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

Transportin 1

MIP, transportin
This gene encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. Alternate splicing of this gene results in two transcript variants encoding different proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Interleukin-6, MIP-2, CAN, HAD, IL-8
Papers on MIP
Selective solid-phase extraction using molecularly imprinted polymer as a sorbent for the analysis of fenarimol in food samples.
Roy et al., Lucknow, India. In Food Chem, Jun 2016
Binding study of molecularly imprinted and non-imprinted polymer (MIP and NIP) showed that MIP possesses a higher affinity towards this analyte compared to NIP.
Understanding the relationships between molecule structure and imprinting effect of two acetyl-nitrogen heterocyclic compounds.
Luo et al., Beijing, China. In J Mol Recognit, Feb 2016
The TAT-MIP showed excellent imprinting effect, whereas the TRAT-MIP did not.
IL-17 induces MIP-1α expression in primary mouse astrocytes via TRPC channel.
Yao et al., Nanjing, China. In Inflammopharmacology, Feb 2016
UNASSIGNED: Our previous study demonstrated IL-17-mediated induction of MIP-1α through its binding to the cognate IL-17RA and MIP-1α was involved in astrocyte activation.
TCF1 links GIPR signaling to the control of beta cell function and survival.
Drucker et al., Toronto, Canada. In Nat Med, Jan 2016
We demonstrate that mice with selective ablation of GIPR in beta cells (MIP-Cre:Gipr(Flox/Flox); Gipr(-/-βCell)) exhibit lower levels of meal-stimulated insulin secretion, decreased expansion of adipose tissue mass and preservation of insulin sensitivity when compared to MIP-Cre controls.
Molecularly imprinted polymers for separating and sensing of macromolecular compounds and microorganisms.
Kutner et al., Warsaw, Poland. In Biotechnol Adv, Jan 2016
The present review article focuses on gathering, summarizing, and critically evaluating the results of the last decade on separating and sensing macromolecular compounds and microorganisms with the use of molecularly imprinted polymer (MIP) synthetic receptors.
Molecularly imprinted polymer for caffeic acid by precipitation polymerization and its application to extraction of caffeic acid and chlorogenic acid from Eucommia ulmodies leaves.
Haginaka et al., Nishinomiya, Japan. In J Pharm Biomed Anal, Jan 2016
Binding experiments and Scatchard analyses revealed that the binding capacity and affinity of the MIP to CA are higher than those of the NIP.
Molecularly imprinted polymers as recognition materials for electronic tongues.
Kutner et al., Warsaw, Poland. In Biosens Bioelectron, Jan 2016
Merging these two sensing devices led to a synergetic hybrid sensor, an MIP based e-tongue.
Endurance and Resistance Training Affect High Fat Diet-Induced Increase of Ceramides, Inflammasome Expression, and Systemic Inflammation in Mice.
Mooren et al., Gießen, Germany. In J Diabetes Res, Dec 2015
Furthermore, ET reduced levels of MIP-1γ, while RT decreased levels of IL-18, MIP-1γ, Timp-1, and CD40 in serum (p < 0.001), respectively.
Structural Biology and Regulation of Protein Import into the Nucleus.
Kobe et al., Australia. In J Mol Biol, Nov 2015
The pathways involve transport factors that are members of the β-karyopherin family, which can bind cargo directly (e.g., importin-β, transportin-1, transportin-3, importin-13) or through adaptor proteins (e.g., importin-α, snurportin-1, symportin-1), as well as unrelated transport factors such as Hikeshi, involved in the transport of heat-shock proteins, and NTF2, involved in the transport of RanGDP.
The calcium-sensing receptor as a mediator of inflammation.
Garofalo et al., Galveston, United States. In Semin Cell Dev Biol, Sep 2015
We describe in vitro studies in which we demonstrated that peripheral blood mononuclear cells in culture produce the chemokines MIP-1α and RANTES in proportion to the medium calcium concentration and they produce the chemokine MCP-1 in quantities inversely related to medium calcium concentration.
