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  • 1
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    A synthetic HIV-1 protease inhibitor with antiviral activity arrests HIV-like particle maturation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-01-26
    Description: A synthetic peptidemimetic substrate of the human immunodeficiency virus 1 (HIV-1) protease with a nonhydrolyzable pseudodipeptidyl insert at the protease cleavage site was prepared. The peptide U-81749 inhibited recombinant HIV-1 protease in vitro (inhibition constant Ki of 70 nanomolar) and HIV-1 replication in human peripheral blood lymphocytes (inhibitory concentration IC50 of 0.1 to 1 micromolar). Moreover, 10 micromolar concentrations of U-81749 significantly inhibited proteolysis of the HIV-1 gag polyprotein (p55) to the mature viral structural proteins p24 and p17 in cells infected with a recombinant vaccinia virus expressing the HIV-1 gag-pol genes. The HIV-1 like particles released from inhibitor-treated cells contained almost exclusively p55 and other gag precursors, but not p24. Incubation of HIV-like particles recovered from drug-treated cultures in drug-free medium indicated that inhibition of p55 proteolysis was at least partially reversible, suggesting that U-81749 was present within the particles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McQuade, T J -- Tomasselli, A G -- Liu, L -- Karacostas, V -- Moss, B -- Sawyer, T K -- Heinrikson, R L -- Tarpley, W G -- New York, N.Y. -- Science. 1990 Jan 26;247(4941):454-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Infectious Disease Research Unit, Upjohn Company, Kalamazoo, MI 49001.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2405486" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiviral Agents/*pharmacology ; DNA, Viral/genetics ; Endopeptidases/*metabolism ; Fusion Proteins, gag-pol/genetics/metabolism ; Gene Products, gag/metabolism ; HIV Protease ; HIV-1/*drug effects/genetics/physiology ; Humans ; Lymphocytes/microbiology ; Molecular Sequence Data ; Molecular Structure ; Oligopeptides/*pharmacology ; Protease Inhibitors/*pharmacology ; Protein Precursors/metabolism ; RNA, Viral/metabolism ; Transfection ; Virus Replication/drug effects
    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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    Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-20
    Description: The highly symmetric pyruvate dehydrogenase multienzyme complexes have molecular masses ranging from 5 to 10 million daltons. They consist of numerous copies of three different enzymes: pyruvate dehydrogenase, dihydrolipoyl transacetylase, and lipoamide dehydrogenase. The three-dimensional crystal structure of the catalytic domain of Azotobacter vinelandii dihydrolipoyl transacetylase has been determined at 2.6 angstrom (A) resolution. Eight trimers assemble as a hollow truncated cube with an edge of 125 A, forming the core of the multienzyme complex. Coenzyme A must enter the 29 A long active site channel from the inside of the cube, and lipoamide must enter from the outside. The trimer of the catalytic domain of dihydrolipoyl transacetylase has a topology identical to chloramphenicol acetyl transferase. The atomic structure of the 24-subunit cube core provides a framework for understanding all pyruvate dehydrogenase and related multienzyme complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mattevi, A -- Obmolova, G -- Schulze, E -- Kalk, K H -- Westphal, A H -- de Kok, A -- Hol, W G -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1544-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Groningen, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549782" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Azotobacter vinelandii/enzymology ; Chloramphenicol O-Acetyltransferase/genetics ; Humans ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Pyruvate Dehydrogenase Complex/*chemistry/genetics ; Sequence Homology, Nucleic Acid
    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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    Regulation of proteolysis at the neutrophil-substrate interface by secretory leukoprotease inhibitor (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-13
    Description: Human neutrophils can initiate the rapid degradation of extracellular matrix macromolecules by localizing the destructive process to sites of cell-substrate contact. Although plasma and its filtrates contain multiple proteinase inhibitors, these inhibitors did not prevent neutrophils from attacking either underlying fibronectin or elastin. However, subjacent substrates could be protected from neutrophils by recombinant secretory leukoprotease inhibitor, a structurally unique serine proteinase inhibitor whose natural counterpart is normally confined to human mucous secretions. The identification of this extravascular proteinase inhibitor as a potent regulator of subjacent proteolysis could lead to the development of a new class of anti-inflammatory therapeutics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, W G -- Weiss, S J -- AI 21301/AI/NIAID NIH HHS/ -- HL 28024/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):178-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Simpson Memorial Research Institute, University of Michigan, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2371565" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Adhesion ; Cells, Cultured ; Elastin/metabolism ; Extracellular Matrix/*metabolism ; Fibronectins/metabolism ; Humans ; Neutrophils/*metabolism ; Proteinase Inhibitory Proteins, Secretory ; *Proteins ; Recombinant Proteins/metabolism ; Serine Proteinase Inhibitors/*metabolism ; Solubility
