메뉴 건너뛰기




Volumn 18, Issue 2, 2000, Pages 49-52

Continuous weak-affinity immunosensing

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN ANTIBODY COMPLEX; IMMUNOSENSOR; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; REVIEW;

EID: 0033976397     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-7799(99)01411-0     Document Type: Short Survey
Times cited : (36)

References (28)
  • 1
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen M.et al. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem., Int. Ed. Engl. 37:1998;2754-2794.
    • (1998) Angew. Chem., Int. Ed. Engl. , vol.37 , pp. 2754-2794
    • Mammen, M.1
  • 2
    • 0029670264 scopus 로고    scopus 로고
    • Detection of low affinity interactions between peptides and heat shock proteins by chemiluminescence of enhanced avidity reactions (CLEAR)
    • Causey L.D., Dwyer D.S. Detection of low affinity interactions between peptides and heat shock proteins by chemiluminescence of enhanced avidity reactions (CLEAR). Nat. Biotechnol. 14:1996;348-351.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 348-351
    • Causey, L.D.1    Dwyer, D.S.2
  • 3
    • 0028155937 scopus 로고
    • High sensitivity, low affinity - Paradox of T-cell receptor recognition
    • Karjalainen K. High sensitivity, low affinity - paradox of T-cell receptor recognition. Curr. Opin. Immunol. 6:1994;9-12.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 9-12
    • Karjalainen, K.1
  • 4
    • 0028078572 scopus 로고
    • Virus receptors: Binding, adhesion strengthening, and changes in viral structure
    • Haywood A.M. Virus receptors: binding, adhesion strengthening, and changes in viral structure. J. Virol. 68:1994;1-5.
    • (1994) J. Virol. , vol.68 , pp. 1-5
    • Haywood, A.M.1
  • 5
    • 0030679644 scopus 로고    scopus 로고
    • Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity
    • Dustin M.L.et al. Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity. J. Biol. Chem. 272:1997;30889-30898.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30889-30898
    • Dustin, M.L.1
  • 6
    • 0029013298 scopus 로고
    • The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer
    • Reilly P.L.et al. The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. J. Immunol. 155:1995;529-532.
    • (1995) J. Immunol. , vol.155 , pp. 529-532
    • Reilly, P.L.1
  • 7
    • 0027313133 scopus 로고
    • Structure and function of sphingoglycolipids in transmembrane signaling and cell-cell interactions
    • Hakomori S.-I. Structure and function of sphingoglycolipids in transmembrane signaling and cell-cell interactions. Biochem. Soc. Trans. 21:1993;583-595.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 583-595
    • Hakomori, S.-I.1
  • 8
    • 0026160606 scopus 로고
    • Affinity capture of Arg8-Vasopressin-receptor using immobilized antisense peptide
    • Lu F.X.et al. Affinity capture of Arg8-Vasopressin-receptor using immobilized antisense peptide. Proc. Natl. Acad. Sci. U. S. A. 88:1991;3637-3641.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3637-3641
    • Lu, F.X.1
  • 9
    • 0030224808 scopus 로고    scopus 로고
    • Peptides as affinity surfaces for protein purification
    • Pingali A.et al. Peptides as affinity surfaces for protein purification. J. Mol. Recog. 9:1996;426-432.
    • (1996) J. Mol. Recog. , vol.9 , pp. 426-432
    • Pingali, A.1
  • 10
    • 77956916522 scopus 로고    scopus 로고
    • Weak affinity chromatography
    • P. et al. Bailon. Humana Press. (in press)
    • Strandh M.et al. Weak affinity chromatography. Bailon P.et al. Affinity Chromatography: Methods and Protocols. 2000;Humana Press. (in press).
    • (2000) Affinity Chromatography: Methods and Protocols
    • Strandh, M.1
  • 11
    • 0002665096 scopus 로고
    • Weak-affinity chromatography
    • Zopf D., Ohlson S. Weak-affinity chromatography. Nature. 346:1990;87-88.
    • (1990) Nature , vol.346 , pp. 87-88
    • Zopf, D.1    Ohlson, S.2
  • 12
    • 0023872902 scopus 로고
    • Novel approach to affinity chromatography using 'weak' monoclonal antibodies
    • Ohlson S.et al. Novel approach to affinity chromatography using 'weak' monoclonal antibodies. Anal. Biochem. 169:1988;204-208.
    • (1988) Anal. Biochem. , vol.169 , pp. 204-208
    • Ohlson, S.1
  • 13
    • 0031910838 scopus 로고    scopus 로고
    • Exploitation of a monoclonal antibody for weak affinity-based separation in capillary gel electrophoresis
    • Ljungberg H.et al. Exploitation of a monoclonal antibody for weak affinity-based separation in capillary gel electrophoresis. Electrophoresis. 19:1997;461-464.
    • (1997) Electrophoresis , vol.19 , pp. 461-464
    • Ljungberg, H.1
  • 14
    • 0030007515 scopus 로고    scopus 로고
    • Low affinity, antibody binding of an Escherichia coli-derived component
