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

Tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase

tankyrase, tankyrase 1, TNKS
Top mentioned proteins: POLYMERASE, TRF1, CAN, Axin, tankyrase 2
Papers on tankyrase
Development and structural analysis of adenosine site binding tankyrase inhibitors.
New
Lehtiö et al., Oulu, Finland. In Bioorg Med Chem Lett, Feb 2016
The scaffold also enables a fine modulation of selectivity towards either tankyrase 1 or tankyrase 2. In order to get insight about the binding mode of the inhibitors, we solved crystal structures of the compounds in complex with tankyrase 2. The compounds bind to the adenosine pocket of the catalytic domain and cause changes in the protein structure that are modulated by the chemical modifications of the compounds.
Induction of Functional 3D Ciliary Epithelium-Like Structure From Mouse Induced Pluripotent Stem Cells.
New
Takahashi et al., Nagasaki, Japan. In Invest Ophthalmol Vis Sci, Feb 2016
In addition, tankyrase inhibitor prevented the induction of the CE-like double-layered structure by GSK-3β inhibitor.
Tankyrase Inhibition Causes Reversible Intestinal Toxicity in Mice with a Therapeutic Index < 1.
New
Schutten et al., San Francisco, United States. In Toxicol Pathol, Jan 2016
Wnt inhibitors, including tankyrase inhibitors, are being explored as potential anticancer agents.
Tankyrase inhibition impairs directional migration and invasion of lung cancer cells by affecting microtubule dynamics and polarity signals.
New
Trusolino et al., Torino, Italy. In Bmc Biol, Dec 2015
Using a panel of lung cancer cell lines as a model system, we found that abrogation of tankyrase activity by two different, structurally unrelated small-molecule inhibitors (one introduced and characterized here for the first time) or by RNA interference-based genetic silencing weakened cell migration, invasion, and directional movement induced by the motogenic cytokine hepatocyte growth factor.
Loss of ATRX Suppresses Resolution of Telomere Cohesion to Control Recombination in ALT Cancer Cells.
New
Impact
Smith et al., New York City, United States. In Cancer Cell, Oct 2015
In the absence of ATRX, the histone variant macroH2A1.1 binds to the poly(ADP-ribose) polymerase tankyrase 1, preventing it from localizing to telomeres and resolving cohesion.
Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal.
New
Impact
Xu et al., Seattle, United States. In Nature, Feb 2015
Second, we find that RNF146 directly interacts with the PAR polymerase tankyrase (TNKS).
Chemical Disruption of Wnt-dependent Cell Fate Decision-making Mechanisms in Cancer and Regenerative Medicine.
Review
Chen et al., Dallas, United States. In Curr Med Chem, 2014
In this review, we will discuss how medicinal chemistry efforts focused on first in class small molecules targeting two Wnt pathway components - the polytopic Porcupine (Porcn) acyltransferase and the cytoplasmic Tankyrase (Tnks) poly-ADP-ribosylases - have contributed to our understanding of the druggable genome and expanded the armamentarium of chemicals that can be used to influence cell fate decision-making.
Human Cytomegalovirus Inhibits the PARsylation Activity of Tankyrase-A Potential Strategy for Suppression of the Wnt Pathway.
Arav-Boger et al., Baltimore, United States. In Viruses, 2014
Since Tankyrase (TNKS) negatively regulates Axin1, we investigated the effect of HCMV on TNKS expression and poly-ADP ribose polymerase (PARsylation) activity, during virus replication.
Recent advances in the structure-based rational design of TNKSIs.
Review
Liu et al., Jinan, China. In Mol Biosyst, 2014
This article provides a fairly comprehensive overview of the structural biology of the TNKS-inhibitor complex and the current medicinal chemistry strategies being used in the structure-based rational design of tankyrase-specific inhibitors.
New PARP targets for cancer therapy.
Impact
Chang et al., Cambridge, United States. In Nat Rev Cancer, 2014
The best-studied PARPs generate PAR modifications and include PARP1 and the tankyrase PARP5A, both of which are targets for cancer therapy with inhibitors in either clinical trials or preclinical development.
The antimitotic potential of PARP inhibitors, an unexplored therapeutic alternative.
Review
Costoya et al., Santiago de Compostela, Spain. In Curr Top Med Chem, 2013
One of these processes is the assembly and maintenance of the mitotic spindle where the presence of PARP-1 and tankyrase 1 (TNKS1), two of the best-characterized members of the PARP superfamily, is of critical importance.
Tankyrase inhibitors as therapeutic targets for cancer.
Review
Rahim et al., Hyderābād, India. In Curr Top Med Chem, 2013
Tankyrase 1 and 2 belonging to the family of poly(ADP-ribosyl)ases play an important role in PARsylation by utilizing NAD+ as a substrate in order to generate ADP-ribose polymers.
Review of poly (ADP-ribose) polymerase (PARP) mechanisms of action and rationale for targeting in cancer and other diseases.
Review
Boothman et al., Dallas, United States. In Crit Rev Eukaryot Gene Expr, 2013
Other PARP forms, including tankyrase 1 (PARP 5a), which plays an important role in enhancing telomere elongation by telomerase, have been found to be potential targets in cancer therapy.
Proteasome regulation by ADP-ribosylation.
Impact
Steller et al., New York City, United States. In Cell, 2013
We identify the ADP-ribosyltransferase tankyrase (TNKS) and the 19S assembly chaperones dp27 and dS5b as direct binding partners of the proteasome regulator PI31.
Tankyrase-targeted therapeutics: expanding opportunities in the PARP family.
Review
Impact
Ashworth et al., London, United Kingdom. In Nat Rev Drug Discov, 2012
Efforts to pharmacologically target PARP enzymes have largely focused on PARP1 and the closely related PARP2, but recent work highlighting the role of another family member, tankyrase 1 (TANK1; also known as PARP5A and ARTD5), in the control of WNT signalling has fuelled interest in the development of additional inhibitors to target this enzyme class.
GDP-mannose-4,6-dehydratase is a cytosolic partner of tankyrase 1 that inhibits its poly(ADP-ribose) polymerase activity.
GeneRIF
Smith et al., New York City, United States. In Mol Cell Biol, 2012
GMD inhibits tankyrase 1 poly(ADP-ribose) polymerase activity in vitro, dependent on the GMD tankyrase 1 binding motif. In vivo, depletion of GMD led to degradation of tankyrase 1, dependent on the catalytic PARP activity of tankyrase 1.
Tankyrase 1 regulates centrosome function by controlling CPAP stability.
GeneRIF
Smith et al., New York City, United States. In Embo Rep, 2012
CPAP degradation and function is controlled by the poly(ADP-ribose) polymerase tankyrase 1.
Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment.
GeneRIF
Xu et al., Seattle, United States. In Proc Natl Acad Sci U S A, 2012
analyses also reveal the structural basis for TNKS substrate recruitment, and shed light on the overall structure of TNKS that should help in developing specific inhibitors of Wnt/beta-catenin signaling
Expression of TNKS1 is correlated with pathologic grade and Wnt/β-catenin pathway in human astrocytomas.
GeneRIF
Yang et al., Changsha, China. In J Clin Neurosci, 2012
TNKS1 may have a key role in astrocytomas through its involvement in the Wnt/beta-catenin signaling pathway.
Novel binding mode of a potent and selective tankyrase inhibitor.
GeneRIF
Huang et al., Cambridge, United States. In Plos One, 2011
crystal structure of the catalytic domain of TNKS1 in complex with IWR2, which reveals a novel binding site for tankyrase inhibitors
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