    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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    Optical coherence tomography (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-11-22
    Description: A technique called optical coherence tomography (OCT) has been developed for noninvasive cross-sectional imaging in biological systems. OCT uses low-coherence interferometry to produce a two-dimensional image of optical scattering from internal tissue microstructures in a way that is analogous to ultrasonic pulse-echo imaging. OCT has longitudinal and lateral spatial resolutions of a few micrometers and can detect reflected signals as small as approximately 10(-10) of the incident optical power. Tomographic imaging is demonstrated in vitro in the peripapillary area of the retina and in the coronary artery, two clinically relevant examples that are representative of transparent and turbid media, respectively.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4638169/" 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/PMC4638169/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, D -- Swanson, E A -- Lin, C P -- Schuman, J S -- Stinson, W G -- Chang, W -- Hee, M R -- Flotte, T -- Gregory, K -- Puliafito, C A -- 1-R01-GM35459-06/GM/NIGMS NIH HHS/ -- R01 GM035459/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 Nov 22;254(5035):1178-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1957169" target="_blank"〉PubMed〈/a〉
    Keywords: Coronary Disease/diagnosis ; Coronary Vessels/pathology ; Humans ; Image Processing, Computer-Assisted ; In Vitro Techniques ; Retinal Diseases/diagnosis/pathology ; Tomography/*methods
    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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  • 5
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    CD26 antigen and HIV fusion? (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Broder, C C -- Nussbaum, O -- Gutheil, W G -- Bachovchin, W W -- Berger, E A -- New York, N.Y. -- Science. 1994 May 20;264(5162):1156-9; author reply 1162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909959" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*physiology ; Antigens, Differentiation, T-Lymphocyte/*physiology ; Base Sequence ; *Cell Fusion ; Cell Line ; Dipeptidyl Peptidase 4 ; Gene Products, env/*physiology ; Giant Cells/physiology ; HIV-1/*physiology ; Humans ; Hybrid Cells ; Molecular Sequence Data
    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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  • 6
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    Regulation of the Ets-related transcription factor Elf-1 by binding to the retinoblastoma protein (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-28
    Description: The retinoblastoma gene product (Rb) is a nuclear phosphoprotein that regulates cell cycle progression. Elf-1 is a lymphoid-specific Ets transcription factor that regulates inducible gene expression during T cell activation. In this report, it is demonstrated that Elf-1 contains a sequence motif that is highly related to the Rb binding sites of several viral oncoproteins and binds to the pocket region of Rb both in vitro and in vivo. Elf-1 binds exclusively to the underphosphorylated form of Rb and fails to bind to Rb mutants derived from patients with retinoblastoma. Co-immunoprecipitation experiments demonstrated an association between Elf-1 and Rb in resting normal human T cells. After T cell activation, the phosphorylation of Rb results in the release of Elf-1, which is correlated temporally with the activation of Elf-1-mediated transcription. Overexpression of a phosphorylation-defective form of Rb inhibited Elf-1-dependent transcription during T cell activation. These results demonstrate that Rb interacts specifically with a lineage-restricted Ets transcription factor. This regulated interaction may be important for the coordination of lineage-specific effector functions such as lymphokine production with cell cycle progression in activated T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, C Y -- Petryniak, B -- Thompson, C B -- Kaelin, W G -- Leiden, J M -- R01 AI29673-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 May 28;260(5112):1330-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493578" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Cycle ; Cell Line ; DNA-Binding Proteins/chemistry/*metabolism ; Eye Neoplasms/genetics ; Humans ; Lymphocyte Activation ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma/genetics ; Retinoblastoma Protein/*metabolism ; T-Lymphocytes/immunology/*metabolism ; Transcription Factors/chemistry/*metabolism ; Transcription, Genetic
