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  • Mice  (597)
  • Female  (489)
  • Models, Molecular  (214)
  • American Association for the Advancement of Science (AAAS)  (1,215)
  • 1990-1994  (1,215)
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  • 1
    Publication Date: 1994-02-25
    Description: Activation of the serine-threonine kinase p34cdc2 at an inappropriate time during the cell cycle leads to cell death that resembles apoptosis. Premature activation of p34cdc2 was shown to be required for apoptosis induced by a lymphocyte granule protease. The kinase was rapidly activated and tyrosine dephosphorylated at the initiation of apoptosis. DNA fragmentation and nuclear collapse could be prevented by blocking p34cdc2 activity with excess peptide substrate, or by inactivating p34cdc2 in a temperature-sensitive mutant. Premature p34cdc2 activation may be a general mechanism by which cells induced to undergo apoptosis initiate the disruption of the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, L -- Nishioka, W K -- Th'ng, J -- Bradbury, E M -- Litchfield, D W -- Greenberg, A H -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1143-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108732" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; CDC2 Protein Kinase/*metabolism ; DNA Damage ; Deoxyribonucleases/pharmacology ; Enzyme Activation ; Enzyme Induction ; Membrane Glycoproteins/pharmacology ; Mice ; Mitosis ; Molecular Sequence Data ; Perforin ; Phosphorylation ; Pore Forming Cytotoxic Proteins ; Serine Endopeptidases/pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1994-01-07
    Description: Coexpression of the human Met receptor and its ligand, hepatocyte growth factor/scatter factor (HGF/SF), in NIH 3T3 fibroblasts causes the cells to become tumorigenic in nude mice. The resultant tumors display lumen-like morphology, contain carcinoma-like focal areas with intercellular junctions resembling desmosomes, and coexpress epithelial (cytokeratin) and mesenchymal (vimentin) cytoskeletal markers. The tumor cells also display enhanced expression of desmosomal and tight-junction proteins. The apparent mesenchymal to epithelial conversion of the tumor cells mimics the conversion that occurs during embryonic kidney development, suggesting that Met-HGF/SF signaling plays a role in this process as well as in tumors that express both epithelial and mesenchymal markers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsarfaty, I -- Rong, S -- Resau, J H -- Rulong, S -- da Silva, P P -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, National Cancer Institute (NCI)-Frederick Cancer Research and Development Center, MD 21702-1201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7505952" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Transformation, Neoplastic ; Desmosomes/ultrastructure ; Epithelial Cells ; Hepatocyte Growth Factor/metabolism/pharmacology ; Keratins/biosynthesis ; Kidney/embryology/metabolism ; Mesoderm/cytology ; Mice ; Mice, Nude ; Neoplasms, Experimental/metabolism/*pathology ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-met ; *Proto-Oncogenes ; Receptor Protein-Tyrosine Kinases/genetics/*metabolism ; Signal Transduction ; Transfection ; Vimentin/biosynthesis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, C -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1216.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122099" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Clinical Trials as Topic ; Female ; Humans ; Informed Consent ; *Institute of Medicine (U.S.) ; National Institutes of Health (U.S.) ; *Pregnancy ; *Pregnant Women ; Research Subjects ; United States ; *Women's Health
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-26
    Description: The interaction of B7-related molecules on antigen-presenting cells with CD28 or CTLA-4 antigens on T cells provides a second signal for T cell activation. Selection inhibition of the B7-CD28 or B7-CTLA-4 interactions produces antigen-specific T cell unresponsiveness in vitro and suppresses immune function in vivo. To determine whether selective inhibition of the B7-CD28 or B7-CTLA-4 interactions could suppress spontaneous autoimmune disease, a B7-binding protein was generated by genetic fusion of the extracellular domain of murine CTLA-4 to the Fc portion of a mouse immunoglobulin G2a monoclonal antibody (muCTLA4Ig). In lupus-prone NZB/NZW filial generation (F1) mice, treatment with muCTLA4Ig blocked autoantibody production and prolonged life, even when treatment was delayed until the most advanced stage of clinical illness. These findings suggest a possible role for human CTLA4Ig in the treatment of autoimmune diseases in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finck, B K -- Linsley, P S -- Wofsy, D -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1225-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7520604" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antibodies, Antinuclear/biosynthesis ; Antibodies, Monoclonal ; Antigens, CD ; Antigens, CD80/metabolism ; Antigens, Differentiation/immunology/metabolism/*therapeutic use ; B-Lymphocytes/immunology ; CTLA-4 Antigen ; Female ; Humans ; *Immunoconjugates ; Immunotherapy ; Lupus Erythematosus, Systemic/immunology/*therapy ; Mice ; Mice, Inbred NZB ; Mice, Inbred Strains ; Recombinant Fusion Proteins/therapeutic use ; T-Lymphocytes/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1994-06-24
    Description: Two ternary complexes of rat DNA polymerase beta (pol beta), a DNA template-primer, and dideoxycytidine triphosphate (ddCTP) have been determined at 2.9 A and 3.6 A resolution, respectively. ddCTP is the triphosphate of dideoxycytidine (ddC), a nucleoside analog that targets the reverse transcriptase of human immunodeficiency virus (HIV) and is at present used to treat AIDS. Although crystals of the two complexes belong to different space groups, the structures are similar, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces. In the pol beta active site, the attacking 3'-OH of the elongating primer, the ddCTP phosphates, and two Mg2+ ions are all clustered around Asp190, Asp192, and Asp256. Two of these residues, Asp190 and Asp256, are present in the amino acid sequences of all polymerases so far studied and are also spatially similar in the four polymerases--the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, T7 RNA polymerase, and rat DNA pol beta--whose crystal structures are now known. A two-metal ion mechanism is described for the nucleotidyl transfer reaction and may apply to all polymerases. In the ternary complex structures analyzed, pol beta binds to the DNA template-primer in a different manner from that recently proposed for other polymerase-DNA models.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelletier, H -- Sawaya, M R -- Kumar, A -- Wilson, S H -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- ES06839/ES/NIEHS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1891-903.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, San Diego 92093-0317.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7516580" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; DNA/chemistry/metabolism ; DNA Polymerase I/*chemistry/metabolism ; DNA Primers/*chemistry/metabolism ; DNA-Directed RNA Polymerases/chemistry/metabolism ; Deoxycytosine Nucleotides/*chemistry/metabolism ; Dideoxynucleotides ; HIV Reverse Transcriptase ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; RNA-Directed DNA Polymerase/chemistry/metabolism ; Rats ; Recombinant Proteins ; Templates, Genetic ; Thymine Nucleotides/chemistry/metabolism ; Viral Proteins ; Zidovudine/analogs & derivatives/chemistry/metabolism
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  • 6
    Publication Date: 1994-10-14
    Description: Mice deficient for the gene encoding alpha-calcium-calmodulin-dependent kinase II (alpha-CaMKII knockout mice) provide a promising tool to link behavioral and cellular abnormalities with a specific molecular lesion. The heterozygous mouse exhibited a well-circumscribed syndrome of behavioral abnormalities, consisting primarily of a decreased fear response and an increase in defensive aggression, in the absence of any measured cognitive deficits. Unlike the heterozygote, the homozygote displayed abnormal behavior in all paradigms tested. At the cellular level, both extracellular and whole-cell patch clamp recordings indicated that serotonin release in putative serotonergic neurons of the dorsal raphe was reduced. Thus, alpha-CaMKII knockout mice, in particular the heterozygote, may provide a model for studying the molecular and cellular basis underlying emotional disorders involving fear and aggression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, C -- Rainnie, D G -- Greene, R W -- Tonegawa, S -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Cancer Research, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939668" target="_blank"〉PubMed〈/a〉
    Keywords: *Aggression ; Animals ; Behavior, Animal ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/deficiency/genetics/*physiology ; *Fear ; Fluoxetine/pharmacology ; Gene Dosage ; Heterozygote ; Homozygote ; In Vitro Techniques ; Membrane Potentials ; Mice ; Mice, Knockout ; Mutation ; Neurons/metabolism ; Patch-Clamp Techniques ; Raphe Nuclei/metabolism ; Serotonin/metabolism/pharmacology ; Synaptic Transmission/drug effects
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-04
    Description: Conversion of external signals into proliferative responses may be mediated by interactions between signaling pathways that control cell proliferation. Interactions between G alpha s, the alpha subunit of the heterotrimeric guanine nucleotide binding protein that stimulates adenylyl cyclase, and Ras, an important element in growth factor signaling, were studied. Expression of activated G alpha s in NIH 3T3 cells increased intracellular concentrations of adenosine 3',5'-monophosphate (cAMP) and inhibited H-Ras-stimulated DNA synthesis and mitogen-activated protein kinase activity. Activated G alpha s and 8-Br-cAMP suppressed H-Ras-induced transformation of NIH 3T3 cells. Apparently, G alpha s inhibits proliferative signals from Ras by stimulating cAMP production and activating protein kinase A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J -- Iyengar, R -- CA-44998/CA/NCI NIH HHS/ -- DK-38761/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Mount Sinai School of Medicine, City University of New York, NY 10029.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122111" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Enzyme Activation ; GTP-Binding Proteins/genetics/*physiology ; *Genes, ras ; Mice ; Mitogen-Activated Protein Kinase 1 ; Mutagenesis, Site-Directed ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Signal Transduction ; Transfection
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  • 8
    Publication Date: 1994-03-11
    Description: The gamma chain of the interleukin-2 (IL-2) receptor is shared with the functional IL-4 receptor and is causatively related to X-linked severe combined immunodeficiency (XSCID), which is ascribed to a profound T cell defect. Studies with monoclonal antibodies specific for the IL-2 receptor gamma chain showed that the gamma chain participates in the functional high-affinity receptor complexes for IL-7 that are involved in the differentiation of T and B cells. Participation of the gamma subunit in more than one receptor may enable the elucidation of the mechanisms of XSCID development and lymphocyte differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, M -- Takeshita, T -- Higuchi, M -- Nakamura, M -- Sudo, T -- Nishikawa, S -- Sugamura, K -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1453-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128231" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; B-Lymphocytes/*immunology ; Cell Line ; Cells, Cultured ; Female ; Genetic Linkage ; Interleukin-7/*metabolism/pharmacology ; Mice ; Mice, Inbred C57BL ; Receptors, Interleukin/*metabolism ; Receptors, Interleukin-2/genetics/immunology/*metabolism ; Receptors, Interleukin-7 ; Severe Combined Immunodeficiency/genetics/immunology ; T-Lymphocytes/*immunology ; X Chromosome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 1994-04-01
    Description: The crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L -- Durley, R C -- Mathews, F S -- Davidson, V L -- GM41574/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):86-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, 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/8140419" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/metabolism ; Computer Graphics ; Cytochrome c Group/*chemistry/metabolism ; Electron Transport ; Hydrogen Bonding ; *Indolequinones ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/metabolism ; Paracoccus denitrificans/*chemistry/enzymology ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Quinones/chemistry/metabolism ; Software ; Tryptophan/analogs & derivatives/chemistry/metabolism
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  • 10
    Publication Date: 1994-08-26
    Description: Experimental autoimmune encephalomyelitis (EAE) is a cell-mediated autoimmune disease that serves as an animal model for multiple sclerosis. Oral administration of myelin basic protein (MBP) suppresses EAE by inducing peripheral tolerance. T cell clones were isolated from the mesenteric lymph nodes of SJL mice that had been orally tolerized to MBP. These clones were CD4+ and were structurally identical to T helper cell type 1 (TH1) encephalitogenic CD4+ clones in T cell receptor usage, major histocompatibility complex restriction, and epitope recognition. However, they produced transforming growth factor-beta with various amounts of interleukin-4 and interleukin-10 and suppressed EAE induced with either MBP or proteolipid protein. Thus, mucosally derived TH2-like clones induced by oral antigen can actively regulate immune responses in vivo and may represent a different subset of T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Kuchroo, V K -- Inobe, J -- Hafler, D A -- Weiner, H L -- AR/A143220/AR/NIAMS NIH HHS/ -- NS29352/NS/NINDS NIH HHS/ -- NS30843/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1237-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7520605" target="_blank"〉PubMed〈/a〉
    Keywords: Administration, Oral ; Amino Acid Sequence ; Animals ; CD4-Positive T-Lymphocytes/*immunology ; Clone Cells ; Encephalomyelitis, Autoimmune, Experimental/*immunology ; Epitopes/immunology ; *Immune Tolerance ; Interleukin-10/biosynthesis ; Interleukin-4/biosynthesis ; Lymph Nodes/immunology ; Major Histocompatibility Complex ; Mesentery/immunology ; Mice ; Molecular Sequence Data ; Myelin Basic Protein/administration & dosage/*immunology ; Myelin Proteins/immunology ; Myelin Proteolipid Protein ; Receptors, Antigen, T-Cell/immunology ; Transforming Growth Factor beta/biosynthesis
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  • 11
    Publication Date: 1994-09-23
    Description: Indirect evidence implicates gamma delta T cells in the cross-regulation of CD4 alpha beta T cell responses. Adoptive transfer of small numbers of gamma delta T cells from ovalbumin (OVA)-tolerant mice selectively suppressed TH2-dependent immunoglobulin E (IgE) antibody production without affecting parallel IgG responses. Challenge of these gamma delta T cells in vitro with specific antigen resulted in production of high levels of interferon gamma. The effects of the gamma delta T cells may be mediated by direct inhibition of OVA-specific CD4+ TH2 cell proliferation or selection for specific CD4 TH2 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McMenamin, C -- Pimm, C -- McKersey, M -- Holt, P G -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1869-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cell Biology, Institute for Child Health Research, West Perth, Western Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7916481" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/*immunology ; Dose-Response Relationship, Immunologic ; *Immune Tolerance ; Immunoglobulin E/*biosynthesis ; Immunoglobulin G/biosynthesis ; Immunotherapy, Adoptive ; Interferon-gamma/biosynthesis ; Interleukin-2/biosynthesis ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Ovalbumin/immunology ; Receptors, Antigen, T-Cell, gamma-delta/*immunology ; T-Lymphocyte Subsets/*immunology ; Transforming Growth Factor beta/biosynthesis
