About: Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy

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About: Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 1993

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1993 (uk) article scientifique publié en 1993 (fr) im April 1993 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 1993 (ast) scientific article published on 01 April 1993 (en)
publication date	wds:Q57840153-EDCAF5FA-B67F-4B1F-BE9D-C3ADB67396CA
publication date	1993-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57840153-87D15E48-140C-4F36-9830-4001E518FB1C
language of work or name	English
cites work	wds:Q57840153-06EBEE5C-2E28-4952-AB97-BBCE2C83013F wds:Q57840153-0915F09C-C1C5-4DCB-8D38-7E14E0C4AD58 wds:Q57840153-12755E4A-7E1A-4977-A891-A70DA3FABD4A wds:Q57840153-1C7EEFCA-F30C-4534-BE75-C501024BFA07 wds:Q57840153-439312F5-8B30-497F-A7D9-F34A8DC22915 wds:Q57840153-6617D28A-7C38-4DDE-A106-B037A1C8CDFA wds:Q57840153-6F83DAAB-BFBF-49F1-A300-8FB0D1CD138F wds:Q57840153-7032351B-A128-4240-A1FD-F1EB590AB60D wds:Q57840153-91349CF9-A875-442F-B5A3-A8AE380F5727 wds:Q57840153-972FF362-054D-4C8D-9B6D-46556FBC4345 wds:Q57840153-AC1F068C-78EB-48B6-8482-8B4A43A2E211 wds:Q57840153-EF6B4ECE-FD39-473F-AE5C-4B51F53029D9 wds:Q57840153-F8B7A96A-2E52-488A-B55E-A3F7C5D1961B wds:Q57840153-FAB04DBC-FD46-4D34-B85C-38B7D21D7093
cites work	Use of T7 RNA polymerase to direct expression of cloned genes Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli Escherichia coli secretion of an active chimeric antibody fragment. Single-chain antigen-binding proteins Relationship between nuclear magnetic resonance chemical shift and protein secondary structure A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli 15N-labeled P22 c2 repressor for nuclear magnetic resonance studies of protein-DNA interactions. The Effect of Folding Catalysts on the In Vivo Folding Process of Different Antibody Fragments Expressed in Escherichia coli Assembly of a functional immunoglobulin Fv fragment in Escherichia coli A comparison of strategies to stabilize immunoglobulin Fv-fragments The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique. Affinity labeling of a phosphorylcholine binding mouse myeloma protein Magnesium ion-independent ribonucleic acid depolymerases in bacteria
author name string	wds:Q57840153-1401A93C-7C20-4F3A-9093-3DE6514AE29E wds:Q57840153-1E15D46D-4F10-4E6C-A720-5D819853E5E8 wds:Q57840153-5621ADC7-C568-497F-8E7E-DA8BA74DC362 wds:Q57840153-B746990A-FD3B-478B-8200-A9FFB1DB8FBD
author name string	A Ross T A Holak C Freund B Guth
rdfs:label	Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (en) Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (nl)
skos:prefLabel	Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (en) Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (nl)
name	Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (en) Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (nl)
author	wds:Q57840153-12DDE61A-6388-4858-B589-A0DB4617C316
author	Andreas Plückthun
title	wds:Q57840153-9DFD6702-897E-4E60-BA9E-15CDCAADC999
title	Characterization of the linker peptide of the single-chain Fv fragment of an antibody by NMR spectroscopy (en)
page(s)	wds:Q57840153-ADFF0F0F-5DC6-4E4E-8988-CB5C5B3AD743
page(s)	97-100
instance of	wds:Q57840153-DCBBD9B6-CB66-4696-AF06-90986EB81137
instance of	scholarly article
main subject	wds:Q57840153-19C3AE4F-92A8-4B38-9F7A-2EA4276EDA33 wds:Q57840153-243C1801-646F-43FF-A879-A88A1C234DA3 wds:Q57840153-78FA7831-09EC-42FE-9C7E-24661A2A447E wds:Q57840153-93275995-E1AC-405E-A3C5-10D6435D50F5 wds:Q57840153-B4FDD558-B7FE-4E8F-88AF-1C179B796089 wds:Q57840153-D176FE41-5003-42F9-9898-164A511C465C wds:Q57840153-F26C5206-7B79-4B11-94BD-CBABF3758831
main subject	NMR spectroscopy spectroscopy antibody cell biology biophysics molecular biology structural biology
PubMed ID	wds:Q57840153-7E6D324A-DC11-4175-A445-DDEBAA0AD05C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8458438
PubMed ID	8458438
published in	wds:Q57840153-3B8244F1-D299-4A15-B05B-2838461D4023
published in	FEBS Letters
issue	wds:Q57840153-3F79137C-8A26-49E6-9FAF-F6D96A501CE5
volume	wds:Q57840153-0AB97FD8-3EC8-49D7-9E45-D6F8B826A25E
issue	2
volume	320
number of pages	wds:Q57840153-C7BABB18-2929-497E-8F41-2C638D86CCF6
number of pages	4 (xsd:decimal)
DOI	wds:Q57840153-DD9936C1-D105-4E42-A449-FD0F9D073A3D
DOI	http://dx.doi.org/10.1016/0014-5793(93)80070-B
DOI	10.1016/0014-5793(93)80070-B
describes a project that uses	wds:Q57840153-12967330-4535-4B63-B9EB-49B38DD6C7A3
describes a project that uses	NMR spectroscopy
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57840153
is cites work of	Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p Bacterial expression and refolding of single-chain Fv fragments with C-terminal cysteines. Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli. Cyclophilin A binds to linear peptide motifs containing a consensus that is present in many human proteins Reversible dimer formation and stability of the anti-tumour single-chain Fv antibody MFE-23 by neutron scattering, analytical ultracentrifugation, and NMR and FT-IR spectroscopy GYF domain proteomics reveals interaction sites in known and novel target proteins Quantitative analysis of fluorescent caspase substrate cleavage in intact cells and identification of novel inhibitors of apoptosis

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