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  1. Article ; Online: The Molecular Imaging of Natural Killer Cells.

    Shapovalova, Mariya / Pyper, Sean R / Moriarity, Branden S / LeBeau, Aaron M

    Molecular imaging

    2018  Volume 17, Page(s) 1536012118794816

    Abstract: The recent success of autologous T cell-based therapies in hematological malignancies has spurred interest in applying similar immunotherapy strategies to the treatment of solid tumors. Identified nearly 4 decades ago, natural killer (NK) cells represent ...

    Abstract The recent success of autologous T cell-based therapies in hematological malignancies has spurred interest in applying similar immunotherapy strategies to the treatment of solid tumors. Identified nearly 4 decades ago, natural killer (NK) cells represent an arguably better cell type for immunotherapy development. Natural killer cells are cytotoxic lymphocytes that mediate the direct killing of transformed cells with reduced or absent major histocompatibility complex (MHC) and are the effector cells in antibody-dependent cell-mediated cytotoxicity. Unlike T cells, they do not require human leukocyte antigen (HLA) matching allowing for the adoptive transfer of allogeneic NK cells in the clinic. The development of NK cell-based therapies for solid tumors is complicated by the presence of an immunosuppressive tumor microenvironment that can potentially disarm NK cells rendering them inactive. The molecular imaging of NK cells in vivo will be crucial for the development of new therapies allowing for the immediate assessment of therapeutic response and off-target effects. A number of groups have investigated methods for detecting NK cells by optical, nuclear, and magnetic resonance imaging. In this review, we will provide an overview of the advances made in imaging NK cells in both preclinical and clinical studies.
    MeSH term(s) Humans ; Intravital Microscopy ; Killer Cells, Natural/cytology ; Luminescent Measurements ; Magnetic Resonance Imaging ; Molecular Imaging
    Language English
    Publishing date 2018-09-21
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2137435-1
    ISSN 1536-0121 ; 1535-3508
    ISSN (online) 1536-0121
    ISSN 1535-3508
    DOI 10.1177/1536012118794816
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The Molecular Imaging of Natural Killer Cells

    Mariya Shapovalova / Sean R. Pyper MD, PhD / Branden S. Moriarity PhD / Aaron M. LeBeau PhD

    Molecular Imaging, Vol

    2018  Volume 17

    Abstract: The recent success of autologous T cell-based therapies in hematological malignancies has spurred interest in applying similar immunotherapy strategies to the treatment of solid tumors. Identified nearly 4 decades ago, natural killer (NK) cells represent ...

    Abstract The recent success of autologous T cell-based therapies in hematological malignancies has spurred interest in applying similar immunotherapy strategies to the treatment of solid tumors. Identified nearly 4 decades ago, natural killer (NK) cells represent an arguably better cell type for immunotherapy development. Natural killer cells are cytotoxic lymphocytes that mediate the direct killing of transformed cells with reduced or absent major histocompatibility complex (MHC) and are the effector cells in antibody-dependent cell-mediated cytotoxicity. Unlike T cells, they do not require human leukocyte antigen (HLA) matching allowing for the adoptive transfer of allogeneic NK cells in the clinic. The development of NK cell-based therapies for solid tumors is complicated by the presence of an immunosuppressive tumor microenvironment that can potentially disarm NK cells rendering them inactive. The molecular imaging of NK cells in vivo will be crucial for the development of new therapies allowing for the immediate assessment of therapeutic response and off-target effects. A number of groups have investigated methods for detecting NK cells by optical, nuclear, and magnetic resonance imaging. In this review, we will provide an overview of the advances made in imaging NK cells in both preclinical and clinical studies.
    Keywords Biology (General) ; QH301-705.5 ; Medical technology ; R855-855.5
    Subject code 610 ; 570
    Language English
    Publishing date 2018-09-01T00:00:00Z
    Publisher Hindawi - SAGE Publishing
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: PPARalpha: energy combustion, hypolipidemia, inflammation and cancer.

