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  • 1
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    13-LOX and leaf senescence [Plant Biology] (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-03-24
    Description: Leaf senescence is the terminal stage in the development of perennial plants. Massive physiological changes occur that lead to the shut down of photosynthesis and a cessation of growth. Leaf senescence involves the selective destruction of the chloroplast as the site of photosynthesis. Here, we show that 13-lipoxygenase (13-LOX) accomplishes...
    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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  • 2
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    Rescaling MO [Engineering] (2015)
    National Academy of Sciences
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    Publication Date: 2015-07-01
    Description: Nanocrystals are promising structures, but they are too large for achieving maximum energy storage performance. We show that rescaling 3-nm particles through lithiation followed by delithiation leads to high-performance energy storage by realizing high capacitance close to the theoretical capacitance available via ion-to-atom redox reactions. Reactive force-field (ReaxFF) molecular dynamics...
    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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  • 3
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    Vector-free microfluidic delivery platform [Applied Biological Sciences] (2013)
    National Academy of Sciences
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    Publication Date: 2013-02-06
    Description: Intracellular delivery of macromolecules is a challenge in research and therapeutic applications. Existing vector-based and physical methods have limitations, including their reliance on exogenous materials or electrical fields, which can lead to toxicity or off-target effects. We describe a microfluidic approach to delivery in which cells are mechanically deformed as...
    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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  • 4
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    Purinergic signaling in human pluripotent stem cells is regulated by the housekeeping gene encoding hypoxanthine guanine phosphoribosyltransferase [Developmental Biology] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-02-29
    Description: Lesch–Nyhan disease (LND) is an X-linked genetic disorder caused by mutations of the hypoxanthine guanine phosphoribosyltransferase (HPRT) purine biosynthesis gene and characterized by aberrant purine metabolism, deficient basal ganglia dopamine levels, dystonia, and severe neurobehavioral manifestations, including compulsive self-injurious behavior. Although available evidence has identified important roles for purinergic signaling in brain development, the mechanisms linking HPRT deficiency, purinergic pathways, and neural dysfunction of LND are poorly understood. In these studies aimed at characterizing purinergic signaling in HPRT deficiency, we used a lentivirus vector stably expressing an shRNA targeted to the HPRT gene to produce HPRT-deficient human CVB induced pluripotent stem cells and human HUES11 embryonic stem cells. Both CVB and HUES11 cells show 〉99% HPRT knockdown and demonstrate markedly decreased expression of the purinergic P2Y1 receptor mRNA. In CVB cells, P2Y1 mRNA and protein down-regulation by HPRT knockdown is refractory to activation by the P2Y1 receptor agonist ATP and shows aberrant purinergic signaling, as reflected by marked deficiency of the transcription factor pCREB and constitutive activation of the MAP kinases phospho-ERK1/2. Moreover, HPRT-knockdown CVB cells also demonstrate marked reduction of phosphorylated β-catenin. These results indicate that the housekeeping gene HPRT regulates purinergic signaling in pluripotent human stem cells, and that this regulation occurs at least partly through aberrant P2Y1-mediated expression and signaling. We propose that such mechanisms may play a role in the neuropathology of HPRT-deficiency LND and may point to potential molecular targets for modulation of this intractable neurological phenotype.
    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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  • 5
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    CaP matrix-induced stem cell differentiation [Cell Biology] (2014)
    National Academy of Sciences
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    Publication Date: 2014-01-22
    Description: Synthetic matrices emulating the physicochemical properties of tissue-specific ECMs are being developed at a rapid pace to regulate stem cell fate. Biomaterials containing calcium phosphate (CaP) moieties have been shown to support osteogenic differentiation of stem and progenitor cells and bone tissue formation. By using a mineralized synthetic matrix mimicking...
