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  • 1
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    Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-15
    Description: RAFT1 (rapamycin and FKBP12 target 1; also called FRAP or mTOR) is a member of the ATM (ataxia telangiectasia mutated)-related family of proteins and functions as the in vivo mediator of the effects of the immunosuppressant rapamycin and as an important regulator of messenger RNA translation. In mammalian cells RAFT1 interacted with gephyrin, a widely expressed protein necessary for the clustering of glycine receptors at the cell membrane of neurons. RAFT1 mutants that could not associate with gephyrin failed to signal to downstream molecules, including the p70 ribosomal S6 kinase and the eIF-4E binding protein, 4E-BP1. The interaction with gephyrin ascribes a function to the large amino-terminal region of an ATM-related protein and reveals a role in signal transduction for the clustering protein gephyrin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabatini, D M -- Barrow, R K -- Blackshaw, S -- Burnett, P E -- Lai, M M -- Field, M E -- Bahr, B A -- Kirsch, J -- Betz, H -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- DA-00266/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1161-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johns Hopkins University School of Medicine, Department of Neuroscience, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325225" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Gene Expression ; HeLa Cells ; Humans ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; Phosphoproteins/*metabolism ; Phosphorylation ; *Phosphotransferases (Alcohol Group Acceptor) ; Rats ; Receptors, Glycine/metabolism ; Repressor Proteins/metabolism ; Ribosomal Protein S6 Kinases/*metabolism ; *Signal Transduction ; Sirolimus/*pharmacology ; TOR Serine-Threonine Kinases
    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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  • 2
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    5200-year-old acupuncture in central Europe? (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dorfer, L -- Moser, M -- Spindler, K -- Bahr, F -- Egarter-Vigl, E -- Dohr, G -- New York, N.Y. -- Science. 1998 Oct 9;282(5387):242-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9841386" target="_blank"〉PubMed〈/a〉
    Keywords: Acupuncture Therapy/*history ; Europe ; History, Ancient ; Humans ; Male ; Mummies ; Tattooing
    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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  • 3
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    Acetaminophen: potentially toxic metabolite formed by human fetal and adult liver microsomes and isolated fetal liver cells (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-28
    Description: A reactive metabolite of acetaminophen is hepatotoxic in humans when the drug is ingested in large overdoses. The ability of the human fetal and adult liver to oxidize acetaminophen by trapping the potentially toxic metabolite as a glutathione conjugate has been measured. Oxidation by fetal liver was approximately ten times slower than by adult liver. However, there was a definite increase in acetaminophen oxidation with fetal age. Isolated human fetal liver cells conjugated acetaminophen with sulfate but not with glucuronic acid. The results indicate that the human fetal liver is able to detoxify acetaminophen by conjugation. However, it also catalyzes the formation of an active metabolite of acetaminophen through oxidation. Hence the fetus remains at risk should a large dose of the drug cross into the fetal circulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rollins, D E -- von Bahr, C -- Glaumann, H -- Moldeus, P -- Rane, A -- New York, N.Y. -- Science. 1979 Sep 28;205(4413):1414-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/38505" target="_blank"〉PubMed〈/a〉
    Keywords: Acetaminophen/*metabolism/toxicity ; Biotransformation ; Cytochrome P-450 Enzyme System/metabolism ; Female ; Glutathione/metabolism ; Humans ; Liver/embryology ; Maternal-Fetal Exchange ; Microsomes, Liver/*metabolism ; NADP/metabolism ; Pregnancy
    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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