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  • Molecular Weight  (58)
  • American Association for the Advancement of Science (AAAS)  (58)
  • American Chemical Society
  • Elsevier
  • 1985-1989  (58)
  • 1980-1984
  • 1965-1969
  • 1989  (19)
  • 1985  (39)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (58)
  • American Chemical Society
  • Elsevier
Years
  • 1985-1989  (58)
  • 1980-1984
  • 1965-1969
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-01-20
    Description: Human and murine mononuclear phagocytes express a high-affinity receptor for immunoglobulin G that plays a central role in macrophage antibody-dependent cellular cytotoxicity and clearance of immune complexes. The receptor (FcRI) may also be involved in CD4-independent infection of human macrophages by human immunodeficiency virus. This report describes the isolation of cDNA clones encoding the human FcRI by a ligand-mediated selection technique. Expression of the cDNAs in COS cells gave rise to immunoglobulin G binding of the expected affinity and subtype specificity. RNA blot analysis revealed expression of a 1.7-kilobase transcript in macrophages and in cells of the promonocytic cell line U937 induced with interferon-gamma. The extracellular region of FcRI consists of three immunoglobulin-like domains, two of which share homology with low-affinity receptor domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, J M -- Seed, B -- New York, N.Y. -- Science. 1989 Jan 20;243(4889):378-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911749" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Cercopithecus aethiops ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Molecular Weight ; Polymorphism, Genetic ; Receptors, Fc/*genetics ; Transfection
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1989 Oct 6;246(4926):32-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2781301" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Mass Spectrometry/*instrumentation ; Molecular Weight ; Proteins/*analysis
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-24
    Description: Cruciform DNA, a non-double helix form of DNA, can be generated as an intermediate in genetic recombination as well as from palindromic sequences under the effect of supercoiling. Eukaryotic cells are equipped with a DNA-binding protein that selectively recognizes cruciform DNA. Biochemical and immunological data showed that this protein is HMG1, an evolutionarily conserved, essential, and abundant component of the nucleus. The interaction with a ubiquitous protein points to a critical role for cruciform DNA conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bianchi, M E -- Beltrame, M -- Paonessa, G -- New York, N.Y. -- Science. 1989 Feb 24;243(4894 Pt 1):1056-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidleberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2922595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics/*metabolism ; Electrophoresis, Polyacrylamide Gel ; High Mobility Group Proteins/genetics/isolation & purification/*metabolism ; Immunoassay ; Immunoblotting ; Liver/analysis ; Molecular Sequence Data ; Molecular Weight ; *Nucleic Acid Conformation ; Peptide Fragments/genetics/isolation & purification ; Protein Biosynthesis ; Rats ; Transcription, Genetic
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  • 4
    Publication Date: 1989-06-23
    Description: Although the T cell receptor (TCR) alpha beta heterodimer and its encoding genes have been characterized, a cell-free form of this receptor, which is needed for the study of functional or ligand-binding properties of the receptor, has not previously been isolated. When the cell-free supernatant products of activated cloned T helper (TH) cells were found to mediate helper activity with antigen specificity identical to that of intact T cells, experiments were carried out to determine whether this functional activity was mediated by a cell-free form of TCR-related material. A disulfide-linked dimer indistinguishable from the T cell surface alpha beta heterodimer was precipitated from cell-free supernatants of cloned TH cells with F23.1, a monoclonal antibody specific for a TCR V beta 8 determinant. Moreover, when cell-free TH products were bound to and eluted from immobilized F23.1, these affinity-purified materials had antigen-specific and major histocompatibility complex-restricted helper activity that synergized with recombinant lymphokines in the generation of B cell antibody responses. These findings suggest that the factor isolated from T cell supernatants is a cell-free form of the TCR alpha beta dimer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guy, R -- Ullrich, S J -- Foo-Philips, M -- Hathcock, K S -- Appella, E -- Hodes, R J -- New York, N.Y. -- Science. 1989 Jun 23;244(4911):1477-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2472009" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens/*immunology ; B-Lymphocytes/immunology ; Disulfides ; Epitopes/immunology ; Hemocyanin/immunology ; Histocompatibility Antigens/immunology ; Immunoglobulin G/immunology ; Immunosorbent Techniques ; Interleukin-2/pharmacology ; Interleukin-4 ; Interleukins/pharmacology ; Lymphocyte Activation ; Macromolecular Substances ; Mice ; Molecular Weight ; Receptors, Antigen, T-Cell/*immunology/isolation & purification ; Recombinant Proteins ; Serum Albumin, Bovine/immunology ; T-Lymphocytes, Helper-Inducer/*immunology ; Trinitrobenzenes/immunology
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  • 5
    Publication Date: 1989-04-28
    Description: Transcriptional activation of the human interleukin-2 (IL-2) gene, like induction of the IL-2 receptor alpha (IL-2R alpha) gene and the type 1 human immunodeficiency virus (HIV-1), is shown to be modulated by a kappa B-like enhancer element. Mutation of a kappa B core sequence identified in the IL-2 promoter (-206 to -195) partially inhibits both mitogen- and HTLV-I Tax-mediated activation of this transcription unit and blocks the specific binding of two inducible cellular factors. These kappa B-specific proteins (80 to 90 and 50 to 55 kilodaltons) similarly interact with the functional kappa B enhancer present in the IL-2R alpha promoter. These data suggest that these kappa B-specific proteins have a role in the coordinate regulation of this growth factor-growth factor receptor gene system that controls T cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoyos, B -- Ballard, D W -- Bohnlein, E -- Siekevitz, M -- Greene, W C -- A127053-01/PHS HHS/ -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):457-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mount Sinai Medical Center, Department of Microbiology, New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2497518" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Cloning, Molecular ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; *Enhancer Elements, Genetic ; *Gene Expression Regulation ; Genes, Viral ; HIV-1/genetics ; HTLV-I Antigens/pharmacology ; Humans ; Immunoglobulin kappa-Chains/*genetics ; Interleukin-2/*genetics ; Molecular Weight ; Mutation ; Phytohemagglutinins/pharmacology ; Plasmids ; Promoter Regions, Genetic ; RNA, Messenger/biosynthesis ; T-Lymphocytes/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators ; Transcription Factors/pharmacology ; Transcription, Genetic ; Transfection
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-03-31
    Description: C/EBP is a rat liver nuclear protein capable of sequence-specific interaction with DNA. The DNA sequences to which C/EBP binds in vitro have been implicated in the control of messenger RNA synthesis. It has therefore been predicted that C/EBP will play a role in regulating gene expression in mammalian cells. The region of the C/EBP polypeptide required for direct interaction with DNA has been identified and shown to bear amino acid sequence relatedness with the product of the myc, fos, and jun proto-oncogenes. The arrangement of these related amino acid sequences led to the prediction of a new structural motif, termed the "leucine zipper," that plays a role in facilitating sequence-specific interaction between protein and DNA. Experimental tests now provide support for the leucine zipper hypothesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landschulz, W H -- Johnson, P F -- McKnight, S L -- New York, N.Y. -- Science. 1989 Mar 31;243(4899):1681-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Carnegie Institution of Washington, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2494700" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; CCAAT-Enhancer-Binding Proteins ; Cross-Linking Reagents ; DNA/*metabolism ; Glutaral ; Leucine ; Liver/*analysis ; Macromolecular Substances ; Molecular Weight ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Protein Conformation ; Rats ; Repetitive Sequences, Nucleic Acid ; Structure-Activity Relationship
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  • 7
    Publication Date: 1989-06-23
    Description: Chloride channels mediate absorption and secretion of fluid in epithelia, and the regulation of these channels is now known to be defective in cystic fibrosis. Indanyl-oxyacetic acid 94 (IAA-94) is a high-affinity ligand for the chloride channel, and an affinity resin based on that structure was developed. Solubilized proteins from kidney and trachea membranes were applied to the affinity matrix, and four proteins with apparent molecular masses of 97, 64, 40, and 27 kilodaltons were eluted from the column by excess IAA-94. A potential-dependent 36Cl- uptake was observed after reconstituting these proteins into liposomes. Three types of chloride channels with single-channel conductances of 26, 100, and 400 picosiemens were observed after fusion of these liposomes with planar lipid bilayers. Similar types of chloride channels have been observed in epithelia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landry, D W -- Akabas, M H -- Redhead, C -- Edelman, A -- Cragoe, E J Jr -- Al-Awqati, Q -- DK-20999/DK/NIDDK NIH HHS/ -- DK-39532/DK/NIDDK NIH HHS/ -- DK-41146/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Jun 23;244(4911):1469-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2472007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteriorhodopsins/metabolism ; Cattle ; Chloride Channels ; Chlorides/*isolation & purification/physiology ; Chlorine/metabolism ; Chromatography, Affinity ; Electric Conductivity ; Electrophoresis, Polyacrylamide Gel ; Indans ; *Ion Channels/physiology ; Kidney Cortex/*analysis ; Light ; Liposomes/metabolism ; Membrane Potentials/drug effects ; Membrane Proteins/*isolation & purification/physiology ; Molecular Weight ; Radioisotopes ; Trachea/*analysis ; Valinomycin/pharmacology