    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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  • 6
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    Epigenetic modification of Nrf2 in 5-fluorouracil-resistant colon cancer cells: involvement of TET-dependent DNA demethylation (2014)
    Springer Nature
    Details
    Publication Date: 2014-04-18
    Description: Epigenetic modification of Nrf2 in 5-fluorouracil-resistant colon cancer cells: involvement of TET-dependent DNA demethylation Cell Death and Disease 5, e1183 (April 2014). doi:10.1038/cddis.2014.149 Authors: K A Kang, M J Piao, K C Kim, H K Kang, W Y Chang, I C Park, Y S Keum, Y J Surh & J W Hyun
    Keywords: colon cancer cells5-fluorouracil resistanceepigenetic modificationDNA demethylaseNrf2oxidative stress
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 7
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    Endothelial apoptosis as the primary lesion initiating intestinal radiation damage in mice (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-14
    Description: Gastrointestinal (GI) tract damage by chemotherapy or radiation limits their efficacy in cancer treatment. Radiation has been postulated to target epithelial stem cells within the crypts of Lieberkuhn to initiate the lethal GI syndrome. Here, we show in mouse models that microvascular endothelial apoptosis is the primary lesion leading to stem cell dysfunction. Radiation-induced crypt damage, organ failure, and death from the GI syndrome were prevented when endothelial apoptosis was inhibited pharmacologically by intravenous basic fibroblast growth factor (bFGF) or genetically by deletion of the acid sphingomyelinase gene. Endothelial, but not crypt, cells express FGF receptor transcripts, suggesting that the endothelial lesion occurs before crypt stem cell damage in the evolution of the GI syndrome. This study provides a basis for new approaches to prevent radiation damage to the bowel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paris, F -- Fuks, Z -- Kang, A -- Capodieci, P -- Juan, G -- Ehleiter, D -- Haimovitz-Friedman, A -- Cordon-Cardo, C -- Kolesnick, R -- CA52462/CA/NCI NIH HHS/ -- CA85704/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 13;293(5528):293-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Signal Transduction and, Department of Radiation Oncology, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11452123" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Annexin A5/metabolism ; *Apoptosis/drug effects/radiation effects ; Bone Marrow/radiation effects ; Bone Marrow Transplantation ; Capillaries ; Endothelium, Vascular/drug effects/pathology/*radiation effects ; Fibroblast Growth Factors/pharmacology ; Humans ; In Situ Nick-End Labeling ; Intestinal Mucosa/blood supply/cytology/pathology/*radiation effects ; Intestines/blood supply/pathology/*radiation effects ; Mice ; Mice, Inbred C57BL ; Neoplasms/pathology/radiotherapy ; Receptors, Fibroblast Growth Factor/metabolism ; Sphingomyelin Phosphodiesterase/deficiency/genetics/metabolism ; Stem Cells/radiation effects ; Tumor Suppressor Protein p53/deficiency/metabolism ; Whole-Body Irradiation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Development of transgenic fungi that kill human malaria parasites in mosquitoes (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-26
    Description: Metarhizium anisopliae infects mosquitoes through the cuticle and proliferates in the hemolymph. To allow M. anisopliae to combat malaria in mosquitoes with advanced malaria infections, we produced recombinant strains expressing molecules that target sporozoites as they travel through the hemolymph to the salivary glands. Eleven days after a Plasmodium-infected blood meal, mosquitoes were treated with M. anisopliae expressing salivary gland and midgut peptide 1 (SM1), which blocks attachment of sporozoites to salivary glands; a single-chain antibody that agglutinates sporozoites; or scorpine, which is an antimicrobial toxin. These reduced sporozoite counts by 71%, 85%, and 90%, respectively. M. anisopliae expressing scorpine and an [SM1](8):scorpine fusion protein reduced sporozoite counts by 98%, suggesting that Metarhizium-mediated inhibition of Plasmodium development could be a powerful weapon for combating malaria.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153607/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153607/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fang, Weiguo -- Vega-Rodriguez, Joel -- Ghosh, Anil K -- Jacobs-Lorena, Marcelo -- Kang, Angray -- St Leger, Raymond J -- 5R21A1079429-02/PHS HHS/ -- R01 AI031478/AI/NIAID NIH HHS/ -- R21 AI079429/AI/NIAID NIH HHS/ -- R21 AI088033/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2011 Feb 25;331(6020):1074-7. doi: 10.1126/science.1199115.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Entomology, University of Maryland, 4112 Plant Sciences Building, College Park, MD 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles gambiae/*microbiology/*parasitology/physiology ; Antibodies, Protozoan/immunology ; Base Sequence ; Cloning, Molecular ; Defensins/genetics/metabolism ; Feeding Behavior ; Female ; Hemolymph/metabolism/microbiology/parasitology ; Humans ; Insect Vectors/*microbiology/*parasitology/physiology ; Malaria, Falciparum/transmission ; Metarhizium/*genetics/physiology ; Molecular Sequence Data ; Oligopeptides/genetics/metabolism ; Organisms, Genetically Modified ; Pest Control, Biological ; Plasmodium falciparum/*physiology ; Protozoan Proteins/immunology ; Salivary Glands/metabolism/parasitology ; Spores, Fungal/physiology ; Sporozoites/physiology ; Transformation, Genetic ; Transgenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
