Fluorescein

immunglobulin heavy chain variable region ; Homo sapiens







15 Article(s)
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Title
Pub. Year
#Total Relationships
1 32232139 Computational Design of an Allosteric Antibody Switch by Deletion and Rescue of a Complex Structural Constellation. 2020 Mar 25 1
2 29637646 Biophysical characterization and molecular simulation of electrostatically driven self-association of a single-chain antibody. 2018 Jul 1
3 29038485 A versatile pretargeting approach for tumour-selective delivery and activation of TNF superfamily members. 2017 Oct 16 1
4 24338724 A novel platform for antibody library selection in mammalian cells based on a growth signalobody. 2014 Jun 3
5 25072845 A bifunctional converter: fluorescein quenching scFv/fluorogen activating protein for photostability and improved signal to noise in fluorescence experiments. 2014 Aug 20 1
6 23350721 Tumor-targeting antibody-anticalin fusion proteins for in vivo pretargeting applications. 2013 Feb 20 2
7 19687511 Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity. 2009 Oct 29 1
8 18218715 Characterization of the 4D5Flu single-chain antibody with a stimulus-responsive elastin-like peptide linker: a potential reporter of peptide linker conformation. 2008 Mar 1
9 17012279 In vitro evolution of single-chain antibodies using mRNA display. 2006 1
10 16195542 Change of the unbinding mechanism upon a mutation: a molecular dynamics study of an antibody-hapten complex. 2005 Oct 2
11 16195545 A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex. 2005 Oct 2
12 15465055 Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. 2004 Oct 22 3
13 15504336 An antigen-mediated selection system for mammalian cells that produce glycosylated single-chain Fv. 2004 Nov 26 1
14 9636161 Antigen binding forces of individually addressed single-chain Fv antibody molecules. 1998 Jun 23 1
15 9171284 Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions. 1997 May 9 1