    • Ohlin M., Borrebaeck C.A.K. Low affinity, antibody binding of an Escherichia coli-derived component. FEMS Immunol. Med. Microbiol. 13:1996;161-168.
    • (1996) FEMS Immunol. Med. Microbiol. , vol.13 , pp. 161-168
    • Ohlin, M.1    Borrebaeck, C.A.K.2
  • 15
    • 0031975762 scopus 로고    scopus 로고
    • Affinity and kinetic analysis of l-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1
    • Nicholson M.W.et al. Affinity and kinetic analysis of l-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1. J. Biol. Chem. 273:1998;763-770.
    • (1998) J. Biol. Chem. , vol.273 , pp. 763-770
    • Nicholson, M.W.1
  • 16
    • 0032456502 scopus 로고    scopus 로고
    • Studies of interactions with weak affinities and low molecular weight compounds using surface plasmon resonance technology
    • Strandh M.et al. Studies of interactions with weak affinities and low molecular weight compounds using surface plasmon resonance technology. J. Mol. Recog. 11:1998;188-190.
    • (1998) J. Mol. Recog. , vol.11 , pp. 188-190
    • Strandh, M.1
  • 17
    • 0032556246 scopus 로고    scopus 로고
    • Probing low affinity and multivalent interactions with surface plasmon resonance: Ligands for concanavalin
    • Mann D.A.et al. Probing low affinity and multivalent interactions with surface plasmon resonance: ligands for concanavalin. J. Am. Chem. Soc. 120:1998;10575-10582.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10575-10582
    • Mann, D.A.1
  • 18
    • 0032123275 scopus 로고    scopus 로고
    • From absolute to exquisite specificity. Reflections on the fuzzy nature of species, specificity and antigenic sites
    • van Regenmortel M.H. From absolute to exquisite specificity. Reflections on the fuzzy nature of species, specificity and antigenic sites. J. Immunol. Methods. 216:1998;37-48.
    • (1998) J. Immunol. Methods , vol.216 , pp. 37-48
    • Van Regenmortel, M.H.1
  • 20
    • 0027916175 scopus 로고
    • Biospecific interaction analysis using biosensor technology
    • Malmqvist M. Biospecific interaction analysis using biosensor technology. Nature. 361:1993;186-187.
    • (1993) Nature , vol.361 , pp. 186-187
    • Malmqvist, M.1
  • 21
    • 0026551323 scopus 로고
    • Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis
    • Fägerstam L.G.et al. Biospecific interaction analysis using surface plasmon resonance detection applied to kinetic, binding site and concentration analysis. J. Chromatogr. 597:1992;397-410.
    • (1992) J. Chromatogr. , vol.597 , pp. 397-410
    • Fägerstam, L.G.1
  • 22
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson B.et al. Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198:1991;268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1
  • 23
    • 0021239430 scopus 로고
    • Radioimmunoassay of a glucose-containing tetrasaccharide using a monoclonal antibody
    • Lundblad A.et al. Radioimmunoassay of a glucose-containing tetrasaccharide using a monoclonal antibody. J. Immunol. Methods. 68:1984;217-226.
    • (1984) J. Immunol. Methods. , vol.68 , pp. 217-226
    • Lundblad, A.1
  • 24
    • 0342538938 scopus 로고    scopus 로고
    • Detection and characterization of oligosaccharides in column effluents using surface plasmon resonance
    • Blikstad I.et al. Detection and characterization of oligosaccharides in column effluents using surface plasmon resonance. Anal. Biochem. 233:1996;42-49.
    • (1996) Anal. Biochem. , vol.233 , pp. 42-49
    • Blikstad, I.1
  • 25
    • 0032401843 scopus 로고    scopus 로고
    • Determination of binding constants by equilibrium titration with circulating sample in a surface plasmon resonance biosensor
    • Schuck P.et al. Determination of binding constants by equilibrium titration with circulating sample in a surface plasmon resonance biosensor. Anal. Biochem. 265:1998;79-91.
    • (1998) Anal. Biochem. , vol.265 , pp. 79-91
    • Schuck, P.1
  • 26
    • 0032535149 scopus 로고    scopus 로고
    • Equilibrium analysis of high affinity interactions using BIACORE
    • Myszka D.G.et al. Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 265:1998;326-330.
    • (1998) Anal. Biochem. , vol.265 , pp. 326-330
    • Myszka, D.G.1
  • 27
    • 0031733261 scopus 로고    scopus 로고
    • Affinity screening for weak monoclonal antibodies
    • Leickt L.et al. Affinity screening for weak monoclonal antibodies. J. Immunol. Methods. 220:1998;19-23.
    • (1998) J. Immunol. Methods , vol.220 , pp. 19-23
    • Leickt, L.1
  • 28
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to single epitope of an antigen
    • Jespers L.S.et al. Guiding the selection of human antibodies from phage display repertoires to single epitope of an antigen. Biotechnology. 12:1994;899-903.
    • (1994) Biotechnology , vol.12 , pp. 899-903
    • Jespers, L.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.