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T cells recognize peptides derived from antigen proteins bound to class II major histocompatibility complex molecules.
CD8+ T lymphocytes recognize tumor and viral antigens bound to class I major histocompatibility complexes (MHC).
Helper T cells express T cell receptors (TCR) that recognize antigen bound to Class II MHC molecules.
In this process, short peptide fragments derived from pathogens within the host cell are bound to class I receptor structures and transported to the cell surface.
The methodology was first tested on the complex of the human TCR HA1.7 specific for the hemagglutinin antigen peptide (HA) from influenza A virus bound to class II molecule HLA-DR4 (PDB code: 1j8h) [27].
Indeed, this finding is consistent with the observation that post-translational modifications of proteins only rarely contribute to the cognate T cell epitopes bound to class II MHC [15], [16], [17], perhaps because these modifications are removed in lysosomes.
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Some T cells recognize class I MHC molecules on the surface of cells; others bind to class II molecules.
Helper T cells display a coreceptor called CD4, which binds to class II MHC molecules, and cytotoxic T cells have on their surfaces the coreceptor CD8, which recognizes class I MHC molecules.
Beclin-1, a Bcl-2-interacting protein, also binds to class III PI3Ks and helps to regulate autophagy.
Therefore, it is fully possible that in vivo, OAA HDAC inhibitors only bind to class I HDAC targets in a subset of protein complexes.
7. The NCoR/SMRT/SMRTER co-repressors bind to Class I HDACs and in mammals and Drosophila these complexes regulate commitment and differentiation of neural progenitors.
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