Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains.
about
Evolutionary relationship between the T3 chains of the T-cell receptor complex and the immunoglobulin supergene familyEvolution of immunoglobulin light chains: cDNA clones specifying sandbar shark constant regionsAtomic structure of an alphabeta T cell receptor (TCR) heterodimer in complex with an anti-TCR fab fragment derived from a mitogenic antibody.Resolution of hypervariable regions in T-cell receptor beta chains by a modified Wu-Kabat index of amino acid diversity.Molecular analysis of the helper T cell response in murine interstitial nephritis. T cells recognizing an immunodominant epitope use multiple T cell receptor V beta genes with similarities across CDR3.T-cell antigen receptors with identical variable regions but different diversity and joining region gene segments have distinct specificities but cross-reactive idiotypes.Gaucher disease: molecular heterogeneity and phenotype-genotype correlations.Binding of soluble natural ligands to a soluble human T-cell receptor fragment produced in Escherichia coli.Preferential V beta gene usage and lack of junctional sequence conservation among human T cell receptors specific for a tetanus toxin-derived peptide: evidence for a dominant role of a germline-encoded V region in antigen/major histocompatibility coFunctional analysis of the antigen binding site on the T cell receptor alpha chainA bacterially expressed single-chain Fv construct from the 2B4 T-cell receptor.Molecular modeling of a T-cell receptor bound to a major histocompatibility complex molecule: implications for T-cell recognition.The sizes of the CDR3 hypervariable regions of the murine T-cell receptor beta chains vary as a function of the recombined germ-line segments.Allelic variations in the human T cell receptor V beta 6.7 gene products.T cell receptor gene usage in the response to lambda repressor cI protein. An apparent bias in the usage of a V alpha gene elementChanges at peptide residues buried in the major histocompatibility complex (MHC) class I binding cleft influence T cell recognition: a possible role for indirect conformational alterations in the MHC class I or bound peptide in determining T cell reInfluence of the NH2-terminal amino acid of the T cell receptor alpha chain on major histocompatibility complex (MHC) class II + peptide recognition.Conserved structure of amphibian T-cell antigen receptor beta chain.Characterization of a single-chain T-cell receptor expressed in Escherichia coliSimilarity between fluorescein-specific T-cell receptor and antibody in chemical details of antigen recognition.A soluble, single-chain T-cell receptor fragment endowed with antigen-combining properties.Profound alteration in an alpha beta T-cell antigen receptor repertoire due to polymorphism in the first complementarity-determining region of the beta chainA static accessibility model of protein antigenicity.Conservation of immunoglobulin variable and joining region structure and the design of universal anti-immunoglobulin antibodies reactive with antigen-binding T cell receptors.Predicted complementarity determining regions of the T cell antigen receptor determine antigen specificity.The outline structure of the T-cell alpha beta receptor.The V beta complementarity determining region 1 of a major histocompatibility complex (MHC) class I-restricted T cell receptor is involved in the recognition of peptide/MHC I and superantigen/MHC II complex.CDR3 length in antigen-specific immune receptorsTCR Mechanobiology: Torques and Tunable Structures Linked to Early T Cell Signaling.Complementary DNA sequences of the constant regions of T-cell antigen receptors α, β and γ in mandarin fish, Siniperca chuatsi Basilewsky, and their transcriptional changes after stimulation with Flavobacterium columnare.Conformational integrity and ligand binding properties of a single chain T-cell receptor expressed in Escherichia coli.Production of the constant domain of murine T-cell receptor beta-chain in Escherichia coli.
P2860
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P2860
Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@ast
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@en
type
label
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@ast
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@en
prefLabel
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@ast
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@en
P2093
P2860
P356
P1476
Secondary, tertiary, and quate ...... bulin-like polypeptide chains.
@en
P2093
P2860
P304
P356
10.1073/PNAS.83.3.742
P407
P577
1986-02-01T00:00:00Z