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-11-03
    Description: An important control point in gene expression is at the level of messenger RNA (mRNA) stability. The mRNAs of certain regulatory cellular proteins such as oncogenes, cytokines, lymphokines, and transcriptional activators are extremely labile. These messages share a common AUUUA pentamer in their 3' untranslated region, which confers cytoplasmic instability. A cytosolic protein was identified that binds specifically to RNA molecules containing four reiterations of the AUUUA structural element. This protein consists of three subunits and binds rapidly to AUUUA-containing RNA. Such protein-RNA complexes are resistant to the actions of denaturing and reducing agents, demonstrating very stable binding. The time course, stability, and specificity of the protein-AUUUA interaction suggests the possibility that the formation of this complex may target susceptible mRNA for rapid cytoplasmic degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malter, J S -- CA01427-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):664-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Tulane University School of Medicine, New Orleans, LA 70112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814487" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding, Competitive ; Carrier Proteins/isolation & purification/*metabolism ; Cell Line ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Weight ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/*metabolism ; *RNA-Binding Proteins ; Ribonuclease, Pancreatic
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  • 9
    Publication Date: 1989-11-03
    Description: The isolated head fragment of myosin is a motor protein that is able to use energy liberated from the hydrolysis of adenosine triphosphate to cause sliding movement of actin filaments. Expression of a myosin fragment nearly equivalent to the amino-terminal globular head domain, generally referred to as subfragment 1, has been achieved by transforming the eukaryotic organism Dictyostelium discoideum with a plasmid that carries a 2.6-kilobase fragment of the cloned Dictyostelium myosin heavy chain gene under the control of the Dictyostelium actin-15 promoter. The recombinant fragment of the myosin heavy chain was purified 2400-fold from one of the resulting cell lines and was found to be functional by the following criteria: the myosin head fragment copurified with the essential and regulatory myosin light chains, decorated actin filaments, and displayed actin-activated adenosine triphosphatase activity. In addition, motility assays in vitro showed that the recombinant myosin fragment is capable of supporting sliding movement of actin filaments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manstein, D J -- Ruppel, K M -- Spudich, J A -- GM 33289/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):656-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2530629" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Cell Line ; Cloning, Molecular ; Dictyostelium/*genetics ; *Gene Expression ; *Genes ; Genetic Vectors ; Molecular Weight ; Myosin Subfragments/*genetics/isolation & purification ; Myosins/genetics/metabolism ; Plasmids ; Promoter Regions, Genetic
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  • 10
    Publication Date: 1989-09-22
    Description: GABAA (gamma-aminobutyric acid A)-benzodiazepine receptors expressed in mammalian cells and assembled from one of three different alpha subunit variants (alpha 1, alpha 2, or alpha 3) in combination with a beta 1 and a gamma 2 subunit display the pharmacological properties of either type I or type II receptor subtypes. These receptors contain high-affinity binding sites for benzodiazepines. However, CL 218 872, 2-oxoquazepam, and methyl beta-carboline-3-carboxylate (beta-CCM) show a temperature-modulated selectivity for alpha 1 subunit-containing receptors. There were no significant differences in the binding of clonazepam, diazepam, Ro 15-1788, or dimethoxy-4-ethyl-beta-carboline-3-carboxylate (DMCM) to all three recombinant receptors. Receptors containing the alpha 3 subunit show greater GABA potentiation of benzodiazepine binding than receptors containing the alpha 1 or alpha 2 subunit, indicating that there are subtypes within the type II class. Thus, diversity in benzodiazepine pharmacology is generated by heterogeneity of the alpha subunit of the GABAA receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pritchett, D B -- Luddens, H -- Seeburg, P H -- New York, N.Y. -- Science. 1989 Sep 22;245(4924):1389-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Neuroendocrinology, Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2551039" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Diazepam/metabolism ; Flumazenil/metabolism ; Flunitrazepam/metabolism ; Humans ; Molecular Weight ; Pyridazines/metabolism ; Receptors, GABA-A/classification/*genetics/metabolism ; Recombinant Proteins/metabolism ; Transfection
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-12-08
    Description: Hematogenous metastasis requires the arrest and extravasation of blood-borne tumor cells, possibly involving direct adhesive interactions with vascular endothelium. Cytokine activation of cultured human endothelium increases adhesion of melanoma and carcinoma cell lines. An inducible 110-kD endothelial cell surface glycoprotein, designated INCAM-110, appears to mediate adhesion of melanoma cells. In addition, an inducible endothelial receptor for neutrophils, ELAM-1, supports the adhesion of a human colon carcinoma cell line. Thus, activation of vascular endothelium in vivo that results in increased expression of INCAM-110 and ELAM-1 may promote tumor cell adhesion and affect the incidence and distribution of metastases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, G E -- Bevilacqua, M P -- HL 07727/HL/NHLBI NIH HHS/ -- P01 HL36028/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Dec 8;246(4935):1303-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2588007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Cell Adhesion/physiology ; Cell Adhesion Molecules/analysis/*physiology ; Colonic Neoplasms/pathology ; Endothelium, Vascular/analysis/*cytology/physiology ; Humans ; Melanoma/*pathology ; Melanoma, Experimental/pathology ; Molecular Weight ; Tumor Cells, Cultured
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  • 12
    Publication Date: 1989-12-22
    Description: DNA has been volatilized by pulsed laser ablation of a thin film of a frozen aqueous DNA solution. The target film was irradiated in vacuum by a pulsed laser at power densities sufficient to ablate the ice matrix. The expanding ablated water vapor entrained embedded DNA molecules and expelled them into the gas phase. Ejection of DNA molecules as large as 410 kilodaltons was verified by collection of the ablation products and subsequent mass analysis by polyacrylamide gel electrophoresis with autoradiographic detection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, R W -- Rainbow, M J -- Lohr, D E -- Williams, P -- CA 00911/CA/NCI NIH HHS/ -- GM 37788/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Arizona State University, Tempe 85287.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2595370" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; *Dna ; Freezing ; *Lasers ; Molecular Weight ; Phosphorus Radioisotopes ; Plasmids ; Solutions ; Volatilization
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  • 13
    Publication Date: 1989-01-27
    Description: Differential gene expression in the mother cell chamber of sporulating cells of Bacillus subtilis is determined in part by an RNA polymerase sigma factor called sigma K (or sigma 27). The sigma K factor was assigned as the product of the sporulation gene spoIVCB on the basis of the partial aminoterminal amino acid sequence of the purified protein. The spoIVCB gene is now shown to be a truncated gene capable of specifying only the amino terminal half of sigma K. The carboxyl terminal half is specified by another sporulation gene, spoIIIC, to which spoIVCB becomes joined inframe at an intermediate stage of sporulation by site-specific recombination within a 5-base pair repeated sequence. Juxtaposition of spoIVCB and spoIIIC need not be reversible in that the mother cell and its chromosome are discarded at the end of the developmental cycle. The rearrangement of chromosomal DNA could account for the presence of sigma K selectively in the mother cell and may be a precedent for the generation of cell type-specific regulatory proteins in other developmental systems where cells undergo terminal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stragier, P -- Kunkel, B -- Kroos, L -- Losick, R -- New York, N.Y. -- Science. 1989 Jan 27;243(4890):507-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2536191" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus subtilis/*genetics/physiology ; Base Sequence ; Cloning, Molecular ; DNA Probes ; DNA Restriction Enzymes ; DNA, Bacterial/genetics ; DNA-Directed RNA Polymerases/metabolism ; *Gene Expression Regulation ; *Gene Rearrangement ; *Genes, Bacterial ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nucleic Acid Hybridization ; Sigma Factor/genetics ; Spores, Bacterial ; Transcription Factors/*genetics
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-10
