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10.1016/j.it.2021.12.005

http://scihub22266oqcxt.onion/10.1016/j.it.2021.12.005
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35033428!8755460!35033428
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suck abstract from ncbi

pmid35033428      Trends+Immunol 2022 ; 43 (2): 148-162
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  • K63 ubiquitination in immune signaling #MMPMID35033428
  • Madiraju C; Novack JP; Reed JC; Matsuzawa SI
  • Trends Immunol 2022[Feb]; 43 (2): 148-162 PMID35033428show ga
  • Ubc13-catalyzed K63 ubiquitination is a major control point for immune signaling. Recent evidence has shown that the control of multiple immune functions, including chronic inflammation, pathogen responses, lymphocyte activation, and regulatory signaling, is altered by K63 ubiquitination. In this review, we detail the novel cellular sensors that are dependent on K63 ubiquitination for their function in the immune signaling network. Many pathogens, including severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), can target K63 ubiquitination to inhibit pathogen immune responses; we describe novel details of the pathways involved and summarize recent clinically relevant SARS-CoV-2-specific responses. We also discuss recent evidence that regulatory T cell (Treg) versus T helper (T(H)) 1 and T(H)17 cell subset regulation might involve K63 ubiquitination. Knowledge gaps that merit future investigation and clinically relevant pathways are also addressed.
  • |*COVID-19[MESH]
  • |*Lysine/metabolism[MESH]
  • |Humans[MESH]
  • |SARS-CoV-2[MESH]
  • |Signal Transduction[MESH]
  • |Ubiquitin-Protein Ligases/metabolism[MESH]


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