    Pyper, Sean R / Viswakarma, Navin / Yu, Songtao / Reddy, Janardan K

    Nuclear receptor signaling

    2010  Volume 8, Page(s) e002

    Abstract: The peroxisome proliferator-activated receptor alpha (PPARalpha, or NR1C1) is a nuclear hormone receptor activated by a structurally diverse array of synthetic chemicals known as peroxisome proliferators. Endogenous activation of PPARalpha in liver has ... ...

    Abstract The peroxisome proliferator-activated receptor alpha (PPARalpha, or NR1C1) is a nuclear hormone receptor activated by a structurally diverse array of synthetic chemicals known as peroxisome proliferators. Endogenous activation of PPARalpha in liver has also been observed in certain gene knockout mouse models of lipid metabolism, implying the existence of enzymes that either generate (synthesize) or degrade endogenous PPARalpha agonists. For example, substrates involved in fatty acid oxidation can function as PPARalpha ligands. PPARalpha serves as a xenobiotic and lipid sensor to regulate energy combustion, hepatic steatosis, lipoprotein synthesis, inflammation and liver cancer. Mainly, PPARalpha modulates the activities of all three fatty acid oxidation systems, namely mitochondrial and peroxisomal beta-oxidation and microsomal omega-oxidation, and thus plays a key role in energy expenditure. Sustained activation of PPARalpha by either exogenous or endogenous agonists leads to the development of hepatocellular carcinoma resulting from sustained oxidative and possibly endoplasmic reticulum stress and liver cell proliferation. PPARalpha requires transcription coactivator PPAR-binding protein (PBP)/mediator subunit 1(MED1) for its transcriptional activity.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Energy Metabolism ; Humans ; Inflammation/metabolism ; Lipid Metabolism Disorders/metabolism ; Neoplasms/metabolism ; PPAR alpha/metabolism
    Chemical Substances PPAR alpha
    Language English
    Publishing date 2010-04-16
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2230618-3
    ISSN 1550-7629 ; 1550-7629
    ISSN (online) 1550-7629
    ISSN 1550-7629
    DOI 10.1621/nrs.08002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: PRIC295, a Nuclear Receptor Coactivator, Identified from PPARα-Interacting Cofactor Complex.

    Pyper, Sean R / Viswakarma, Navin / Jia, Yuzhi / Zhu, Yi-Jun / Fondell, Joseph D / Reddy, Janardan K

    PPAR research

    2010  Volume 2010

    Abstract: The peroxisome proliferator-activated receptor-α (PPARα) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPARα in rodents leads to the development of hepatocellular carcinomas. The ability of PPARα to induce expression ... ...

    Abstract The peroxisome proliferator-activated receptor-α (PPARα) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPARα in rodents leads to the development of hepatocellular carcinomas. The ability of PPARα to induce expression of its target genes depends on Mediator, an evolutionarily conserved complex of cofactors and, in particular, the subunit 1 (Med1) of this complex. Here, we report the identification and characterization of PPARα-interacting cofactor (PRIC)-295 (PRIC295), a novel coactivator protein, and show that it interacts with the Med1 and Med24 subunits of the Mediator complex. PRIC295 contains 10 LXXLL signature motifs that facilitate nuclear receptor binding and interacts with PPARα and five other members of the nuclear receptor superfamily in a ligand-dependent manner. PRIC295 enhances the transactivation function of PPARα, PPARγ, and ERα. These data demonstrate that PRIC295 interacts with nuclear receptors such as PPARα and functions as a transcription coactivator under in vitro conditions and may play an important role in mediating the effects in vivo as a member of the PRIC complex with Med1 and Med24.
    Language English
    Publishing date 2010-09-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2237981-2
    ISSN 1687-4765 ; 1687-4757
    ISSN (online) 1687-4765
    ISSN 1687-4757
    DOI 10.1155/2010/173907
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: PRIC295, a Nuclear Receptor Coactivator, Identified from PPAR-Interacting Cofactor Complex

    Sean R. Pyper / Navin Viswakarma / Yuzhi Jia / Yi-Jun Zhu / Joseph D. Fondell / Janardan K. Reddy

    PPAR Research, Vol

    2010  Volume 2010

    Abstract: The peroxisome proliferator-activated receptor- (PPAR) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPAR in rodents leads to the development of hepatocellular carcinomas. The ability of PPAR to induce expression of ... ...