    Description: Pituitary-specific expression of the growth hormone (GH) gene is governed by a transcription factor, GHF-1, that binds to two sites within its promoter. Recently, GHF-1 was shown to be a member of the homeobox family of DNA-binding proteins. An important question is whether GHF-1 controls the expression of other pituitary specific genes, such as prolactin (Prl), expressed in closely related cell types. To this end, GHF-1 was purified from extracts of GH- and Prl-expressing pituitary tumor cells and identified as a 33-kilodalton polypeptide. Although GHF-1 bound to and activated the GH promoter, it did not recognize the Prl promoter. However, at least one other factor in the same extracts, which was easily separated from GHF-1, bound to several sites within the Prl but not the GH promoter. Antibodies to GHF-1 did not react with the Prl binding activity. These results imply that the pituitary-specific expression of GH and Prl is governed by two distinct trans-acting factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castrillo, J L -- Bodner, M -- Karin, M -- DK-38527/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 10;243(4892):814-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2563596" target="_blank"〉PubMed〈/a〉
    Keywords: DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; *Genes, Homeobox ; Growth Hormone/*genetics ; Humans ; Molecular Weight ; Peptide Mapping ; Pituitary Gland/physiology ; Prolactin/genetics ; Promoter Regions, Genetic ; Transcription Factors/*genetics ; Tumor Cells, Cultured
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  • 15
    Publication Date: 1989-05-05
    Description: Cells of the mouse cell line 3T3-F442A can be induced by various hormones to differentiate into adipocytes, whereas cells of 3T3-C2, a subclone of 3T3, cannot. However, transfection of DNA from uninduced 3T3-F422A cells into 3T3-C2 cells permits recovery of 3T3-C2 transfectants that differentiate into adipocytes in the presence of insulin. DNA isolated from human fat tissue, when transfected into 3T3-C2 mouse cells, also gives rise to mouse transfectants that are induced to differentiate into adipocytes by the addition of insulin. Apparently, transfection of a trans-regulatory gene (or genes) from 3T3-F442A or human fat cells into 3T3-C2 cells is sufficient to commit 3T3-C2 cells to adipocyte differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, S -- Teicher, L C -- Kazim, D -- Pollack, R E -- Wise, L S -- New York, N.Y. -- Science. 1989 May 5;244(4904):582-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2470149" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adipose Tissue/*cytology ; Animals ; Cell Differentiation/drug effects ; Cell Line ; DNA/*genetics ; DNA Probes ; DNA Restriction Enzymes ; Dexamethasone/pharmacology ; Fibroblasts/*cytology ; Glycerolphosphate Dehydrogenase/metabolism ; Humans ; Insulin/pharmacology ; Mice ; Molecular Weight ; Nucleic Acid Hybridization ; RNA, Messenger/analysis ; *Transfection
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  • 16
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-01-13
    Description: Proteins can be secreted from animal cells by either a constitutive or a regulated pathway; those destined for regulated secretion are actively sorted into dense-core secretory granules. Although sorting is generally assumed to be accomplished by specific carriers, the nature of these carriers remains elusive. In this study, peptide hormones were used as affinity ligands to purify a set of 25-kilodalton proteins from canine pancreatic tissue. Their ligand specificities and patterns of expression have the characteristics of sorting carriers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chung, K N -- Walter, P -- Aponte, G W -- Moore, H P -- 1F32GM1178-01/GM/NIGMS NIH HHS/ -- GM 35239/GM/NIGMS NIH HHS/ -- R23 AM 38310-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Jan 13;243(4888):192-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology Anatomy, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Antibody Complex ; Carrier Proteins/isolation & purification/*metabolism ; Cell Line ; Chromatography, Affinity/methods ; Dogs ; Golgi Apparatus/*metabolism ; Immune Sera ; Immunohistochemistry ; Intracellular Membranes/*metabolism ; Molecular Weight ; Pancreas/*metabolism ; Prolactin
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  • 17
    Publication Date: 1989-06-30
    Description: The growth of human mammary cells may be regulated by a balance between growth stimulatory and growth inhibitory pathways. Polypeptides of 47 and 65 kilodaltons (mammastatin) were isolated from conditioned medium of normal human mammary cells. Monoclonal antibodies against mammastatin were generated that blocked its activity and were used for purification and further characterization of the protein. Mammastatin inhibited the growth of 5 transformed human mammary cell lines, but had no effect on the growth of 11 transformed human cell lines derived from nonmammary tissues. Mammastatin appeared to be a heat-labile protein distinct from transforming growth factor-beta (TGF-beta). By immunoperoxidase staining it was detected in cultured normal human mammary cells, but was decreased in transformed mammary cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ervin, P R Jr -- Kaminski, M S -- Cody, R L -- Wicha, M S -- New York, N.Y. -- Science. 1989 Jun 30;244(4912):1585-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Michigan Cancer Center, Ann Arbor 48109.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2662405" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Breast/analysis/cytology/*metabolism ; Breast Neoplasms/metabolism/pathology ; Cell Division ; Cell Line, Transformed ; Chromatography ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Epithelium/metabolism ; Female ; Growth Inhibitors/*biosynthesis/isolation & purification/pharmacology ; Hot Temperature ; Humans ; Immunoassay ; Immunoenzyme Techniques ; Molecular Weight ; *Peptide Biosynthesis ; Peptides/isolation & purification/pharmacology ; Trypsin/pharmacology ; Tumor Cells, Cultured
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  • 18
    Publication Date: 1989-06-16
    Description: A recently developed cloning system based on the propagation of large DNA molecules as linear, artificial chromosomes in the yeast Saccharomyces cerevisiae provides a potential method of cloning the entire human genome in segments of several hundred kilobase pairs. Most application of this system will require the ability to recover specific sequences from libraries of yeast artificial chromosome clones and to propagate these sequences in yeast without alterations. Two single-copy genes have now been cloned from a library of yeast artificial chromosome clones that was prepared from total human DNA. Multiple, independent isolates were obtained of the genes encoding factor IX and plasminogen activator inhibitor type 2. The clones, which ranged in size from 60 to 650 kilobases, were stable on prolonged propagation in yeast and appear to contain faithful replicas of human DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brownstein, B H -- Silverman, G A -- Little, R D -- Burke, D T -- Korsmeyer, S J -- Schlessinger, D -- Olson, M V -- GM40606/GM/NIGMS NIH HHS/ -- HD07271/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 16;244(4910):1348-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2544027" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Fungal ; *Cloning, Molecular ; DNA/*isolation & purification ; DNA Restriction Enzymes ; Factor IX/genetics ; Gene Library ; *Genome, Human ; Glycoproteins/genetics ; Humans ; Molecular Weight ; Plasminogen Inactivators ; Saccharomyces cerevisiae/genetics
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  • 19
    Publication Date: 1989-10-06
    Description: Electrospray ionization has recently emerged as a powerful technique for producing intact ions in vacuo from large and complex species in solution. To an extent greater than has previously been possible with the more familiar "soft" ionization methods, this technique makes the power and elegance of mass spectrometric analysis applicable to the large and fragile polar molecules that play such vital roles in biological systems. The distinguishing features of electrospray spectra for large molecules are coherent sequences of peaks whose component ions are multiply charged, the ions of each peak differing by one charge from those of adjacent neighbors in the sequence. Spectra have been obtained for biopolymers including oligonucleotides and proteins, the latter having molecular weights up to 130,000, with as yet no evidence of an upper limit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fenn, J B -- Mann, M -- Meng, C K -- Wong, S F -- Whitehouse, C M -- New York, N.Y. -- Science. 1989 Oct 6;246(4926):64-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Engineering Department, Yale University, New Haven, CT 06520.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2675315" target="_blank"〉PubMed〈/a〉
    Keywords: Ions ; Mass Spectrometry/*methods ; Molecular Weight ; Proteins/*analysis
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  • 20
    Publication Date: 1985-11-15
    Description: A newly identified protein from HTLV-III/LAV, the virus implicated as the etiologic agent of the acquired immune deficiency syndrome, was studied. This protein, which has a molecular weight of 27,000 (p27), was shown by amino acid sequencing to have a coding origin 3' to the env gene on the HTLV-III genome. The presence of antibodies to p27 in virus-exposed individuals indicated that this gene is functional in the natural host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Lee, T H -- McLane, M F -- Kanki, P J -- Groopman, J E -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA23885/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):810-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Viral/*immunology ; Antibody Formation ; Antigens, Viral/*immunology ; Deltaretrovirus/genetics/*immunology ; Electrophoresis, Polyacrylamide Gel ; Haplorhini/microbiology ; Humans ; Male ; Molecular Weight ; Repetitive Sequences, Nucleic Acid
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  • 21
    Publication Date: 1985-05-31
    Description: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
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  • 22
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071048" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*diagnosis ; Antibodies, Monoclonal ; Humans ; Molecular Weight ; Nerve Tissue Proteins/immunology
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  • 23
    Publication Date: 1985-05-31