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  • 12
    Publication Date: 1994-09-02
    Description: As a step toward developing poliovirus as a vaccine vector, poliovirus recombinants were constructed by fusing exogenous peptides (up to 400 amino acids) and an artificial cleavage site for viral protease 3Cpro to the amino terminus of the viral polyprotein. Viral replication proceeded normally. An extended polyprotein was produced in infected cells and proteolytically processed into the complete array of viral proteins plus the foreign peptide, which was excluded from mature virions. The recombinants retained exogenous sequences through successive rounds of replication in culture and in vivo. Infection of animals with recombinants elicited a humoral immune response to the foreign peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andino, R -- Silvera, D -- Suggett, S D -- Achacoso, P L -- Miller, C J -- Baltimore, D -- Feinberg, M B -- AI22346/AI/NIAID NIH HHS/ -- AI35545/AI/NIAID NIH HHS/ -- RR00169/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073288" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Bacterial/biosynthesis ; Antibodies, Viral/biosynthesis ; Antigens, Bacterial/genetics/immunology ; Antigens, Viral/genetics/immunology ; Base Sequence ; Cloning, Molecular ; *Genetic Engineering ; Genetic Vectors ; HeLa Cells ; Humans ; Macaca fascicularis ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Poliovirus/*genetics/immunology/physiology ; Poliovirus Vaccine, Oral/*genetics ; *Protein Biosynthesis ; Proteins/metabolism ; Recombinant Proteins/biosynthesis/metabolism ; Vaccines, Synthetic/genetics/*immunology ; Virus Replication
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  • 13
    Publication Date: 1994-10-14
    Description: Schizophrenia is a complex illness characterized by multiple types of symptoms involving many aspects of cognition and emotion. Most efforts to identify its underlying neural substrates have focused on a strategy that relates a single symptom to a single brain region. An alternative hypothesis, that the variety of symptoms could be explained by a lesion in midline neural circuits mediating attention and information processing, is explored. Magnetic resonance images from patients and controls were transformed with a "bounding box" to produce an "average schizophrenic brain" and an "average normal brain." After image subtraction of the two averages, the areas of difference were displayed as an effect size map. Specific regional abnormalities were observed in the thalamus and adjacent white matter. An abnormality in the thalamus and related circuitry explains the diverse symptoms of schizophrenia parsimoniously because they could all result from a defect in filtering or gating sensory input, which is one of the primary functions of the thalamus in the human brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andreasen, N C -- Arndt, S -- Swayze, V 2nd -- Cizadlo, T -- Flaum, M -- O'Leary, D -- Ehrhardt, J C -- Yuh, W T -- MH31593/MH/NIMH NIH HHS/ -- MH40856/MH/NIMH NIH HHS/ -- MHCRC 43271/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):294-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mental Health Clinical Research Center, College of Medicine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939669" target="_blank"〉PubMed〈/a〉
    Keywords: Brain/pathology ; Female ; Humans ; Image Processing, Computer-Assisted ; Magnetic Resonance Imaging/*methods ; Male ; Schizophrenia/*pathology ; Software ; Subtraction Technique ; Thalamus/*pathology
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  • 14
    Publication Date: 1994-09-09
    Description: Endogenous DNA adducts may contribute to the etiology of human genetic disease and cancer. One potential source of endogenous DNA adducts is lipid peroxidation, which generates mutagenic carbonyl compounds such as malondialdehyde. A sensitive mass spectrometric method permitted detection and quantitation of the major malondialdehyde-DNA adduct, a pyrimidopurinone derived from deoxyguanosine. DNA from disease-free human liver was found to contain 5400 adducts per cell, a frequency comparable to that of adducts formed by exogenous carcinogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chaudhary, A K -- Nokubo, M -- Reddy, G R -- Yeola, S N -- Morrow, J D -- Blair, I A -- Marnett, L J -- CA47479/CA/NCI NIH HHS/ -- ES00267/ES/NIEHS NIH HHS/ -- GM42056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1580-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉A. B. Hancock Jr. Memorial Laboratory for Cancer Research, Vanderbilt University School of Medicine, Nashville, TN 37232-0146.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8079172" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Animals ; Carbon Tetrachloride/toxicity ; DNA/*chemistry ; DNA Damage ; Deoxyguanosine/*analogs & derivatives/analysis/*metabolism ; Female ; Gas Chromatography-Mass Spectrometry ; Humans ; Lipid Peroxidation ; Liver/*chemistry ; Male ; Malondialdehyde/*metabolism ; Rats ; Rats, Sprague-Dawley
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-24
    Description: Glycosyl-phosphatidylinositol (GPI)-anchored proteins have been reported to reside in clusters collected over small membrane invaginations called caveolae. The detection of different GPI-anchored proteins with fluorescently labeled monoclonal antibodies showed that these proteins are not constitutively concentrated in caveolae; they enter these structures independently after cross-linking with polyclonal secondary antibodies. Analysis of the cell surface distribution of the GPI-anchored folate receptor by electron microscopy confirms these observations. Thus, multimerization of GPI-anchored proteins regulates their sequestration in caveolae, but in the absence of agents that promote clustering they are diffusely distributed over the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayor, S -- Rothberg, K G -- Maxfield, F R -- DK27083/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1948-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, 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/7516582" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antibodies, Monoclonal ; Antigens, CD/analysis/immunology/metabolism ; Antigens, CD55 ; Antigens, Surface/analysis/immunology/metabolism ; Antigens, Thy-1 ; Carrier Proteins/analysis/immunology/*metabolism ; Caveolin 1 ; *Caveolins ; Cell Membrane/*metabolism/ultrastructure ; Fluorescent Antibody Technique ; Folate Receptors, GPI-Anchored ; Folic Acid/metabolism ; Glycosylphosphatidylinositols/analysis/*metabolism ; Humans ; Immunoglobulin G/metabolism ; Membrane Glycoproteins/analysis/immunology/metabolism ; Membrane Proteins/analysis ; Mice ; Microscopy, Electron ; *Receptors, Cell Surface ; Tumor Cells, Cultured
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  • 16
    Publication Date: 1994-12-16
    Description: Representational difference analysis was used to isolate unique sequences present in more than 90 percent of Kaposi's sarcoma (KS) tissues obtained from patients with acquired immunodeficiency syndrome (AIDS). These sequences were not present in tissue DNA from non-AIDS patients, but were present in 15 percent of non-KS tissue DNA samples from AIDS patients. The sequences are homologous to, but distinct from, capsid and tegument protein genes of the Gammaherpesvirinae, herpesvirus saimiri and Epstein-Barr virus. These KS-associated herpesvirus-like (KSHV) sequences appear to define a new human herpesvirus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, Y -- Cesarman, E -- Pessin, M S -- Lee, F -- Culpepper, J -- Knowles, D M -- Moore, P S -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1865-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, 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/7997879" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*complications ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA, Viral/*analysis/chemistry/genetics ; Female ; Herpesviridae/*genetics ; Herpesvirus 2, Saimiriine/genetics ; Herpesvirus 4, Human/genetics ; Humans ; Male ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Open Reading Frames ; Polymerase Chain Reaction ; Retrospective Studies ; Sarcoma, Kaposi/etiology/*virology ; Sequence Homology, Amino Acid
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  • 17
    Publication Date: 1994-11-11
    Description: Signals mediated by the T cell receptor (TCR) are required for thymocyte maturation and selection. To examine the role of TCR zeta chain signals in development, TCR expression was restored in zeta-deficient mice with transgenic zeta chains that partially or completely lacked sequences required for signal transduction. The zeta chain played a role in thymic development by promoting TCR surface expression, but zeta-mediated signals were not essential because TCRs that contained signaling-deficient zeta chains promoted T cell maturation and transduced signals associated with thymic selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shores, E W -- Huang, K -- Tran, T -- Lee, E -- Grinberg, A -- Love, P E -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1047-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematologic Products, Food and Drug Administration, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7526464" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/analysis/genetics ; Antigens, CD4/analysis ; Antigens, CD5 ; Antigens, CD8/analysis ; Antigens, Differentiation, T-Lymphocyte/analysis ; *DNA-Binding Proteins ; Down-Regulation ; Gene Expression ; *Homeodomain Proteins ; Lectins, C-Type ; Lymph Nodes/immunology ; Membrane Proteins/genetics/*physiology ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Proteins/genetics ; RNA, Messenger/genetics/metabolism ; Receptors, Antigen, T-Cell/genetics/*physiology ; Signal Transduction ; T-Lymphocytes/cytology/*immunology ; Thymus Gland/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shreeve, J -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):34-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140418" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ethiopia ; Female ; *Fossils ; History, Ancient ; *Hominidae ; Humans ; Male ; *Skull
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-11
    Description: Long-tailed manakins mate in leks and cooperate in multiyear male-male partnerships. An alpha male is responsible for virtually all mating, whereas a beta male assists in the courtship displays. Such altruism by the beta male poses a problem for evolutionary theory because most theoretical treatments and empirical examples of cooperative behavior involve kin selection or reciprocity. Here it is shown that alpha and beta partners are not relatives and that reciprocity is not involved. Instead, direct, though long-delayed benefits to beta males are demonstrated, which include rare copulations, ascension to alpha status, and female lek fidelity. These benefits maintain this unusual form of male-male cooperation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McDonald, D B -- Potts, W K -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1030-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Archbold Biological Station, Lake Placid, FL 33852-2057.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973654" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Birds/genetics/*physiology ; *Cooperative Behavior ; Copulation ; Female ; Heterozygote ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; *Sexual Behavior, Animal
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  • 20
    Publication Date: 1994-02-04
    Description: The three-dimensional structure of a catalytic antibody (1F7) with chorismate mutase activity has been determined to 3.0 A resolution as a complex with a transition state analog. The structural data suggest that the antibody stabilizes the same conformationally restricted pericyclic transition state as occurs in the uncatalyzed reaction. Overall shape and charge complementarity between the combining site and the transition state analog dictate preferential binding of the correct substrate enantiomer in a conformation appropriate for reaction. Comparison with the structure of a chorismate mutase enzyme indicates an overall similarity between the catalytic mechanism employed by the two proteins. Differences in the number of specific interactions available for restricting the rotational degrees of freedom in the transition state, and the lack of multiple electrostatic interactions that might stabilize charge separation in this highly polarized metastable species, are likely to account for the observed 10(4) times lower activity of the antibody relative to that of the natural enzymes that catalyze this reaction. The structure of the 1F7 Fab'-hapten complex provides confirmation that the properties of an antibody catalyst faithfully reflect the design of the transition state analog.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haynes, M R -- Stura, E A -- Hilvert, D -- Wilson, I A -- AI-23498/AI/NIAID NIH HHS/ -- GM-38273/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):646-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303271" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*chemistry/metabolism ; Bacillus subtilis/enzymology ; Binding Sites ; Binding Sites, Antibody ; Catalysis ; Chorismate Mutase/*chemistry/metabolism ; Chorismic Acid/metabolism ; Crystallization ; Haptens ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/metabolism ; Models, Molecular ; Thermodynamics
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-05-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischman, J -- New York, N.Y. -- Science. 1994 May 20;264(5162):1082-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8178166" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Female ; *Fossils ; Hominidae/*anatomy & histology ; Humans ; *Labor, Obstetric ; Pelvic Bones/*anatomy & histology ; Pelvimetry ; Pregnancy
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolberg, R -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1859-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bedding and Linens ; Disease Vectors ; Dracunculiasis/prevention & control ; Female ; Fishes ; Humans ; Insect Control/*methods ; Malaria/prevention & control ; Male ; Parasitic Diseases/*prevention & control ; Pest Control, Biological/*methods ; Schistosomiasis/prevention & control ; World Health Organization
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischman, J -- Ray, L B -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1459.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985005" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Contraception ; Female ; Humans ; Male ; *Reproduction/genetics/physiology ; Sex Differentiation
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-12
