs. Protein Eng. 11:1998;415-420.
    • (1998) Protein Eng. , vol.11 , pp. 415-420
    • Botti, S.A.1    Felder, C.E.2    Sussman, J.L.3    Silman, I.4
  • 3
    • 0033613931 scopus 로고    scopus 로고
    • Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly
    • Bourne Y., Taylor P., Bougis P.E., Marchot P. Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. J. Biol. Chem. 274:1999;2963-2970.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2963-2970
    • Bourne, Y.1    Taylor, P.2    Bougis, P.E.3    Marchot, P.4
  • 4
    • 0032500701 scopus 로고    scopus 로고
    • A comparison of the crystallographic structures of two catalytic antibodies with esterase activity
    • Buchbinder J.L., Stephenson R.C., Scanlan T.S., Fletterick R.J. A comparison of the crystallographic structures of two catalytic antibodies with esterase activity. J. Mol. Biol. 282:1998;1033-1041.
    • (1998) J. Mol. Biol. , vol.282 , pp. 1033-1041
    • Buchbinder, J.L.1    Stephenson, R.C.2    Scanlan, T.S.3    Fletterick, R.J.4
  • 6
    • 0027935954 scopus 로고
    • Further studies on the occurrence of serum autoantibodies against a membrane-bound acetylcholinesterase fraction in ALS/MND patients and controls
    • Conradi S., Ronnevi L.O. Further studies on the occurrence of serum autoantibodies against a membrane-bound acetylcholinesterase fraction in ALS/MND patients and controls. J. Neurol. Sci. 124(Suppl.):1994;167-169.
    • (1994) J. Neurol. Sci. , vol.124 , Issue.SUPPL. , pp. 167-169
    • Conradi, S.1    Ronnevi, L.O.2
  • 7
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation
    • De Ferrari G.V., Canales M.A., Shin I., Weiner L.M., Silman I., Inestrosa N.C. A structural motif of acetylcholinesterase that promotes amyloid β-peptide fibril formation. Biochemistry. 40:2001;10447-10457.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 8
    • 0022490455 scopus 로고
    • A simplified procedure for the purification of large quantities of fetal bovine serum acetylcholinesterase
    • De la Hoz D., Doctor B.P., Ralston J.S., Rush R.S., Wolfe A.D. A simplified procedure for the purification of large quantities of fetal bovine serum acetylcholinesterase. Life Sci. 39:1986;195-199.
    • (1986) Life Sci. , vol.39 , pp. 195-199
    • De la Hoz, D.1    Doctor, B.P.2    Ralston, J.S.3    Rush, R.S.4    Wolfe, A.D.5
  • 9
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon M. The determination of enzyme inhibitor constants. Biochem. J. 55:1953;170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 11
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson G., Wlodawar A. Catalytic triads and their relatives. Trends Biochem. Sci. 23:1998;347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawar, A.2
  • 13
    • 0016311758 scopus 로고
    • Do immunoglobulins have proteolytic activity?
    • Erhan S., Greller L.D. Do immunoglobulins have proteolytic activity? Nature. 251:1974;353-355.
    • (1974) Nature , vol.251 , pp. 353-355
    • Erhan, S.1    Greller, L.D.2
  • 14
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao Q.S., Sun M., Rees A.R., Paul S. Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 253:1995;658-664.
    • (1995) J. Mol. Biol. , vol.253 , pp. 658-664
    • Gao, Q.S.1    Sun, M.2    Rees, A.R.3    Paul, S.4
  • 18
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid β-peptides into Alzheimer's fibrils: Possible role of the peripheral site of the enzyme
    • Inestrosa N.C., Alvarez A., Perez C.A., Moreno R.D., Vicente M., Linker C., Casanueva O.I., Soto C., Garrido J. Acetylcholinesterase accelerates assembly of amyloid β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron. 16:1996;881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6    Casanueva, O.I.7    Soto, C.8    Garrido, J.9
  • 19
    • 0027489204 scopus 로고
    • Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: Production of a catalytic antibody with a cholinesterase activity
    • Izadyar L., Friboulet A., Remy M.-H., Roseto A., Thomas D. Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity. Proc. Natl. Acad. Sci. U.S.A. 90:1993;8876-8880.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8876-8880
    • Izadyar, L.1    Friboulet, A.2    Remy, M.-H.3    Roseto, A.4    Thomas, D.5
  • 20
    • 0028926386 scopus 로고
    • Anti-acetylcholinesterase antibodies display cholinesterase-like activity
    • Johnson G., Moore S.W. Anti-acetylcholinesterase antibodies display cholinesterase-like activity. Eur. J. Immunol. 25:1995;25-29.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 25-29
    • Johnson, G.1    Moore, S.W.2
  • 21
    • 0033583819 scopus 로고    scopus 로고
    • The adhesion function of acetylcholinesterase is located at the peripheral anionic site
    • Johnson G., Moore S.W. The adhesion function of acetylcholinesterase is located at the peripheral anionic site. Biochem. Biophys. Res. Commun. 258:1999;758-762.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 758-762
    • Johnson, G.1    Moore, S.W.2
  • 22
    • 0035087714 scopus 로고    scopus 로고
    • Cholinesterase-like catalytic antibodies: Reaction with substrates and inhibitors
    • Johnson G., Moore S.W. Cholinesterase-like catalytic antibodies: reaction with substrates and inhibitors. Mol. Immunol. 37:2000;707-719.