    Description: In this study, two glycoproteins (gp160 and gp120) that are encoded by human T-cell lymphoma virus type III (HTLV-III) were the antigens most consistently recognized by antibodies found in patients with the acquired immune deficiency syndrome (AIDS) and with the AIDS-related complex (ARC) and in healthy homosexual males. The techniques used to detect the glycoproteins were radioimmunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (RIP/SDS-PAGE). Although most antibody-positive samples from ARC patients and from healthy homosexual males also reacted with the virus core protein p24, less than half of the AIDS patients revealed a positive band with p24 under the same conditions. The ability to detect antibodies against a profile of both the major env gene encoded antigens and the gag gene encoded antigens suggests that the RIP/SDS-PAGE may be a valuable confirmatory assay for establishing the presence or absence of antibodies to HTLV-III in human serum samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barin, F -- McLane, M F -- Allan, J S -- Lee, T H -- Groopman, J E -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1094-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986291" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Antibodies, Viral/*immunology ; Antibody Specificity ; Antigens, Viral/*immunology ; Deltaretrovirus/*immunology ; Electrophoresis, Polyacrylamide Gel ; Humans ; Immunologic Techniques ; Molecular Weight ; Viral Envelope Proteins/*immunology
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  • 24
    Publication Date: 1985-06-21
    Description: Fibroblasts possess several distinct mechanisms that control cellular adhesion to extracellular matrix macromolecules. Monoclonal antibodies to a 140-kilodalton (kD) cell surface glycoprotein inhibited the adhesion of fibroblastic Chinese hamster ovary cells to fibronectin-coated substrata but did not inhibit adhesion to substrata coated with vitronectin, laminin, serum, or other adhesive macromolecules. Thus the 140-kD glycoprotein appears to be involved in the fibronectin-mediated adhesion mechanism but not in other adhesion processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, P J -- Juliano, R L -- GM26165/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 21;228(4706):1448-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4012302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Cell Adhesion ; Cell Membrane/immunology/*metabolism ; Cells, Cultured ; Cricetinae ; Cricetulus ; Fibroblasts/metabolism ; Fibronectins/*metabolism ; Glycoproteins/immunology/*metabolism ; Molecular Weight
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  • 25
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-11-01
    Description: Antigens that bind to erythrocytes were identified in the supernatant fluids of a cultured human malaria parasite (Plasmodium falciparum). A 175-kilodalton (175K) antigen bound only to erythrocytes susceptible to invasion. The 175K antigen from the Camp or the FCR-3 strain also bound to merozoites. However, the antigen did not bind to merozoites when merozoites and supernatant antigens were from different strains unless proteinase inhibitors were present. Moreover, erythrocytes coated with supernatant antigens from the Camp or FCR-3 strain were invaded normally by merozoites of the homologous strain but were partially resistant to invasion by merozoites of the heterologous strain. The 175K antigen may be a receptor acting as a "bridge" between erythrocytes and merozoites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camus, D -- Hadley, T J -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):553-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3901257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Protozoan/*metabolism ; Chymotrypsin/metabolism ; Electrophoresis, Polyacrylamide Gel ; Erythrocytes/*metabolism ; Guinea Pigs ; Humans ; Macaca mulatta ; Molecular Weight ; Neuraminidase/metabolism ; Plasmodium falciparum/*immunology ; Protease Inhibitors/pharmacology ; Rabbits ; Trypsin/metabolism
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  • 26
    Publication Date: 1985-07-12
    Description: A specific label for voltage-dependent calcium channels is essential for the isolation and purification of the membrane protein that constitutes the calcium channel and for a better understanding of its function. A fraction of Crotalus atrox that increases voltage-dependent calcium currents in single, dispersed guinea pig ventricular cells was isolated. In the doses used, neither sodium nor potassium currents were changed. The fraction was active in the absence of detectable phospholipase or protease activity, and the active component, designated atrotoxin, produced its effect rapidly and reversibly. The effect was produced by extracellular but not intracellular application of the agent. The increase in Ca2+ current was blocked by the Ca2+ channel blockers cobalt and nitrendipine. The active fraction completely blocked specific [3H]nitrendipine binding to guinea pig ventricular membrane preparations. The inhibition of nitrendipine binding by atrotoxin was apparently via an allosteric mechanism. Thus atrotoxin was shown to bind to the Ca2+ channel and to act as a specific Ca2+ channel agonist.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, S L -- Yatani, A -- Hawkes, M J -- Redding, K -- Brown, A M -- 1R01 HL3293S/HL/NHLBI NIH HHS/ -- 1R01-HL33662-01/HL/NHLBI NIH HHS/ -- 5R01-HL25145-05/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jul 12;229(4709):182-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3160111" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Calcium/*metabolism ; Cell Membrane/metabolism ; Crotalid Venoms/*pharmacology ; Dose-Response Relationship, Drug ; Guinea Pigs ; In Vitro Techniques ; Molecular Weight ; Myocardium/*metabolism ; Nifedipine/analogs & derivatives/metabolism ; Nitrendipine ; Potassium/metabolism ; Rats ; Sodium/metabolism
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  • 27
    Publication Date: 1985-06-07
    Description: Measles virus generally produces acute illness. Rarely, however, persistent infection of brain cells occurs, resulting in a chronic and fatal neurological disease, subacute sclerosing panencephalitis (SSPE). Evidence indicates that expression of the measles virus matrix protein is selectively restricted in this persistent infection, but the mechanism underlying this restriction has not been identified. Defective translation of matrix messenger RNA has been described in one SSPE cell line. This report presents evidence that in a different SSPE tissue culture cell line IP-3-Ca, the matrix protein is synthesized but fails to accumulate. A general scheme is proposed to reconcile the different levels at which restriction of matrix protein has been observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sheppard, R D -- Raine, C S -- Bornstein, M B -- Udem, S A -- CA13330-12/CA/NCI NIH HHS/ -- NS 08952/NS/NINDS NIH HHS/ -- NS 11920/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1219-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001938" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Gene Expression Regulation ; Humans ; Hydrolysis ; Measles virus/genetics/growth & development/*metabolism ; Molecular Weight ; Mutation ; Protein Processing, Post-Translational ; Subacute Sclerosing Panencephalitis/*microbiology ; Viral Matrix Proteins ; Viral Proteins/*biosynthesis/genetics ; Virus Replication
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  • 28
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-11-01
    Description: A primary intracellular substrate for pp60v-src kinase in a variety of avian and mammalian cells is a protein of 34 to 39 kilodaltons (kD). After incubation of chicken embryo fibroblasts (CEF) with [3H]myristic acid for 4 hours, the 36-kD protein contained covalently bound myristic acid by several criteria: (i) the radioactively labeled material comigrated with the 36-kD protein on sodium dodecyl sulfate-polyacrylamide gels in one and two dimensions, (ii) the labeled material was insoluble in chloroform-methanol, and (iii) radioactively labeled myristate could be recovered from the purified 36-kD protein. The resistance of the acyl fatty acid moiety to hydrolysis by hydroxylamine suggested that the covalent linkage to the 36-kD protein may be through an amide linkage. The [3H]myristic-acid labeling of the 36-kD protein in Rous sarcoma virus-transformed CEF showed a reduction of up to 45 percent when compared to an identical amount of 36-kD protein derived from normal cells; this reduction was not due to general changes in myristic acid metabolism in transformed cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soric, J -- Gordon, J A -- CA-15823/CA/NCI NIH HHS/ -- CA-35378/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 1;230(4725):563-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses ; *Cell Transformation, Viral ; Chick Embryo ; Electrophoresis, Polyacrylamide Gel ; Hydrolysis ; Hydroxylamine ; Hydroxylamines/pharmacology ; Methionine/metabolism ; Molecular Weight ; Myristic Acid ; Myristic Acids/*metabolism ; Oncogene Protein pp60(v-src) ; Retroviridae Proteins/*metabolism ; Time Factors
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  • 29
    Publication Date: 1985-05-31
    Description: There is substantial evidence that human serum contains antibodies to many autoantigens. For example, all healthy people have autoantibodies (immunoglobulin M) to some undefined brain antigens. In this study immunoblots and immunohistochemical staining were used to detect antibodies to neural tissues in serum samples from 200 healthy people and 200 patients with various neurological diseases. Ninety-nine percent of the 400 subjects had serum immunoglobulin M and 95 percent had immunoglobulin G that bound to a 200-kilodalton protein in homogenates of neural tissues. In most cases there were no antibodies to anything else in the homogenates. The 200-kilodalton protein was the heaviest of the neurofilament triplet proteins. These observations do not support a role for antibodies to the 200-kilodalton protein of neurofilaments in the pathogenesis of neurological diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stefansson, K -- Marton, L S -- Dieperink, M E -- Molnar, G K -- Schlaepfer, W W -- Helgason, C M -- New York, N.Y. -- Science. 1985 May 31;228(4703):1117-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4039466" target="_blank"〉PubMed〈/a〉
