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  • 1
    Electronic Resource
    Electronic Resource
    Effect of nitridation on magnetic properties of Fe53Pt47 thin film (2002)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 91 (2002), S. 3145-3149 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The Fe53Pt47 thin films with varying thickness were prepared using dc magnetron sputtering at various substrate temperatures (i.e., from 250 to 600 °C) on to CrMo seeded glass substrates. The powder x-ray diffraction studies reveal that the ordered fct γ2-FePt phase begins to appear starting from the substrate temperature of 250 °C. The estimated ordering parameters show that the films prepared at 300 °C are well ordered and ordering parameters increase slowly as increasing substrate temperatures. On nitridation of the Fe53Pt47 thin films, expansion of the face centered tetragonal crystal lattice along the c axis is observed. The saturation magnetization is decreased with decreasing film thickness. This has been explained mainly on the basis of size and surface effects of nanocrystals in the films including intergranular interactions. Maximum coercivity of 8.7 kOe is observed for the film thickness of 350 nm. The drastic decrease in magnetization with the increase in nitridation time duration has been attributed to the spin pairing effects as a result of electron supply from interstitial nitrogen atoms to the 3d bands of iron atoms. We observed an increase of Hc from 7.8 kOe for non-nitrided Fe53Pt47 film to 10.8 kOe for a 3 h nitrided film. © 2002 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1436301
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  • 2
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    {beta}2 integrin-derived signals induce cell survival and proliferation of AML blasts by activating a Syk/STAT signaling axis (2013)
    American Society of Hematology (ASH)
    In: Blood
    Details
    Publication Date: 2013-05-10
    Description: Spleen tyrosine kinase (Syk) induces cell survival and proliferation in a high proportion of acute myeloid leukemia (AML) blasts, but the underlying molecular events of Syk signaling have not been investigated. Proteomic techniques have allowed us to identify the multiprotein complex that is nucleated by constitutively active Syk in AML cells. This complex differs from the B-lymphoid Syk interactome with respect to several proteins, especially the integrin receptor Mac-1, the Fc- receptor I (FcRI), and the transcription factors STAT3 and STAT5. We show in several AML cell line models that tonic signals derived from the Fc- chain lead to Syk-dependent activation of STAT3 and STAT5, which in turn induces cell survival and proliferation. Moreover, stimulation of Mac-1 or FcRI intensifies the constitutive Syk-mediated STAT3/5 activation in AML cells, a scenario likely to take place in the bone marrow niche. In accordance with these findings, we observed that β 2 integrins, including Mac-1, trigger proliferation of AML cells in an AML cell/stroma coculture model. Taken together, we identified an oncogenic integrin/Syk/STAT3/5 signaling axis that might serve as a therapeutic target of AML in the future.
    Keywords: Myeloid Neoplasia
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology (ASH)
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  • 3
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    Sumoylation of Ran by RanBP2 [Enzymology] (2015)
    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Details
    Publication Date: 2015-09-26
