21 research outputs found

    HNO Binding in a Heme Protein: Structures, Spectroscopic Properties, and Stabilities

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    HNO can interact with numerous heme proteins, but atomic level structures are largely unknown. In this work, various structural models for the first stable HNO heme protein complex, MbHNO (Mb, myoglobin), were examined by quantum chemical calculations. This investigation led to the discovery of two novel structural models that can excellently reproduce numerous experimental spectroscopic properties. They are also the first atomic level structures that can account for the experimentally observed high stabilities. These two models involve two distal His conformations as reported previously for MbCNR and MbNO. However, a unique dual hydrogen bonding feature of the HNO binding was not reported before in heme protein complexes with other small molecules such as CO, NO, and O<sub>2</sub>. These results shall facilitate investigations of HNO bindings in other heme proteins

    Unprecedented Fe(IV) Species in a Diheme Protein MauG: A Quantum Chemical Investigation on the Unusual Mössbauer Spectroscopic Properties

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    Ferryl species are important catalytic intermediates in heme enzymes. A recent experimental investigation of a diheme protein MauG reported the first case of using two Fe(IV) species as an alternative to compound I in catalysis. Both Fe(IV) species have unusual Mössbauer properties, which was found to originate from novel structural features based on a quantum chemical investigation. With comparison with the previously reported Fe<sup>IV</sup>O and Fe<sup>IV</sup>−OH species, results here provide evidence of new mechanisms by which proteins influence the properties of ferryl species by directly providing the O via Tyr or stabilizing exogenous O via hydrogen bonding interaction. These results expand our ability to identify and evaluate high-valent heme proteins and models

    The region of TFIIS containing the LW motif mediates a protein–protein interaction

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    <p><b>Copyright information:</b></p><p>Taken from "A sequence motif conserved in diverse nuclear proteins identifies a protein interaction domain utilised for nuclear targeting by human TFIIS"</p><p>Nucleic Acids Research 2006;34(8):2219-2229.</p><p>Published online 28 Apr 2006</p><p>PMCID:PMC1450333.</p><p>© The Author 2006. Published by Oxford University Press. All rights reserved</p> Pull-down assay of S-labelled hIWS1 binding to immobilized GST-fusion proteins containing regions of TFIIS (indicated above the lanes). Graphical representation of this data is shown below in comparison with 20% of the labelled input protein and a pull-down using GST alone

    Table_1_Long Non-coding Antisense RNA TNRC6C-AS1 Is Activated in Papillary Thyroid Cancer and Promotes Cancer Progression by Suppressing TNRC6C Expression.DOCX

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    <p>Context: Evidences have shown the important role of long non-coding antisense RNAs in regulating its cognate sense gene in cancer biology.</p><p>Objective: Investigate the regulatory role of a long non-coding antisense RNA TNRC6C-AS1 on its sense partner TNRC6C, and their effects on the aggressiveness and iodine-uptake ability of papillary thyroid cancer (PTC).</p><p>Design: TNRC6C-AS1 was identified as the target long non-coding RNA in PTC by using microarray analysis and computational analysis. In vitro gain/loss-of-function experiments were performed to investigate the effects of TNRC6C-AS1 and TNRC6C on proliferation, apoptosis, migration, invasion and iodine-uptake ability of TPC1 cells. Expression levels of TNRC6C-AS1 and TNRC6C of 30 cases of PTC tissues and its adjacent normal thyroid tissues were determined.</p><p>Results: Downregulation of TNRC6C-AS1 or overexpression of TNRC6C inhibited proliferation, migration and invasion of TPC1 cells, while apoptosis and iodine uptake was promoted in TPC1 cells. Suppression of TNRC6C-AS1 significantly increased the expression of TNRC6C in TPC1 cells. The inhibitory effect of TNRC6C-AS1 knockdown on cell proliferation, migration and invasion was attenuated when the expression of TNRC6C was suppressed simultaneously, indicating TNRC6C is a functional target of TNRC6C-AS1. The expression of TNRC6C-AS1 was significantly higher, while the TNRC6C mRNA and protein were significantly lower in PTC tissues than normal adjacent tissues. There was a significant inverse correlation between TNRC6C-AS1 and TNRC6C mRNA in PTC tissue samples.</p><p>Conclusions: TNRC6C-AS1 promotes the progression of PTC and inhibits its ability of iodine accumulation by suppressing the expression of TNRC6C. Targeting TNRC6C-AS1 - TNRC6C axis may be a new promising treatment for PTC.</p

    Safety and Effectiveness of Natalizumab: First Report of Interim Results of Post-Marketing Surveillance in Japan

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    <p><b>Article full text</b></p> <p><br></p> <p>The full text of this article can be found here<b>. </b><a href="https://link.springer.com/article/10.1007/s40120-017-0084-6">https://link.springer.com/article/10.1007/s40120-017-0084-6</a></p><p></p> <p><br></p> <p><b>Provide enhanced content for this article</b></p> <p><br></p> <p>If you are an author of this publication and would like to provide additional enhanced content for your article then please contact <a href="http://www.medengine.com/Redeem/”mailto:[email protected]”"><b>[email protected]</b></a>.</p> <p><br></p> <p>The journal offers a range of additional features designed to increase visibility and readership. All features will be thoroughly peer reviewed to ensure the content is of the highest scientific standard and all features are marked as ‘peer reviewed’ to ensure readers are aware that the content has been reviewed to the same level as the articles they are being presented alongside. Moreover, all sponsorship and disclosure information is included to provide complete transparency and adherence to good publication practices. This ensures that however the content is reached the reader has a full understanding of its origin. No fees are charged for hosting additional open access content.</p> <p><br></p> <p>Other enhanced features include, but are not limited to:</p> <p><br></p> <p>• Slide decks</p> <p>• Videos and animations</p> <p>• Audio abstracts</p> <p>• Audio slides</p

    Overexpression and purification of Rv3852 in <i>E</i>. <i>coli</i>.

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    <p>Coomassie blue stained 12% SDS-PAGE. Lane 1: uninduced lysate; Lane 2: IPTG induced lysate; Lane 3: cytosolic fraction of IPTG induced lysate; Lane 4: membrane fraction of IPTG induced lysate (1% Triton-X100); Lane 5: purified Rv3852 (0.1% Triton-X100). Arrow indicates recombinant Rv3852.</p

    Identification of Mb3882.

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    <p>Detected sequences in MALDI-TOF MS are highlighted in bold. The 5 tetrapeptide repeats (4 PAKK and 1 KKAP) are italicized. Mb3882 was not identified in the DMSO treated group.</p><p>Identification of Mb3882.</p

    EMSA.

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    <p>(A) Recombinant Rv3852 abrogated the mobility of proU2 on 1% agarose gel. (B) agrimophol or a1 interfered with recombinant Rv3852’s mobility shift of proU2 on 1% agarose gel in a concentration-dependent manner.</p

    Survival of WT and KO in Pcit-Tyl-4.5 at indicated time points.

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    <p>Means ± S. E. M. of triplicate samples represent three independent experiments. Some error bars are smaller than the symbols.</p
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