    Keywords: Autoantibodies/*analysis ; Cytoskeleton/*immunology ; Humans ; Immunoglobulin G/immunology ; Immunoglobulin M/immunology ; Intermediate Filament Proteins/*immunology ; Molecular Weight ; Nerve Tissue Proteins/immunology ; Nervous System Diseases/immunology
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  • 30
    Publication Date: 1985-05-17
    Description: The multifunctional nature of coated pit receptors predicts that these proteins will contain multiple domains. To establish the genetic basis for these domains (LDL) receptor. This gene is more than 45 kilobases in length and contains 18 exons, most of which correlate with functional domains previously defined at the protein level. Thirteen of the 18 exons encode protein sequences that are homologous to sequences in other proteins: five of these exons encode a sequence similar to one in the C9 component of complement; three exons encode a sequence similar to a repeat sequence in the precursor for epidermal growth factor (EGF) and in three proteins of the blood clotting system (factor IX, factor X, and protein C); and five other exons encode nonrepeated sequences that are shared only with the EGF precursor. The LDL receptor appears to be a mosaic protein built up of exons shared with different proteins, and it therefore belongs to several supergene families.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450672/" 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/PMC4450672/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Goldstein, J L -- Brown, M S -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):815-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Base Sequence ; Cloning, Molecular ; Complement C9/genetics ; Dna ; Endonucleases ; Epidermal Growth Factor/genetics ; Factor IX/genetics ; Factor X/genetics ; *Genes ; Glycoproteins/genetics ; Humans ; Hyperlipoproteinemia Type II/genetics ; Molecular Weight ; Protein C ; Protein Precursors ; Protein Processing, Post-Translational ; Receptors, LDL/*genetics ; Repetitive Sequences, Nucleic Acid ; Single-Strand Specific DNA and RNA Endonucleases ; Transcription, Genetic
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-07-19
    Description: In addition to nerve growth factor (NGF), many proteins present in soluble tissue extracts and in the extracellular matrix influence the survival and development of cultured neurons. The structure, synthesis, and mechanism of action of NGF as a neurotrophic factor are considered along with the experiments on the new putative trophic molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thoenen, H -- Edgar, D -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):238-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409599" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cattle ; Cell Survival ; Cells, Cultured ; Chick Embryo ; Chickens ; Cyclic AMP/physiology ; DNA/genetics ; Extracellular Matrix/physiology ; Humans ; Ion Channels/physiology ; Male ; Mice ; Molecular Weight ; Myocardium/cytology ; Nerve Growth Factors/genetics/isolation & purification/*physiology ; Neurons/physiology ; Protein Precursors/genetics ; RNA, Messenger/metabolism ; Rats ; Receptors, Cell Surface/physiology ; Receptors, Nerve Growth Factor ; Sympathetic Nervous System/cytology
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  • 32
    Publication Date: 1985-08-16
    Description: At least seven chromosome-sized DNA molecules (750 to 2000 kilobases in length and one fraction of undetermined molecular weight) from cultured clones and isolates of Plasmodium falciparum have been separated by pulsed-field gradient gel electrophoresis. Whereas asexual blood stages and sexual stages of the same line have identical molecular karyotypes, the length of chromosome-sized DNA molecules among different geographical isolates and several clones derived from a single patient is different. These length alterations of chromosomes are the result of DNA rearrangements that must occur unrelated to sexual differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van der Ploeg, L H -- Smits, M -- Ponnudurai, T -- Vermeulen, A -- Meuwissen, J H -- Langsley, G -- New York, N.Y. -- Science. 1985 Aug 16;229(4714):658-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3895435" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/*ultrastructure ; DNA/*isolation & purification ; Electrophoresis, Polyacrylamide Gel/methods ; Molecular Weight ; Plasmodium falciparum/*genetics ; Species Specificity
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-13
    Description: A psbA gene encoding the target of photosystem II herbicide inhibition, the 32,000-dalton thylakoid membrane protein, has been cloned from a mutant of Anacystis nidulans R2, which is resistant to 3-(3,4-dichlorophenyl)-1,1-dimethylurea-(diuron). A cloned DNA fragment from within the coding region of this gene transforms wild-type cells to herbicide resistance, proving that mutation within psbA is responsible for that phenotype. The mutation consists of a single nucleotide change that replaces serine at position 264 of the wild-type protein with alanine in that of the diuron-resistant mutant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golden, S S -- Haselkorn, R -- New York, N.Y. -- Science. 1985 Sep 13;229(4718):1104-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3929379" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cyanobacteria/*genetics ; Diuron ; Drug Resistance ; Electrophoresis, Polyacrylamide Gel ; *Herbicides ; Membrane Proteins/genetics ; Molecular Weight ; *Mutation ; Phenotype
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  • 34
    Publication Date: 1985-05-24
    Description: Experiments were conducted to test the hypothesis that tumor-derived transforming growth factor-alpha (TGF-alpha) is responsible for the increased bone resorption and hypercalcemia seen in some malignant diseases. Homogeneous synthetic TGF-alpha prepared by the solid-phase synthesis method stimulated bone resorption directly in vitro in a concentration-dependent manner. Incubation times of 72 hours or more were required to stimulate resorption, which is similar to the time course of bone resorption by epidermal growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibbotson, K J -- Twardzik, D R -- D'Souza, S M -- Hargreaves, W R -- Todaro, G J -- Mundy, G R -- AM-28149/AM/NIADDK NIH HHS/ -- CA-29537/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 24;228(4702):1007-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3859011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Resorption/*drug effects ; Bone and Bones/drug effects ; Dose-Response Relationship, Drug ; History, 20th Century ; Kinetics ; Molecular Weight ; Organ Culture Techniques ; Peptides/chemical synthesis/*pharmacology ; Rats ; Transforming Growth Factors
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-12-13
    Description: The pol gene of Rous sarcoma virus is positioned downstream of the gag gene in a different, briefly overlapping reading frame; nevertheless, the primary translation product of pol is a gag-pol fusion protein. Two mechanisms, ribosomal frameshifting and RNA splicing, have been considered to explain this phenomenon. The frameshifting model is supported by synthesis of both gag protein and gag-pol fusion protein in a cell-free mammalian translation system programmed by a single RNA species that was synthesized from cloned viral DNA with a bacteriophage RNA polymerase. Under these conditions, the ratio of the gag protein to the fusion protein (about 20 to 1) is similar to that previously observed in infected cells, the frameshifting is specific for the gag-pol junction, and it is unaffected by large deletions in gag. In addition, synthesis of the fusion protein is ten times less efficient in an Escherichia coli cell-free translation system and cannot be explained by transcriptional errors or in vitro modification of the RNA. Ribosomal frameshifting may affect production of other proteins in higher eukaryotes, including proteins encoded by several retroviruses and transposable elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacks, T -- Varmus, H E -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1237-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/*genetics ; Base Sequence ; Cell-Free System ; *Gene Expression Regulation ; Gene Products, gag ; Molecular Weight ; *Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/*genetics ; Rabbits ; Retroviridae Proteins/genetics ; Ribosomes/*metabolism
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  • 36
    Publication Date: 1985-06-07
    Description: Human T-lymphotropic virus type III (HTLV-III) is thought to play an etiologic role in the development of the acquired immune deficiency syndrome (AIDS). In this study the serologic characterization of a new simian retrovirus that is related to HTLV-III is described. This new virus, here referred to as STLV-III, was isolated from sick macaques at the New England Regional Primate Research Center. Radioimmunoprecipitation analysis revealed STLV-III-specific proteins of 160, 120, 55, and 24 kilodaltons, all similar in size to the major gag and env proteins of HTLV-III. These antigens were recognized by representative macaque serum samples and human reference serum samples positive for HTLV-III antibodies. Monoclonal antibodies directed to p24, the major core protein of HTLV-III, also immunoprecipitated a 24-kilodalton species in lysates of cells infected with the macaque virus. This HTLV-III-related virus, which naturally infects a nonhuman primate species, may provide a useful model for the study of HTLV-III and the pathogenesis of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanki, P J -- McLane, M F -- King, N W Jr -- Letvin, N L -- Hunt, R D -- Sehgal, P -- Daniel, M D -- Desrosiers, R C -- Essex, M -- 5TRRR07000/RR/NCRR NIH HHS/ -- CA18216/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1199-201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3873705" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*veterinary ; Animals ; Antigens, Viral/analysis ; Glycoproteins/immunology ; Lymphoma/microbiology ; Macaca/*microbiology ; Molecular Weight ; Monkey Diseases/microbiology ; Retroviridae/*immunology/isolation & purification ; T-Lymphocytes/*microbiology ; Viral Proteins/immunology
