The tripartite motif family identifies cell compartments
By Alexandre Reymond, G. Meroni, Anna Fantozzi, G. Merla, S. Cairo, L. Luzi, D. Riganelli, E. Zanaria, S. Messali, S. Cainarca and 4 more. EMBO Journal, 2001
1,412 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/50846e0f258906d86251013e1f0b15dfb6939540
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Citations in the corpus
- Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach (2007, background): “TRIM5 is a member of the large tripartite motif family in primate genomes, characterized by having RING finger, B-box and coiled-coil domains, as well as an additional SPRY domain found in the a isoform (40).”
- TRIM proteins and cancer (2011, background): “Members of the family of tripartite motif (TRIM)-containing proteins could be defined as E3 ubiquitin ligases as they contain a RING-finger domain , although not all proteins containing a RING-finger domain function as E3 ubiquitin ligase”
- Inflammatory caspases and inflammasomes: master switches of inflammation (2007, background): “proteins with various functions and is characterized by the presence of a B-Box, and a conserved Coiled Coil domain.(128) The B-Box is often preceded by a RING domain and a Coiled Coil domain, and followed by a PRY and SPRY domains.”
- Interferon-Stimulated Genes: A Complex Web of Host Defenses (2014, background): “The Cterminal coiled-coil domain is involved in self-association and can lead to the formation of large complexes that occupy many discrete and uncharacterized subcellular compartments (159).”
- TRIM family proteins: retroviral restriction and antiviral defence (2005, background): “Subsequently, the TRIM family grew slowly, until the availability of new genome sequences combined with a functional genomics approach enabled many new members to be identifie”
- TRIM family proteins and their emerging roles in innate immunity (2008, background): “Recent studies have shown that many members of the tripartite motif-containing (TRIM) superfamily are expressed in response to IFNs and are involved in a broad range of biological processes that are associated with innate immunit”
- TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases (2005, background): “The TRIM/RBCC family The striking feature of this protein family is the presence of the tripartite motif, hence the name TRIM.”
- Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1 (2004, background): “TRIM5 possesses a coiled-coil domain which causes the protein to aggregate and form cytoplasmic bodie”
- Retroviral Restriction Factor TRIM5α Is a Trimer (2005, background): “TRIM5 is a member of the tripartite motif (TRIM) family of proteins which contain RING, B-box, and coiled-coil domains (26).”
- Genome-Wide and Functional Annotation of Human E3 Ubiquitin Ligases Identifies MULAN, a Mitochondrial E3 that Regulates the Organelle's Dynamics and Signaling (2008, background): “Proteins lacking a RNF domain are not listed (e.g., TRIM14, TRIM16, TRIM29).”
- The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys (2004, background): “The only monkey cDNA insert common to both HIV-1–GFP-resistant clones was predicted to encode TRIM5α, a member of the tripartite motif (TRIM) family of proteins containing RING domains, B-boxes and coiled coil”