    Description: The transcription factor nuclear factor-kappa B (NF-kappa B) is critical for the inducible expression of multiple cellular and viral genes involved in inflammation and infection including interleukin-1 (IL-1), IL-6, and adhesion molecules. The anti-inflammatory drugs sodium salicylate and aspirin inhibited the activation of NF-kappa B, which further explains the mechanism of action of these drugs. This inhibition prevented the degradation of the NF-kappa B inhibitor, I kappa B, and therefore NF-kappa B was retained in the cytosol. Sodium salicylate and aspirin also inhibited NF-kappa B-dependent transcription from the Ig kappa enhancer and the human immunodeficiency virus (HIV) long terminal repeat (LTR) in transfected T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopp, E -- Ghosh, S -- R01 AI 33443-01A1/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):956-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052854" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspirin/*pharmacology ; Cell Line ; Enhancer Elements, Genetic ; Gene Expression/drug effects ; Genes, Reporter ; HIV Long Terminal Repeat ; HIV-1/genetics ; Humans ; Immunoglobulin kappa-Chains/genetics ; Lipopolysaccharides/pharmacology ; Mice ; NF-kappa B/*antagonists & inhibitors/metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Protein Biosynthesis/drug effects ; Proto-Oncogene Proteins/metabolism ; Sodium Salicylate/*pharmacology ; T-Lymphocytes/metabolism ; Transcription Factor RelB ; *Transcription Factors ; Transfection ; Tumor Cells, Cultured
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  • 25
    Publication Date: 1994-07-01
    Description: Here it is shown, with the use of protein-protein photocrosslinking, that the carboxyl-terminal region of the alpha subunit of RNA polymerase (RNAP) is in direct physical proximity to the activating region of the catabolite gene activator protein (CAP) in the ternary complex of the lac promoter, RNAP, and CAP. These results strongly support the proposal that transcription activation by CAP involves protein-protein contact between the carboxyl-terminal region of the alpha subunit and the activating region of CAP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Ebright, Y W -- Ebright, R H -- GM41376/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):90-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, New Brunswick, NJ 08855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016656" target="_blank"〉PubMed〈/a〉
    Keywords: Azides/metabolism ; Cross-Linking Reagents ; Crystallography, X-Ray ; Cyclic AMP Receptor Protein/chemistry/*metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Lac Operon ; Models, Molecular ; *Promoter Regions, Genetic ; Pyridines/metabolism ; *Transcriptional Activation
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  • 26
    Publication Date: 1994-03-25
    Description: The European wild boar was crossed with the domesticated Large White pig to genetically dissect phenotypic differences between these populations for growth and fat deposition. The most important effects were clustered on chromosome 4, with a single region accounting for a large part of the breed difference in growth rate, fatness, and length of the small intestine. The study is an advance in genome analyses and documents the usefulness of crosses between divergent outbred populations for the detection and characterization of quantitative trait loci. The genetic mapping of a major locus for fat deposition in the pig could have implications for understanding human obesity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersson, L -- Haley, C S -- Ellegren, H -- Knott, S A -- Johansson, M -- Andersson, K -- Andersson-Eklund, L -- Edfors-Lilja, I -- Fredholm, M -- Hansson, I -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, Uppsala.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134840" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*anatomy & histology ; Animals ; *Chromosome Mapping ; Crosses, Genetic ; Disease Models, Animal ; Female ; *Genes ; Genetic Markers ; Humans ; Intestine, Small/anatomy & histology ; Likelihood Functions ; Male ; Obesity/genetics ; Phenotype ; Swine/anatomy & histology/*genetics/growth & development
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  • 27
    Publication Date: 1994-10-21
    Description: The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Z W -- Koh, M -- Van Driessche, G -- Van Beeumen, J J -- Bartsch, R G -- Meyer, T E -- Cusanovich, M A -- Mathews, F S -- GM-20530/GM/NIGMS NIH HHS/ -- GM-21277/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):430-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, 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/7939681" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chromatium/*enzymology ; Computer Graphics ; Crystallography, X-Ray ; Cytochrome c Group/*chemistry ; Electron Transport ; Flavin-Adenine Dinucleotide/metabolism ; Hydrogen Bonding ; Models, Molecular ; Oxidoreductases/*chemistry ; Protein Conformation ; Protein Structure, Secondary
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: Estrogen hormones produce physiological actions within a variety of target sites in the body and during development by activating a specific receptor protein. Hormone responsiveness for the estrogen receptor protein was investigated at different stages of development with the use of gene knockout techniques because no natural genetic mutants have been described. A mutant mouse line without a functional estrogen receptor was created and is being used to assess estrogen responsiveness. Both sexes of these mutant animals are infertile and show a variety of phenotypic changes, some of which are associated with the gonads, mammary glands, reproductive tracts, and skeletal tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korach, K S -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1524-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Receptor Biology Section, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985022" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Estrogens/*physiology ; Female ; Heterozygote ; Homozygote ; Humans ; Infertility, Female/etiology ; Infertility, Male/etiology ; Male ; Mice ; Mice, Knockout ; Mutation ; Phenotype ; Receptors, Estrogen/genetics/*physiology ; Signal Transduction
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  • 29
    Publication Date: 1994-03-25
    Description: Fas is an apoptosis-signaling receptor molecule on the surface of a number of cell types. Molecular cloning and nucleotide sequence analysis revealed a human Fas messenger RNA variant capable of encoding a soluble Fas molecule lacking the transmembrane domain because of the deletion of an exon encoding this region. The expression of soluble Fas was confirmed by flow cytometry and immunocytochemical analysis. Supernatants from cells transfected with the variant messenger RNA blocked apoptosis induced by the antibody to Fas. Levels of soluble Fas were elevated in patients with systemic lupus erythematosus, and mice injected with soluble Fas displayed autoimmune features.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, J -- Zhou, T -- Liu, C -- Shapiro, J P -- Brauer, M J -- Kiefer, M C -- Barr, P J -- Mountz, J D -- P01 AR03555/AR/NIAMS NIH HHS/ -- P50 AI23694/AI/NIAID NIH HHS/ -- P60 AR20614/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1759-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Alabama at Birmingham.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7510905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antigens, CD95 ; Antigens, Surface/chemistry/genetics/immunology/*physiology ; *Apoptosis ; Arthritis, Rheumatoid/blood ; Base Sequence ; Cell Line ; Cell Membrane/chemistry ; Humans ; Lupus Erythematosus, Systemic/blood ; Mice ; Molecular Sequence Data ; RNA, Messenger/genetics ; Solubility ; T-Lymphocyte Subsets/immunology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-30
    Description: The cellular proto-oncogene c-myc is involved in cell proliferation and transformation but is also implicated in the induction of programmed cell death (apoptosis). The same characteristics have been described for the tumor suppressor gene p53, the most commonly mutated gene in human cancer. In quiescent mouse fibroblasts expressing wild-type p53 protein, activation of c-Myc was found to induce apoptosis and cell cycle reentry, preceded by stabilization of p53. In contrast, in quiescent p53-null fibroblasts, activation of c-Myc induced cell cycle reentry but not apoptosis. These results suggest that p53 mediates apoptosis as a safeguard mechanism to prevent cell proliferation induced by oncogene activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hermeking, H -- Eick, D -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2091-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Klinische Molekularbiologie und Tumorgenetik Forschungszentrum fur Umwelt und Gesundheit, GSF, Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091232" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Apoptosis ; Cell Line ; Estradiol/pharmacology ; G1 Phase ; Gene Expression Regulation ; Genes, myc ; Genes, p53 ; Mice ; Proto-Oncogene Proteins c-myc/*metabolism ; Tamoxifen/analogs & derivatives/pharmacology ; Transfection ; Tumor Suppressor Protein p53/*metabolism
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinholster, G -- New York, N.Y. -- Science. 1994 Apr 8;264(5156):197-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8146647" target="_blank"〉PubMed〈/a〉
    Keywords: Apnea/*complications/history ; Female ; *Forensic Medicine ; History, 20th Century ; Humans ; Infant ; *Infanticide ; Male ; *Publishing/history ; Sudden Infant Death/*etiology
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  • 32
    Publication Date: 1994-04-29
    Description: In a search for genes that regulate circadian rhythms in mammals, the progeny of mice treated with N-ethyl-N-nitrosourea (ENU) were screened for circadian clock mutations. A semidominant mutation, Clock, that lengthens circadian period and abolishes persistence of rhythmicity was identified. Clock segregated as a single gene that mapped to the midportion of mouse chromosome 5, a region syntenic to human chromosome 4. The power of ENU mutagenesis combined with the ability to clone murine genes by map position provides a generally applicable approach to study complex behavior in mammals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3839659/" 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/PMC3839659/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vitaterna, M H -- King, D P -- Chang, A M -- Kornhauser, J M -- Lowrey, P L -- McDonald, J D -- Dove, W F -- Pinto, L H -- Turek, F W -- Takahashi, J S -- P30-CA07175/CA/NCI NIH HHS/ -- R01-DK40493/DK/NIDDK NIH HHS/ -- T32 NS071040/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- etc. -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):719-25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Physiology, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171325" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Circadian Rhythm/*genetics ; Ethylnitrosourea ; Female ; *Genes ; Genotype ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; *Mutagenesis ; Phenotype
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-09-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plotkin, S A -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1383-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pasteur-Merieux-Connaught, Marnes-la-Coquette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073277" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Chickenpox/prevention & control ; Chickenpox Vaccine ; Child ; Clinical Trials as Topic ; Cytomegalovirus/*immunology ; Cytomegalovirus Infections/prevention & control ; Female ; Herpes Zoster/prevention & control ; Herpesvirus 3, Human/*immunology ; Humans ; Vaccines, Attenuated/immunology ; *Viral Vaccines/immunology
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  • 34
    Publication Date: 1994-03-18
    Description: Engagement of antigen receptor complexes induces rapid activation of Src-family kinases and association with phosphatidylinositol-3' kinase (PI-3 kinase). Here it was found that the Src homology 3 (SH3) domain of Lyn and Fyn bound to a proline-rich region (residues 84 to 99) within the 85-kilodalton subunit (p85) of PI-3 kinase. The binding of SH3 to the purified kinase led to a five- to sevenfold increase in the specific activity of PI-3 kinase. Ligand-induced receptor stimulation activated PI-3 kinase, and this activation was blocked by a peptide containing residues 84 to 99 of p85. These data demonstrate a mechanism for PI-3 kinase activation and show that binding of SH3 domains to proline-rich target sequences can regulate enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pleiman, C M -- Hertz, W M -- Cambier, J C -- A120519/PHS HHS/ -- A121768/PHS HHS/ -- A129903/PHS HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1609-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128248" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*enzymology ; Enzyme Activation ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism ; Proline/chemistry ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-fyn ; *src-Family Kinases
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Borstel, R C -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1144-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7832907" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anticarcinogenic Agents ; *Antimutagenic Agents ; Carcinogenicity Tests/*statistics & numerical data ; DNA Repair ; Humans ; Mice
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-05-20
    Description: A predictive rule for protein folding is presented that involves two recurrent glycine-based motifs that cap the carboxyl termini of alpha helices. In proteins, helices that terminated in glycine residues were found predominantly in one of these two motifs. These glycine structures had a characteristic pattern of polar and apolar residues. Visual inspection of known helical sequences was sufficient to distinguish the two motifs from each other and from internal glycines that fail to terminate helices. These glycine motifs--in which the local sequence selects between available structures--represent an example of a stereochemical rule for protein folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aurora, R -- Srinivasan, R -- Rose, G D -- GM 29458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 May 20;264(5162):1126-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, 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/8178170" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Glycine/*chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oligopeptides/chemistry ; *Protein Folding ; *Protein Structure, Secondary
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  • 37
    Publication Date: 1994-04-29
    Description: To facilitate molecular genetic analysis of vertebrate development, haploid genetics was used to construct a recombination map for the zebrafish Danio (Brachydanio) rerio. The map consists of 401 random amplified polymorphic DNAs (RAPDs) and 13 simple sequence repeats spaced at an average interval of 5.8 centimorgans. Strategies that exploit the advantages of haploid genetics and RAPD markers were developed that quickly mapped lethal and visible mutations and that placed cloned genes on the map. This map is useful for the position-based cloning of mutant genes, the characterization of chromosome rearrangements, and the investigation of evolution in vertebrate genomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Postlethwait, J H -- Johnson, S L -- Midson, C N -- Talbot, W S -- Gates, M -- Ballinger, E W -- Africa, D -- Andrews, R -- Carl, T -- Eisen, J S -- 1RO1AI26734/AI/NIAID NIH HHS/ -- HD07470/HD/NICHD NIH HHS/ -- NS23915/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Apr 29;264(5159):699-703.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Neurosciences, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171321" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chromosome Mapping ; Cloning, Molecular ; Female ; Genetic Markers ; Genotype ; Male ; Mutation ; Phenotype ; Polymerase Chain Reaction ; Repetitive Sequences, Nucleic Acid ; Software ; Zebrafish/*genetics
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  • 38