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  • 37
    Publication Date: 1985-06-07
    Description: Infection of human T cells by human T-lymphotropic virus, type I (HTLV-I), a retrovirus, is uniformly associated with the constitutive expression of large numbers of cellular receptors for interleukin-2 (IL-2). Comparison with normal T cells shows that neither IL-2 receptor gene organization nor IL-2 receptor messenger RNA processing are altered in the leukemic cells. However, mitogenic stimuli activate IL-2 receptor gene expression in normal T cells, whereas these stimuli paradoxically inhibit IL-2 receptor gene transcription in HTLV-I-infected leukemic T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kronke, M -- Leonard, W J -- Depper, J M -- Greene, W C -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1215-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988127" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/physiology ; Cells, Cultured ; DNA/genetics ; Deltaretrovirus ; Humans ; Leukemia/*genetics ; Molecular Weight ; Poly A/genetics ; RNA, Messenger/genetics ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-2 ; T-Lymphocytes/microbiology/*physiology ; Transcription, Genetic
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  • 38
    Publication Date: 1985-06-07
    Description: The 55 codons upstream of the gene sequence encoding the hepatitis B surface antigen (HBsAg) are called the pre-S(2) region. It has been proposed that polypeptides of high molecular weight that contain the pre-S(2) region should be included in future hepatitis B virus (HBV) vaccines. The pre-S(2) region and the S gene product [25 kilodalton (kD)] together compose a polypeptide of high molecular weight (33 kD). As an initial attempt to determine the relevance of the 33-kD polypeptide to development of an HBV vaccine, the murine immune response to pre-S(2)-encoded determinants as compared to S-encoded determinants on the same polypeptide was examined. The results indicate (i) the pre-S(2) region is significantly more immunogenic than the S region of HBsAg, (ii) the 26 amino acid residues at the NH2-terminus of the 33-kD polypeptide represent a dominant antibody binding site on the pre-S(2) region, (iii) the immune response to the pre-S(2) region is regulated by H-2-linked genes distinct from those that regulate the response to the S region, and (iv) immunization of an S region nonresponder strain with HBV envelope particles that contain both the pre-S(2) and S regions can circumvent nonresponsiveness to the S region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milich, D R -- Thornton, G B -- Neurath, A R -- Kent, S B -- Michel, M L -- Tiollais, P -- Chisari, F V -- AI 00585/AI/NIAID NIH HHS/ -- AI 20001/AI/NIAID NIH HHS/ -- AI 20720/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1195-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Antibody Specificity ; Epitopes ; Genes, MHC Class II ; Genes, Viral ; Hepatitis B Antibodies/immunology ; Hepatitis B Surface Antigens/genetics/*immunology ; Mice ; Molecular Weight ; Protein Precursors/genetics/immunology ; Viral Hepatitis Vaccines/*immunology ; Viral Proteins/genetics/immunology
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  • 39
    Publication Date: 1985-01-25
    Description: The expression of a previously unidentified gene product, encoded by the hepatitis B virus (HBV) genome, has been achieved with a recombinant SV40 expression vector. Antibodies against synthetic peptides representing defined regions of this protein were used to screen cells infected with recombinant virus as well as tissues naturally infected with HBV. A 24,000-dalton protein (p24) was detected in cells infected with recombinant virus and a 28,000-dalton protein (p28) was detected in tissues infected with HBV. The peptides or recombinant-derived protein were used as antigens to screen sera from individuals infected with HBV. Specific antibodies were detected predominantly in sera from patients with hepatocellular carcinoma. The presence of p28 in tissues infected with HBV and the appearance of specific antibodies in infectious sera establish the existence of an additional marker for HBV infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moriarty, A M -- Alexander, H -- Lerner, R A -- Thornton, G B -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):429-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2981434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinoma, Hepatocellular/diagnosis/*immunology ; Cell Line ; Cloning, Molecular ; Enzyme-Linked Immunosorbent Assay ; Genetic Vectors ; Hepatitis B/diagnosis/*immunology ; Hepatitis B Antibodies/*analysis/immunology ; Hepatitis B Antigens/*analysis/immunology ; Humans ; Liver/*immunology ; Liver Neoplasms/diagnosis/*immunology ; Molecular Weight ; Peptides/immunology ; Simian virus 40/genetics ; Viral Proteins/immunology
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  • 40
    Publication Date: 1985-08-02
    Description: Crude fractions of urine from pregnant women are immunosuppressive in vitro. An 85-kilodalton immunosuppressive glycoprotein purified to homogeneity from such urine inhibited in vitro assays of human T-cell and monocyte activity at concentrations of 10(-9) to 10(-11) molar. This material was nontoxic and blocked early events required for normal T-cell proliferation in vitro. On the basis of its tissue source and its in vitro activity, the name "uromodulin" is proposed for this glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muchmore, A V -- Decker, J M -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2409603" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/drug effects ; Chromatography/methods ; Collodion ; Cytotoxicity, Immunologic/drug effects ; Electrophoresis, Polyacrylamide Gel ; Epitopes ; Female ; Hemolytic Plaque Technique ; Humans ; Immunosuppressive Agents/isolation & purification/*urine ; In Vitro Techniques ; Isoelectric Focusing ; Lymphocyte Activation/drug effects ; Molecular Weight ; *Mucoproteins ; Pregnancy ; Pregnancy Proteins/isolation & purification/pharmacology/*urine ; T-Lymphocytes/drug effects ; Uromodulin
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-11-29
    Description: Clathrin-coated membranes are intimately associated with a variety of protein transport processes in eukaryotic cells, yet no direct test of clathrin function has been possible. The data presented demonstrate that Saccharomyces cerevisiae does not require clathrin for either cell growth or protein secretion. Antiserum to the yeast clathrin heavy chain has been used to isolate a molecular clone of the heavy chain gene (CHC1) from a library of yeast DNA in lambda gt11. Clathrin-deficient mutant yeast have been obtained by replacing the single chromosomal CHC1 gene with a disrupted version of the cloned DNA. Cells harboring a nonfunctional chc1 allele produce no immunoreactive heavy chain polypeptide, and vesicles prepared from mutant cells are devoid of clathrin heavy and light chains. Although clathrin-deficient cells grow two to three times more slowly than normal, secretion of invertase occurs at a nearly normal rate. Therefore protein transport through the secretory pathway is not obligately coupled to the formation of clathrin-coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Payne, G S -- Schekman, R -- New York, N.Y. -- Science. 1985 Nov 29;230(4729):1009-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2865811" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; *Cell Physiological Phenomena ; Clathrin/genetics/immunology/*physiology ; Coated Pits, Cell-Membrane/*physiology ; Endosomes/*physiology ; Eukaryotic Cells/*physiology ; Genes ; Genes, Fungal ; Genetic Engineering ; Glycoside Hydrolases/secretion ; Macromolecular Substances ; Molecular Weight ; Proteins/*secretion ; Saccharomyces cerevisiae/genetics ; beta-Fructofuranosidase
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  • 42
    Publication Date: 1985-05-17
    Description: Retinal S antigen chromatographically purified from whole retina, induces experimental autoimmune uveoretinitis in laboratory animals. The 48K protein, a soluble protein found in rod outer segments, is purified through its specific binding to photoexcited rhodopsin and is involved in the quenching of light-induced guanosine 3',5'-monophosphate-phosphodiesterase activity. Biochemical, immunological, functional, and pathological tests showed that retinal S antigen and the 48K protein are identical.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfister, C -- Chabre, M -- Plouet, J -- Tuyen, V V -- De Kozak, Y -- Faure, J P -- Kuhn, H -- New York, N.Y. -- Science. 1985 May 17;228(4701):891-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988124" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Animals ; *Antigens/isolation & purification ; Arrestin ; Autoimmune Diseases/etiology ; Cattle ; Eye Proteins/immunology/isolation & purification/pharmacology ; Light ; Molecular Weight ; Photoreceptor Cells/*enzymology ; Rats ; Retina/analysis/*immunology ; Rod Cell Outer Segment/analysis/immunology ; Uveitis/etiology
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-06
    Description: Coronavirus-like particles were found by electron microscopy in stools from infants with necrotizing enterocolitis. Stool samples from these infants as well as control specimens were passaged in cultures of human fetal intestinal organs. Two samples yielded virus-like particles and these have now been passaged 14 times (HEC 14). Gradient-purified HEC 14 strains had typical coronavirus morphology on electron microscopy and contained five major proteins with molecular sizes ranging from 190 to 23 kilodaltons. Infants with necrotizing enterocolitis developed specific antibody to the viral antigens between the acute and convalescent stages of the disease, as shown by examining serum specimens by single radial hemolysis, immunoenzymatic assay, and Western immunoblotting. No cross-reactivity was shown with other coronavirus strains tested, or with the newly isolated viruses of the Breda-Berne group, responsible for calf or horse diarrhea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Resta, S -- Luby, J P -- Rosenfeld, C R -- Siegel, J D -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):978-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992091" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/analysis ; Coronaviridae/immunology/*isolation & purification ; Coronaviridae Infections/*microbiology ; Cross Infection ; Disease Outbreaks ; Enterocolitis, Pseudomembranous/*microbiology ; Feces/microbiology ; Humans ; Infant ; Microscopy, Electron ; Molecular Weight ; Viral Proteins/immunology
