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  • Kinetics  (107)
  • American Association for the Advancement of Science (AAAS)  (107)
  • 2010-2014  (21)
  • 1990-1994  (86)
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  • 1
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    Inhibition of HIV replication in acute and chronic infections in vitro by a Tat antagonist (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: The human immunodeficiency virus-1 (HIV-1) trans-activator Tat is an attractive target for the development of antiviral drugs because inhibition of Tat would arrest the virus at an early stage. The drug Ro 5-3335 [7-chloro-5-(2-pyrryl)-3H-1,4-benzodiazepine-2(H)-one], inhibited gene expression by HIV-1 at the level of transcriptional trans-activation by Tat. The compound did not inhibit the basal activity of the promoter. Both Tat and its target sequence TAR were required for the observed inhibitory activity. Ro 5-3335 reduced the amount of cell-associated viral RNA and antigen in acutely, as well as in chronically infected cells in vitro (median inhibition concentration 0.1 to 1 micromolar). Effective inhibition of viral replication was also observed 24 hours after cells were transfected with infectious recombinant HIV-1 DNA. The compound was active against both HIV-1 and HIV-2 and against 3'-azido-3'-deoxythymidine (AZT)-resistant clinical isolates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, M C -- Schutt, A D -- Holly, M -- Slice, L W -- Sherman, M I -- Richman, D D -- Potash, M J -- Volsky, D J -- AI 27397/AI/NIAID NIH HHS/ -- AI 27670/AI/NIAID NIH HHS/ -- AI 29164/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1799-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, Hoffmann-La Roche, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763331" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*pharmacology ; Benzodiazepinones/*pharmacology ; Cell Line ; Gene Products, tat/*antagonists & inhibitors ; HIV Long Terminal Repeat/drug effects ; HIV-1/drug effects/genetics/*physiology ; HIV-2/drug effects/*physiology ; Humans ; Kinetics ; Promoter Regions, Genetic/drug effects ; Pyrroles/*pharmacology ; Virus Replication/*drug effects ; Zidovudine/pharmacology ; tat Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: A two-fold (C2) symmetric inhibitor of the protease of human immunodeficiency virus type-1 (HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the enzyme in a highly symmetric fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J -- Neidhart, D J -- VanDrie, J -- Kempf, D J -- Wang, X C -- Norbeck, D W -- Plattner, J J -- Rittenhouse, J W -- Turon, M -- Wideburg, N -- AI 27220/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer-Assisted Molecular Design, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Drug Design ; Endopeptidases/*metabolism ; Gene Products, pol/*metabolism ; HIV Protease ; HIV-1/*enzymology ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Protease Inhibitors/*pharmacology ; Protein Conformation ; Sugar Alcohols/*pharmacology ; Valine/*analogs & derivatives/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Evidence for an alternative glycolytic pathway in rapidly proliferating cells (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-09-18
    Description: Proliferating cells, including cancer cells, require altered metabolism to efficiently incorporate nutrients such as glucose into biomass. The M2 isoform of pyruvate kinase (PKM2) promotes the metabolism of glucose by aerobic glycolysis and contributes to anabolic metabolism. Paradoxically, decreased pyruvate kinase enzyme activity accompanies the expression of PKM2 in rapidly dividing cancer cells and tissues. We demonstrate that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells. We used mass spectrometry to show that the phosphate from PEP is transferred to the catalytic histidine (His11) on human PGAM1. This reaction occurred at physiological concentrations of PEP and produced pyruvate in the absence of PKM2 activity. The presence of histidine-phosphorylated PGAM1 correlated with the expression of PKM2 in cancer cell lines and tumor tissues. Thus, decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway that decouples adenosine triphosphate production from PEP-mediated phosphotransfer, allowing for the high rate of glycolysis to