A recombinant immunotoxin containing a disulfide-stabilized Fv fragment. - Wikidata - wikimedia - TriplyDB

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

http://www.wikidata.org/entity/Q36476431

about

Making artificial antibodies: a format for phage display of combinatorial heterodimeric arrays The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi Engineered hapten-binding antibody derivatives for modulation of pharmacokinetic properties of small molecules and targeted payload delivery Novel immunotherapies in lymphoid malignancies Listeriolysin O as cytotoxic component of an immunotoxin In vitro antibody evolution targeting germline hot spots to increase activity of an anti-CD22 immunotoxin.Production of unique immunotoxin cancer therapeutics in algal chloroplasts A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity.Delivery and therapeutic potential of human granzyme B.Recombinant immunotoxins for cancer therapy.Intrathecal administration of single-chain immunotoxin, LMB-7 [B3(Fv)-PE38], produces cures of carcinomatous meningitis in a rat model SV40 Pseudovirion gene delivery of a toxin to treat human adenocarcinomas in mice.Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments A guide to taming a toxin--recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer.Disulfide-stabilized single-chain antibody-targeted superantigen: construction of a prokaryotic expression system and its functional analysis.Antibody fusion proteins: anti-CD22 recombinant immunotoxin moxetumomab pasudotox Rapid humanization of the Fv of monoclonal antibody B3 by using framework exchange of the recombinant immunotoxin B3(Fv)-PE38.Fab-based bispecific antibody formats with robust biophysical properties and biological activity Remodeling domain interfaces to enhance heterodimer formation Expression cloning of cDNAs that render cancer cells resistant to Pseudomonas and diphtheria toxin and immunotoxins.Fungal ribotoxins: molecular dissection of a family of natural killers.The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6.A combinatorial library strategy for the rapid humanization of anticarcinoma BR96 Fab.Comparison of strategies for the construction of libraries of artificial antibodies.Immunotoxins: the role of the toxin.Construction of a disulfide-stabilized diabody against fibroblast growth factor-2 and the inhibition activity in targeting breast cancer.Fab-dsFv: A bispecific antibody format with extended serum half-life through albumin binding.Improved antitumor activity of a recombinant anti-Lewis(y) immunotoxin not requiring proteolytic activation.Inhibition activity of a disulfide-stabilized diabody against basic fibroblast growth factor in lung cancer.Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae.Potential applications of designed ankyrin repeat proteins in diagnostics and therapeutics.Identification of residues that stabilize the single-chain Fv of monoclonal antibodies B3.The future of antiviral immunotoxins.Fluorescent Citrine-IgG fusion proteins produced in mammalian cells.Killing of target cells by redirected granzyme B in the absence of perforin.Targeting of T lymphocytes to melanoma cells through chimeric anti-GD3 immunoglobulin T-cell receptors.Conjugation of an antibody Fv fragment to a virus coat protein: cell-specific targeting of recombinant polyoma-virus-like particles Design, characterization and anti-tumour cytotoxicity of a panel of recombinant, mammalian ribonuclease-based immunotoxins.The making of bispecific antibodies Bioinformatics in molecular immunology laboratories demonstrated: Modeling an anti-CMV scFv antibody.

P2860

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P2860

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

http://www.wikidata.org/entity/Q36476431

description

1993 nî lūn-bûn

@nan

1993年の論文

@ja

1993年学术文章

@wuu

1993年学术文章

@zh-cn

1993年学术文章

@zh-hans

1993年学术文章

@zh-my

1993年学术文章

@zh-sg

1993年學術文章

@yue

1993年學術文章

@zh

1993年學術文章

@zh-hant

name

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@ast

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@en

type

label

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@ast

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@en

prefLabel

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@ast

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@en

P1433

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P2860

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P932

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P356

PNAS.90.16.7538

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

A recombinant immunotoxin containing a disulfide-stabilized Fv fragment.

@en

P2093

Brinkmann U

http://www.w3.org/2001/XMLSchema#string

Jung SH

http://www.w3.org/2001/XMLSchema#string

Lee B

http://www.w3.org/2001/XMLSchema#string

Pastan I

http://www.w3.org/2001/XMLSchema#string

Reiter Y

http://www.w3.org/2001/XMLSchema#string

P2860

A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals

Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A

Rapid and efficient site-specific mutagenesis without phenotypic selection

Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli

Recombinant toxins for cancer treatment.

Selection of an active single chain Fv antibody from a protein linker library prepared by enzymatic inverse PCR.

Recombinant anti-erbB2 immunotoxins containing Pseudomonas exotoxin

Anti-tumor activities of immunotoxins made of monoclonal antibody B3 and various forms of Pseudomonas exotoxin.

B3(Fv)-PE38KDEL, a single-chain immunotoxin that causes complete regression of a human carcinoma in mice.

A rapid method of cloning functional variable-region antibody genes in Escherichia coli as single-chain immunotoxins.

P304

7538-7542

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scholarly article

P356

10.1073/PNAS.90.16.7538

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P407

P433

16

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P478

90

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P577

1993-08-01T00:00:00Z

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P5875

14843354

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P698

8356052

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P932

47177

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