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As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.Articles
Structures of butyrophilin multimers reveal a plier-like mechanism for Vγ9Vδ2 T cell receptor activation
Keywords T cell activation butyrophilins Vγ9Vδ2 T cell receptor phosphoantigen germline-encoded region CDR3 molecular glue dual-ligand recognition innate and adaptive immunity Get full text access Log in, subscribe or purchase for full access. References 1. Rossjohn, J. ∙ Gras, S. ∙ Miles, J.J. ... T cell antigen receptor recognition of antigen-presenting molecules Annu. Rev. Immunol. 2015; 33:169-200 2. Vantourout, P. ∙ Hayday, A. Six-of-the-best: unique contributions of γδ T cells to immunology Nat. Rev.
Cryo-EM structural insights into Vγ9Vδ2 TCR activation via multiple butyrophilins
Abstract Human Vγ9Vδ2 T cells detect cancerous and pathogen-infected cells through an "inside-out" mechanism wherein intracellular domains of butyrophilin (BTN) proteins recognize phosphoantigens (pAgs) to prime BTN ectodomains to engage with the T cell receptor (TCR) to activate Vγ9Vδ2 T cells.
CircRNA‐406918 enhances the degradation of advanced glycation end products in photoaged human dermal fibroblasts via targeting cathepsin D
ORIGINAL ARTICLE Yingying Qu and Mengyao Wang contributed equally to this work. Abstract Background Lysosomal cathepsin D (CTSD) can degrade internalized advanced glycation end products (AGEs) in dermal fibroblasts. CTSD expression is decreased in photoaged fibroblasts, which contributes to intracellular AGEs deposition and further plays a role in AGEs accumulation of photoaged skin. The mechanism under downregulated CTSD expression is unclear.
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