support the anabolic metabolism observed in many proliferating cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030121/" 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/PMC3030121/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vander Heiden, Matthew G -- Locasale, Jason W -- Swanson, Kenneth D -- Sharfi, Hadar -- Heffron, Greg J -- Amador-Noguez, Daniel -- Christofk, Heather R -- Wagner, Gerhard -- Rabinowitz, Joshua D -- Asara, John M -- Cantley, Lewis C -- 1K08CA136983/CA/NCI NIH HHS/ -- 1P01CA120964-01A/CA/NCI NIH HHS/ -- 5 T32 CA009361-28/CA/NCI NIH HHS/ -- 5P30CA006516-43/CA/NCI NIH HHS/ -- K08 CA136983/CA/NCI NIH HHS/ -- K08 CA136983-02/CA/NCI NIH HHS/ -- P01 CA089021/CA/NCI NIH HHS/ -- P01 CA089021-10/CA/NCI NIH HHS/ -- P01 CA120964/CA/NCI NIH HHS/ -- P01 CA120964-01A1/CA/NCI NIH HHS/ -- P01 GM047467/GM/NIGMS NIH HHS/ -- P01 GM047467-20/GM/NIGMS NIH HHS/ -- P01CA089021/CA/NCI NIH HHS/ -- P01GM047467/GM/NIGMS NIH HHS/ -- P30 CA006516/CA/NCI NIH HHS/ -- P30 CA006516-43S1/CA/NCI NIH HHS/ -- R01 AI078063/AI/NIAID NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- R01-GM56302/GM/NIGMS NIH HHS/ -- R21 CA128620/CA/NCI NIH HHS/ -- R21/R33 DK070299/DK/NIDDK NIH HHS/ -- R33 DK070299/DK/NIDDK NIH HHS/ -- R33 DK070299-03/DK/NIDDK NIH HHS/ -- T32 CA009172/CA/NCI NIH HHS/ -- T32 CA009361/CA/NCI NIH HHS/ -- T32 CA009361-28/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2010 Sep 17;329(5998):1492-9. doi: 10.1126/science.1188015.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20847263" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Cell Line ; Cell Line, Tumor ; *Cell Proliferation ; Female ; Glucose/*metabolism ; Glyceric Acids/metabolism ; *Glycolysis ; Histidine/metabolism ; Humans ; Isoenzymes/metabolism ; Kinetics ; Male ; Mammary Neoplasms, Animal/metabolism ; Mice ; Neoplasms/*metabolism/pathology ; Phosphoenolpyruvate/metabolism ; Phosphoglycerate Mutase/*metabolism ; Phosphopyruvate Hydratase/metabolism ; Phosphorylation ; Prostatic Neoplasms/metabolism ; Pyruvate Kinase/*metabolism ; Pyruvic Acid/metabolism ; Recombinant Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-01
    Description: Rhodopsin and the visual pigments are a distinct group within the family of G-protein-linked receptors in that they have a covalently bound ligand, the 11-cis-retinal chromophore, whereas all of the other receptors bind their agonists through noncovalent interactions. The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296. Two rhodopsin mutants have been constructed, K296G and K296A, in which the covalent linkage to the chromophore is removed. Both mutants form a pigment with an absorption spectrum close to that of the wild type when reconstituted with the Schiff base of an n-alkylamine and 11-cis-retinal. In addition, the pigment formed from K296G and the n-propylamine Schiff base of 11-cis-retinal was found to activate transducin in a light-dependent manner, with 30 to 40% of the specific activity measured for the wild-type protein. It appears that the covalent bond is not essential for binding of the chromophore or for catalytic activation of transducin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhukovsky, E A -- Robinson, P R -- Oprian, D D -- 5T32 GM07596-11/GM/NIGMS NIH HHS/ -- EY07965/EY/NEI NIH HHS/ -- R01 EY007965/EY/NEI NIH HHS/ -- S07 RR07044/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):558-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1990431" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Kinetics ; Mutagenesis, Site-Directed ; Protein Binding ; Retinaldehyde/*metabolism ; Rhodopsin/genetics/*metabolism/radiation effects ; Schiff Bases ; Spectrophotometry ; Transducin/*metabolism/radiation effects