    Publication Date: 1994-06-03
    Description: Multi-wavelength anomalous diffraction (MAD) has been used to determine the structure of the regulatory enzyme of de novo synthesis of purine nucleotides, glutamine 5-phosphoribosyl-1-pyrophosphate (PRPP) amidotransferase, from Bacillus subtilis. This allosteric enzyme, a 200-kilodalton tetramer, is subject to end product regulation by purine nucleotides. The metalloenzyme from B. subtilis is a paradigm for the higher eukaryotic enzymes, which have been refractory to isolation in stable form. The two folding domains of the polypeptide are correlated with functional domains for glutamine binding and for transfer of ammonia to the substrate PRPP. Eight molecules of the feedback inhibitor adenosine monophosphate (AMP) are bound to the tetrameric enzyme in two types of binding sites: the PRPP catalytic site of each subunit and an unusual regulatory site that is immediately adjacent to each active site but is between subunits. An oxygen-sensitive [4Fe-4S] cluster in each subunit is proposed to regulate protein turnover in vivo and is distant from the catalytic site. Oxygen sensitivity of the cluster is diminished by AMP, which blocks a channel through the protein to the cluster. The structure is representative of both glutamine amidotransferases and phosphoribosyltransferases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, J L -- Zaluzec, E J -- Wery, J P -- Niu, L -- Switzer, R L -- Zalkin, H -- Satow, Y -- DK-42303/DK/NIDDK NIH HHS/ -- GM-24658/GM/NIGMS NIH HHS/ -- R37 DK042303/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1427-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197456" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Allosteric Regulation ; Amidophosphoribosyltransferase/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Bacillus subtilis/*enzymology ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Oxygen/pharmacology ; Protein Folding ; Protein Structure, Secondary ; Saccharomyces cerevisiae
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, F E -- Pan, K M -- Huang, Z -- Baldwin, M -- Fletterick, R J -- Prusiner, S B -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):530-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143-0518.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7909169" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Mice ; Mice, Transgenic ; Models, Biological ; Mutation ; PrPSc Proteins ; Prion Diseases/*metabolism/transmission ; Prions/*biosynthesis/chemistry/genetics/metabolism ; Protein Conformation ; Protein Structure, Secondary
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-01
    Description: In Caenorhabditis, the vulva is formed in the central body region from three of six equivalent cells and is induced by the gonad. In some nematodes, however, the vulva is located in the posterior body region. Vulval development has been analyzed in three such genera. The same precursor cells give rise to the vulva in Caenorhabditis and in the posterior vulva species, but in the latter the cells first migrate posteriorly. In two such species, the vulva is not induced by the gonad, but instead relies on intrinsic properties of precursor cells. Thus, evolution of organ position involves changes in induction and competence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommer, R J -- Sternberg, P W -- New York, N.Y. -- Science. 1994 Jul 1;265(5168):114-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8016644" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Caenorhabditis elegans/cytology/*growth & development ; Cell Communication ; Cell Differentiation ; Female ; Gonads/cytology/physiology ; Rhabditoidea/cytology/*growth & development ; Species Specificity ; Vulva/cytology/growth & development
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  • 41
    Publication Date: 1994-04-01
    Description: Fetal cardiomyocytes isolated from transgenic mice carrying a fusion gene of the alpha-cardiac myosin heavy chain promoter with a beta-galactosidase reporter were examined for their ability to form stable intracardiac grafts. Embryonic day 15 transgenic cardiomyocytes delivered directly into the myocardium of syngeneic hosts formed stable grafts, as identified by nuclear beta-galactosidase activity. Grafted cardiomyocytes were observed as long as 2 months after implantation, the latest date assayed. Intracardiac graft formation did not induce overtly negative effects on the host myocardium and was not associated with chronic immune rejection. Electron microscopy revealed the presence of nascent intercalated disks connecting the engrafted fetal cardiomyocytes and the host myocardium. These results suggest that intracardiac grafting might provide a useful approach for myocardial repair, provided that the grafted cells can contribute to myocardial function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soonpaa, M H -- Koh, G Y -- Klug, M G -- Field, L J -- HL45453/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Krannert Institute of Cardiology, Indiana University School of Medicine, Indianapolis 46202-4800.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140423" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Communication ; Cell Differentiation ; Cell Nucleus/metabolism ; *Cell Transplantation ; DNA/biosynthesis ; DNA Primers ; Electrocardiography ; Fetal Heart/*cytology ; *Fetal Tissue Transplantation ; Gap Junctions/physiology/ultrastructure ; Genetic Markers ; Heart/physiology ; Intercellular Junctions/physiology/*ultrastructure ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Myocardium/*cytology/ultrastructure ; beta-Galactosidase/analysis
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Messing, R B -- Gust, L D -- Petersen, D W -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1518-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Carcinogenicity Tests ; Chloroform/administration & dosage/*toxicity ; Female ; Humans ; Kidney Neoplasms/*chemically induced ; Rats ; Risk Factors ; *Water Supply
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-11
    Description: Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barford, D -- Flint, A J -- Tonks, N K -- CA53840/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Mar 11;263(5152):1397-404.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉W.M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128219" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Phosphates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/*chemistry/isolation & purification/metabolism ; Substrate Specificity ; Tungsten Compounds/metabolism
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  • 44
    Publication Date: 1994-05-13
    Description: Many tumors express tumor-specific antigens capable of being presented to CD8+ T cells by major histocompatibility complex (MHC) class I molecules. Antigen presentation models predict that the tumor cell itself should present these antigens to T cells. However, when conditions for the priming of tumor-specific responses were examined in mice, no detectable presentation of MHC class I-restricted tumor antigens by the tumor itself was found. Rather, tumor antigens were exclusively presented by host bone marrow-derived cells. Thus, MHC class I-restricted antigens are efficiently transferred in vivo to bone marrow-derived antigen-presenting cells, which suggests that human leukocyte antigen matching may be less critical in the application of tumor vaccines than previously thought.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, A Y -- Golumbek, P -- Ahmadzadeh, M -- Jaffee, E -- Pardoll, D -- Levitsky, H -- New York, N.Y. -- Science. 1994 May 13;264(5161):961-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7513904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/*immunology ; Antigens, Neoplasm/*immunology ; Bone Marrow/immunology ; Bone Marrow Cells ; Colonic Neoplasms/immunology ; Epitopes ; Female ; Granulocyte-Macrophage Colony-Stimulating Factor/genetics/immunology ; H-2 Antigens/immunology ; Histocompatibility Antigens Class I/*immunology ; Melanoma, Experimental/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Nucleocapsid Proteins ; *Nucleoproteins ; T-Lymphocytes, Cytotoxic/*immunology ; Tumor Cells, Cultured ; Viral Core Proteins/immunology
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  • 45
    Publication Date: 1994-09-23
    Description: The proposal that nitric oxide (NO) or its reactant products mediate toxicity in brain remains controversial in part because of the use of nonselective agents that block NO formation in neuronal, glial, and vascular compartments. In mutant mice deficient in neuronal NO synthase (NOS) activity, infarct volumes decreased significantly 24 and 72 hours after middle cerebral artery occlusion, and the neurological deficits were less than those in normal mice. This result could not be accounted for by differences in blood flow or vascular anatomy. However, infarct size in the mutant became larger after endothelial NOS inhibition by nitro-L-arginine administration. Hence, neuronal NO production appears to exacerbate acute ischemic injury, whereas vascular NO protects after middle cerebral artery occlusion. The data emphasize the importance of developing selective inhibitors of the neuronal isoform.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Z -- Huang, P L -- Panahian, N -- Dalkara, T -- Fishman, M C -- Moskowitz, M A -- NS10828/NS/NINDS NIH HHS/ -- NS2636/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1883-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stroke Research Laboratory, Massachusetts General Hospital, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7522345" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/antagonists & inhibitors/deficiency/*metabolism ; Animals ; Arginine/analogs & derivatives/pharmacology ; Brain/enzymology/*metabolism ; Brain Ischemia/complications/*metabolism ; Cerebral Infarction/*etiology ; Cerebrovascular Circulation ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mutation ; Neurons/*enzymology ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase ; Nitroarginine
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-22
    Description: Many recent studies have implicated dietary factors in the cause and prevention of important diseases, including cancer, coronary heart disease, birth defects, and cataracts. There is strong evidence that vegetables and fruits protect against these diseases; however, the active constituents are incompletely identified. Whether fat per se is a major cause of disease is a question still under debate, although saturated and partially hydrogenated fats probably increase the risk of coronary heart disease. One clear conclusion from existing epidemiologic evidence is that many individuals in the United States have suboptimal diets and that the potential for disease prevention by improved nutrition is substantial.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willett, W C -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):532-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Nutrition, Harvard School of Public Health, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Coronary Disease/etiology/prevention & control ; Dairy Products ; *Diet ; Dietary Carbohydrates/administration & dosage ; Dietary Fats/administration & dosage ; Dietary Proteins/administration & dosage ; Female ; Fruit ; Humans ; Male ; Neoplasms/etiology/prevention & control ; *Nutritional Physiological Phenomena ; *Preventive Medicine ; United States ; Vegetables
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  • 47
    Publication Date: 1994-08-19
    Description: A small molecule called PD 153035 inhibited the epidermal growth factor (EGF) receptor tyrosine kinase with a 5-pM inhibition constant. The inhibitor was specific for the EGF receptor tyrosine kinase and inhibited other purified tyrosine kinases only at micromolar or higher concentrations. PD 153035 rapidly suppressed autophosphorylation of the EGF receptor at low nanomolar concentrations in fibroblasts or in human epidermoid carcinoma cells and selectively blocked EGF-mediated cellular processes including mitogenesis, early gene expression, and oncogenic transformation. PD 153035 demonstrates an increase in potency over that of other tyrosine kinase inhibitors of four to five orders of magnitude for inhibition of isolated EGF receptor tyrosine kinase and three to four orders of magnitude for inhibition of cellular phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fry, D W -- Kraker, A J -- McMichael, A -- Ambroso, L A -- Nelson, J M -- Leopold, W R -- Connors, R W -- Bridges, A J -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1093-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, MI 48105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066447" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Cell Transformation, Neoplastic/drug effects ; Epidermal Growth Factor/pharmacology ; Fibroblast Growth Factor 2/pharmacology ; Gene Expression/drug effects ; Humans ; Kinetics ; Mice ; Mitosis/drug effects ; Phosphorylation/drug effects ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Quinazolines/*antagonists & inhibitors ; Receptor, Epidermal Growth Factor/*antagonists & inhibitors ; Tumor Cells, Cultured ; Tyrosine/metabolism
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  • 48
    Publication Date: 1994-06-03
    Description: The low density lipoprotein receptor-related protein (LRP) has been proposed to mediate in concert with the LDL receptor (LDLR) the uptake of dietary lipoproteins into the hepatocytes. This hypothesis was tested by transient inactivation of LRP in vivo. Receptor-associated protein (RAP), a dominant negative regulator of LRP function, was transferred by an adenoviral vector to the livers of mice lacking LDLR (LDLR-/-). The inactivation of LRP by RAP was associated with a marked accumulation of chylomicron remnants in LDLR-/- mice and to a lesser degree in normal mice, suggesting that both LDLR and LRP are involved in remnant clearance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Willnow, T E -- Sheng, Z -- Ishibashi, S -- Herz, J -- HL20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1471-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7515194" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; Apolipoprotein B-48 ; Apolipoproteins B/*metabolism ; Carrier Proteins/genetics/*physiology ; Cholesterol/blood ; Chylomicrons/blood/*metabolism ; Gene Transfer Techniques ; Genetic Vectors ; Glycoproteins/genetics/*physiology ; LDL-Receptor Related Protein-Associated Protein ; Liver/*metabolism ; Low Density Lipoprotein Receptor-Related Protein-1 ; Male ; Mice ; Mice, Inbred C57BL ; Receptors, Immunologic/antagonists & inhibitors/*metabolism ; Receptors, LDL/metabolism ; Triglycerides/blood ; alpha-Macroglobulins/metabolism
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-02-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):754-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303290" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Caenorhabditis elegans/genetics ; Caspase 1 ; Cells, Cultured ; Free Radicals/metabolism ; Metalloendopeptidases/*genetics/metabolism ; Mice ; Mice, Knockout ; Neurons/cytology ; Oxygen/metabolism ; Proto-Oncogene Proteins/genetics/physiology ; Proto-Oncogene Proteins c-bcl-2 ; Rats ; bcl-2-Associated X Protein ; bcl-X Protein
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, J E -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):24-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140414" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/*prevention & control ; Female ; Government Agencies ; Health Education ; Health Knowledge, Attitudes, Practice ; *Health Promotion ; Humans ; Indonesia/epidemiology ; Male ; United States ; World Health Organization
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  • 51
    Publication Date: 1994-10-07
