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Volumn 415, Issue 1, 2003, Pages 94-100

A protein isolated from Escherichia coli, identified as GroEL, reacts with anti-β spectrin antibodies

Author keywords

Anti spectrin antibodies; Escherichia coli; GroEL; Spectrin like proteins; Tandem MS MS

Indexed keywords

BETA SPECTRIN ANTIBODY; CHAPERONIN; DETERGENT; EPITOPE; PROTEIN ANTIBODY; UNCLASSIFIED DRUG; UREA;

EID: 0037497368     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-9861(03)00223-6     Document Type: Article
Times cited : (4)

References (30)
  • 1
    • 0014411415 scopus 로고
    • Selective solubilization of a protein component of the red cell membrane
    • Marchesi V.T., Steers E. Selective solubilization of a protein component of the red cell membrane. Science. 159:1968;203-204.
    • (1968) Science , vol.159 , pp. 203-204
    • Marchesi, V.T.1    Steers, E.2
  • 2
    • 0029186874 scopus 로고
    • Actin-binding proteins. 1: Spectrin superfamily
    • Hartwig J.H. Actin-binding proteins. 1: Spectrin superfamily. Protein Profile. 2:1995;703-800.
    • (1995) Protein Profile , vol.2 , pp. 703-800
    • Hartwig, J.H.1
  • 4
    • 0021705094 scopus 로고
    • Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins
    • Pollard T.D. Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins. J. Cell Biol. 99:1984;1970-1980.
    • (1984) J. Cell Biol. , vol.99 , pp. 1970-1980
    • Pollard, T.D.1
  • 5
    • 0024325082 scopus 로고
    • A spectrin-like protein present on membranes of Amoeba proteus as studied with monoclonal antibodies
    • Choi E.Y., Jeon K.W. A spectrin-like protein present on membranes of Amoeba proteus as studied with monoclonal antibodies. Exp. Cell Res. 185:1989;154-165.
    • (1989) Exp. Cell Res. , vol.185 , pp. 154-165
    • Choi, E.Y.1    Jeon, K.W.2
  • 6
    • 0031057350 scopus 로고    scopus 로고
    • Local accumulation of alpha-spectrin-related protein under plasma membrane during capping and phagocytosis in Acanthamoeba
    • Kwiatkowska K., Sobota A. Local accumulation of alpha-spectrin-related protein under plasma membrane during capping and phagocytosis in Acanthamoeba. Cell Motil. Cytoskeleton. 36:1997;253-265.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 253-265
    • Kwiatkowska, K.1    Sobota, A.2
  • 7
    • 0024115388 scopus 로고
    • The detection of a spectrin-like protein in Trypanosoma cruzi with a polyclonal antibody
    • Alcina A., Hargreaves A.J., Avila J., Hesketh J.E., Fresno M. The detection of a spectrin-like protein in Trypanosoma cruzi with a polyclonal antibody. Cell. Biol. Int. Rep. 12:1988;979-985.
    • (1988) Cell. Biol. Int. Rep. , vol.12 , pp. 979-985
    • Alcina, A.1    Hargreaves, A.J.2    Avila, J.3    Hesketh, J.E.4    Fresno, M.5
  • 8
    • 0024031397 scopus 로고
    • Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei
    • Schneider A., Lutz H.U., Marugg R., Gehr P., Seebeck T. Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei. J. Cell Sci. 90:1988;307-315.
    • (1988) J. Cell Sci. , vol.90 , pp. 307-315
    • Schneider, A.1    Lutz, H.U.2    Marugg, R.3    Gehr, P.4    Seebeck, T.5
  • 9
    • 0029328319 scopus 로고
    • Detection and immunolocalisation of human erythrocyte spectrin immunoanalogues in Toxoplasma gondii (Protozoan, Parasite)
    • Ghazali M., Roidier M.H., Moundi B.E., Babin P., Fernandez B., Jacquemin J.L. Detection and immunolocalisation of human erythrocyte spectrin immunoanalogues in Toxoplasma gondii (Protozoan, Parasite). J. Eukaryot. Microbiol. 42:1995;427-433.
    • (1995) J. Eukaryot. Microbiol. , vol.42 , pp. 427-433
    • Ghazali, M.1    Roidier, M.H.2    Moundi, B.E.3    Babin, P.4    Fernandez, B.5    Jacquemin, J.L.6
  • 10
    • 0033858271 scopus 로고    scopus 로고
    • A putative spectrin-containing membrane skeleton in hyphal tips of Neurospora crassa
    • Degouseé N., Gupta G., Lew R.R., Heath B. A putative spectrin-containing membrane skeleton in hyphal tips of Neurospora crassa. Fungal Genet. Biol. 30:2000;33-44.
    • (2000) Fungal Genet. Biol. , vol.30 , pp. 33-44
    • Degouseé, N.1    Gupta, G.2    Lew, R.R.3    Heath, B.4
  • 11
    • 0027175830 scopus 로고
    • Immunodetection of spectrin antigens in plant cells
    • De Ruijter N., Emons A.M. Immunodetection of spectrin antigens in plant cells. Cell Biol. Int. 17:1993;169-182.
    • (1993) Cell Biol. Int. , vol.17 , pp. 169-182