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-02-01
    Description: Two surface antigens were isolated from young or adult schistosomes by affinity chromatography with monoclonal antibodies. Vaccination with an antigen having a molecular weight of 155,000 gave partial protection against challenge in some batches of mice and in a group of cynomolgus monkeys. Vaccination with an antigen having a molecular weight of 53,000 gave similar levels of protection in mice. The results demonstrate that protection can be obtained with single antigens, but the precise requirements for reproducible vaccination are as yet unknown.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, M A -- Clegg, J A -- New York, N.Y. -- Science. 1985 Feb 1;227(4686):535-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3966161" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, Helminth/*immunology/isolation & purification ; Antigens, Surface/*immunology/isolation & purification ; Chromatography, Affinity ; Immunoglobulin E/biosynthesis ; Immunoglobulin G/biosynthesis ; Immunoglobulin M/biosynthesis ; Macaca fascicularis ; Macrophage Activation ; Mice ; Molecular Weight ; Schistosoma mansoni/*immunology ; Schistosomiasis/immunology/*prevention & control ; *Vaccination ; Vaccines
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  • 45
    Publication Date: 1985-12-13
    Description: An immunoreactive form of the anion channel protein of erythrocytes, band 3, has been identified in the rat kidney. It is found in the intercalated cells of the distal tubule and collecting ducts. Immunostaining specific for band 3 is confined to the basolateral plasma membrane of these cells, where this protein probably mediates the transport of bicarbonate across the tubular wall. Double-immunolabeling studies demonstrate that band 3 is colocalized with immunoreactive forms of ankyrin and spectrin along the basolateral plasma membrane. The polarized distribution of band 3 may be the result of the association of its cytoplasmic domain with ankyrin, which in turn links band 3 to spectrin and the cytoskeleton. These observations help to explain how the collecting ducts of the kidney can direct the transport of bicarbonate ions, thus maintaining the acid-base balance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drenckhahn, D -- Schluter, K -- Allen, D P -- Bennett, V -- K04 AM00926/AM/NIADDK NIH HHS/ -- R01 AM29808/AM/NIADDK NIH HHS/ -- R01 GM33996/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1287-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2933809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anion Exchange Protein 1, Erythrocyte/*metabolism ; Ankyrins ; Bicarbonates/*metabolism ; Cell Membrane/metabolism ; Fluorescent Antibody Technique ; Immunosorbent Techniques ; Kidney/metabolism/*ultrastructure ; Kidney Tubules, Collecting/metabolism/ultrastructure ; Kidney Tubules, Distal/metabolism/ultrastructure ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Molecular Weight ; Rats ; Spectrin/*metabolism
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-09-06
    Description: Gonadotropin-releasing hormone analogs can cause regression of hormone-dependent breast carcinomas. These effects are thought to be mediated through the inhibition of gonadotropic and steroid hormones. These analogs may also act directly on the tumor because they are effective in treating breast cancer in some postmenopausal women. The presence of specific binding sites for gonadotropin-releasing hormone was demonstrated in human breast carcinomas by means of a novel approach of ligand immunoblotting. The results indicate a possible mechanism by which the peptide has direct effects on this tissue. These binding proteins were not detectable in non-neoplastic breast tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eidne, K A -- Flanagan, C A -- Millar, R P -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):989-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2992093" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Breast Neoplasms/*metabolism ; Female ; Gonadotropin-Releasing Hormone/*metabolism ; Humans ; Membrane Proteins/metabolism ; Menopause ; Middle Aged ; Molecular Weight ; Receptors, Cell Surface/*metabolism ; Receptors, LHRH
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-07-05
    Description: The granulocyte-macrophage colony-stimulating factors are well-characterized specific glycoproteins that interact to control the production, differentiation, and function of two related white cell populations of the blood, the granulocytes and monocyte-macrophages. Widely produced in the body, these regulators probably play an important role in resistance to infections. The proliferation of myeloid leukemia cells remains dependent on stimulation by colony-stimulating factors, although one of them also has the ability to suppress leukemic populations by inducing terminal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Metcalf, D -- CA-22556/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):16-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990035" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow Cells ; Cell Differentiation ; Cell Division ; Cell Survival ; Cloning, Molecular ; Colony-Stimulating Factors/*physiology ; Granulocytes/*physiology ; *Hematopoiesis ; Humans ; Leukemia, Myeloid, Acute/physiopathology ; Macrophages/*physiology ; Mice ; Molecular Weight ; Receptors, Cell Surface/physiology ; Receptors, Colony-Stimulating Factor ; Species Specificity
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  • 48
    Publication Date: 1985-10-18
    Description: A scheme for partial purification of biologically active v-sis-coded protein from cells transformed with simian sarcoma virus (SSV) has made possible a functional comparison of the transforming protein with platelet-derived growth factor (PDGF). The SSV-transforming gene product is capable of specifically binding PDGF receptors, stimulating tyrosine phosphorylation of PDGF receptors, and inducing DNA synthesis in quiescent fibroblasts. Each of these activities was specifically inhibited by antibodies to different regions of the v-sis gene product. Moreover, viral infection of a variety of cell types revealed a strict correlation between those cells possessing PDGF receptors and those susceptible to transformation by SSV. These findings provide evidence that SSV-transforming activity is mediated by the interaction of a virus-coded mitogen with PDGF receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leal, F -- Williams, L T -- Robbins, K C -- Aaronson, S A -- New York, N.Y. -- Science. 1985 Oct 18;230(4723):327-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2996133" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/metabolism ; Cattle ; Cell Line ; *Cell Transformation, Viral ; Cells, Cultured ; Fibroblasts/metabolism ; *Genes ; *Genes, Viral ; Humans ; Kinetics ; Mink ; Molecular Weight ; Muscle, Smooth/metabolism ; Muscle, Smooth, Vascular/metabolism ; Platelet-Derived Growth Factor/*metabolism ; Receptors, Cell Surface/isolation & purification/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/genetics/*metabolism
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  • 49
    Publication Date: 1985-01-11
    Description: The molecular size of the plasma LDL (low density lipoprotein) receptor synthesized by cultured fibroblasts from a patient with the internalization-defective form of familial hypercholesterolemia (FH 274) was smaller by 10,000 daltons than the size of the normal LDL receptor. The segment of the gene encoding the truncated portion of the FH 274 receptor was cloned into bacteriophage lambda. Comparison of the nucleotide sequences of the normal and FH 274 genes revealed a 5-kilobase deletion, which eliminated the exons encoding the membrane-spanning region and the carboxyl terminal cytoplasmic domain of the receptor. The deletion appeared to be caused by a novel intrastrand recombination between two repetitive sequences of the Alu family that were oriented in opposite directions. The truncated receptors lack membrane-spanning regions and cytoplasmic domains; they are largely secreted into the culture medium, but a small fraction remains adherent to the cell surface. The surface-adherent receptors bind LDL, but they are unable to cluster in coated pits, thus explaining the internalization-defective phenotype.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4449727/" 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/PMC4449727/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehrman, M A -- Schneider, W J -- Sudhof, T C -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 11;227(4683):140-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3155573" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda ; Base Sequence ; Cell Membrane ; Cloning, Molecular ; Coated Pits, Cell-Membrane/metabolism ; Cytoplasm ; Fibroblasts ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Male ; Molecular Weight ; Mutation ; Receptors, LDL/*genetics ; Recombination, Genetic ; *Repetitive Sequences, Nucleic Acid
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  • 50
    Publication Date: 1985-04-26