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Pseudo--half-knot formation with RNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: A pseudo--half-knot can be formed by binding an oligonucleotide asymmetrically to an RNA hairpin loop. This binding motif was used to target the human immunodeficiency virus TAR element, an important viral RNA structure that is the receptor for Tat, the major viral transactivator protein. Oligonucleotides complementary to different halves of the TAR structure bound with greater affinity than molecules designed to bind symmetrically around the hairpin. The pseudo--half-knot--forming oligonucleotides altered the TAR structure so that specific recognition and binding of a Tat-derived peptide was disrupted. This general binding motif may be used to disrupt the structure of regulatory RNA hairpins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, D J -- Vickers, T A -- Bruice, T W -- Freier, S M -- Jenison, R D -- Manoharan, M -- Zounes, M -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ISIS Pharmaceuticals, Carlsbad, CA 92008.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502560" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Viral/metabolism ; Gene Products, tat/metabolism ; HIV/*genetics ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; tat Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Prevention of HIV-1 infection and preservation of CD4 function by the binding of CPFs to gp120 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-20
    Description: Infection by human immunodeficiency virus type-1 (HIV-1) is initiated when its envelope protein, gp120, binds to its receptor, the cell surface glycoprotein CD4. Small molecules, termed N-carbomethoxycarbonyl-prolyl-phenylalanyl benzyl esters (CPFs), blocked this binding. CPFs interacted with gp120 and did not interfere with the binding of CD4 to class II major histocompatibility complex molecules. One CPF isomer, CPF(DD), preserved CD4-dependent T cell function while inhibiting HIV-1 infection of H9 tumor cells and human T cells. Although the production of viral proteins in infected T cells is unaltered by CPF(DD), this compound prevents the spread of infection in an in vitro model system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finberg, R W -- Diamond, D C -- Mitchell, D B -- Rosenstein, Y -- Soman, G -- Norman, T C -- Schreiber, S L -- Burakoff, S J -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):287-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Antiviral Agents/*pharmacology ; Benzyl Compounds/pharmacology ; Cell Line ; Genes, MHC Class II ; HIV Envelope Protein gp120/*immunology ; HIV-1/drug effects/immunology/*physiology ; Humans ; Kinetics ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    The trk proto-oncogene product: a signal transducing receptor for nerve growth factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-26
    Description: The trk proto-oncogene encodes a 140-kilodalton, membrane-spanning protein tyrosine kinase (p140prototrk) that is expressed only in neural tissues. Nerve growth factor (NGF) stimulates phosphorylation of p140prototrk in neural cell lines and in embryonic dorsal root ganglia. Affinity cross-linking and equilibrium binding experiments with 125I-labeled NGF indicate that p140prototrk binds NGF specifically in cultured cells with a dissociation constant of 10(-9) molar. The identification of p140prototrk as an NGF receptor indicates that this protein participates in the primary signal transduction mechanism of NGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaplan, D R -- Hempstead, B L -- Martin-Zanca, D -- Chao, M V -- Parada, L F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):554-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eukaryotic Signal Transduction Group, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/physiology ; Cross-Linking Reagents ; Embryo, Mammalian ; Ganglia, Spinal/*metabolism ; Humans ; Kinetics ; Mice ; Nerve Growth Factors/metabolism/*physiology ; Neuroblastoma ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; *Proto-Oncogenes ; Receptor, trkA ; Receptors, Cell Surface/metabolism/*physiology ; Receptors, Nerve Growth Factor ; *Signal Transduction
    Print ISSN: 0036-8075
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  • 8
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    Induction by NGF of meiotic maturation of Xenopus oocytes expressing the trk proto-oncogene product (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-04-26