    • De Ruijter, N.1    Emons, A.M.2
  • 13
  • 15
    • 0027478733 scopus 로고
    • Evidence for membrane skeleton in higher plants. A spectrin-like polypeptide co-isolates with rice root plasma membranes
    • Faraday C.D., Spanswick R.M. Evidence for membrane skeleton in higher plants. A spectrin-like polypeptide co-isolates with rice root plasma membranes. FEBS Lett. 318:1993;313-316.
    • (1993) FEBS Lett. , vol.318 , pp. 313-316
    • Faraday, C.D.1    Spanswick, R.M.2
  • 16
    • 0025933220 scopus 로고
    • Identification of a 220 kDa membrane-associated plant cell protein immunologically related to human beta spectrin
    • Michaud D., Guillet G., Rogers P.A., Charest P.M. Identification of a 220. kDa membrane-associated plant cell protein immunologically related to human beta spectrin FEBS Lett. 294:1991;77-80.
    • (1991) FEBS Lett. , vol.294 , pp. 77-80
    • Michaud, D.1    Guillet, G.2    Rogers, P.A.3    Charest, P.M.4
  • 18
    • 0035036229 scopus 로고    scopus 로고
    • Association of spectrin-like proteins with the actin-organized aggregate of endoplasmic reticulum in the Spitzenkorper of gravitropically tip-growing plant cells
    • Braun M. Association of spectrin-like proteins with the actin-organized aggregate of endoplasmic reticulum in the Spitzenkorper of gravitropically tip-growing plant cells. Plant Physiol. 125:2001;1611-1619.
    • (2001) Plant Physiol. , vol.125 , pp. 1611-1619
    • Braun, M.1
  • 19
    • 0037479487 scopus 로고    scopus 로고
    • Polypeptides immunologically related to spectrin are present in bacterial cells
    • Bisikirska B., Lorenz M., Nietubyć M., Sikorski A.F. Polypeptides immunologically related to spectrin are present in bacterial cells. Cell. Mol. Biol. Lett. 1:1996;171-176.
    • (1996) Cell. Mol. Biol. Lett. , vol.1 , pp. 171-176
    • Bisikirska, B.1    Lorenz, M.2    Nietubyć, M.3    Sikorski, A.F.4
  • 20
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Dijnovic-Carugo K., Gautel M., Ylanne J., Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 513:2002;119-123.
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Dijnovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 21
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 24
    • 0032102792 scopus 로고    scopus 로고
    • Identifying proteins and post-translational modifications by mass spectrometry
    • Küster B., Mann M. Identifying proteins and post-translational modifications by mass spectrometry. Curr. Opin. Struct. Biol. 8:1998;393-400.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 393-400
    • Küster, B.1    Mann, M.2
  • 26
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 20:1999;3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 27
    • 0031616684 scopus 로고    scopus 로고
    • A new algorithm for analysis of the homology in protein primary structure
    • Leluk J. A new algorithm for analysis of the homology in protein primary structure. Comput. Chem. 22:1998;123-131.
    • (1998) Comput. Chem. , vol.22 , pp. 123-131
    • Leluk, J.1
  • 28
    • 0028232947 scopus 로고
    • The stability and hydrophobicity of cytosolic mandrial malate dehydrogenases and their relation to chaperonin-assisted folding
    • Staniforth R.A., Cortes A., Burston S.G., Atkinson T., Holbrook J.J., Clarke A.R. The stability and hydrophobicity of cytosolic mandrial malate dehydrogenases and their relation to chaperonin-assisted folding. FEBS Lett. 344:1994;129-135.
    • (1994) FEBS Lett. , vol.344 , pp. 129-135
    • Staniforth, R.A.1    Cortes, A.2    Burston, S.G.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6
  • 29
    • 0029121418 scopus 로고
    • Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides
    • Ybarra J., Horowitz P.M. Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides. J. Biol. Chem. 270:1995;22962-22967.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22962-22967
    • Ybarra, J.1    Horowitz, P.M.2
  • 30
    • 0029117578 scopus 로고
    • Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization
    • Blennow A., Surin B.P., Ehring H., McLaren N.F., Spangfort M.D. Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization. Biochim. Biophys. Acta. 1252:1995;69-78.
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 69-78
    • Blennow, A.1    Surin, B.P.2    Ehring, H.3    McLaren, N.F.4    Spangfort, M.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.