    Description: The SUMO E3 ligase complex RanBP2/RanGAP1*SUMO1/Ubc9 localizes at cytoplasmic nuclear pore complex (NPC) filaments and is a docking site in nucleocytoplasmic transport. RanBP2 has four Ran binding domains (RBDs), two of which flank RanBP2's E3 ligase region. We thus wondered whether the small GTPase Ran is a target for RanBP2-dependent sumoylation. Indeed, Ran is sumoylated both by a reconstituted and the endogenous RanBP2 complex in semi-permeabilized cells. Generic inhibition of SUMO isopeptidases or depletion of the SUMO isopeptidase SENP1 enhances sumoylation of Ran in semi-permeabilized cells. As Ran is typically associated with transport receptors, we tested the influence of Crm1, Imp β, Transportin, and NTF2 on Ran sumoylation. Surprisingly, all inhibited Ran sumoylation. Mapping Ran sumoylation sites revealed that transport receptors may simply block access of the E2-conjugating enzyme Ubc9, however the acceptor lysines are perfectly accessible in Ran/NTF2 complexes. Isothermal titration calorimetry revealed that NTF2 prevents sumoylation by reducing RanGDP's affinity to RanBP2's RBDs to undetectable levels. Taken together, our findings indicate that RanGDP and not RanGTP is the physiological target for the RanBP2 SUMO E3 ligase complex. Recognition requires interaction of Ran with RanBP2's RBDs, which is prevented by the transport factor NTF2.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
    Published by The American Society for Biochemistry and Molecular Biology (ASBMB)
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  • 4
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    Aging predisposes to acute inflammatory induced pathology after tumor immunotherapy (2013)
    Rockefeller University Press
    Details
    Publication Date: 2013-10-22
    Description: Cancer commonly occurs in the elderly and immunotherapy (IT) is being increasingly applied to this population. However, the majority of preclinical mouse tumor models assessing potential efficacy and toxicities of therapeutics use young mice. We assessed the impact of age on responses to systemic immune stimulation. In contrast to young mice, systemic cancer IT regimens or LPS given to aged mice resulted in rapid and lethal toxicities affecting multiple organs correlating with heightened proinflammatory cytokines systemically and within the parenchymal tissues. This inflammatory response and increased morbidity with age was independent of T cells or NK cells. However, prior in vivo depletion of macrophages in aged mice resulted in lesser cytokine levels, increased survival, and decreased liver histopathology. Furthermore, macrophages from aged mice and normal human elderly volunteers displayed heightened TNF and IL-6 production upon in vitro stimulation. Treatment of both TNF knockout mice and in vivo TNF blockade in aged mice resulted in significant increases in survival and lessened pathology. Importantly, TNF blockade in tumor-bearing, aged mice receiving IT displayed significant anti-tumor effects. These data demonstrate the critical role of macrophages in the age-associated hyper-inflammatory cytokine responses to systemic immunostimulation and underscore the importance of performing preclinical assessments in aged mice.
    Print ISSN: 0022-1007
    Electronic ISSN: 1540-9538
    Topics: Medicine
    Published by Rockefeller University Press
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  • 5
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    Cutting Edge: Feed-Forward Activation of Phospholipase C{gamma}2 via C2 Domain-Mediated Binding to SLP65 [CUTTING EDGE] (2013)
    The American Association of Immunologists (AAI)
    Details
    Publication Date: 2013-11-16
    Description: Ag-mediated B cell stimulation relies on phospholipase C2 (PLC2) for Ca 2+ mobilization. Enzymatic activity of PLC2 is triggered upon Src homology 2 domain–mediated binding to the tyrosine-phosphorylated adaptor SLP65. However, SLP65 phosphorylation outlasts the elevation of cytosolic Ca 2+ concentration suggesting additional levels of PLC2 regulation. We show in this article that the functionality of the PLC2/SLP65 complex is controlled by the weakly characterized C2 domain of PLC2. Usually C2 domains bind membrane lipids, but that of PLC2 docks in a Ca 2+ -regulated manner to a distinct phosphotyrosine of SLP65. Hence, early Ca 2+ fluxing provides feed-forward signal amplification by promoting anchoring of the PLC2 C2 domain to phospho-SLP65. As the cellular Ca 2+ resources become exhausted, the concomitant decline of Ca 2+ dampens the C2-phosphotyrosine interaction so that PLC2 activation terminates despite sustained SLP65 phosphorylation.
