Article

Dramatic Activation of an Antibody by a Single Amino Acid Change in Framework

2021-09-07

Abstract excerpt

Antibody function is typically entirely dictated by the Complementarity Determining Regions (CDRs) that directly bind to the antigen, while the framework region acts as a scaffold for the CDRs and maintains overall structure of the variable domain. We recently reported that the rabbit monoclonal antibody 4A11 (rbt4A11) disrupts signaling through both TGFβ2 and TGFβ3 1 . Here, we report a dramatic, unexpected disco...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: ac032bf4-ddd7-5dcf-965c-609a8dd538c2
DOI: 10.21203/rs.3.rs-862975/v1

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Dramatic Activation of an Antibody by a Single Amino Acid Change in FrameworkDOI 10.21203/rs.3.rs-862975/v1Read

Natural and man-made V-gene repertoires for antibody discoverySemantic proximity Read

Computational Stabilization of the Human VH Germline Repertoire to Enable Conditional Multi-Specific Therapeutic DevelopmentSemantic proximity Read

Structure guided homology model based design and engineering of mouse antibodies for humanizationSemantic proximity Read

Diverse human VH antibody fragments with bio-therapeutic properties from the Crescendo MouseSemantic proximity Read

A Two-in-One antibody engineered from a humanized interleukin 4 antibody through mutation in heavy chain complementarity-determining regionsSemantic proximity Read

Humanization of the anti-CD18 antibody 6.7: an unexpected effect of a framework residue in binding to antigen.Semantic proximity Read

AI-assisted protein design to rapidly convert antibody sequences to intrabodies targeting diverse peptides and histone modificationsSemantic proximity Read

A universal combinatorial design of antibody framework to graft distinct CDR sequences: a bioinformatics approach.Semantic proximity Read

A single backmutation in the human kIV framework of a previously unsuccessfully humanized antibody restores the binding activity and increases the secretion in cos cells.Semantic proximity Read

<i>In silico</i> design of stable single-domain antibodies with high affinitySemantic proximity Read

Broadly Reactive Anti-VHH Antibodies for Characterizing, Blocking, or Activating Nanobody-Based CAR-T CellsSemantic proximity Read

Tuning antibody stability and function by rational designs of framework mutations.Semantic proximity Read