The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
TRAF6 (TNF receptor-associated factor 6) is a human TRAF-family cytosolic signaling adaptor that also functions as a RING-type E3 ubiquitin ligase (EC 2.3.2.27). Recent literature consistently describes a conserved multi-domain architecture with N-terminal RING and multiple zinc fingers, a coiled-coil/TRAF-N region, and a C-terminal TRAF-C/MATH (TRAF) domain responsible for receptor/adaptor binding (li2024tumornecrosisfactor pages 2-4, wu2024traf6inhibitorsfrom pages 1-2). In this family, the trimeric TRAF-C domain can act as a “cap” and the TRAF-N coiled-coil as a “stalk,” providing an interaction platform that positions the N-terminal RING/zinc-finger catalytic region for ubiquitin-chain assembly and signaling complex formation (yang2025tnfreceptorassociatedfactors pages 7-8).
Functionally, TRAF6 is best understood as a signal-proximal ubiquitin ligase/scaffold that converts receptor stimulation into polyubiquitin-based signaling scaffolds which recruit and activate downstream kinases (e.g., TAK1 and IKK) to drive NF-κB and MAPK activation (li2024tumornecrosisfactor pages 2-4, li2024tumornecrosisfactor pages 1-2).
TRAF6 catalyzes ubiquitin transfer in the canonical E1–E2–E3 cascade as an E3 ligase, promoting formation of polyubiquitin chains that serve primarily as non-degradative signaling scaffolds, rather than proteasomal degradation signals (li2024tumornecrosisfactor pages 1-2, li2024tumornecrosisfactor pages 2-4).
The most consistently supported E2 complex for TRAF6 is Ubc13/UBE2N–Uev1A/UBE2V1, which is directly linked to TRAF6-mediated assembly of K63-linked polyubiquitin chains (li2024tumornecrosisfactor pages 2-4, wu2024traf6inhibitorsfrom pages 1-2). A 2024 inhibitor-discovery study notes a defined TRAF6–Ubc13 interaction surface, highlighting TRAF6 residues Gln54, Asp57, Ile72, Leu74 as contributing to E2 engagement (wu2024traf6inhibitorsfrom pages 1-2).
Recent review-level synthesis emphasizes that TRAF6 preferentially supports K63-linked polyubiquitination, distinguishing it from K48-linked chains that more commonly target proteins for proteasomal degradation (li2024tumornecrosisfactor pages 2-4, li2024tumornecrosisfactor pages 1-2). Representative TRAF6-linked K63-modified signaling substrates/adaptors cited in 2024 review pages include IKKγ/NEMO, TAK1, IRAK1, and TRAF6 itself (li2024tumornecrosisfactor pages 2-4). The same review corpus notes that TRAF6 can participate in K48-linked ubiquitination in selected contexts, indicating that TRAF6 signaling can be coupled to regulated proteostasis depending on cellular conditions (li2024tumornecrosisfactor pages 11-13).
Across recent primary studies, TRAF6 is described/observed as a cytosolic adaptor that associates with the cytoplasmic tails of transmembrane receptors and with inducible cytosolic signaling assemblies (ayyasamy20241433ζsuppressesrankl pages 1-2). Two 2024 mechanistic papers broaden this view:
A central, repeatedly cited role is TRAF6 in TLR/IL-1 receptor family signaling, where TRAF6 is recruited downstream of receptor-proximal adaptors/kinases to promote TAK1 and IKK activation, leading to NF-κB and MAPK transcriptional programs (li2024tumornecrosisfactor pages 2-4).
TRAF6 is essential in RANKL–RANK signaling, acting as a key adaptor/E3 ligase required for osteoclastogenic downstream cascades (MAPK, PI3K/AKT, IκB phosphorylation) and NF-κB activation (ayyasamy20241433ζsuppressesrankl pages 1-2). This pathway-level role is also emphasized in bone-disease-focused synthesis (yang2025tnfreceptorassociatedfactors pages 7-8).
A major 2024 development is the high-resolution demonstration that EBV LMP1 uses a direct TRAF6-binding motif (CTAR2 region) to drive NF-κB/JNK/p38/IRF7 signaling and lymphoma cell survival (giehler2024epsteinbarrvirusdrivenb pages 1-3). Importantly, structural/functional analyses indicate the LMP1–TRAF6 interface differs from CD40–TRAF6, implying that certain inhibitors could potentially exploit viral-specific binding geometries (giehler2024epsteinbarrvirusdrivenb pages 7-9).