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    Structure and reactivity of a mononuclear non-haem iron(III)-peroxo complex (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-28
    Description: Oxygen-containing mononuclear iron species--iron(III)-peroxo, iron(III)-hydroperoxo and iron(IV)-oxo--are key intermediates in the catalytic activation of dioxygen by iron-containing metalloenzymes. It has been difficult to generate synthetic analogues of these three active iron-oxygen species in identical host complexes, which is necessary to elucidate changes to the structure of the iron centre during catalysis and the factors that control their chemical reactivities with substrates. Here we report the high-resolution crystal structure of a mononuclear non-haem side-on iron(III)-peroxo complex, [Fe(III)(TMC)(OO)](+). We also report a series of chemical reactions in which this iron(III)-peroxo complex is cleanly converted to the iron(III)-hydroperoxo complex, [Fe(III)(TMC)(OOH)](2+), via a short-lived intermediate on protonation. This iron(III)-hydroperoxo complex then cleanly converts to the ferryl complex, [Fe(IV)(TMC)(O)](2+), via homolytic O-O bond cleavage of the iron(III)-hydroperoxo species. All three of these iron species--the three most biologically relevant iron-oxygen intermediates--have been spectroscopically characterized; we note that they have been obtained using a simple macrocyclic ligand. We have performed relative reactivity studies on these three iron species which reveal that the iron(III)-hydroperoxo complex is the most reactive of the three in the deformylation of aldehydes and that it has a similar reactivity to the iron(IV)-oxo complex in C-H bond activation of alkylaromatics. These reactivity results demonstrate that iron(III)-hydroperoxo species are viable oxidants in both nucleophilic and electrophilic reactions by iron-containing enzymes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306242/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3306242/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cho, Jaeheung -- Jeon, Sujin -- Wilson, Samuel A -- Liu, Lei V -- Kang, Eun A -- Braymer, Joseph J -- Lim, Mi Hee -- Hedman, Britt -- Hodgson, Keith O -- Valentine, Joan Selverstone -- Solomon, Edward I -- Nam, Wonwoo -- 5P41RR001209/RR/NCRR NIH HHS/ -- GM 40392/GM/NIGMS NIH HHS/ -- P41 RR001209/RR/NCRR NIH HHS/ -- P41 RR001209-31/RR/NCRR NIH HHS/ -- R01 GM040392/GM/NIGMS NIH HHS/ -- R01 GM040392-25/GM/NIGMS NIH HHS/ -- RR-001209/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Oct 26;478(7370):502-5. doi: 10.1038/nature10535.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bioinspired Science, Ewha Womans University, Seoul 120-750, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031443" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehydes/metabolism ; Crystallography, X-Ray ; Enzymes/chemistry/metabolism ; Hydrogen Peroxide/*chemistry/metabolism ; Iron/*chemistry/metabolism ; Ligands ; Models, Molecular ; Nonheme Iron Proteins/chemistry/metabolism ; Oxygen/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 10
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    The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-06-11
    Description: The mammalian target of rapamycin (mTOR) protein kinase is a master growth promoter that nucleates two complexes, mTORC1 and mTORC2. Despite the diverse processes controlled by mTOR, few substrates are known. We defined the mTOR-regulated phosphoproteome by quantitative mass spectrometry and characterized the primary sequence motif specificity of mTOR using positional scanning peptide libraries. We found that the phosphorylation response to insulin is largely mTOR dependent and that mTOR exhibits a unique preference for proline, hydrophobic, and aromatic residues at the +1 position. The adaptor protein Grb10 was identified as an mTORC1 substrate that mediates the inhibition of phosphoinositide 3-kinase typical of cells lacking tuberous sclerosis complex 2 (TSC2), a tumor suppressor and negative regulator of mTORC1. Our work clarifies how mTORC1 inhibits growth factor signaling and opens new areas of investigation in mTOR biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3177140/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3177140/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, Peggy P -- Kang, Seong A -- Rameseder, Jonathan -- Zhang, Yi -- Ottina, Kathleen A -- Lim, Daniel -- Peterson, Timothy R -- Choi, Yongmun -- Gray, Nathanael S -- Yaffe, Michael B -- Marto, Jarrod A -- Sabatini, David M -- AI47389/AI/NIAID NIH HHS/ -- CA103866/CA/NCI NIH HHS/ -- CA112967/CA/NCI NIH HHS/ -- ES015339/ES/NIEHS NIH HHS/ -- GM68762/GM/NIGMS NIH HHS/ -- R01 CA103866/CA/NCI NIH HHS/ -- R01 CA103866-09/CA/NCI NIH HHS/ -- R01 CA129105/CA/NCI NIH HHS/ -- R01 CA129105-05/CA/NCI NIH HHS/ -- R37 AI047389/AI/NIAID NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Jun 10;332(6035):1317-22. doi: 10.1126/science.1199498.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21659604" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; GRB10 Adaptor Protein/*metabolism ; Humans ; Insulin/metabolism ; Intercellular Signaling Peptides and Proteins/*metabolism ; Mass Spectrometry ; Mice ; Multiprotein Complexes ; Naphthyridines/pharmacology ; Phosphoproteins/metabolism ; Phosphorylation ; Proteins/*metabolism ; Proteome/metabolism ; *Signal Transduction ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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