Transmembrane helical interactions: zeta chain dimerization and functional association with the T cell antigen receptor.
about
The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptorOrchestration of secretory protein folding by ER chaperonesStudies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyl transferase.Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complexStructural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling.Mutations in or near the transmembrane domain alter PMEL amyloid formation from functional to pathogenicThe organizing principle in the formation of the T cell receptor-CD3 complex.Identification of a juxtamembrane mechanosensitive domain in the platelet mechanosensor glycoprotein Ib-IX complex.A conserved cysteine residue of Bacillus subtilis SpoIIIJ is important for endospore developmentMolecular mechanisms for the assembly of the T cell receptor-CD3 complex.Structural characteristics of zebrafish orthologs of adaptor molecules that associate with transmembrane immune receptors.Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine-containing sequenceProtein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable componentsConvergence on a distinctive assembly mechanism by unrelated families of activating immune receptors.A lysosomal targeting signal in the cytoplasmic tail of the beta chain directs HLA-DM to MHC class II compartments.Essential and partially overlapping role of CD3gamma and CD3delta for development of alphabeta and gammadelta T lymphocytesSingle-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Diverse mechanisms regulate the surface expression of immunotherapeutic target ctla-4.Membrane insertion of the bacterial signal transduction protein ToxR and requirements of transcription activation studied by modular replacement of different protein substructures.Ceramide synthesis enhances transport of GPI-anchored proteins to the Golgi apparatus in yeast.Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1.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.The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane.Widespread intronic polyadenylation diversifies immune cell transcriptomes.
P2860
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P2860
Transmembrane helical interactions: zeta chain dimerization and functional association with the T cell antigen receptor.
description
1992 nî lūn-bûn
@nan
1992 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Transmembrane helical interact ...... h the T cell antigen receptor.
@ast
Transmembrane helical interact ...... h the T cell antigen receptor.
@en
type
label
Transmembrane helical interact ...... h the T cell antigen receptor.
@ast
Transmembrane helical interact ...... h the T cell antigen receptor.
@en
prefLabel
Transmembrane helical interact ...... h the T cell antigen receptor.
@ast
Transmembrane helical interact ...... h the T cell antigen receptor.
@en
P2093
P2860
P1433
P1476
Transmembrane helical interact ...... th the T cell antigen receptor
@en
P2093
Bonifacino JS
Klausner RD
Manolios N
Rutledge T
P2860
P304
P356
10.1002/J.1460-2075.1992.TB05402.X
P407
P577
1992-09-01T00:00:00Z