Impaired islet function in commonly used transgenic mouse lines due to human growth hormone minigene expression.
Schraenen et al., Leuven, Belgium. In Cell Metab, 2015
Although this minigene is present in the transgenes as a secondcistron, and thus not thought to be expressed, we found that three commonly used lines, Pdx1-Cre(Late), RIP-Cre, and MIP-GFP, each expressed significant amounts of hGH in pancreatic islets.
[Contemporary concepts in studies on cyclic AMP and its role in the inflammatory reaction].
Wyska et al., Laizhou, China. In Postepy Hig Med Dosw (online), 2014
In the course of the inflammatory response, the increase in cAMP level may lead to an increase in IL-10 expression, inhibition of TNF-α, IL-12, and MIP-1β release, as well as to a reduction inthe permeability of blood vessels.
Arginine methylation of the nuclear poly(a) binding protein weakens the interaction with its nuclear import receptor, transportin.
Wahle et al., Halle, Germany. In J Biol Chem, 2011
Transportin binding might delay methylation of PABPN1 until after nuclear import.
Circulating interleukin (IL)-8, IL-2R, IL-12, and IL-15 levels are independently prognostic in primary myelofibrosis: a comprehensive cytokine profiling study.
Pardanani et al., Rochester, United States. In J Clin Oncol, 2011
RESULTS: In total, 127 PMF patients were studied; comparison with normal controls (n = 35) revealed significantly increased interleukin-1β (IL-1β), IL-1RA, IL-2R, IL-6, IL-8, IL-10, IL-12, IL-13, IL-15, tumor necrosis factor α (TNF-α), granulocyte colony-stimulating factor (G-CSF), interferon alfa (IFN-α), macrophage inflammatory protein 1α (MIP-1α), MIP-1β, hepatocyte growth factor (HGF), IFN-γ-inducible protein 10 (IP-10), monokine induced by IFN-γ (MIG), monocyte chemotactic protein 1 (MCP-1), and vascular endothelial growth factor (VEGF) levels and decreased IFN-γ levels.
Localization of retinitis pigmentosa 2 to cilia is regulated by Importin beta2.
Margolis et al., Ann Arbor, United States. In J Cell Sci, 2011
Data demonstrate that Importin beta2 is necessary for localization of retinitis pigmentosa 2 (RP2) to the primary cilium, and identify two distinct binding sites of RP2, which interact independently with Importin beta2.
The rational development of molecularly imprinted polymer-based sensors for protein detection.
Horgan et al., United Kingdom. In Chem Soc Rev, 2011
In this critical review we describe many methods used for imprinting recognition for protein targets in polymers and their incorporation with a number of transducer platforms with the aim of identifying the most promising approaches for the preparation of MIP-based protein sensors (277 references).
ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import.
Haass et al., München, Germany. In Embo J, 2010
Nuclear import of fused in sarcoma (FUS) is dependent on Transportin, and interference with this transport pathway leads to cytoplasmic redistribution and recruitment of fused in sarcoma (FUS) into stress granules.
A glycine-rich domain of hnRNP H/F promotes nucleocytoplasmic shuttling and nuclear import through an interaction with transportin 1.
McNally et al., Milwaukee, United States. In Mol Cell Biol, 2010
Results suggest that hnRNP H and F are nuclear shuttling proteins whose posttranslational modifications may alter interaction with transportin 1, nuclear localization, and hence function.
Transportin regulates major mitotic assembly events: from spindle to nuclear pore assembly.
Forbes et al., San Diego, United States. In Mol Biol Cell, 2009
The interplay of the two negative regulators, transportin and importin beta, along with the positive regulator RanGTP, allows precise choreography of multiple cell cycle assembly events.
Deficiency of MIP/MTMR14 phosphatase induces a muscle disorder by disrupting Ca(2+) homeostasis.
Qu et al., Cleveland, United States. In Nat Cell Biol, 2009
Here we report that mice deficient in the newly identified PtdInsP (phosphatidylinositol phosphate) phosphatase MIP/MTMR14 (muscle-specific inositol phosphatase) show muscle weakness and fatigue.
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