Ayyasamy et al. (2024-07; https://doi.org/10.1016/j.jbc.2024.107487) show that 14-3-3ζ binds TRAF6 (interaction increases rapidly after RANKL stimulation), reduces the RANK–TRAF6 interaction, and promotes TRAF6 ubiquitination and proteasome-dependent degradation, dampening downstream RANKL signaling (ayyasamy20241433ζsuppressesrankl pages 4-5, ayyasamy20241433ζsuppressesrankl pages 5-7). Mechanistic support includes proteasome inhibitor blockade of TRAF6 loss (MG132/lactacystin conditions) and TRAF6 immunoprecipitation followed by ubiquitin detection (ayyasamy20241433ζsuppressesrankl pages 5-7, ayyasamy20241433ζsuppressesrankl pages 7-8). Functionally, 14-3-3ζ deficiency increases osteoclastogenesis and resorption readouts (e.g., CTX ELISA and dentine pit formation assays are described), while 14-3-3ζ re-expression suppresses osteoclastogenic transcription factors (p65/NFATc1) and MAPK/AKT phosphorylation (ayyasamy20241433ζsuppressesrankl pages 1-2, ayyasamy20241433ζsuppressesrankl pages 4-5).
Evidence from the article’s figures directly illustrates: (i) suppression of osteoclast formation/resorption phenotypes (ayyasamy20241433ζsuppressesrankl media 5629ff81), (ii) increased 14-3-3ζ–TRAF6 interaction and reduced RANK–TRAF6 association (ayyasamy20241433ζsuppressesrankl media 5d4d160c), and (iii) enhanced TRAF6 ubiquitination and proteasomal degradation linked to signaling suppression (ayyasamy20241433ζsuppressesrankl media 0ea8acbf).
Li et al. (2024-01; https://doi.org/10.34133/research.0315) report that during ALPK1/TIFA-dependent sensing of bacterial ADP-heptose, TRAF6 undergoes stimulus-dependent LLPS and is recruited into TIFA condensates. Within these condensates, TRAF6 markedly amplifies K63-linked polyubiquitin synthesis when reconstituted with E1 and the Ubc13/Uev1A E2 complex, enriching ubiquitin machinery (Ub, Ubc13/Uev1A) and downstream effectors (e.g., NEMO/TAK1/TABs) to accelerate pathway activation (li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 5-7). Quantitative details include: ~6–7 puncta per cell after 10 μM ADP-LD-Hep stimulation and a reported NF-κB activation IC50 ≈ 2.3 μM for ADP-LD-Hep activation (li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 7-9).
Mechanistically, these results support a current expert view that TRAF6 signaling output is not only determined by enzyme identity (E2 pairing and linkage type), but also by higher-order mesoscale organization (condensates that retain long K63 chains and concentrate enzymatic components) (li2024adphepinducedliquidphase pages 7-9).
Giehler et al. (2024-01; https://doi.org/10.1038/s41467-023-44455-w) establish a direct protein–protein interaction between EBV LMP1 CTAR2 and TRAF6. The critical LMP1 TRAF6-binding motif is P379VQLSY (PVQxxY), and mutational analysis identified P379, V380, Q381, Y384 as essential for binding in quantitative AlphaScreen PPI assays (giehler2024epsteinbarrvirusdrivenb pages 1-3, giehler2024epsteinbarrvirusdrivenb pages 3-4). Structural/biophysical mapping includes NMR HSQC perturbations with the LMP1 peptide and modeling based on the RANK–TRAF6 template, implicating TRAF6 interface residues including F471/Y473 as critical binding determinants (giehler2024epsteinbarrvirusdrivenb pages 7-9).
Therapeutic implication demonstrated experimentally: a RANK-derived TRAF6 inhibitor peptide blocks TRAF6–LMP1 binding with IC50 = 177 nM and reduces viability/proliferation of EBV-transformed lymphoblastoid cells when delivered as a cell-penetrating peptide (tested at 100 μM for 4 days) (giehler2024epsteinbarrvirusdrivenb pages 9-10, giehler2024epsteinbarrvirusdrivenb pages 10-12).
A clinical trials tool search for the literal phrase “TRAF6 inhibitor” did not retrieve clearly relevant interventional trials, implying that TRAF6-directed therapeutics are not yet widely represented as explicit clinical interventions under that label in the indexed registry results available to this workflow (OpenTargets Search: -TRAF6).