    Description: Loss of heterozygosity data from familial tumors suggest that BRCA1, a gene that confers susceptibility to ovarian and early-onset breast cancer, encodes a tumor suppressor. The BRCA1 region is also subject to allelic loss in sporadic breast and ovarian cancers, an indication that BRCA1 mutations may occur somatically in these tumors. The BRCA1 coding region was examined for mutations in primary breast and ovarian tumors that show allele loss at the BRCA1 locus. Mutations were detected in 3 of 32 breast and 1 of 12 ovarian carcinomas; all four mutations were germline alterations and occurred in early-onset cancers. These results suggest that mutation of BRCA1 may not be critical in the development of the majority of breast and ovarian cancers that arise in the absence of a mutant germline allele.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Futreal, P A -- Liu, Q -- Shattuck-Eidens, D -- Cochran, C -- Harshman, K -- Tavtigian, S -- Bennett, L M -- Haugen-Strano, A -- Swensen, J -- Miki, Y -- CA48711/CA/NCI NIH HHS/ -- CA55914/CA/NCI NIH HHS/ -- CA56749/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939630" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age of Onset ; Alleles ; BRCA1 Protein ; Base Sequence ; Breast Neoplasms/*genetics ; Chromosomes, Human, Pair 17 ; Female ; *Genes, Tumor Suppressor ; Genetic Predisposition to Disease ; *Germ-Line Mutation ; Heterozygote ; Humans ; Middle Aged ; Molecular Sequence Data ; Neoplasm Proteins/*genetics ; Ovarian Neoplasms/*genetics ; Transcription Factors/*genetics
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  • 52
    Publication Date: 1994-10-07
    Description: In this study, a protein that interacts with sequences encoded by the first exon of the protein kinase Bcr was cloned. The Bcr-associated protein 1 (Bap-1) is a member of the 14-3-3 family of proteins. Bap-1 interacts with full-length c-Bcr and with the chimeric Bcr-Abl tyrosine kinase of Philadelphia chromosome (Ph1)-positive human leukemias. Bap-1 is a substrate for the Bcr serine-threonine kinase and is also phosphorylated on tyrosine by Bcr-Abl but not by c-Abl. Bap-1 may function in the regulation of c-Bcr and may contribute to the transforming activity of Bcr-Abl in vivo. 14-3-3 proteins are essential for cell proliferation and have a role in determining the timing of mitosis in yeast. Through direct binding to sequences present in Bcr and in other proteins implicated in signaling, the mammalian 14-3-3 proteins may link specific signaling protein components to mitogenic and cell-cycle control pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reuther, G W -- Fu, H -- Cripe, L D -- Collier, R J -- Pendergast, A M -- CA61033/CA/NCI NIH HHS/ -- DK01965/DK/NIDDK NIH HHS/ -- GM07184/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Oct 7;266(5182):129-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939633" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Animals ; Cell Division ; Cell Line ; Cell Transformation, Neoplastic ; Fusion Proteins, bcr-abl/*metabolism ; Humans ; Mice ; Phosphorylation ; Poly(ADP-ribose) Polymerases/metabolism ; Protein-Tyrosine Kinases/*metabolism ; Proteins/isolation & purification/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-bcr ; Rats ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; *Tyrosine 3-Monooxygenase
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-10-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolff, M S -- Landrigan, P J -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):526-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7818673" target="_blank"〉PubMed〈/a〉
    Keywords: Body Burden ; Breast Neoplasms/*chemically induced/epidemiology ; DDT/*adverse effects ; Dichlorodiphenyl Dichloroethylene/analysis ; Environmental Exposure/adverse effects ; Environmental Pollutants/*adverse effects ; Female ; Humans ; Pesticide Residues/analysis ; United States
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-01-07
    Description: Heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) may participate in membrane traffic events. A complementary DNA (cDNA) was isolated from a mouse pituitary cDNA library that corresponded to an alternatively spliced form of the gene encoding the G protein alpha subunit G alpha i2. The cDNA was identical to that encoding G alpha i2 except that the region encoding for the carboxyl-terminal 24 amino acids was replaced by a longer region encoding 35 amino acids that have no sequence similarity with G alpha i2 or other members of the G protein family. This alternative spliced product and the corresponding protein (sGi2) were present in several tissues. Specific antibodies revealed that sGi2 was localized in the Golgi apparatus, suggesting a role in membrane transport. Thus, alternative splicing may generate from a single gene two G protein alpha subunits with differential cellular localization and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Montmayeur, J P -- Borrelli, E -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):95-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes, CNRS, INSERM U184, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8272874" target="_blank"〉PubMed〈/a〉
    Keywords: *Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Membrane/metabolism ; Coatomer Protein ; DNA, Complementary/genetics ; GTP-Binding Protein alpha Subunit, Gi2 ; *GTP-Binding Protein alpha Subunits, Gi-Go ; GTP-Binding Proteins/analysis/chemistry/genetics/*metabolism ; Golgi Apparatus/chemistry/*metabolism ; Mice ; Microtubule-Associated Proteins/analysis ; Molecular Sequence Data ; Oncogene Proteins/analysis/chemistry/genetics/*metabolism ; *Proto-Oncogene Proteins
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-01-14
    Description: Comparative studies suggest that sex chromosomes begin as ordinary autosomes that happen to carry a major sex determining locus. Over evolutionary time the Y chromosome is selected to stop recombining with the X chromosome, perhaps in response to accumulation of alleles beneficial to the heterogametic but harmful to the homogametic sex. Population genetic theory predicts that a nonrecombining Y chromosome should degenerate. Here this prediction is tested by application of specific selection pressures to Drosophila melanogaster populations. Results demonstrate the decay of a nonrecombining, nascent Y chromosome and the capacity for recombination to ameliorate such decay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, W R -- New York, N.Y. -- Science. 1994 Jan 14;263(5144):230-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, Santa Cruz 95064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8284674" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crosses, Genetic ; Drosophila melanogaster/*genetics/physiology ; Female ; Haplotypes ; Male ; Mutation ; *Recombination, Genetic ; *Y Chromosome
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monro, A M -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1141.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973684" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinogenicity Tests/*statistics & numerical data ; Carcinogens/*administration & dosage/toxicity ; Dose-Response Relationship, Drug ; Female ; Humans ; Male ; Mice ; Mutagenicity Tests ; Neoplasms/*chemically induced ; Rats ; Risk Assessment
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  • 57
    Publication Date: 1994-09-30
    Description: A small proportion of breast cancer, in particular those cases arising at a young age, is due to the inheritance of dominant susceptibility genes conferring a high risk of the disease. A genomic linkage search was performed with 15 high-risk breast cancer families that were unlinked to the BRCA1 locus on chromosome 17q21. This analysis localized a second breast cancer susceptibility locus, BRCA2, to a 6-centimorgan interval on chromosome 13q12-13. Preliminary evidence suggests that BRCA2 confers a high risk of breast cancer but, unlike BRCA1, does not confer a substantially elevated risk of ovarian cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wooster, R -- Neuhausen, S L -- Mangion, J -- Quirk, Y -- Ford, D -- Collins, N -- Nguyen, K -- Seal, S -- Tran, T -- Averill, D -- CA-48711/CA/NCI NIH HHS/ -- CN-05222/CN/NCI NIH HHS/ -- HG-00571/HG/NHGRI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2088-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Carcinogenesis, Institute of Cancer Research, Sutton, Surrey, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091231" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; Female ; Genes, Retinoblastoma ; Genetic Markers ; Genetic Predisposition to Disease ; Humans ; Lod Score ; Male ; Ovarian Neoplasms/genetics ; Pedigree ; Phenotype
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  • 58
    Publication Date: 1994-02-25
    Description: Adult liver has the unusual ability to fully regenerate after injury. Although regeneration is accomplished by the division of mature hepatocytes, the replicative potential of these cells is unknown. Here, the replicative capacity of adult liver cells and their medical usefulness as donor cells for transplantation were investigated by transfer of adult mouse liver cells into transgenic mice that display an endogenous defect in hepatic growth potential and function. The transplanted liver cell populations replaced up to 80 percent of the diseased recipient liver. These findings demonstrate the enormous growth potential of adult hepatocytes, indicating the feasibility of liver cell transplantation as a method to replace lost or diseased hepatic parenchyma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhim, J A -- Sandgren, E P -- Degen, J L -- Palmiter, R D -- Brinster, R L -- HD-23657/HD/NICHD NIH HHS/ -- HD09172/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1149-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108734" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Genetic Markers ; Hepatectomy ; Liver/*cytology/physiology ; Liver Diseases/*surgery ; Liver Regeneration ; *Liver Transplantation ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitotic Index ; Stem Cells/cytology/physiology
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-10-28
    Description: Organismal morphogenesis is driven by a complex series of developmentally coordinated changes in cell shape, size, and number. These changes in cell morphology are in turn dependent on alterations in basic cytoarchitecture. Elucidating the mechanisms of development thus requires an understanding of the cytoskeletal elements that organize the cytoplasm of differentiating cells. Drosophila oogenesis has emerged as a versatile system for the study of cytoskeletal function during development. A series of highly coordinated changes in cytoskeletal organization are required to produce a mature Drosophila oocyte, and these cytoskeletal transformations are amenable to a variety of experimental approaches. Genetic, molecular, and cytological studies have shed light on the specific functions of the cytoskeleton during oogenesis. The results of these studies are reviewed here, and their mechanistic implications are considered.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cooley, L -- Theurkauf, W E -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):590-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939713" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cytoplasm/metabolism ; Drosophila/*physiology ; Female ; Microtubules/*physiology ; Models, Biological ; Oocytes/cytology/*physiology ; *Oogenesis ; RNA, Messenger/metabolism
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  • 60
    Publication Date: 1994-03-25
    Description: The Drosophila decapentaplegic (dpp) gene encodes a transforming growth factor-beta (TGF-beta)-like protein that plays a key role in several aspects of development. Transduction of the DPP signal was investigated by cloning of serine-threonine kinase transmembrane receptors from Drosophila because this type of receptor is specific for the TGF-beta-like ligands. Here evidence is provided demonstrating that the Drosophila saxophone (sax) gene, a previously identified female sterile locus, encodes a TGF-beta-like type I receptor. Embryos from sax mothers and dpp embryos exhibit similar mutant phenotypes during early gastrulation, and these two loci exhibit genetic interactions, which suggest that they are utilized in the same pathway. These data suggest that sax encodes a receptor for dpp.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, T -- Finelli, A L -- Padgett, R W -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1756-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute, Rutgers University, Piscataway, NJ 08855-0759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134837" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Drosophila/embryology/*genetics/metabolism ; *Drosophila Proteins ; Embryo, Nonmammalian/metabolism ; Female ; *Genes, Insect ; Insect Hormones/genetics/*metabolism ; Male ; Molecular Sequence Data ; Mutation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/*genetics/metabolism ; Signal Transduction ; Transforming Growth Factor beta/genetics/*metabolism
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  • 61
    Publication Date: 1994-12-02
    Description: In many mammalian species, the placenta is the site of synthesis of proteins in the prolactin and growth hormone family. Analysis of two such proteins, proliferin (PLF) and proliferin-related protein (PRP), revealed that they are potent regulators of angiogenesis; PLF stimulated and PRP inhibited endothelial cell migration in cell culture and neovascularization in vivo. The mouse placenta secretes an angiogenic activity during the middle of pregnancy that corresponds primarily to PLF, but later in gestation releases a factor that inhibits angiogenesis, which was identified as PRP. Incubation of placental tissue with PLF led to the specific binding of this hormone to capillary endothelial cells. Thus PLF and PRP may regulate the initiation and then the cessation of placental neovascularization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jackson, D -- Volpert, O V -- Bouck, N -- Linzer, D I -- CA52750/CA/NCI NIH HHS/ -- HD24518/HD/NICHD NIH HHS/ -- HD29962/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1581-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527157" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Movement/drug effects ; Cornea/blood supply ; Culture Techniques ; Endothelium, Vascular/*cytology/drug effects/metabolism ; Female ; Fibroblast Growth Factor 2/pharmacology ; Glycoproteins/metabolism/*pharmacology ; Growth Substances/metabolism/*pharmacology ; Intercellular Signaling Peptides and Proteins ; *Neovascularization, Pathologic ; Placenta/*blood supply ; Pregnancy ; Pregnancy Proteins/*pharmacology ; Rats
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  • 62
    Publication Date: 1994-09-02
    Description: Although sexual isolation is one of the most important causes of speciation, its genetic basis is largely unknown. Here evidence is presented that suggests that sexual isolation between two closely related species of Drosophila is largely caused by differences in female cuticular hydrocarbons. This difference maps to only one of the three major chromosomes, implying that reproductive isolation might have a fairly simple genetic basis. The effect of the hydrocarbons on courtship may help explain the ubiquitous asymmetry of sexual isolation between many pairs of Drosophila species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coyne, J A -- Crittenden, A P -- Mah, K -- GM 38462/GM/NIGMS NIH HHS/ -- GM 50355/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1461-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolution, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073292" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Chromosome Mapping ; Crosses, Genetic ; Drosophila/*genetics/physiology ; Female ; *Genes, Insect ; Genetic Markers ; Male ; Pheromones/analysis/*genetics/physiology ; Reproduction ; Species Specificity