    Description: The effect of nerve growth factor (NGF) was assessed in Xenopus oocytes expressing the human trk proto-oncogene product, p140prototrk. Oocytes injected with trk messenger RNA expressed polypeptides recognized by antibodies to the trk gene product. Exposure of these oocytes to nanomolar amounts of NGF resulted in specific surface binding of 125I-labeled NGF, tyrosine phosphorylation of p140prototrk, and meiotic maturation, as determined by germinal vesicle breakdown and maturation promoting factor (p34cdc2) kinase activation. Thus the trk proto-oncogene product can act as a receptor for NGF in a functionally productive manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nebreda, A R -- Martin-Zanca, D -- Kaplan, D R -- Parada, L F -- Santos, E -- New York, N.Y. -- Science. 1991 Apr 26;252(5005):558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1850550" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Enzyme Activation ; Female ; Humans ; In Vitro Techniques ; Kinetics ; Meiosis/*drug effects ; Microinjections ; Nerve Growth Factors/metabolism/*pharmacology ; Oocytes/cytology/drug effects/*physiology ; Progesterone/pharmacology ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Proteins/*genetics/metabolism ; *Proto-Oncogenes ; RNA, Messenger/administration & dosage/genetics ; Receptor, trkA ; Receptors, Cell Surface/drug effects/metabolism ; Receptors, Nerve Growth Factor ; Xenopus laevis
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  • 9
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    Identification of a competitive HGF antagonist encoded by an alternative transcript (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-29
    Description: We identified a naturally occurring hepatocyte growth factor (HGF) variant, whose predicted sequence extends only through the second kringle domain of this plasminogen-related molecule. This smaller molecule, derived from an alternative HGF transcript, lacked mitogenic activity but specifically inhibited HGF-induced mitogenesis. Cross-linking studies demonstrated that the truncated molecule competes with HGF for binding to the HGF receptor, which has been identified as the c-met protooncogene product. Thus, the same gene encodes both a growth factor and its direct antagonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A M -- Rubin, J S -- Bottaro, D P -- Hirschfield, D W -- Chedid, M -- Aaronson, S A -- New York, N.Y. -- Science. 1991 Nov 29;254(5036):1382-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1720571" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Northern ; Cell Line ; Culture Media ; DNA/genetics ; DNA Replication/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Hepatocyte Growth Factor ; Humans ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plasmids ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger ; Thymidine/metabolism ; *Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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  • 10
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    Quantitation of hepatic glycogenolysis and gluconeogenesis in fasting humans with 13C NMR (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-10-25
    Description: The rate of net hepatic glycogenolysis was assessed in humans by serially measuring hepatic glycogen concentration at 3- to 12-hour intervals during a 68-hour fast with 13C nuclear magnetic resonance spectroscopy. The net rate of gluconeogenesis was calculated by subtracting the rate of net hepatic glycogenolysis from the rate of glucose production in the whole body measured with tritiated glucose. Gluconeogenesis accounted for 64 +/- 5% (mean +/- standard error of the mean) of total glucose production during the first 22 hours of fasting. In the subsequent 14-hour and 18-hour periods of the fast, gluconeogenesis accounted for 82 +/- 5% and 96 +/- 1% of total glucose production, respectively. These data show that gluconeogenesis accounts for a substantial fraction of total glucose production even during the first 22 hours of a fast in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothman, D L -- Magnusson, I -- Katz, L D -- Shulman, R G -- Shulman, G I -- DK-34576/DK/NIDDK NIH HHS/ -- DK-40936/DK/NIDDK NIH HHS/ -- MO1-RR-00125-26/RR/NCRR NIH HHS/ -- R01 DK040936/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Oct 25;254(5031):573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948033" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Blood Glucose/metabolism ; Carbon Isotopes ; Fasting ; Female ; Glucagon/blood ; *Gluconeogenesis ; Humans ; Hydrocortisone/blood ; Insulin/blood ; Kinetics ; Liver/*metabolism ; Liver Glycogen/*metabolism ; Magnetic Resonance Spectroscopy/methods ; Male ; Nitrogen/*urine
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