Open Targets evidence links TRAF6 to multiple disease areas with association scores and evidence counts, including severe acute respiratory syndrome, ovarian neoplasm, vertebral column disorder, renal osteodystrophy, and autosomal dominant hypohidrotic ectodermal dysplasia (OpenTargets Search: -TRAF6). These associations support prioritization of TRAF6 as a mechanistically plausible node in inflammatory, neoplastic, and bone-related disease processes, but require disease-specific causal validation beyond association.
TRAF6 should be annotated as a cytosolic receptor-proximal E3 ubiquitin ligase/adaptor whose primary biochemical output is Ubc13/Uev1A-dependent K63 polyubiquitin chain assembly, enabling recruitment/activation of TAK1/IKK and MAPK modules to drive inflammatory and differentiation programs (li2024tumornecrosisfactor pages 2-4, li2024adphepinducedliquidphase pages 7-9). Current 2024 mechanistic advances emphasize that TRAF6 signaling strength and specificity are controlled by (i) regulated degradation/turnover (e.g., 14-3-3ζ-driven ubiquitination and proteasomal degradation in RANKL signaling) and (ii) higher-order organization into inducible condensates that spatially concentrate ubiquitination enzymes and effectors (ayyasamy20241433ζsuppressesrankl pages 5-7, li2024adphepinducedliquidphase pages 7-9). Therapeutic strategies in 2024 are predominantly preclinical, spanning computational small-molecule identification, and targeted disruption of TRAF6 recruitment interfaces (notably virus-specific LMP1–TRAF6 engagement) (wu2024traf6inhibitorsfrom pages 1-2, giehler2024epsteinbarrvirusdrivenb pages 9-10).
The following table compiles identity, biochemical function, pathways, localization, 2023–2024 advances, and translational angles in a compact format.
| Aspect | Key points | Best recent sources with year and URL |
|---|---|---|
| Identity/domains | • Human TRAF6 / TNF receptor-associated factor 6 matches UniProt Q9Y4K3 context • TRAF-family adaptor and E3 ubiquitin ligase • Domain architecture: N-terminal RING, multiple zinc fingers, coiled-coil/TRAF-N, C-terminal TRAF-C/MATH receptor-binding domain • TRAF-C recognizes receptor motifs; trimeric TRAF-C and stalk-like TRAF-N are emphasized in recent structural summaries (li2024tumornecrosisfactor pages 2-4, yang2025tnfreceptorassociatedfactors pages 7-8, li2024tumornecrosisfactor pages 1-2, wu2024traf6inhibitorsfrom pages 1-2) | Li et al., 2024, Journal of Cancer — https://doi.org/10.7150/jca.90059 ; Yang et al., 2025, Frontiers in Physiology — https://doi.org/10.3389/fphys.2025.1527814 ; Wu et al., 2024, Marine Drugs — https://doi.org/10.3390/md22060260 |
| Enzymatic activity | • TRAF6 functions as a RING-type E3 ubiquitin ligase and signaling scaffold • Works with E1/E2 enzymes to assemble signaling-active ubiquitin chains • Central output is activation of TAK1/IKK → NF-κB and MAPK signaling • Recent reviews also note TRAF6 can participate in both non-degradative signaling and degradative ubiquitin control depending on chain type/context (li2024tumornecrosisfactor pages 11-13, li2024tumornecrosisfactor pages 2-4, li2024tumornecrosisfactor pages 1-2, wu2024traf6inhibitorsfrom pages 1-2) | Li et al., 2024 — https://doi.org/10.7150/jca.90059 ; Wu et al., 2024 — https://doi.org/10.3390/md22060260 |
| Key E2 partners | • Best-supported E2 complex is Ubc13/UBE2N–Uev1A/UBE2V1 • This partnership is specifically linked to TRAF6-catalyzed K63-linked polyubiquitination • A recent inhibitor-development paper highlights a defined TRAF6–Ubc13 interaction surface including Gln54, Asp57, Ile72, Leu74 on TRAF6 • Ubc13/Uev1A is also used in in vitro condensate reconstitution assays for TRAF6-driven ubiquitin-chain synthesis (li2024tumornecrosisfactor pages 2-4, wu2024traf6inhibitorsfrom pages 1-2, li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 5-7) | Li et al., 2024 — https://doi.org/10.7150/jca.90059 ; Wu et al., 2024 — https://doi.org/10.3390/md22060260 ; Li et al., 2024, Research — https://doi.org/10.34133/research.0315 |
