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Volumn 8, Issue 4, 1998, Pages 443-450

Antibody engineering

Author keywords

[No Author keywords available]

Indexed keywords

BISPECIFIC ANTIBODY;

EID: 0032143550     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80121-8     Document Type: Article
Times cited : (87)

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    • Ryabova LA, Desplancq D, Spirin AS, Plückthun A. Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. of special interest Nat Biotechnol. 15:1997;79-84 A thorough study describing the optimization of the production of functional scFv molecules by in vitro transcription and translation.
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    • Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist scFv
    • d < 10 nM). This is a rapid and perhaps general route for generating highly specific agonist antibodies.
    • d < 10 nM). This is a rapid and perhaps general route for generating highly specific agonist antibodies.
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    • Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies
    • of outstanding interest. Tumor targeting was undertaken using scFv molecules with varying affinities (320 to 1 nM) for the tumor-associated antigen HER2/neu. The extent and specificity of tumor localization was greatly improved by increasing the antigen-binding affinity.
    • Adams GP, Schier R, Marshall K, Wolf EJ, McCall AM, Marks JD, Weiner LM. Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies. of outstanding interest Cancer Res. 58:1998;485-490 Tumor targeting was undertaken using scFv molecules with varying affinities (320 to 1 nM) for the tumor-associated antigen HER2/neu. The extent and specificity of tumor localization was greatly improved by increasing the antigen-binding affinity.
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    • Targeting by affinity-matured recombinant antibody fragments of an angiogenesis associated fibronectin isoform
    • of outstanding interest. The targeting of a scFv molecule to the tumor neovasculature-associated antigen oncofetal fibronectin was greatly improved using both affinity-matured and dimeric fragments. Imaging in real time was possible by IR photodetection using a fluorophore that was chemically coupled to the antibody fragment.
    • Neri D, Carnemolla B, Nissim A, Leprini A, Querze G, Balza E, Pini A, Tarli L, Halin C, Neri P, et al. Targeting by affinity-matured recombinant antibody fragments of an angiogenesis associated fibronectin isoform. of outstanding interest Nat Biotechnol. 15:1997;1271-1275 The targeting of a scFv molecule to the tumor neovasculature-associated antigen oncofetal fibronectin was greatly improved using both affinity-matured and dimeric fragments. Imaging in real time was possible by IR photodetection using a fluorophore that was chemically coupled to the antibody fragment.
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    • Neri, D.1    Carnemolla, B.2    Nissim, A.3    Leprini, A.4    Querze, G.5    Balza, E.6    Pini, A.7    Tarli, L.8    Halin, C.9    Neri, P.10
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    • Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology
    • of special interest. A small and well-characterized library was used for the evaluation of the phage display technology SIP. This method apparently selects for many properties of the displayed molecule, including folding, stability and affinity.
    • Pedrazzi G, Schwesinger F, Honneger A, Krebber C, Plückthun A. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. of special interest FEBS Lett. 415:1997;289-293 A small and well-characterized library was used for the evaluation of the phage display technology SIP. This method apparently selects for many properties of the displayed molecule, including folding, stability and affinity.
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    • Selective phage infection mediated by epitope expression on F pilus
    • of special interest. Genetically fusing a peptide to pilin prevents the infection of E. coli by wild-type M13 phages. Infection can be selectively restored by displaying on the phage a specific scFv that is capable of interacting with the pilin-peptide fusion. This work directly provides a foundation for identifying anti-peptide antibodies from scFv libraries.
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    • In vitro selection and evolution of functional proteins by using ribosome display
    • of outstanding interest. This is the first successful demonstration of ribosome display technology using proteins. This method, together with that in [68], is anticipated be generally useful for the identification and molecular evolution of proteins or peptides that bind targets of interest.
    • Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. of outstanding interest Proc Natl Acad Sci USA. 94:1997;4937-4942 This is the first successful demonstration of ribosome display technology using proteins. This method, together with that in [68], is anticipated be generally useful for the identification and molecular evolution of proteins or peptides that bind targets of interest.
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    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
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    • 5-fold were obtained in a single cycle.
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    • An efficient route to human bispecific IgG
    • of outstanding interest. The production of human bispecific IgG (BsIgG) by co-expressing two different antibodies is inefficient due to unwanted pairings of the component heavy and light chains. A broadly applicable method was developed that overcomes these problems, enabling near quantitative formation and efficient recovery of human BsIgG. This technology substantially expands the clinical potential of human BsIgG.
    • Merchant AM, Zhu Z, Yuan JQ, Goddard A, Adams CW, Presta LG, Carter P. An efficient route to human bispecific IgG. of outstanding interest Nat Biotechnol. 16:1998;677-681 The production of human bispecific IgG (BsIgG) by co-expressing two different antibodies is inefficient due to unwanted pairings of the component heavy and light chains. A broadly applicable method was developed that overcomes these problems, enabling near quantitative formation and efficient recovery of human BsIgG. This technology substantially expands the clinical potential of human BsIgG.
    • (1998) Nat Biotechnol , vol.16 , pp. 677-681
    • Merchant, A.M.1    Zhu, Z.2    Yuan, J.Q.3    Goddard, A.4    Adams, C.W.5    Presta, L.G.6    Carter, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.