    Abstract The peroxisome proliferator-activated receptor- (PPAR) plays a key role in lipid metabolism and energy combustion. Chronic activation of PPAR in rodents leads to the development of hepatocellular carcinomas. The ability of PPAR to induce expression of its target genes depends on Mediator, an evolutionarily conserved complex of cofactors and, in particular, the subunit 1 (Med1) of this complex. Here, we report the identification and characterization of PPAR-interacting cofactor (PRIC)-295 (PRIC295), a novel coactivator protein, and show that it interacts with the Med1 and Med24 subunits of the Mediator complex. PRIC295 contains 10 LXXLL signature motifs that facilitate nuclear receptor binding and interacts with PPAR and five other members of the nuclear receptor superfamily in a ligand-dependent manner. PRIC295 enhances the transactivation function of PPAR, PPAR, and ER. These data demonstrate that PRIC295 interacts with nuclear receptors such as PPAR and functions as a transcription coactivator under in vitro conditions and may play an important role in mediating the effects in vivo as a member of the PRIC complex with Med1 and Med24.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2010-01-01T00:00:00Z
    Publisher Hindawi Limited
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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  6. Article: Binding linkage in a telomere DNA-protein complex at the ends of Oxytricha nova chromosomes.

    Buczek, Pawel / Orr, Rochelle S / Pyper, Sean R / Shum, Mili / Kimmel, Emily / Ota, Irene / Gerum, Shawn E / Horvath, Martin P

    Journal of molecular biology

    2005  Volume 350, Issue 5, Page(s) 938–952

    Abstract: Alpha and beta protein subunits of the telomere end binding protein from Oxytricha nova (OnTEBP) combine with telomere single strand DNA to form a protective cap at the ends of chromosomes. We tested how protein-protein interactions seen in the co- ... ...

    Abstract Alpha and beta protein subunits of the telomere end binding protein from Oxytricha nova (OnTEBP) combine with telomere single strand DNA to form a protective cap at the ends of chromosomes. We tested how protein-protein interactions seen in the co-crystal structure relate to DNA binding through use of fusion proteins engineered as different combinations of domains and subunits derived from OnTEBP. Joining alpha and beta resulted in a protein that bound single strand telomere DNA with high affinity (K(D-DNA)=1.4 nM). Another fusion protein, constructed without the C-terminal protein-protein interaction domain of alpha, bound DNA with 200-fold diminished affinity (K(D-DNA)=290 nM) even though the DNA-binding domains of alpha and beta were joined through a peptide linker. Adding back the alpha C-terminal domain as a separate protein restored high-affinity DNA binding. The binding behaviors of these fusion proteins and the native protein subunits are consistent with cooperative linkage between protein-association and DNA-binding equilibria. Linking DNA-protein stability to protein-protein contacts at a remote site may provide a trigger point for DNA-protein disassembly during telomere replication when the single strand telomere DNA must exchange between a very stable OnTEBP complex and telomerase.
    MeSH term(s) Animals ; Chromosomes/metabolism ; DNA/metabolism ; Multiprotein Complexes ; Oxytricha/chemistry ; Oxytricha/genetics ; Protein Binding ; Protein Subunits ; Protozoan Proteins ; Recombinant Fusion Proteins ; Telomere/metabolism ; Telomere-Binding Proteins/metabolism
    Chemical Substances Multiprotein Complexes ; Protein Subunits ; Protozoan Proteins ; Recombinant Fusion Proteins ; Telomere-Binding Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 2005-07-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2005.05.040
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
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