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  • 63
    Publication Date: 1994-07-29
    Description: Rasmussen's encephalitis is a progressive childhood disease of unknown cause characterized by severe epilepsy, hemiplegia, dementia, and inflammation of the brain. During efforts to raise antibodies to recombinant glutamate receptors (GluRs), behaviors typical of seizures and histopathologic features mimicking Rasmussen's encephalitis were found in two rabbits immunized with GluR3 protein. A correlation was found between the presence of Rasmussen's encephalitis and serum antibodies to GluR3 detected by protein immunoblot analysis and by immunoreactivity to transfected cells expressing GluR3. Repeated plasma exchanges in one seriously ill child transiently reduced serum titers of GluR3 antibodies, decreased seizure frequency, and improved neurologic function. Thus, GluR3 is an autoantigen in Rasmussen's encephalitis, and an autoimmune process may underlie this disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rogers, S W -- Andrews, P I -- Gahring, L C -- Whisenand, T -- Cauley, K -- Crain, B -- Hughes, T E -- Heinemann, S F -- McNamara, J O -- NS17771/NS/NINDS NIH HHS/ -- NS28709/NS/NINDS NIH HHS/ -- NS30990R29/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):648-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salt Lake City Geriatric Research Education and Clinical Center, Veterans Affairs Medical Center, UT.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8036512" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Specificity ; Autoantibodies/blood/*immunology ; Brain/pathology ; Cell Line ; Child ; Disease Models, Animal ; Encephalitis/complications/*immunology/pathology/therapy ; Female ; Humans ; Male ; Plasma Exchange ; Rabbits ; Receptors, Glutamate/*immunology ; Recombinant Fusion Proteins/immunology ; Seizures/etiology/immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-10-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crabbe, J C -- Belknap, J K -- Buck, K J -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):352-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939673" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/genetics ; Animals ; Chromosome Mapping ; Mice ; Receptors, Dopamine D2/*genetics/physiology
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  • 65
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-08
    Description: In Thunberg's thermal grill illusion, first demonstrated in 1896, a sensation of strong, often painful heat is elicited by touching interlaced warm and cool bars to the skin. Neurophysiological recordings from two classes of ascending spinothalamic tract neurons that are sensitive to innocuous or noxious cold showed differential responses to the grill. On the basis of these results, a simple model of central disinhibition, or unmasking, predicted a quantitative correspondence between grill-evoked pain and cold-evoked pain, which was verified psychophysically. This integration of pain and temperature can explain the thermal grill illusion and the burning sensation of cold pain and may also provide a basis for the cold-evoked, burning pain of the classic thalamic pain syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craig, A D -- Bushnell, M C -- DA07402/DA/NIDA NIH HHS/ -- NS25616/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jul 8;265(5169):252-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neurobiology, Barrow Neurological Institute, Phoenix, AZ 85013.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023144" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Cats ; *Cold Temperature ; Female ; Hot Temperature ; Humans ; Male ; Middle Aged ; Models, Biological ; Neurons, Afferent/*physiology ; Pain/*physiopathology ; Spinothalamic Tracts/*physiology
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1994 Mar 25;263(5154):1686-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8134831" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/*isolation & purification ; Female ; History, Ancient ; Humans ; *Mummies ; Mycobacterium tuberculosis/genetics/*isolation & purification ; Peru ; Polymerase Chain Reaction ; Tuberculosis/*history/transmission
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1994 Jul 15;265(5170):315.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023151" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; HIV Infections/*blood/transmission ; Humans ; Infant, Newborn ; Pregnancy ; Pregnancy Complications, Infectious/*blood ; Vitamin A/*blood
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-16
    Description: The biologically relevant interactions of a transcription factor are those that are important for function in the organism. Here, a transgenic rescue assay was used to determine which molecular functions of Drosophila CCAAT/enhancer binding protein (C/EBP), a basic region-leucine zipper transcription factor, are required for it to fulfill its essential role during development. Chimeric proteins that contain the Drosophila C/EBP (DmC/EBP) basic region, a heterologous zipper, and a heterologous activation domain could functionally substitute for DmC/EBP. Mammalian C/EBPs were also functional in Drosophila. In contrast, 9 of 25 single amino acid substitutions in the basic region disrupted biological function. Thus, the conserved basic region specifies DmC/EBP activity in the organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rorth, P -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1878-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997882" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Basic-Leucine Zipper Transcription Factors ; CCAAT-Enhancer-Binding Proteins ; DNA/metabolism ; DNA-Binding Proteins/chemistry/genetics/*physiology ; Drosophila/genetics/*growth & development ; Female ; G-Box Binding Factors ; *Leucine Zippers ; Male ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*physiology ; Recombinant Fusion Proteins ; Transcription Factors/chemistry/genetics/*physiology ; Transcriptional Activation
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: The mammalian embryo cannot develop without the placenta. Its specialized cells (trophoblast, endoderm, and extraembryonic mesoderm) form early in development. They attach the embryo to the uterus (implantation) and form vascular connections necessary for nutrient transport. In addition, the placenta redirects maternal endocrine, immune, and metabolic functions to the embryo's advantage. These complex activities are sensitive to disruption, as shown by the high incidence of early embryonic mortality and pregnancy diseases in humans, as well as the numerous peri-implantation lethal mutations in mice. Integration of molecular and developmental approaches has recently produced insights into the molecules that control these processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cross, J C -- Werb, Z -- Fisher, S J -- HD 22210/HD/NICHD NIH HHS/ -- HD 26732/HD/NICHD NIH HHS/ -- HD 30367/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1508-18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985020" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastocyst/physiology ; Cell Differentiation ; Embryo Implantation/*physiology ; Embryonic and Fetal Development/genetics/*physiology ; Female ; Gene Expression Regulation, Developmental ; Hormones/physiology ; Humans ; Immune Tolerance ; Male ; Placenta/cytology/*physiology ; Trophoblasts/physiology ; Uterus/physiology
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  • 70
    Publication Date: 1994-06-24
    Description: Mice lacking the known subunit of the type I interferon (IFN) receptor were completely unresponsive to type I IFNs, suggesting that this receptor chain is essential for type I IFN-mediated signal transduction. These mice showed no overt anomalies but were unable to cope with viral infections, despite otherwise normal immune responses. Comparison of mice lacking either type I or type II IFN receptors showed that, at least in response to some viruses, both IFN systems are essential for antiviral defense and are functionally nonredundant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, U -- Steinhoff, U -- Reis, L F -- Hemmi, S -- Pavlovic, J -- Zinkernagel, R M -- Aguet, M -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1918-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology I, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009221" target="_blank"〉PubMed〈/a〉
    Keywords: Alphavirus Infections/immunology ; Animals ; Antibodies, Viral/biosynthesis ; Disease Susceptibility ; Immunity, Innate ; Interferon Type I/*physiology ; Interferon-gamma/*physiology ; Lymphocytic Choriomeningitis/immunology ; Membrane Proteins ; Mice ; Mutation ; Receptor, Interferon alpha-beta ; Receptors, Interferon/genetics/*physiology ; Rhabdoviridae Infections/immunology ; Semliki forest virus ; Signal Transduction ; T-Lymphocytes/immunology ; Vesicular stomatitis Indiana virus ; Virus Diseases/*immunology
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1164-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066455" target="_blank"〉PubMed〈/a〉
    Keywords: Abortion, Legal ; Child ; Congresses as Topic ; Contraception ; Education ; Egypt ; Family Planning Services ; Female ; Humans ; Infant ; *Internationality ; Mortality ; *Population Control ; *Population Growth ; Pregnancy ; United Nations
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  • 72
    Publication Date: 1994-12-09
    Description: Cystic fibrosis (CF) is caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR). A potential animal model of CF, the CFTR-/- mouse, has had limited utility because most mice die from intestinal obstruction during the first month of life. Human CFTR (hCFTR) was expressed in CFTR-/- mice under the control of the rat intestinal fatty acid-binding protein gene promoter. The mice survived and showed functional correction of ileal goblet cell and crypt cell hyperplasia and cyclic adenosine monophosphate-stimulated chloride secretion. These results support the concept that transfer of the hCFTR gene may be a useful strategy for correcting physiologic defects in patients with CF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, L -- Dey, C R -- Wert, S E -- DuVall, M D -- Frizzell, R A -- Whitsett, J A -- DK38518/DK/NIDDK NIH HHS/ -- HL49004/HL/NHLBI NIH HHS/ -- HL51832/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1705-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Children's Hospital Medical Center, Division of Pulmonary Biology, Cincinnati, OH 45229-3039.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527588" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Carrier Proteins/genetics ; Chlorides/metabolism ; Colforsin/pharmacology ; Colon/chemistry/pathology ; Cystic Fibrosis/genetics/metabolism/pathology/*therapy ; Cystic Fibrosis Transmembrane Conductance Regulator ; Disease Models, Animal ; Fatty Acid-Binding Proteins ; Gene Expression ; *Genetic Therapy ; Humans ; Intestinal Mucosa/chemistry/*pathology/secretion ; Intestine, Small/chemistry/pathology ; Membrane Proteins/analysis/*genetics/physiology ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neoplasm Proteins ; *Nerve Tissue Proteins ; Promoter Regions, Genetic ; RNA, Messenger/analysis/genetics ; Rats ; Recombinant Proteins/biosynthesis ; *Tumor Suppressor Proteins
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jitsukawa, M -- Djerassi, C -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1048-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, Asia/Pacific Research Center, Stanford University, CA 94305-6055.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066442" target="_blank"〉PubMed〈/a〉
    Keywords: Abortion, Legal ; Acquired Immunodeficiency Syndrome/transmission ; Condoms ; *Contraceptives, Oral/administration & dosage/adverse effects ; Drug Approval ; *Family Planning Services ; Female ; *Government Regulation ; Health Knowledge, Attitudes, Practice ; Humans ; Internationality ; Japan ; Legislation, Drug ; Male ; Mifepristone/administration & dosage ; Pregnancy ; Risk Assessment
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  • 74
    Publication Date: 1994-06-24
    Description: Fragile sites are chemically induced nonstaining gaps in chromosomes. Different fragile sites vary in frequency in the population and in the chemistry of their induction. DNA sequences encompassing and including the rare, autosomal, folate-sensitive fragile site, FRA16A, were isolated by positional cloning. The molecular basis of FRA16A was found to be expansion of a normally polymorphic p(CCG)n repeat. This repeat was adjacent to a CpG island that was methylated in fragile site-expressing individuals. The FRA16A locus in individuals who do not express the fragile site is not a site of DNA methylation (imprinting), which suggests that the methylation associated with fragile sites may be a consequence and not a cause of their genesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nancarrow, J K -- Kremer, E -- Holman, K -- Eyre, H -- Doggett, N A -- Le Paslier, D -- Callen, D F -- Sutherland, G R -- Richards, R I -- New York, N.Y. -- Science. 1994 Jun 24;264(5167):1938-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cytogenetics and Molecular Genetics, Women's and Children's Hospital, North Adelaide, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8009225" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Fragile Sites ; *Chromosome Fragility ; Chromosomes, Artificial, Yeast ; *Chromosomes, Human, Pair 16 ; Dinucleoside Phosphates/metabolism ; Female ; Fragile X Syndrome/genetics ; Humans ; Male ; Methylation ; Molecular Sequence Data ; Pedigree ; Polymerase Chain Reaction ; Repetitive Sequences, Nucleic Acid
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  • 75
    Publication Date: 1994-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curtsinger, J W -- Fukui, H H -- Xiu, L -- Khazaeli, A -- Pletcher, S -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):826; author reply 828.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973640" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/physiology ; Drosophila/*physiology ; Female ; Male ; Mortality
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  • 76
    Publication Date: 1994-03-04
    Description: The enzyme acetylcholinesterase generates a strong electrostatic field that can attract the cationic substrate acetylcholine to the active site. However, the long and narrow active site gorge seems inconsistent with the enzyme's high catalytic rate. A molecular dynamics simulation of acetylcholinesterase in water reveals the transient opening of a short channel, large enough to pass a water molecule, through a thin wall of the active site near tryptophan-84. This simulation suggests that substrate, products, or solvent could move through this "back door," in addition to the entrance revealed by the crystallographic structure. Electrostatic calculations show a strong field at the back door, oriented to attract the substrate and the reaction product choline and to repel the other reaction product, acetate. Analysis of the open back door conformation suggests a mutation that could seal the back door and thus test the hypothesis that thermal motion of this enzyme may open multiple routes of access to its active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gilson, M K -- Straatsma, T P -- McCammon, J A -- Ripoll, D R -- Faerman, C H -- Axelsen, P H -- Silman, I -- Sussman, J L -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1276-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Houston, TX 77204-5641.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122110" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Acetylcholinesterase/*chemistry/metabolism ; Binding Sites ; Catalysis ; Choline/metabolism ; Computer Simulation ; Crystallography, X-Ray ; Electrochemistry ; Models, Molecular ; *Protein Conformation
