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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.


SBS, CYLD, tenomodulin
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, Ubiquitin, V1a, ACID
Papers using SBS antibodies
The Tumor Suppressor CYLD Interacts with TRIP and Regulates Negatively Nuclear Factor κB Activation by Tumor Necrosis Factor
Huber Marcel et al., In The Journal of Experimental Medicine, 1998
... Full-length and partial cDNAs encoding CYLD and candidate proteins were cloned into the pGBKT7 or pGADT7 vectors (CLONTECH Laboratories, Inc.), respectively ...
Papers on SBS
Local trauma in human patellar tendon leads to widespread changes in the tendon gene expression.
Kjaer et al., Nottingham, United Kingdom. In J Appl Physiol, Feb 2016
Results for DNA content were inconclusive, and no changes were detected in expression of Insulin-like growth factor-I, connective tissue growth factor, scleraxis, decorin, fibromodulin, tenascin-C, tenomodulin, VEGFa, CD68, IL-6, MMP12 and MMP13.
Cylindromatosis-A Protective Molecule against Liver Diseases.
Massoumi et al., Regensburg, Germany. In Med Res Rev, Feb 2016
UNASSIGNED: Cylindromatosis (CYLD) is a deubiquitination enzyme involved in the regulation of different cellular processes including inflammation, fibrosis, and cancer.
Deubiquitinase CYLD acts as a negative regulator for bacterium NTHi-induced inflammation by suppressing K63-linked ubiquitination of MyD88.
Li et al., Seoul, South Korea. In Proc Natl Acad Sci U S A, Feb 2016
Deubiquitinase CYLD negatively regulates MyD88-mediated signaling by directly interacting with MyD88 and deubiquitinating nontypeable Haemophilus influenzae (NTHi)-induced K63-linked polyubiquitination of MyD88 at lysine 231.
UV Irradiation Triggers Cylindromatosis Translocation, Modification, and Degradation in a Proteasome-Independent Manner.
Zhang et al., Tianjin, China. In Dna Cell Biol, Jan 2016
UNASSIGNED: The tumor suppressor, cylindromatosis (CYLD), is a negative regulator of NF-κB signaling by removing lysine 63-linked ubiquitin chains from multiple NF-κB signaling components, including TRAF2, TRAF6, and NEMO.
MiR-130b inhibits proliferation and induces apoptosis of gastric cancer cells via CYLD.
Huang et al., Jinan, China. In Tumour Biol, Jan 2016
Bioinformatics analyses showed that cylindromatosis gene (CYLD) was a potential target gene of miR-130b.
Melatonin, bone regulation and the ubiquitin-proteasome connection: A review.
Reiter et al., Winnipeg, Canada. In Life Sci, Jan 2016
Also of significance in regulating osteoclastogenesis is the deubiquitinase, CYLD (cylindramatosis protein), which facilitates the separation of NF-κB from IkBα.
LUBAC-Recruited CYLD and A20 Regulate Gene Activation and Cell Death by Exerting Opposing Effects on Linear Ubiquitin in Signaling Complexes.
Walczak et al., London, United Kingdom. In Cell Rep, Jan 2016
We show here that the deubiquitinases CYLD and A20, but not OTULIN, are recruited to the TNFR1- and NOD2-associated signaling complexes (TNF-RSC and NOD2-SC), at which they cooperate to limit gene activation.
Inherited cylindromas: lessons from a rare tumour.
Ashworth et al., San Francisco, United States. In Lancet Oncol, Sep 2015
Cylindroma is a rare skin tumour that is inherited in several skin-tumour syndromes caused by germline mutations in the tumour suppressor gene, CYLD.
Linear ubiquitination in immunity.
Walczak et al., London, United Kingdom. In Immunol Rev, Jul 2015
Two of them, OTULIN and CYLD, are constitutively associated with LUBAC.
Phenotype-genotype correlations for clinical variants caused by CYLD mutations.
Széll et al., Szeged, Hungary. In Eur J Med Genet, May 2015
In 1996, the gene locus for BSS was mapped to 16q12-13, and, in 2000, mutations in the cylindromatosis (CYLD) gene were determined to cause BSS, familial cylindromatosis (FC; OMIM 132700) and multiple familial trichoepithelioma type 1 (MFT1; OMIM 601606).
Combining mesenchymal stem cell sheets with platelet-rich plasma gel/calcium phosphate particles: a novel strategy to promote bone regeneration.
Huang et al., Hangzhou, China. In Stem Cell Res Ther, 2014
PRP can promote gene expression of collagen III and tenomodulin by BMSCs and in BMSC sheets.
MicroRNA and transcription factor co-regulatory network analysis reveals miR-19 inhibits CYLD in T-cell acute lymphoblastic leukemia.
Guo et al., Wuhan, China. In Nucleic Acids Res, 2012
miR-19, CYLD and NF-kappaB form a regulatory feed-forward loop, which provides new clues for sustained activation of NF-kappaB in T-ALL.
Downregulation of cylindromatosis gene, CYLD, confers a growth advantage on malignant melanoma cells while negatively regulating their migration activity.
Maesawa et al., Japan. In Int J Oncol, 2012
the role of CYLD-induced RAC1 activation in melanoma cell migration.
Inactivation of the deubiquitinase CYLD in hepatocytes causes apoptosis, inflammation, fibrosis, and cancer.
Talianidis et al., Greece. In Cancer Cell, 2012
Results show that, in the liver, CYLD acts as an important regulator of hepatocyte homeostasis, protecting cells from spontaneous apoptosis by preventing uncontrolled TAK1 and JNK activation.
A pro-inflammatory role of deubiquitinating enzyme cylindromatosis (CYLD) in vascular smooth muscle cells.
Cui et al., Jinan, China. In Biochem Biophys Res Commun, 2012
these results uncover an unexpected role of CYLD in promoting inflammatory responses in VSMCs via a mechanism involving MAPK activation but independent of NF-kappaB activity, contributing to the pathogenesis of vascular disease.
CYLD negatively regulates transforming growth factor-β-signalling via deubiquitinating Akt.
Li et al., Atlanta, United States. In Nat Commun, 2011
CYLD negatively regulates TGFb1 signalling via deubiquitinating Akt.
Caspase 8 inhibits programmed necrosis by processing CYLD.
Ting et al., New York City, United States. In Nat Cell Biol, 2011
Following tumor necrosis factor stimulation, caspase 8 cleaves CYLD to generate a survival signal.
The E3 ligase Itch and deubiquitinase Cyld act together to regulate Tak1 and inflammation.
Venuprasad et al., Detroit, United States. In Nat Immunol, 2011
we have identified an Itch-Cyld-mediated regulatory mechanism in innate inflammatory cells.
The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation.
Pasparakis et al., Köln, Germany. In Immunity, 2011
The development of skin inflammation in FADD(E-KO) mice was triggered by RIP kinase 3 (RIP3)-mediated programmed necrosis (termed necroptosis) of FADD-deficient keratinocytes, which was partly dependent on the deubiquitinating enzyme CYLD and tumor necrosis factor (TNF)-TNF receptor 1 signaling.
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