The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
E3 ubiquitin ligases as T cell anergy factors
Abstract
E3 ubiquitin ligases have emerged as key molecular regulators of immune cell function. Three families of proteins with ubiquitin ligase activity have been described (the HECT, RING and U-box proteins), and each may be involved in the regulation of immune responses during infection by targeting specific inhibitory molecules for proteolytic destruction. Several HECT and RING E3 proteins have now also been linked to the induction and maintenance of immune self-tolerance: c-Cbl, Cbl-b, GRAIL, Itch and Nedd4 each negatively regulate T cell growth factor production and proliferation. This review will discuss the relationship between the ubiquitination of select components of the antigen-sensing signaling apparatus in T cells and the development and maintenance of the clonal anergy state.
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“The E3 ubiquiting ligase family can affect PI3K, mTOR, and Ras/MAPK signaling pathways and help to actively maintain anergy [21,23,24].”
From T cell anergy, exhaustion, senescence, and stemness in the tumor microenvironment (2013) · cites this paper as [24]
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Egr-2 and PD-1 Are Required for Induction and Maintenance of T Cell Anergy: A Dissertation
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REGULATION AND FUNCTION OF MARCH1: MODULATION OF IMMUNITY THROUGH UBIQUITINATION
Jabbour, M. (2010) · UA Campus Repository (The University of Arizona)
Metadata
- Authors
- Mueller, D. L.
- Affiliations
- University of Minnesota (US)
- Corresponding author
- Mueller, Daniel L
- ORCID
- Mueller, Daniel L
- Venue
- Nature Immunology
- Published
- 2004-08-27
- Volume
- 5
- Issue
- 9
- Pages
- 883-890
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W2005935110
- Cited by
- 224
- References
- 73
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 3 · 2021: 7 · 2020: 6 · 2019: 7 · 2018: 7 · 2017: 5 · 2016: 7 · 2015: 5 · 2014: 14 · 2013: 11 · 2012: 7
- FWCI
- 1.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01 GM54706, R01GM054706)
- National Institute of Allergy and Infectious Diseases (P01AI50162, P01-AI 35296, P01AI050162, P01AI035296)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- E3 ubiquitin ligase, T cell anergy, HECT E3 ligases, RING E3 ligases, ubiquitination, self-tolerance, c-Cbl, Cbl-b, GRAIL, pruritus, NEDD4, T cell proliferation
- MeSH terms
- Animals, Humans, T-Lymphocytes, Signal Transduction, Self Tolerance, Clonal Anergy, Models, Immunological, Ubiquitin-Protein Ligases
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