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-17
    Description: Modern molecular genetic and genomic approaches are revolutionizing the study of behavior in the mouse. "Reverse genetics" (from gene to phenotype) with targeted gene transfer provides a powerful tool to dissect behavior and has been used successfully to study the effects of null mutations in genes implicated in the regulation of long-term potentiation and spatial learning in mice. In addition, "forward genetics" (from phenotype to gene) with high-efficiency mutagenesis in the mouse can uncover unknown genes and has been used to isolate a behavioral mutant of the circadian system. With the recent availability of high-density genetic maps and physical mapping resources, positional cloning of virtually any mutation is now feasible in the mouse. Together, these approaches permit a molecular analysis of both known and previously unknown genes regulating behavior.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3830945/" 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/PMC3830945/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, J S -- Pinto, L H -- Vitaterna, M H -- EY08467/EY/NEI NIH HHS/ -- MH39592/MH/NIMH NIH HHS/ -- MH49241/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- etc. -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1724-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Physiology, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209253" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Circadian Rhythm/genetics ; Female ; *Genetic Techniques ; Genetics, Behavioral/*methods ; Learning ; Long-Term Potentiation ; Male ; Mice ; Mice, Inbred Strains ; Mice, Knockout ; Mutagenesis
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  • 78
    Publication Date: 1994-04-15
    Description: The first step in oral absorption of many medically important peptide-based drugs is mediated by an intestinal proton-dependent peptide transporter. This transporter facilitates the oral absorption of beta-lactam antibiotics and angiotensin-converting enzyme inhibitors from the intestine into enterocytes lining the luminal wall. A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. The amino acid sequence deduced from the complementary DNA sequence of the cloned gene indicated that this transport-associated protein shares several conserved structural elements with the cadherin superfamily of calcium-dependent, cell-cell adhesion proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dantzig, A H -- Hoskins, J A -- Tabas, L B -- Bright, S -- Shepard, R L -- Jenkins, I L -- Duckworth, D C -- Sportsman, J R -- Mackensen, D -- Rosteck, P R Jr -- New York, N.Y. -- Science. 1994 Apr 15;264(5157):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8153632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; CHO Cells ; Cadherins/*chemistry ; Carrier Proteins/*chemistry/genetics/isolation & purification/metabolism ; Cephalexin/*metabolism ; Cloning, Molecular ; Cricetinae ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Intestinal Mucosa/*metabolism ; Leucine/analogs & derivatives/metabolism ; *Membrane Transport Proteins ; Mice ; Mice, Inbred A ; Molecular Sequence Data ; Open Reading Frames ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
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  • 79
    Publication Date: 1994-07-22
    Description: Two molecular mechanisms of T cell-mediated cytotoxicity, one perforin-based, the other Fas-based, have been demonstrated. To determine the extent of their contribution to T cell-mediated cytotoxicity, a range of effector cells from normal control or perforin-deficient mice were tested against a panel of target cells with various levels of Fas expression. All cytotoxicity observed was due to either of these mechanisms, and no third mechanism was detected. Thus, the perforin- and Fas-based mechanisms may account for all T cell-mediated cytotoxicity in short-term in vitro assays.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kagi, D -- Vignaux, F -- Ledermann, B -- Burki, K -- Depraetere, V -- Nagata, S -- Hengartner, H -- Golstein, P -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):528-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7518614" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD95 ; Antigens, Surface/*immunology ; Cells, Cultured ; Concanavalin A/pharmacology ; *Cytotoxicity, Immunologic ; Ionomycin/pharmacology ; Leukemia L1210 ; Lymphocyte Culture Test, Mixed ; Lymphocytic choriomeningitis virus/immunology ; Membrane Glycoproteins/*immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Molecular Sequence Data ; Perforin ; Pore Forming Cytotoxic Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Cells, Cultured
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  • 80
    Publication Date: 1994-10-21
    Description: Assembly of antigen receptor V (variable), D (diversity), and J (joining) gene segments requires lymphocyte-specific genes and ubiquitous DNA repair activities. Severe combined immunodeficient (SCID) mice are defective in general double-strand (ds) DNA break repair and V(D)J coding joint formation, resulting in arrested lymphocyte development. A single treatment of newborn SCID mice with DNA-damaging agents restored functional, diverse, T cell receptor beta chain coding joints, as well as development and expansion of thymocytes expressing both CD4 and CD8 coreceptors, but did not promote B cell development. Thymic lymphoma developed in all mice treated with DNA-damaging agents, suggesting an interrelation between V(D)J recombination, dsDNA break repair, and lymphomagenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Danska, J S -- Pflumio, F -- Williams, C J -- Huner, O -- Dick, J E -- Guidos, C J -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):450-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Surgical Research, Hospital for Sick Children Research Institute, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7524150" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; B-Lymphocytes/cytology/immunology ; Base Sequence ; Bleomycin/pharmacology ; Cell Transformation, Neoplastic ; *DNA Damage ; DNA Repair ; Gamma Rays ; *Gene Rearrangement ; Hematopoietic Stem Cells/cytology/immunology ; Lymphoma/etiology/pathology ; Mice ; Mice, SCID ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, alpha-beta/*genetics ; T-Lymphocyte Subsets/cytology/immunology ; T-Lymphocytes/cytology/*immunology ; Thymus Neoplasms/etiology/pathology
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  • 81
    Publication Date: 1994-09-23
    Description: The neuromodulator serotonin (5-hydroxytryptamine, 5-HT) has been associated with mood disorders such as depression, anxiety, and impulsive violence. To define the contribution of 5-HT receptor subtypes to behavior, mutant mice lacking the 5-HT1B receptor were generated by homologous recombination. These mice did not exhibit any obvious developmental or behavioral defects. However, the hyperlocomotor effect of the 5-HT1A/1B agonist RU24969 was absent in mutant mice, indicating that this effect is mediated by 5-HT1B receptors. Moreover, when confronted with an intruder, mutant mice attacked the intruder faster and more intensely than did wild-type mice, suggesting the participation of 5-HT1B receptors in aggressive behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saudou, F -- Amara, D A -- Dierich, A -- LeMeur, M -- Ramboz, S -- Segu, L -- Buhot, M C -- Hen, R -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1875-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, U184 de l'INSERM, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8091214" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression/*physiology ; Animals ; Brain Chemistry ; Chimera ; Female ; Indoles/pharmacology ; Male ; Mice ; Motor Activity/drug effects ; Mutation ; Pindolol/analogs & derivatives/metabolism ; Receptor, Serotonin, 5-HT1B ; Receptors, Serotonin/analysis/genetics/*physiology ; Recombination, Genetic ; Serotonin Receptor Agonists/pharmacology
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, P H -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1303.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973710" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carcinogenicity Tests ; Diet ; Female ; *Fruit ; *Fungicides, Industrial/toxicity ; Humans ; Male ; Mice ; United States ; United States Environmental Protection Agency ; *Vegetables
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  • 83
    Publication Date: 1994-11-04
    Description: The therapeutic responsiveness of genetically defined tumors expressing or devoid of the p53 tumor suppressor gene was compared in immunocompromised mice. Tumors expressing the p53 gene contained a high proportion of apoptotic cells and typically regressed after treatment with gamma radiation or adriamycin. In contrast, p53-deficient tumors treated with the same regimens continued to enlarge and contained few apoptotic cells. Acquired mutations in p53 were associated with both treatment resistance and relapse in p53-expressing tumors. These results establish that defects in apoptosis, here caused by the inactivation of p53, can produce treatment-resistant tumors and suggest that p53 status may be an important determinant of tumor response to therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, S W -- Bodis, S -- McClatchey, A -- Remington, L -- Ruley, H E -- Fisher, D E -- Housman, D E -- Jacks, T -- 5R27CA17575/CA/NCI NIH HHS/ -- CA14051/CA/NCI NIH HHS/ -- R01CA40602/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):807-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973635" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Doxorubicin/*therapeutic use ; Drug Resistance ; Fibrosarcoma/drug therapy/*genetics/radiotherapy/*therapy ; *Gamma Rays ; *Genes, p53/genetics ; Immunocompromised Host ; Mice ; Mice, Nude ; Mutation ; Neoplasm Recurrence, Local ; Neoplasm Transplantation ; Radiation Tolerance
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  • 84
    Publication Date: 1994-03-04
    Description: The invariant chain (Ii) binds nascent major histocompatibility complex (MHC) class II molecules, blocking peptide binding until the complex dissociates in the endosomes. This may serve to differentiate the MHC class I and II antigen presentation pathways and enable class II molecules to efficiently bind peptides in the endosomes. This hypothesis was addressed by probing spleen cells from a combination of knock-out and transgenic mice with a large panel of T cell hybridomas. The Ii molecule blocked the presentation of a range of endogenously synthesized epitopes, but some epitopes actually required Ii. Thus, the influence of Ii on presentation does not follow simple rules. In addition, mice expressing Ii were not tolerant to epitopes unmasked in its absence, a finding with possible implications for autoimmunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bodmer, H -- Viville, S -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1284-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes du CNRS, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7510069" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/*immunology ; *Antigens, Differentiation, B-Lymphocyte ; Epitopes/*immunology ; Histocompatibility Antigens Class II/genetics/*immunology ; Hybridomas ; Mice ; Mice, Knockout ; Mice, Transgenic ; Molecular Sequence Data ; Myelin Basic Protein/immunology ; Recombinant Fusion Proteins/immunology ; T-Lymphocytes/*immunology
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  • 85
    Publication Date: 1994-06-10
    Description: Specific protein-ligand interactions are critical for cellular function, and most proteins select their partners with sharp discrimination. However, the oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence. The crystal structure of OppA reveals a three-domain organization, unlike other periplasmic binding proteins. In OppA-peptide complexes, the ligands are completely enclosed in the protein interior, a mode of binding that normally imposes tight specificity. The protein fulfills the hydrogen bonding and electrostatic potential of the ligand main chain and accommodates the peptide side chains in voluminous hydrated cavities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tame, J R -- Murshudov, G N -- Dodson, E J -- Neil, T K -- Dodson, G G -- Higgins, C F -- Wilkinson, A J -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of York, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202710" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*metabolism ; Binding Sites ; Carrier Proteins/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrogen Bonding ; Ligands ; Lipoproteins/chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Oligopeptides/chemistry/*metabolism ; Protein Conformation ; Protein Structure, Secondary
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-11-18
    Description: The role played in immune surveillance by gamma delta T cells residing in various epithelia has not been clear. It is shown here that activated gamma delta T cells obtained from skin and intestine express the epithelial cell mitogen keratinocyte growth factor (KGF). In contrast, intraepithelial alpha beta T cells, as well as all lymphoid alpha beta and gamma delta T cell populations tested, did not produce KGF or promote the growth of cultured epithelial cells. These results suggest that intraepithelial gamma delta T cells function in surveillance and in repair of damaged epithelial tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boismenu, R -- Havran, W L -- AI32751/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1253-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973709" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Division ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Dendritic Cells/*physiology ; Epithelial Cells ; Fibroblast Growth Factor 10 ; Fibroblast Growth Factor 7 ; *Fibroblast Growth Factors ; Growth Substances/*biosynthesis/genetics ; Keratinocytes/*cytology ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; *Receptors, Antigen, T-Cell, gamma-delta ; T-Lymphocyte Subsets/immunology/metabolism/*physiology
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  • 87
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-02-11
    Description: The population of the developing world is currently expanding at the unprecedented rate of more than 800 million per decade, and despite anticipated reductions in growth during the 21st century, its size is expected to increase from 4.3 billion today to 10.2 billion in 2100. Past efforts to curb this growth have almost exclusively focused on the implementation of family planning programs to provide contraceptive information, services, and supplies. These programs have been partially successful in reducing birth rates. Further investments in them will have an additional but limited impact on population growth; therefore, other policy options, in particular measures to reduce high demand for births and limit population momentum, are needed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bongaarts, J -- New York, N.Y. -- Science. 1994 Feb 11;263(5148):771-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Division, Population Council, New York, NY 10017.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303293" target="_blank"〉PubMed〈/a〉
    Keywords: Contraception ; *Developing Countries ; Family Characteristics ; *Family Planning Policy ; Female ; Humans ; Male ; *Population Control ; *Population Growth
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  • 88
    Publication Date: 1994-09-30