| Ubiquitin linkage specificity | • K63-linked chains are the canonical TRAF6 signaling output and act as scaffolds rather than degradation tags • Representative K63-modified targets mentioned in recent review pages include IKKγ/NEMO, TAK1, IRAK1, and TRAF6 itself • Recent reviews also note TRAF6 can participate in K48-linked ubiquitination in some contexts, supporting proteasomal degradation/regulatory turnover • LLPS work links TRAF6 condensates to synthesis/retention of long K63 polyUb chains (li2024tumornecrosisfactor pages 2-4, li2024tumornecrosisfactor pages 1-2, li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 7-9, li2024adphepinducedliquidphase pages 5-7) | Li et al., 2024 — https://doi.org/10.7150/jca.90059 ; Li et al., 2024, Research — https://doi.org/10.34133/research.0315 |
| Representative substrates | • Recent review pages list IKKγ/NEMO, TAK1, IRAK1, and TRAF6 itself as representative K63-ubiquitinated targets/substrates in TRAF6 signaling • TRAF6 is also described as binding p62 to ubiquitinate mTOR, linking it to growth/autophagy regulation • In disease-focused primary work, TRAF6 directly engages receptor/adaptor complexes such as RANK and TIFA, and viral protein LMP1 recruits TRAF6 as a critical host effector • Evidence base is strongest for receptor-proximal signaling substrates/adaptors rather than a single exclusive substrate class (li2024tumornecrosisfactor pages 11-13, li2024tumornecrosisfactor pages 2-4, ayyasamy20241433ζsuppressesrankl pages 1-2, giehler2024epsteinbarrvirusdrivenb pages 1-3) | Li et al., 2024 — https://doi.org/10.7150/jca.90059 ; Ayyasamy et al., 2024, JBC — https://doi.org/10.1016/j.jbc.2024.107487 ; Giehler et al., 2024, Nature Communications — https://doi.org/10.1038/s41467-023-44455-w |
| Core pathways | • Major pathways in recent evidence: TLR/IL-1R–MyD88–IRAK–TRAF6–TAK1–NF-κB/MAPK • RANK/RANKL–TRAF6 is central for osteoclastogenesis and bone remodeling • Additional pathways in recent review/primary papers include CD40/TRAF6-related signaling, IL-17R via Act1, TCR via CARMA1–BCL10–MALT1, TLR7/8/9–MYD88–IRF7, and ALPK1–TIFA–TRAF6 innate sensing • In EBV biology, LMP1–TRAF6 drives NF-κB/JNK/p38/IRF7 signaling and lymphoma survival (li2024tumornecrosisfactor pages 2-4, ayyasamy20241433ζsuppressesrankl pages 1-2, giehler2024epsteinbarrvirusdrivenb pages 1-3, li2024adphepinducedliquidphase pages 1-2) | Li et al., 2024 — https://doi.org/10.7150/jca.90059 ; Ayyasamy et al., 2024 — https://doi.org/10.1016/j.jbc.2024.107487 ; Giehler et al., 2024 — https://doi.org/10.1038/s41467-023-44455-w ; Li et al., 2024 — https://doi.org/10.34133/research.0315 |
| Localization/complexes | • TRAF6 is a cytosolic adaptor/E3 that assembles on cytoplasmic tails of transmembrane receptors and receptor-proximal signaling complexes • Recent primary data show dynamic association with RANK, TIFA condensates, and viral LMP1 CTAR2 complexes • ADP-heptose studies show TRAF6 forms cytosolic membraneless droplets/condensates with dynamic exchange • Complex partners include TAK1/TAB1/2, NEMO, Ubc13/Uev1A, and receptor scaffolds (ayyasamy20241433ζsuppressesrankl pages 1-2, giehler2024epsteinbarrvirusdrivenb pages 1-3, li2024adphepinducedliquidphase pages 7-9, li2024adphepinducedliquidphase pages 4-5) | Ayyasamy et al., 2024 — https://doi.org/10.1016/j.jbc.2024.107487 ; Giehler et al., 2024 — https://doi.org/10.1038/s41467-023-44455-w ; Li et al., 2024 — https://doi.org/10.34133/research.0315 |
