Structural features of T cell receptor variable regions that enhance domain stability and enable expression as single-chain ValphaVbeta fragments
about
Periplasmic expression of soluble single chain T cell receptors is rescued by the chaperone FkpA.Identification of multiple public TCR repertoires in chronic beryllium disease.Stabilizing mutations increase secretion of functional soluble TCR-Ig fusion proteins.Diversity-oriented approaches for interrogating T-cell receptor repertoire, ligand recognition, and functionChaperone-assisted thermostability engineering of a soluble T cell receptor using phage display.Identification and engineering of human variable regions that allow expression of stable single-chain T cell receptors.A novel T cell receptor single-chain signaling complex mediates antigen-specific T cell activity and tumor controlT Cell Receptor Engineering and Analysis Using the Yeast Display Platform.Increased Fab thermoresistance via VH-targeted directed evolution.An optimized single chain TCR scaffold relying on the assembly with the native CD3-complex prevents residual mispairing with endogenous TCRs in human T-cells.Characterization of the Staphylococcal enterotoxin A: Vβ receptor interaction using human receptor fragments engineered for high affinitySoluble T cell receptor Vβ domains engineered for high-affinity binding to staphylococcal or streptococcal superantigensTumor-targeting domains for chimeric antigen receptor T cells.Single-chain VαVβ T-cell receptors function without mispairing with endogenous TCR chains.A TCRα framework-centered codon shapes a biased T cell repertoire through direct MHC and CDR3β interactions.Protein design of IgG/TCR chimeras for the co-expression of Fab-like moieties within bispecific antibodies.Changing the peptide specificity of a human T-cell receptor by directed evolution.Subtle changes at the variable domain interface of the T-cell receptor can strongly increase affinity.Comparison of T Cell Activities Mediated by Human TCRs and CARs That Use the Same Recognition Domains.Soluble T-cell receptor design influences functional yield in an E. coli chaperone-assisted expression system.Engineering of recombinant human Fcγ receptor I by directed evolution.
P2860
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P2860
Structural features of T cell receptor variable regions that enhance domain stability and enable expression as single-chain ValphaVbeta fragments
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Structural features of T cell ...... le-chain ValphaVbeta fragments
@en
type
label
Structural features of T cell ...... le-chain ValphaVbeta fragments
@en
prefLabel
Structural features of T cell ...... le-chain ValphaVbeta fragments
@en
P2093
P2860
P1433
P1476
Structural features of T cell ...... le-chain ValphaVbeta fragments
@en
P2093
David L Donermeyer
David M Kranz
Michelle L Dossett
Paul M Allen
Philip D Greenberg
Sarah A Richman
P2860
P304
P356
10.1016/J.MOLIMM.2008.09.021
P577
2008-10-29T00:00:00Z