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

Tensin 1

TNS, Tensin, tensin1
The protein encoded by this gene localizes to focal adhesions, regions of the plasma membrane where the cell attaches to the extracellular matrix. This protein crosslinks actin filaments and contains a Src homology 2 (SH2) domain, which is often found in molecules involved in signal transduction. This protein is a substrate of calpain II. A second transcript from this gene has been described, but its full length nature has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, PTEN, HAD, Actin
Papers on TNS
Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study.
Sułkowska et al., Sosnowiec, Poland. In Spectrochim Acta A Mol Biomol Spectrosc, Feb 2016
The influence of glycation process on serum albumin binding to 5-dimethylaminonaphthalene-1-sulfonamide (DNSA), 2-(p-toluidino) naphthalene-6-sulfonic acid (TNS), has been studied.
Enhancer of Zeste Homolog 2 Inhibition Attenuates Renal Fibrosis by Maintaining Smad7 and Phosphatase and Tensin Homolog Expression.
Zhuang et al., Providence, United States. In J Am Soc Nephrol, Jan 2016
Moreover, EZH2 inhibition increased the expression of phosphatase and tensin homolog (PTEN), a protein previously associated with dephosphorylation of tyrosine kinase receptors in the injured kidney and serum-stimulated renal interstitial fibroblasts.
Pudendal but not Tibial Nerve Stimulation Inhibits Bladder Contractions Induced by Stimulation of Pontine Micturition Center in Cats.
Tai et al., Pittsburgh, United States. In Am J Physiol Regul Integr Comp Physiol, Jan 2016
UNASSIGNED: This study examined the possibility that pudendal nerve stimulation (PNS) or tibial nerve stimulation (TNS) inhibits the excitatory pathway from the pontine micturition center (PMC) to urinary bladder.
Phosphatase and Tensin Homolog Is a Growth Repressor of Both Rhizoid and Gametophore Development in the Moss Physcomitrella patens.
Malhó et al., Halle, Germany. In Plant Physiol, Dec 2015
Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a lipid phosphatase implicated in cellular proliferation and survival.
Construction, Enzyme Response and Substrate Capacity of Hyaluronan-Cyclodextrin Supramolecular Assembly.
Li et al., Tianjin, China. In Chem Asian J, Dec 2015
In the other hand, substrate binding models were investigated when environment sensitive fluorescence probes 2-p-toluidino-6-naphthalenesulfoniate sodium (2,6-TNS) and Thioflavin T (ThT) were used.
Zebrafish Olfacto-Retinal Centrifugal Axon Projection and Distribution: Effects of Gonadotropin-Releasing Hormone and Dopaminergic Signaling.
Li et al., United States. In Dev Neurosci, Nov 2015
UNASSIGNED: The terminalis neurons (TNs) have been described in teleost species.
Biotinylated Cyclophane: Synthesis, Cyclophane-Avidin Conjugates, and Their Enhanced Guest-Binding Affinity.
Kusano et al., Fukuoka, Japan. In J Org Chem, Nov 2015
The present conjugate of 1a with avidin (1a-avidin) showed an enhanced guest binding affinity toward fluorescence guests such as TNS and 2,6-ANS.
PTEN ceRNA networks in human cancer.
Pandolfi et al., Pisa, Italy. In Methods, May 2015
In multiple human cancer types, a close link exists between the expression levels of Phosphatase and Tensin Homolog deleted on chromosome 10 (PTEN) and its oncosuppressive activities.
Phosphatase and Tensin Homologue: Novel Regulation by Developmental Signaling.
Jerde, Indianapolis, United States. In J Signal Transduct, 2014
Phosphatase and tensin homologue (PTEN) is a critical cell endogenous inhibitor of phosphoinositide signaling in mammalian cells.
Molecular pathways: intercellular PTEN and the potential of PTEN restoration therapy.
Parsons et al., New York City, United States. In Clin Cancer Res, 2014
Phosphatase and Tensin homolog deleted on chromosome Ten (PTEN) acts as a tumor suppressor through both PI3K-dependent and -independent mechanisms.
Molecular physiology of the tensin brotherhood of integrin adaptor proteins.
Haynie, Tampa, United States. In Proteins, 2014
Such findings are recasting the earlier vision of tensin (TNS) as an actin-filament (F-actin) capping protein in a different light.
Roles of PTEN (Phosphatase and Tensin Homolog) in gastric cancer development and progression.
Lu et al., Nanchang, China. In Asian Pac J Cancer Prev, 2013
Functional inactivation of the tumor suppressor protein PTEN (Phosphatase and Tensin Homolog) has been detected in multiple cases of gastric cancer, and already shown to be closely linked to the development, progression and prognosis of the disease.
Effect of five genetic variants associated with lung function on the risk of chronic obstructive lung disease, and their joint effects on lung function.
SpiroMeta Consortium et al., Leicester, United Kingdom. In Am J Respir Crit Care Med, 2011
TNS1 polymorphism associated with COPD risk and lung function decline
Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
Brautigan et al., Charlottesville, United States. In Mol Cell Proteomics, 2010
data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins
Genome-wide association study identifies five loci associated with lung function.
Tobin et al., Leicester, United Kingdom. In Nat Genet, 2010
Data show expression of TNS1, GSTCD, AGER, HTR4 and THSD4 in lung tissue and indicate potential targets for interventions to alleviate respiratory disease.
Tensin1 requires protein phosphatase-1alpha in addition to RhoGAP DLC-1 to control cell polarization, migration, and invasion.
Brautigan et al., Charlottesville, United States. In J Biol Chem, 2010
Results suggest that PP1alpha bound to tensin1 has effects in reducing migration and invasion that are not mediated through DLC-1, and show the importance of PP1alpha binding to tensin1 for the regulation of cell polarization, migration, and invasion.
The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis.
Lowy et al., Bethesda, United States. In Cancer Cell, 2009
In cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis.
[Tensin expression in mesangial cells of human kidney].
Song et al., Harbin, China. In Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi, 2009
The expression of tensin is increased in mesangial cells with stimulating of high concentrations of glucose.
Tn7 transposition: target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system.
Craig et al., San Francisco, United States. In Cell, 1993
Recombination appears to be activated by the assembly of a nucleoprotein complex containing the DNA substrates and Tns proteins.
Presence of an SH2 domain in the actin-binding protein tensin.
Chen et al., Boston, United States. In Science, 1991
The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported.
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