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The crystal structures representing the catalytic states of zebrafish CYLD for Met1 (show DNMT1 Proteins)- and Lys63-linked Ub chains and two distinct precatalytic states for Met1 (show DNMT1 Proteins)-linked chains are presented.
Our findings underscore a critical tumor-suppressing role for functional intestinal epithelial CYLD in colitis-associated carcinogenesis
Deubiquitinase CYLD negatively regulates MyD88 (show MYD88 Proteins)-mediated signaling by directly interacting with MyD88 (show MYD88 Proteins) and deubiquitinating nontypeable Haemophilus influenzae (NTHi)-induced K63-linked polyubiquitination of MyD88 (show MYD88 Proteins) at lysine 231.
CYLD interrupts the ERK (show EPHB2 Proteins)- and p38 (show CRK Proteins)-/AP-1 (show JUN Proteins) and c-Myc (show MYC Proteins) pathways to suppress Nrf2 (show NFE2L2 Proteins)-operated antioxidative capacity, thereby enhancing oxidative stress in the heart.
Our data demonstrate that inefficient negative selection in the thymus of CYLD(ex7/8) mice result from a defect in mTEC maturation.
The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells.
Data show that the in utero death of NF-NF (show NFASC Proteins)-kappaB (show NFKB1 Proteins) essential modulator (NEMO (show IKBKG Proteins)) and cylindromatosis protein double mutant mice is mediated by TNF (show TNF Proteins) receptor 1 (TNFR1 (show TNFRSF1A Proteins)) signaling and can be rescued by TNFR1 (show TNFRSF1A Proteins) deficiency.
CYLD is a central regulator of apoptotic cell death in murine hepatocytes by controlling NF-kappaB (show NFKB1 Proteins) dependent anti-apoptotic signaling.
In contrast to full-length CYLD, the immune function of short splice variant CYLD (sCYLD) is insufficiently described. To explore sCYLD's function in infection, investigated whether dendritic cell-specific sCYLD regulates the pathogenesis of listeriosis.
The ciliary function of CYLD is partially attributed to its deconjugation of the polyubiquitin (show UBB Proteins) chain from centrosomal protein of 70 kDa (Cep70 (show CEP70 Proteins)), a requirement for Cep70 (show CEP70 Proteins) to interact with gamma-tubulin (show TUBG1 Proteins) and localize at the centrosome.
CYLD negatively regulates nontypeable Haemophilus influenzae-induced IL-8 (show IL8 Proteins) expression via MKP-1 (show DUSP1 Proteins)-dependent inhibition of ERK (show EPHB2 Proteins).
These results demonstrate the involvement of histone deacetylases in the down regulation of Cyld expression in hepatocellular carcinoma cells.
Novel CYLD germline mutations c.1821_1826+1delinsCT/L607Ffs*9, c.2666A>T/p.D889V and c.2712delT/p.905Kfs*8 were identified in unrelated Brooke-Spiegler Syndrome patients.
Study founds the levels of CYLD and SMAD7 (show SMAD7 Proteins) significantly decreased in oral squamous cell carcinoma (OSSC) cells and proposes a model that CYLD suppresses OSCC metastases through SMAD7 (show SMAD7 Proteins). Downregulation of CYLD appears to directly contribute to the distal metastases of primary OSCC and subsequently poor prognosis.
Haplotype analysis was performed for the patients with multiple familial trichoepithelioma type 1, patients with familial cylindromatosis and a patient with Brooke-Spiegler syndrome, all of whom carry the same heterozygous nonsense CYLD mutation.
Ultraviolet radiation induced CYLD translocation from the cytoplasm to microtubules, posttranslational modification and degradation in a proteasome-independent manner.
CYLD interrupts the ERK (show EPHB2 Proteins)- and p38 (show CRK Proteins)-/AP-1 (show FOSB Proteins) and c-Myc (show MYC Proteins) pathways to suppress Nrf2 (show GABPA Proteins)-operated antioxidative capacity, thereby enhancing oxidative stress in the heart.
Data suggest OPTN (optineurin (show OPTN Proteins)) is involved in up-regulation of innate immunity in mitosis; mechanism involves phosphorylation/nuclear translocation of CYLD and phosphorylation/mitochondrial translocation of TBK1 (NF-kB-activating kinase (show TBK1 Proteins)).
CaMKII (show CAMK2G Proteins)-mediated recruitment and upregulation of CYLD is expected to remove K63-linked polyubiquitins and facilitate proteasomal degradation at the postsynaptic density.
This gene is encodes a cytoplasmic protein with three cytoskeletal-associated protein-glycine-conserved (CAP-GLY) domains that functions as a deubiquitinating enzyme. Mutations in this gene have been associated with cylindromatosis, multiple familial trichoepithelioma, and Brooke-Spiegler syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
cylindromatosis (turban tumor syndrome)
, probable ubiquitin carboxyl-terminal hydrolase CYLD-like
, ubiquitin carboxyl-terminal hydrolase CYLD
, deubiquitinating enzyme CYLD
, ubiquitin thioesterase CYLD
, ubiquitin thiolesterase CYLD
, ubiquitin-specific-processing protease CYLD
, probable ubiquitin carboxyl-terminal hydrolase CYLD
, retinitis pigmentosa 1 homolog
, ubiquitin specific peptidase like 2