    • (2000) Mol. Immunol. , vol.37 , pp. 707-719
    • Johnson, G.1    Moore, S.W.2
  • 26
    • 0026613082 scopus 로고
    • 125I-fasciculin to rat brain acetylcholinesterase. The complex still binds diisopropyl fluorophosphate
    • 125I -fasciculin to rat brain acetylcholinesterase. The complex still binds diisopropyl fluorophosphate J. Biol. Chem. 267:1992;22122-22130.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22122-22130
    • Le Du, M.M.1    Marchot, P.2    Bougis, P.E.3    Fontecilla-Camps, J.C.4
  • 28
    • 0033607448 scopus 로고    scopus 로고
    • Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase
    • Munoz F.J., Aldunate R., Inestrosa N.C. Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase. Neuroreport. 10:1999;3621-3625.
    • (1999) Neuroreport , vol.10 , pp. 3621-3625
    • Munoz, F.J.1    Aldunate, R.2    Inestrosa, N.C.3
  • 29
    • 0027217179 scopus 로고
    • Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the active site, the hydrophobic site and the acyl pocket
    • Ordentlich A., Barak D., Kronman C., Flashner Y., Leitner M., Segall Y., Ariel N., Cohen S., Velan B., Shafferman A. Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the active site, the hydrophobic site and the acyl pocket. J. Biol. Chem. 268:1993;17083-17095.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17083-17095
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Flashner, Y.4    Leitner, M.5    Segall, Y.6    Ariel, N.7    Cohen, S.8    Velan, B.9    Shafferman, A.10
  • 30
    • 0028435833 scopus 로고
    • Catalytic activity of anti-ground state antibodies, antibody subunits and human autoantibodies
    • Paul S. Catalytic activity of anti-ground state antibodies, antibody subunits and human autoantibodies. Appl. Biochem. Biotechnol. 47:1994;241-253.
    • (1994) Appl. Biochem. Biotechnol. , vol.47 , pp. 241-253
    • Paul, S.1
  • 32
    • 0034077438 scopus 로고    scopus 로고
    • Autoantibodies to thyroglobulin in health and disease
    • Rose N.R., Burek C.L. Autoantibodies to thyroglobulin in health and disease. Appl. Biochem. Biotechnol. 83:2000;245-251.
    • (2000) Appl. Biochem. Biotechnol. , vol.83 , pp. 245-251
    • Rose, N.R.1    Burek, C.L.2
  • 34
    • 0032488637 scopus 로고    scopus 로고
    • Allosteric control of acetylcholinesterase activity by monoclonal antibodies
    • Saxena A., Hur R., Doctor B.P. Allosteric control of acetylcholinesterase activity by monoclonal antibodies. Biochemistry. 37:1998;145-154.
    • (1998) Biochemistry , vol.37 , pp. 145-154
    • Saxena, A.1    Hur, R.2    Doctor, B.P.3
  • 37
    • 0029134092 scopus 로고
    • Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons
    • Schwarz M., Glick D., Loewenstein Y., Soreq H. Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons. Pharmacol. Ther. 76:1995;283-322.
    • (1995) Pharmacol. Ther. , vol.76 , pp. 283-322
    • Schwarz, M.1    Glick, D.2    Loewenstein, Y.3    Soreq, H.4
  • 38
    • 0028559984 scopus 로고
    • Idiotypic induction of autoimmunity: A new aspect of the idiotypic network
    • Shoenfeld Y. Idiotypic induction of autoimmunity: a new aspect of the idiotypic network. FASEB J. 8:1994;1296-1301.
    • (1994) FASEB J. , vol.8 , pp. 1296-1301
    • Shoenfeld, Y.1
  • 40
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 253:1991;872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 41
    • 0027732733 scopus 로고
    • Monoclonal antibody AE-2 modulates carbamate and organophosphate inhibition of fetal bovine serum acetylcholinesterase
    • Wolfe A.D., Chiang P.K., Doctor B.P., Fryar N., Rhee J.-P., Saeed M. Monoclonal antibody AE-2 modulates carbamate and organophosphate inhibition of fetal bovine serum acetylcholinesterase. Mol. Pharmacol. 44:1993;1152-1157.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 1152-1157
    • Wolfe, A.D.1    Chiang, P.K.2    Doctor, B.P.3    Fryar, N.4    Rhee, J.-P.5    Saeed, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.