Structural insights into the TRIM family of ubiquitin E3 ligases

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

(2014) J. G. Sanchez et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The E3-Ligase TRIM Family of Proteins Regulates Signaling Pathways Triggered by Innate Immune Pattern-Recognition Receptors

(2013) Gijs A. Versteeg et al.   IMMUNITY

Tripartite Motif Ligases Catalyze Polyubiquitin Chain Formation through a Cooperative Allosteric Mechanism

(2013) Frederick C. Streich et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3

(2013) Hao Dou et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Skp2-SCF E3 Ligase Regulates Akt Ubiquitination, Glycolysis, Herceptin Sensitivity, and Tumorigenesis

(2012) Chia-Hsin Chan et al.   CELL

The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA

(2012) Zhiqiang Zhang et al.   NATURE IMMUNOLOGY

Regulation of innate immune signalling pathways by the tripartite motif (TRIM) family proteins

(2011) Taro Kawai et al.   EMBO Molecular Medicine

Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma

(2011) B. Herquel et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

MAGE-RING Protein Complexes Comprise a Family of E3 Ubiquitin Ligases

(2010) Jennifer M. Doyle et al.   MOLECULAR CELL