    Description: A 37-kilodalton protein is synthesized at higher rates in the peripheral and central nervous system of newborn rats than in adult animals. As a specific response to denervation, the synthesis of the 37-kilodalton protein is increased in the mature peripheral and central nervous system; however, this protein accumulates only in the peripheral nervous system. The differences in accumulation of the protein correlate with the apparent differences in the ability of peripheral and central axons to regenerate. The synthesis of the 37-kilodalton protein is inhibited when proper innervation or reinnervation is established.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, H W -- Gebicke-Harter, P J -- Hangen, D H -- Shooter, E M -- NS 04270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 26;228(4698):499-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3983637" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Animals, Newborn/physiology ; Axons/physiology ; Brain/physiology ; Central Nervous System/metabolism/*physiology ; Molecular Weight ; *Nerve Regeneration ; Nerve Tissue Proteins/*biosynthesis ; Optic Nerve/physiology ; Peripheral Nerves/metabolism/*physiology ; Photofluorography ; Rats ; Rats, Inbred Strains ; Sciatic Nerve/physiology ; Spinal Cord/physiology
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  • 51
    Publication Date: 1985-02-15
    Description: The family of tyrosine-specific protein kinases includes proteins encoded by retroviral oncogenes as well as receptors for insulin and several growth factors. Antibodies to pp60src, the protein encoded by the src oncogene of Rous sarcoma virus (RSV), can specifically immunoprecipitate affinity-labeled insulin receptors from cultured human lymphocytes (IM-9 cells). This precipitation is specifically inhibited by the src gene product purified from RSV-transformed rat cells. These observations provide evidence that there is structural homology between the insulin receptors and pp60src.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perrotti, N -- Taylor, S I -- Richert, N D -- Rapp, U R -- Pastan, I H -- Roth, J -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):761-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3918346" target="_blank"〉PubMed〈/a〉
    Keywords: Cross Reactions ; Humans ; Molecular Weight ; Oncogene Protein pp60(v-src) ; *Oncogenes ; Protein Kinases/*immunology ; Protein-Tyrosine Kinases ; Receptor, Insulin/*immunology ; Viral Proteins/*immunology
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  • 52
    Publication Date: 1985-04-19
    Description: The c-fms proto-oncogene is a member of a gene family that has been implicated in tumorigenesis. Glycoproteins encoded by c-fms were identified in cat spleen cells by means of an immune-complex kinase assay performed with monoclonal antibodies to v-fms-coded epitopes. The major form of the normal cellular glycoprotein has an apparent molecular weight of 170,000 and, like the product of the viral oncogene, serves as a substrate for an associated tyrosine-specific protein kinase activity in vitro. The results suggest that the transforming glycoprotein specified by v-fms is a truncated form of a c-fms-coded growth factor receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rettenmier, C W -- Chen, J H -- Roussel, M F -- Sherr, C J -- 1 RO1 CA 38187/CA/NCI NIH HHS/ -- RR-05584-20/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1985 Apr 19;228(4697):320-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2580348" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Cats ; Glycoproteins/immunology/*metabolism ; Humans ; Mice ; Molecular Weight ; Neoplasm Proteins/immunology/*metabolism ; *Oncogenes ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Tyrosine Kinases ; RNA/metabolism ; Rats
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  • 53
    Publication Date: 1985-05-03
    Description: The envelope (env) and structural (gag) gene products of human T-cell leukemia (lymphotropic) virus type III were identified by immunoaffinity chromatography, immunoprecipitation, and two-dimensional oligopeptide mapping methods. The env gene specifies a glycosylated polypeptide with a molecular weight of 160,000 (gp160) that is processed to gp120 and smaller gene products. The gag gene specifies two polypeptides of 70,000 and 55,000 molecular weight (p70 and p55), both of which contain p24, the major structural protein of the mature virion. The techniques in this study can be used to define the extent of variability of the env gene product among different virus isolates and may identify the nature and patterns of the humoral immune response that lead to an immunologically protected state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robey, W G -- Safai, B -- Oroszlan, S -- Arthur, L O -- Gonda, M A -- Gallo, R C -- Fischinger, P J -- N01-CO-23909/CO/NCI NIH HHS/ -- N01-CO-23910/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 3;228(4699):593-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2984774" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Animals ; Antibodies, Viral/immunology ; Chromatography, Affinity ; Deltaretrovirus/*metabolism ; Genes, Viral ; Humans ; Molecular Weight ; Pan troglodytes ; Sarcoma, Kaposi/microbiology ; Viral Envelope Proteins/*isolation & purification ; Viral Proteins/isolation & purification
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  • 54
    Publication Date: 1985-06-07
    Description: A set of naturally occurring immunoglobulin M (IgM) antibodies that are reactive with a defined subset of proteins in the acrosomal cap region of human sperm has been identified. These antibodies are present in a broad spectrum of human sera from males and females, 1 day to 40 years of age, and are absent or markedly deficient in a large proportion of sera from individuals with the acquired immune deficiency syndrome (AIDS) or at risk for AIDS. The subset of proteins with which the IgM antibodies are reactive includes a factor (or factors) capable of inhibiting lectin-induced T-lymphocyte proliferation. The prevalence of the sperm-reactive IgM antibodies indicates that they are not elicited by sperm. Further, immunoreactivity of the sperm proteins resulting in depletion of specific circulating IgM antibodies, or other interactions between the sperm proteins and elements of the immune system, may be a factor in the suppressed state of the immune system in AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodman, T C -- Laurence, J -- Pruslin, F H -- Chiorazzi, N -- Winston, R -- CA 35018-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 7;228(4704):1211-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890184" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Acrosome/*immunology ; Adolescent ; Adult ; Antibodies/analysis ; Child ; Child, Preschool ; Female ; Fluorescent Antibody Technique ; Humans ; Immunoglobulin M/analysis ; Infant ; Male ; Molecular Weight ; Spermatozoa/*immunology ; T-Lymphocytes/immunology
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  • 55
    Publication Date: 1985-09-06
    Description: The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueckler, M -- Caruso, C -- Baldwin, S A -- Panico, M -- Blench, I -- Morris, H R -- Allard, W J -- Lienhard, G E -- Lodish, H F -- GM22996/GM/NIGMS NIH HHS/ -- HL32262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Sep 6;229(4717):941-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3839598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Carrier Proteins/genetics/metabolism ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/genetics ; Erythrocytes/metabolism ; Glucose/*metabolism ; Humans ; Liver Neoplasms, Experimental/metabolism ; *Membrane Proteins/genetics/metabolism ; Molecular Weight ; Monosaccharide Transport Proteins ; Protein Conformation ; RNA, Messenger/genetics ; Tissue Distribution
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  • 56
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-05-17
    Description: The circumsporozite protein, a surface antigen of the sporozoite stage of the monkey malarial parasite Plasmodium knowlesi, was expressed in the yeast Saccharomyces cerevisiae by using an expression vector containing the 5' regulatory region of the yeast alcohol dehydrogenase I gene. It was necessary to eliminate the entire 5' upstream region of the parasite DNA to obtain the expression of this protein. Only the circumsporozoite precursor was produced by the yeast transformants, as detected by immunoblotting. About 55 and 20 percent of the circumsporozoite protein produced in yeast was associated wtih the 25,000 g and 150,000 g particulate fractions, respectively. The protein could be solubilized in Triton X-100 and was stable in solubilized extracts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Godson, G N -- 1 R01 AI21496-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):879-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3890178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Protozoan/*genetics ; Antigens, Surface/*genetics ; Cloning, Molecular ; DNA, Recombinant ; Genes ; Molecular Weight ; Plasmodium/genetics/*immunology ; Protein Precursors/biosynthesis/genetics ; Protozoan Proteins/*genetics ; Saccharomyces cerevisiae/*genetics ; Transformation, Genetic
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  • 57
    Publication Date: 1985-02-08
    Description: The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seki, T -- Chang, H C -- Moriuchi, T -- Denome, R -- Ploegh, H -- Silver, J -- CA38404/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 8;227(4687):649-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Antigens, Thy-1 ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Weight ; Nucleic Acid Hybridization ; Rats
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  • 58
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-02-15
    Description: Extracellular factors from the sea urchin egg induce a change in the electrophoretic mobility of an abundant sperm membrane phosphoprotein. The modified protein was identified as guanylate cyclase. The mobility shift of the cyclase was shown to be associated with a decrease in its enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ward, G E -- Garbers, D L -- Vacquier, V D -- HD-10254/HD/NICHD NIH HHS/ -- HD-12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 15;227(4688):768-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Enzyme Activation ; Female ; Fertilization ; Guanylate Cyclase/*metabolism ; Male ; Membrane Proteins/metabolism ; Molecular Weight ; Phosphoproteins/metabolism ; Sea Urchins ; Sperm Maturation ; *Sperm-Ovum Interactions ; Spermatozoa/*enzymology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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