    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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    Asbestos surface charge heterogeneity and biological effects (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Light, W G -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280676" target="_blank"〉PubMed〈/a〉
    Keywords: *Asbestos ; Humans ; Occupational Diseases/chemically induced ; Structure-Activity Relationship
    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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  • 8
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    The human homologs of the raf (mil) oncogene are located on human chromosomes 3 and 4 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-06
    Description: Two human genes that are homologous to both the murine transforming gene (oncogene) v-raf and the chicken transforming gene v-mil have been mapped by means of human-rodent somatic cell hybrids to human chromosomes previously devoid of known oncogenes. One gene, c-raf-2, which appears to be a processed pseudogene, is located on chromosome 4. The other gene, c-raf-1, which appears to be the active gene, is located on chromosome 3 and has been regionally mapped by chromosomal in situ hybridization to 3p25. This assignment correlates with specific chromosomal abnormalities associated with certain human malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T -- O'Brien, S J -- Nash, W G -- Rapp, U R -- Morton, C C -- Leder, P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):71-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691137" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/genetics ; Animals ; Chromosome Aberrations ; Chromosome Mapping ; *Chromosomes, Human, 1-3 ; *Chromosomes, Human, 4-5 ; Cricetinae ; Humans ; Hybrid Cells ; Kidney Neoplasms/genetics ; Lung Neoplasms/genetics ; Male ; Mice ; Nucleic Acid Hybridization ; *Oncogenes
    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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  • 9
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    Gene for T-cell growth factor: location on human chromosome 4q and feline chromosome B1 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: T-cell growth factor (TCGF) or interleukin-2 (IL-2), an immunoregulatory lymphokine, is produced by lectin- or antigen-activated mature T lymphocytes and in a constitutive manner by certain T-cell lymphoma cell lines. By means of a molecular clone of human TCGF and DNA extracted from a panel of somatic cell hybrids (rodent cells X normal human lymphocytes), the TCGF structural gene was identified on human chromosome 4. In situ hybridization of the TCGF clone to human chromosomes resulted in significant labeling of the midportion of the long arm of chromosome 4, indicating that the TCGF gene was located at band q26-28. Genomic DNA from a panel of hybrids prepared with HUT-102 B2 cells was examined with the same molecular clone. In this clone of cells, which produces human T-cell leukemia virus, the TCGF gene was also located on chromosome 4 and was apparently not rearranged. The homologous TCGF locus in the domestic cat was assigned to chromosome B1 by using a somatic cell hybrid panel that segregates cat chromosomes. Linkage studies as well as high-resolution G-trypsin banding indicate that this feline chromosome is partially homologous to human chromosome 4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seigel, L J -- Harper, M E -- Wong-Staal, F -- Gallo, R C -- Nash, W G -- O'Brien, S J -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):175-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats/*genetics ; Chromosome Banding ; Chromosome Mapping ; *Chromosomes ; *Chromosomes, Human, 4-5 ; Cloning, Molecular ; Deltaretrovirus ; *Genes ; Genetic Linkage ; Humans ; Hybrid Cells ; Interleukin-2/*genetics ; Nucleic Acid Hybridization
    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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  • 10
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    Biologically active chorionic gonadotropin: synthesis by the human fetus (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-04-15
    Description: The kidney, and to a slight extent the liver, of human fetuses were found to synthesize and secrete the alpha subunit common to glycoprotein hormones. Fetal lung and muscle did not synthesize this protein. Since fetal kidney and liver were previously found to synthesize beta chorionic gonadotropin, their ability to synthesize bioactive chorionic gonadotropin was also determined. The newly synthesized hormone bound to mouse Leydig cells and elicited a biological response: namely, the synthesis of testosterone. These results suggest that the human fetus may participate in metabolic homeostasis during its development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGregor, W G -- Kuhn, R W -- Jaffe, R B -- HD08478/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):306-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6682243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chorionic Gonadotropin/*biosynthesis ; Fetus/*metabolism ; Humans ; Kidney/embryology ; Leydig Cells/metabolism ; Liver/embryology ; Luteinizing Hormone/biosynthesis ; Male ; Mice ; Placenta/metabolism ; Testosterone/biosynthesis
    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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