    Print ISSN: 0022-1767
    Electronic ISSN: 1550-6606
    Topics: Medicine
    Published by The American Association of Immunologists (AAI)
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  • 6
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    His6-HA-SUMO1 knock-in mice [Neuroscience] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-12-19
    Description: SUMOylation, an essential posttranslational protein modification, is involved in many eukaryotic cellular signaling pathways. The identification of SUMOylated proteins is difficult, because SUMOylation sites in proteins are hard to predict, SUMOylated protein states are transient in vivo and labile in vitro, only a small substrate fraction is SUMOylated in vivo,...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    IFN-{gamma} Receptor-Deficient Donor T Cells Mediate Protection from Graft-versus-Host Disease and Preserve Graft-versus-Tumor Responses after Allogeneic Bone Marrow Transplantation [CLINICAL IMMUNOLOGY] (2012)
    The American Association of Immunologists (AAI)
    Details
    Publication Date: 2012-08-03
    Description: Graft-versus-host disease (GVHD) is a major complication of allogeneic bone marrow transplantation. It has been previously reported that lung GVHD severity directly correlates with the expansion of donor Th17 cells in the absence of IFN-. However, the consequence of Th17-associated lung GVHD in the presence of IFN- has not been well characterized. In the current study, T cells from IFN- receptor knockout (IFN-R –/– ) mice, capable of producing IFN- but unable to signal in response to IFN-, have been used to elucidate further the role of IFN- in GVHD. We found the transfer of donor T cells from either IFN-R –/– or IFN- knockout (IFN- –/– ) mice resulted in significant increases in donor Th17 cells in the lung. Marked increases in IL-4–producing Th2 cells infiltrating the lungs were also observed in the mice of donor IFN-R –/– T cells. Notably, despite the presence of these cells, these mice did not show the severe immune-mediated histopathological lung injury observed in mice receiving donor IFN- –/– T cells. Increases in lung GVHD did occur in mice with donor IFN-R –/– T cells when treated in vivo with anti–IFN- demonstrating that the cytokine has a protective role on host tissues in GVHD. A survival benefit from acute GVHD was also observed using donor cells from IFN-R –/– T cells compared with control donors. Importantly, tumor-bearing mice receiving IFN-R –/– T cells versus wild-type donor T cells displayed similar graft-versus-tumor (GVT) effects. These results demonstrate the critical role of IFN- on host tissues and cell effector functions in GVHD/GVT.
    Print ISSN: 0022-1767
    Electronic ISSN: 1550-6606
    Topics: Medicine
    Published by The American Association of Immunologists (AAI)
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  • 8
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    The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA [Research Papers] (2012)
    Cold Spring Harbor Laboratory Press
    Details
    Publication Date: 2012-11-02
    Description: The spliceosomal RNA helicase Brr2 catalyzes unwinding of the U4/U6 snRNA duplex, an essential step for spliceosome catalytic activation. Brr2 is regulated in part by the spliceosomal Prp8 protein by an unknown mechanism. We demonstrate that the RNase H (RH) domain of yeast Prp8 binds U4/U6 small nuclear RNA (snRNA) with the single-stranded regions of U4 and U6 preceding U4/U6 stem I, contributing to its binding. Via cross-linking coupled with mass spectrometry, we identify RH domain residues that contact the U4/U6 snRNA. We further demonstrate that the same single-stranded region of U4 preceding U4/U6 stem I is recognized by Brr2, indicating that it translocates along U4 and first unwinds stem I of the U4/U6 duplex. Finally, we show that the RH domain of Prp8 interferes with U4/U6 unwinding by blocking Brr2's interaction with the U4 snRNA. Our data reveal a novel mechanism whereby Prp8 negatively regulates Brr2 and potentially prevents premature U4/U6 unwinding during splicing. They also support the idea that the RH domain acts as a platform for the exchange of U6 snRNA for U1 at the 5' splice site. Our results provide insights into the mechanism whereby Brr2 unwinds U4/U6 and show how this activity is potentially regulated prior to spliceosome activation.
    Print ISSN: 0890-9369
    Topics: Biology
    Published by Cold Spring Harbor Laboratory Press
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  • 9
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    Structure and activity of the only human RNase T2 (2012)
    Oxford University Press
    Details
    Publication Date: 2012-09-27
    Description: Mutations in the gene of human RNase T2 are associated with white matter disease of the human brain. Although brain abnormalities (bilateral temporal lobe cysts and multifocal white matter lesions) and clinical symptoms (psychomotor impairments, spasticity and epilepsy) are well characterized, the pathomechanism of RNase T2 deficiency remains unclear. RNase T2 is the only member of the Rh/T2/S family of acidic hydrolases in humans. In recent years, new functions such as tumor suppressing properties of RNase T2 have been reported that are independent of its catalytic activity. We determined the X-ray structure of human RNase T2 at 1.6 Å resolution. The α+β core fold shows high similarity to those of known T2 RNase structures from plants, while, in contrast, the external loop regions show distinct structural differences. The catalytic features of RNase T2 in presence of bivalent cations were analyzed and the structural consequences of known clinical mutations were investigated. Our data provide further insight into the function of human RNase T2 and may prove useful in understanding its mode of action independent of its enzymatic activity.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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