Rapid evolution of peptide and protein binding properties in vitro
Identifieur interne : 001D36 ( Istex/Checkpoint ); précédent : 001D35; suivant : 001D37Rapid evolution of peptide and protein binding properties in vitro
Auteurs : James A. Wells [États-Unis] ; Henry B. Lowman [États-Unis]Source :
- Current Opinion in Structural Biology [ 0959-440X ] ; 1992.
English descriptors
- Teeft :
- Acad, Affinity, Alkaline phosphatase, Amino, Amino acids, Amino terminus, Antibody, Avidity effects, Bacterial cells, Bacteriophage, Binder, Binding affinity, Binding constants, Binding properties, Binding selection, Carboxyl terminus, Catalytic antibodies, Chain reaction, Circumsporozoite protein, Clone, Codon, Coli, Consensus sequence, Coworkers, Current opinion, Different light chains, Different peptides, Drug design, Epitope, Epitope mapping, Escherichia coli, Filamentous, Filamentous bacteriophage, Filamentous phage, Free peptides, Fusion protein, Gene, Gene viii, Glass slide, Heavy chain, Helper phage, Higher affinity, Human growth hormone, Immunosorbent assay, Independent transformants, Ligand, Light chains, Lowman, Mature gene, Moderate affinity, Monoclonal antibodies, Monoclonal antibody, Monovalent, Monovalent display, Monovalent phage display, Multiple copies, Mutagenesis, Mutant, Natl, Neutrophil elastase, Nucleic acids, Peptide, Peptide libraries, Phage, Phage display, Phage surfaces, Phagemid, Phagemid particles, Phagemid particles display, Phosphatase, Point attachment, Polyvalent, Polyvalent display, Polyvalent fashion, Polyvalent phage, Polyvalent phage display, Possible protein sequences, Proc, Proc natl acad, Protein binding properties, Protein engineering, Random libraries, Random mutagenesis, Rapid evolution, Receptor, Second antibody, Soluble protein, Specific binding, Target protein, Terminus, Tetanus toxoid, Variant, Variant proteins.
Abstract
Abstract: A significant bottleneck in protein engineering arises from the problem of identifying particular molecules with new function from a potentially enormous range of peptide or protein variants. Two areas of emerging technology, phage display and multiple peptide synthesis provide new means of screening huge libraries in vitro for novel binding properties. This review is also published in Current Opinion in Biotechnology 1992, 3:355–362.
Url:
DOI: 10.1016/0959-440X(92)90092-L
Affiliations:
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Lowman</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:FB4F4C2B938233F34CDCD0CB5223A54102BA258D</idno><date when="1992" year="1992">1992</date><idno type="doi">10.1016/0959-440X(92)90092-L</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-HK2RN9ML-3/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001F96</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001F96</idno><idno type="wicri:Area/Istex/Curation">001F96</idno><idno type="wicri:Area/Istex/Checkpoint">001D36</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001D36</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Rapid evolution of peptide and protein binding properties in vitro</title><author><name sortKey="Wells, James A" sort="Wells, James A" uniqKey="Wells J" first="James A." last="Wells">James A. Wells</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>JA Wells and HB Lowman, Department of Protein Engineering, Genentech Inc, 460 Pt San Bruno Blvd, South San Francisco, California 94080</wicri:regionArea><wicri:noRegion>California 94080</wicri:noRegion></affiliation></author><author><name sortKey="Lowman, Henry B" sort="Lowman, Henry B" uniqKey="Lowman H" first="Henry B." last="Lowman">Henry B. Lowman</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>JA Wells and HB Lowman, Department of Protein Engineering, Genentech Inc, 460 Pt San Bruno Blvd, South San Francisco, California 94080</wicri:regionArea><wicri:noRegion>California 94080</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Current Opinion in Structural Biology</title><title level="j" type="abbrev">COSTBI</title><idno type="ISSN">0959-440X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">2</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="597">597</biblScope><biblScope unit="page" to="604">604</biblScope></imprint><idno type="ISSN">0959-440X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0959-440X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Affinity</term><term>Alkaline phosphatase</term><term>Amino</term><term>Amino acids</term><term>Amino terminus</term><term>Antibody</term><term>Avidity effects</term><term>Bacterial cells</term><term>Bacteriophage</term><term>Binder</term><term>Binding affinity</term><term>Binding constants</term><term>Binding properties</term><term>Binding selection</term><term>Carboxyl terminus</term><term>Catalytic antibodies</term><term>Chain reaction</term><term>Circumsporozoite protein</term><term>Clone</term><term>Codon</term><term>Coli</term><term>Consensus sequence</term><term>Coworkers</term><term>Current opinion</term><term>Different light chains</term><term>Different peptides</term><term>Drug design</term><term>Epitope</term><term>Epitope mapping</term><term>Escherichia coli</term><term>Filamentous</term><term>Filamentous bacteriophage</term><term>Filamentous phage</term><term>Free peptides</term><term>Fusion protein</term><term>Gene</term><term>Gene viii</term><term>Glass slide</term><term>Heavy chain</term><term>Helper phage</term><term>Higher affinity</term><term>Human growth hormone</term><term>Immunosorbent assay</term><term>Independent transformants</term><term>Ligand</term><term>Light chains</term><term>Lowman</term><term>Mature gene</term><term>Moderate affinity</term><term>Monoclonal antibodies</term><term>Monoclonal antibody</term><term>Monovalent</term><term>Monovalent display</term><term>Monovalent phage display</term><term>Multiple copies</term><term>Mutagenesis</term><term>Mutant</term><term>Natl</term><term>Neutrophil elastase</term><term>Nucleic acids</term><term>Peptide</term><term>Peptide libraries</term><term>Phage</term><term>Phage display</term><term>Phage surfaces</term><term>Phagemid</term><term>Phagemid particles</term><term>Phagemid particles display</term><term>Phosphatase</term><term>Point attachment</term><term>Polyvalent</term><term>Polyvalent display</term><term>Polyvalent fashion</term><term>Polyvalent phage</term><term>Polyvalent phage display</term><term>Possible protein sequences</term><term>Proc</term><term>Proc natl acad</term><term>Protein binding properties</term><term>Protein engineering</term><term>Random libraries</term><term>Random mutagenesis</term><term>Rapid evolution</term><term>Receptor</term><term>Second antibody</term><term>Soluble protein</term><term>Specific binding</term><term>Target protein</term><term>Terminus</term><term>Tetanus toxoid</term><term>Variant</term><term>Variant proteins</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A significant bottleneck in protein engineering arises from the problem of identifying particular molecules with new function from a potentially enormous range of peptide or protein variants. Two areas of emerging technology, phage display and multiple peptide synthesis provide new means of screening huge libraries in vitro for novel binding properties. This review is also published in Current Opinion in Biotechnology 1992, 3:355–362.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Wells, James A" sort="Wells, James A" uniqKey="Wells J" first="James A." last="Wells">James A. Wells</name></noRegion><name sortKey="Lowman, Henry B" sort="Lowman, Henry B" uniqKey="Lowman H" first="Henry B." last="Lowman">Henry B. Lowman</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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