| 2023-2024 mechanistic advances | • 2024 JBC: 14-3-3ζ binds TRAF6, increases after RANKL, promotes TRAF6 ubiquitination and proteasomal degradation, weakens RANK–TRAF6 interaction, and suppresses osteoclastogenic signaling • 2024 Research: TRAF6 undergoes LLPS/condensation in TIFA microreactors that enrich ubiquitin machinery and favor long K63 polyUb synthesis • 2024 Nat Commun: EBV LMP1 directly binds TRAF6 through a CTAR2 motif (P379VQLSY), with key interface residues defined biochemically/structurally • These studies move TRAF6 biology from linear pathway maps toward regulated PPI interfaces, condensates, and degradative control (ayyasamy20241433ζsuppressesrankl pages 4-5, ayyasamy20241433ζsuppressesrankl pages 5-7, li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 7-9, giehler2024epsteinbarrvirusdrivenb pages 7-9, giehler2024epsteinbarrvirusdrivenb pages 3-4, giehler2024epsteinbarrvirusdrivenb pages 9-10) | Ayyasamy et al., 2024 — https://doi.org/10.1016/j.jbc.2024.107487 ; Li et al., 2024 — https://doi.org/10.34133/research.0315 ; Giehler et al., 2024 — https://doi.org/10.1038/s41467-023-44455-w |
| Therapeutic targeting approaches | • Small-molecule discovery: virtual screening of 52,765 marine compounds yielded candidate TRAF6 binders CMNPD9212-16 and CMNPD12791-8 with favorable in silico ADMET/MD profiles • PPI targeting: EBV study validated peptide disruption of LMP1–TRAF6; a RANK-derived inhibitor peptide blocked binding and reduced viability of EBV-transformed B cells • Pathway modulation in bone disease: recent work supports targeting RANK–TRAF6 signaling or promoting TRAF6 degradation/stability control • No directly relevant TRAF6-targeted interventional clinical trials were retrieved in the tool search, so current implementation remains largely preclinical (wu2024traf6inhibitorsfrom pages 1-2, giehler2024epsteinbarrvirusdrivenb pages 10-12, giehler2024epsteinbarrvirusdrivenb pages 9-10) | Wu et al., 2024 — https://doi.org/10.3390/md22060260 ; Giehler et al., 2024 — https://doi.org/10.1038/s41467-023-44455-w |
| Quantitative/statistical data | • Marine-drug screen: 52,765 compounds screened; 405 docked; 6 advanced; 2 prioritized hits (CMNPD9212-16, CMNPD12791-8) (wu2024traf6inhibitorsfrom pages 1-2) • TIFA/TRAF6 condensate study: ADP-LD-Hep produced about 6–7 puncta per cell; NF-κB activation IC50 ≈ 2.3 μM; in vitro reconstitution used TRAF6 20 μM, Ubc13 1 μM, Uev1A 1 μM, Ub 50 μM, E1 0.1 μM, ATP 2 mM (li2024adphepinducedliquidphase pages 2-4, li2024adphepinducedliquidphase pages 7-9, li2024adphepinducedliquidphase pages 15-16) • 14-3-3ζ study: proteasome inhibitors MG132/lactacystin at 10 nM blocked TRAF6 loss; RANKL stimulation increased 14-3-3ζ–TRAF6 interaction and osteoclast assays used TRAP+ cells with ≥3 nuclei as scoring criterion (ayyasamy20241433ζsuppressesrankl pages 7-8, ayyasamy20241433ζsuppressesrankl pages 5-7, ayyasamy20241433ζsuppressesrankl pages 8-9) • LMP1–TRAF6 study: RANK-derived inhibitor peptide blocked binding with IC50 177 nM; cell-penetrating peptide tested at 100 μM for 4 days reduced LCL proliferation (giehler2024epsteinbarrvirusdrivenb pages 10-12, giehler2024epsteinbarrvirusdrivenb pages 9-10) | Wu et al., 2024 — https://doi.org/10.3390/md22060260 ; Li et al., 2024 — https://doi.org/10.34133/research.0315 ; Ayyasamy et al., 2024 — https://doi.org/10.1016/j.jbc.2024.107487 ; Giehler et al., 2024 — https://doi.org/10.1038/s41467-023-44455-w |
Table: This table summarizes the most evidence-supported features of human TRAF6 (UniProt Q9Y4K3), including its domain architecture, E3 ligase activity, pathway roles, recent mechanistic advances, and preclinical targeting strategies. It is designed as a compact reference for functional annotation grounded only in the gathered evidence.
References
(li2024tumornecrosisfactor pages 2-4): Tingting Li, Zhe Lei, Lin Wei, Kai Yang, Jinhong Shen, and Lin Hu. Tumor necrosis factor receptor-associated factor 6 and human cancer: a systematic review of mechanistic insights, functional roles, and therapeutic potential. Journal of Cancer, 15:560-576, Jan 2024. URL: https://doi.org/10.7150/jca.90059, doi:10.7150/jca.90059. This article has 14 citations and is from a peer-reviewed journal.
(wu2024traf6inhibitorsfrom pages 1-2): Xuexuan Wu, Saiyi Zhong, Nan Zhou, and Lianxiang Luo. Traf6 inhibitors from marine compound library: pharmacophore, virtual screening, fragment replacement, admet, and molecular dynamics. Marine Drugs, 22:260, Jun 2024. URL: https://doi.org/10.3390/md22060260, doi:10.3390/md22060260. This article has 1 citations.
(yang2025tnfreceptorassociatedfactors pages 7-8): Xicheng Yang, LiLi Zhao, and YinQuan Pang. Tnf receptor-associated factors: promising targets of natural products for the treatment of osteoporosis. Frontiers in Physiology, May 2025. URL: https://doi.org/10.3389/fphys.2025.1527814, doi:10.3389/fphys.2025.1527814. This article has 3 citations.
(li2024tumornecrosisfactor pages 1-2): Tingting Li, Zhe Lei, Lin Wei, Kai Yang, Jinhong Shen, and Lin Hu. Tumor necrosis factor receptor-associated factor 6 and human cancer: a systematic review of mechanistic insights, functional roles, and therapeutic potential. Journal of Cancer, 15:560-576, Jan 2024. URL: https://doi.org/10.7150/jca.90059, doi:10.7150/jca.90059. This article has 14 citations and is from a peer-reviewed journal.
(li2024tumornecrosisfactor pages 11-13): Tingting Li, Zhe Lei, Lin Wei, Kai Yang, Jinhong Shen, and Lin Hu. Tumor necrosis factor receptor-associated factor 6 and human cancer: a systematic review of mechanistic insights, functional roles, and therapeutic potential. Journal of Cancer, 15:560-576, Jan 2024. URL: https://doi.org/10.7150/jca.90059, doi:10.7150/jca.90059. This article has 14 citations and is from a peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl pages 1-2): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(li2024adphepinducedliquidphase pages 4-5): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(li2024adphepinducedliquidphase pages 9-12): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 1-3): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 7-9): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl pages 4-5): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl pages 5-7): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl pages 7-8): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl media 5629ff81): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl media 5d4d160c): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl media 0ea8acbf): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(li2024adphepinducedliquidphase pages 2-4): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(li2024adphepinducedliquidphase pages 5-7): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(li2024adphepinducedliquidphase pages 7-9): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 3-4): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 9-10): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 10-12): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(giehler2024epsteinbarrvirusdrivenb pages 12-13): Fabian Giehler, Michael S. Ostertag, Thomas Sommermann, Daniel Weidl, Kai R. Sterz, Helmut Kutz, Andreas Moosmann, Stephan M. Feller, Arie Geerlof, Brigitte Biesinger, Grzegorz M. Popowicz, Johannes Kirchmair, and Arnd Kieser. Epstein-barr virus-driven b cell lymphoma mediated by a direct lmp1-traf6 complex. Nature Communications, Jan 2024. URL: https://doi.org/10.1038/s41467-023-44455-w, doi:10.1038/s41467-023-44455-w. This article has 29 citations and is from a highest quality peer-reviewed journal.
(OpenTargets Search: -TRAF6): Open Targets Query (-TRAF6, 12 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(li2024adphepinducedliquidphase pages 15-16): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.
(ayyasamy20241433ζsuppressesrankl pages 8-9): R. Ayyasamy, S. Fan, P. Czernik, B. Lecka-Czernik, S. Chattopadhyay, and R. Chakravarti. 14-3-3ζ suppresses rankl signaling by destabilizing traf6. Journal of Biological Chemistry, 300:107487, Jul 2024. URL: https://doi.org/10.1016/j.jbc.2024.107487, doi:10.1016/j.jbc.2024.107487. This article has 8 citations and is from a domain leading peer-reviewed journal.
(li2024adphepinducedliquidphase pages 1-2): Liping Li, Jia Wang, Xincheng Zhong, Yaoyao Jiang, Gaofeng Pei, Xikang Yang, Kaixiang Zhang, Siqi Shen, Xue Jin, Gaoge Sun, Chaofei Su, Shuzhen Chen, and Hang Yin. Adp-hep-induced liquid phase condensation of tifa-traf6 activates alpk1/tifa-dependent innate immune responses. Research, Jan 2024. URL: https://doi.org/10.34133/research.0315, doi:10.34133/research.0315. This article has 12 citations and is from a peer-reviewed journal.