    Description: Nucleotide sequence information derived from DNA segments of the human and other genomes is accumulating rapidly. However, it frequently proves difficult to use such short DNA segments to identify clones in genomic libraries or fragments in blots of the whole genome or for in situ analysis of chromosomes. Oligonucleotide probes, consisting of two target-complementary segments, connected by a linker sequence, were designed. Upon recognition of the specific nucleic acid molecule the ends of the probes were joined through the action of a ligase, creating circular DNA molecules catenated to the target sequence. These probes thus provide highly specific detection with minimal background.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nilsson, M -- Malmgren, H -- Samiotaki, M -- Kwiatkowski, M -- Chowdhary, B P -- Landegren, U -- New York, N.Y. -- Science. 1994 Sep 30;265(5181):2085-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beijer Laboratory, Department of Medical Genetics, Biomedical Center, Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7522346" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cells, Cultured ; Chromosomes, Human, Pair 12 ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/*analysis ; DNA, Circular/*analysis ; Genetic Vectors ; Humans ; In Situ Hybridization ; Lymphocytes ; Membrane Proteins/genetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; *Oligonucleotide Probes/chemistry ; Repetitive Sequences, Nucleic Acid ; Templates, Genetic
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-12-02
    Description: Deletions and other genome rearrangements can be caused by radiation and are associated with carcinogenesis and inheritable diseases. The pink-eyed unstable (p(un)) mutation in the mouse is caused by a gene duplication and reverts to wild type by deletion of one copy. Reversion events in the mouse embryo were detected as black spots on the fur of the animals or microscopically as partially black hair in a background of colorless hair. The frequency of partially black hair was increased by x-rays at very low doses. A linear dose-response relation was found between 1 and 100 centigray.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schiestl, R H -- Khogali, F -- Carls, N -- ES06593/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Toxicology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dose-Response Relationship, Radiation ; Embryo, Mammalian/radiation effects ; Female ; *Gene Deletion ; Hair Color/genetics/radiation effects ; Male ; Maternal Exposure ; Melanocytes/radiation effects ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Multigene Family ; Mutagenicity Tests ; Mutation/*radiation effects
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishi, R -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1052-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Anatomy, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066443" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor ; Cell Survival ; Chick Embryo ; Ciliary Neurotrophic Factor ; Mice ; Mice, Knockout ; Mice, Mutant Strains ; Motor Neuron Disease/*drug therapy/pathology ; Motor Neurons/*cytology/drug effects ; Nerve Growth Factors/pharmacology/*physiology ; Nerve Tissue Proteins/pharmacology/*physiology
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  • 91
    Publication Date: 1994-06-10
    Description: In spite of recent advances in identifying genes causing monogenic human disease, very little is known about the genes involved in polygenic disease. Three families were identified with mutations in the unlinked photoreceptor-specific genes ROM1 and peripherin/RDS, in which only double heterozygotes develop retinitis pigmentosa (RP). These findings indicate that the allelic and nonallelic heterogeneity known to be a feature of monogenic RP is complicated further by interactions between unlinked mutations causing digenic RP. Recognition of the inheritance pattern exemplified by these three families might facilitate the identification of other examples of digenic inheritance in human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kajiwara, K -- Berson, E L -- Dryja, T P -- EY00169/EY/NEI NIH HHS/ -- EY08683/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 10;264(5165):1604-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Berman-Gund Laboratory for the Study of Retinal Degenerations, Harvard Medical School, Massachusetts Eye and Ear Infirmary, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8202715" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Electroretinography ; Eye Proteins/chemistry/*genetics ; Female ; Genes, Dominant ; Genes, Recessive ; Genetic Linkage ; Heterozygote ; Humans ; Intermediate Filament Proteins/chemistry/*genetics ; Male ; *Membrane Glycoproteins ; Membrane Proteins/chemistry/*genetics ; Molecular Sequence Data ; Mutation ; *Nerve Tissue Proteins ; Pedigree ; Peripherins ; Retinitis Pigmentosa/*genetics ; Rod Cell Outer Segment/chemistry ; Tetraspanins
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  • 92
    Publication Date: 1994-07-08
    Description: A gene encoding a 35-kilodalton guanosine triphosphate (GTP)-binding protein, Gem, was cloned from mitogen-induced human peripheral blood T cells. Gem and Rad, the product of a gene overexpressed in skeletal muscle in individuals with Type II diabetes, constitute a new family of Ras-related GTP-binding proteins. The distinct structural features of this family include the G3 GTP-binding motif, extensive amino- and carboxyl-terminal extensions beyond the Ras-related domain, and a motif that determines membrane association. Gem was transiently expressed in human peripheral blood T cells in response to mitogenic stimulation; the protein was phosphorylated on tyrosine residues and localized to the cytosolic face of the plasma membrane. Deregulated Gem expression prevented proliferation of normal and transformed 3T3 cells. These results suggest that Gem is a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maguire, J -- Santoro, T -- Jensen, P -- Siebenlist, U -- Yewdell, J -- Kelly, K -- New York, N.Y. -- Science. 1994 Jul 8;265(5169):241-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7912851" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CD4-Positive T-Lymphocytes/metabolism ; Cell Death ; Cell Division ; Cell Line ; Cell Line, Transformed ; Cell Membrane/metabolism ; GTP-Binding Proteins/chemistry/genetics/*metabolism ; Genes, ras ; Guanosine Triphosphate/metabolism ; Humans ; Immediate-Early Proteins/chemistry/genetics/*metabolism ; Mice ; Molecular Sequence Data ; *Monomeric GTP-Binding Proteins ; Mutation ; RNA, Messenger/genetics/metabolism ; Transfection ; *ras Proteins
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  • 93
    Publication Date: 1994-04-01
    Description: Concentration of urine in mammals is regulated by the antidiuretic hormone vasopressin. Binding of vasopressin to its V2 receptor leads to the insertion of water channels in apical membranes of principal cells in collecting ducts. In nephrogenic diabetes insipidus (NDI), the kidney fails to concentrate urine in response to vasopressin. A male patient with an autosomal recessive form of NDI was found to be a compound heterozygote for two mutations in the gene encoding aquaporin-2, a water channel. Functional expression studies in Xenopus oocytes revealed that each mutation resulted in nonfunctional water channel proteins. Thus, aquaporin-2 is essential for vasopressin-dependent concentration of urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deen, P M -- Verdijk, M A -- Knoers, N V -- Wieringa, B -- Monnens, L A -- van Os, C H -- van Oost, B A -- New York, N.Y. -- Science. 1994 Apr 1;264(5155):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, University of Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8140421" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aquaporin 2 ; Aquaporin 6 ; *Aquaporins ; Base Sequence ; Cloning, Molecular ; Deamino Arginine Vasopressin/*pharmacology ; Diabetes Insipidus/*genetics/physiopathology ; Female ; Genes, Recessive ; Heterozygote ; Humans ; Kidney/metabolism/*physiology ; *Kidney Concentrating Ability ; Male ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Oocytes ; Pedigree ; Point Mutation ; Protein Structure, Secondary ; RNA, Complementary/genetics ; Water/metabolism ; Xenopus laevis
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1658.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209240" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*etiology ; Electromagnetic Fields/*adverse effects ; Female ; Humans ; Male ; Melatonin/biosynthesis ; *Neoplasms, Radiation-Induced ; *Occupational Exposure ; Pineal Gland/metabolism/radiation effects
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  • 95
    Publication Date: 1994-12-02
    Description: Professional antigen-presenting cells (APCs) have a distinct compartment in which class II molecules are proposed to acquire antigenic peptides. Genetic evidence suggests that human leukocyte antigen (HLA)-DM, an unusual class II molecule, participates in this process. Peptide acquisition was reconstituted in nonprofessional APCs by transfection of class II, invariant chain (li), and H-2M, the murine equivalent of DM. The H-2M heterodimer appeared in an endosomal compartment, not at the cell surface, and the localization was independent of li. The data presented show that H-2M, class II, and li are the minimally required components for efficient formation of stable class II-peptide complexes, and thus for a functional class II compartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlsson, L -- Peleraux, A -- Lindstedt, R -- Liljedahl, M -- Peterson, P A -- AI-26610/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1569-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉R. W. Johnson Pharmaceutical Research Institute, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7985028" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigen-Presenting Cells/immunology ; *Antigens, Differentiation, B-Lymphocyte ; B-Lymphocytes/immunology ; Cell Line ; Cell Membrane/immunology ; Endosomes/*immunology ; Fluorescent Antibody Technique ; H-2 Antigens/analysis/genetics/*metabolism ; HLA-DR3 Antigen/*metabolism ; HeLa Cells ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
    Publication Date: 1994-05-27
    Description: Septic shock results from excessive stimulation of the host immune system, especially macrophages, by lipopolysaccharide (LPS), or endotoxin, which resides on the outer membrane of bacteria. Protein tyrosine kinase inhibitors of the tyrphostin AG 126 family protect mice against LPS-induced lethal toxicity. The protection correlates with the ability of these agents to block LPS-induced production of tumor necrosis factor alpha (TNF-alpha) and nitric oxide in macrophages as well as LPS-induced production of TNF-alpha in vivo. Furthermore, this inhibitory effect correlated with the potency of AG 126 to block LPS-induced tyrosine phosphorylation of a p42MAPK protein substrate in the murine macrophage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Novogrodsky, A -- Vanichkin, A -- Patya, M -- Gazit, A -- Osherov, N -- Levitzki, A -- New York, N.Y. -- Science. 1994 May 27;264(5163):1319-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Felsenstein Medical Research Center, Petach Tikva, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8191285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzylidene Compounds/*pharmacology ; Biological Assay ; Cell Line ; Cell Survival/drug effects ; Dose-Response Relationship, Drug ; Enzyme-Linked Immunosorbent Assay ; Female ; Lipopolysaccharides/*toxicity ; Macrophage Activation ; Macrophages, Peritoneal/*drug effects/metabolism ; Mice ; Mice, Inbred C57BL ; Mitogen-Activated Protein Kinase 1 ; Nitric Oxide/*biosynthesis ; Nitriles/*pharmacology ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Tumor Necrosis Factor-alpha/analysis/*biosynthesis/toxicity ; *Tyrphostins
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-04-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taubes, G -- New York, N.Y. -- Science. 1994 Apr 22;264(5158):499-500.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8160007" target="_blank"〉PubMed〈/a〉
    Keywords: African Continental Ancestry Group ; Asian Continental Ancestry Group ; Breast Neoplasms/blood/*chemically induced/ethnology ; Case-Control Studies ; DDT/adverse effects ; Dichlorodiphenyl Dichloroethylene/adverse effects/*blood ; European Continental Ancestry Group ; Female ; Humans ; Pesticide Residues/adverse effects/*blood ; Polychlorinated Biphenyls/adverse effects ; Risk Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-03-04
    Description: Physical inclusion of small molecules in larger structural lattices is well known in the crystalline state and is a common feature of the chemistry of zeolites. In the liquid state, a variety of synthetic macrocyclic molecules are available to complex and contain smaller guest species. An alternative strategy for binding is explored: assembly of cavity-forming structures from small subunits. Encapsulation of small guest molecules such as methane can be achieved with a synthetic structure that assembles reversibly through hydrogen bonding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Branda, N -- Wyler, R -- Rebek, J Jr -- New York, N.Y. -- Science. 1994 Mar 4;263(5151):1267-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8122107" target="_blank"〉PubMed〈/a〉
    Keywords: Benzyl Compounds/chemistry ; Chemistry, Physical ; Chloroform ; Hydrogen Bonding ; Imidazoles/chemistry ; Magnetic Resonance Spectroscopy ; Methane/*chemistry ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Physicochemical Phenomena ; Polymers/*chemistry ; Temperature ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1994-07-15
    Description: Inquiry into the determinants of risk-related sexual behavior is important for the development of interventions to reduce the incidence of new cases of human immunodeficiency virus infection. Recent social and behavioral research has revealed much about the individual and social factors influencing risk-taking. Findings from these studies have been important in the development of new educational and community-based interventions for communities at risk in the developed and developing worlds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aggleton, P -- O'Reilly, K -- Slutkin, G -- Davies, P -- New York, N.Y. -- Science. 1994 Jul 15;265(5170):341-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Global Programme on AIDS, World Health Organization, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8023156" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/prevention & ; control/*transmission ; Cultural Characteristics ; Developing Countries ; Disease Outbreaks ; Female ; Global Health ; Humans ; Male ; *Risk-Taking ; *Sexual Behavior ; Socioeconomic Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1994-11-18
    Description: Muscle enhancer factor-2A (MEF2A), a member of the MADS family, induced myogenic development when ectopically expressed in clones of nonmuscle cells of human clones, a function previously limited to the muscle basic helix-loop-helix (bHLH) proteins. During myogenesis, MEF2A and bHLH proteins cooperatively activate skeletal muscle genes and physically interact through the MADS domain of MEF2A and the three myogenic amino acids of the muscle bHLH proteins. Thus, skeletal myogenesis is mediated by two distinct families of mutually inducible and interactive muscle transcription factors, either of which can initiate the developmental cascade.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaushal, S -- Schneider, J W -- Nadal-Ginard, B -- Mahdavi, V -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1236-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cardiology, Children's Hospital, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973707" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; *Gene Expression Regulation ; Genes, Reporter ; Haplorhini ; Helix-Loop-Helix Motifs ; Humans ; MADS Domain Proteins ; MEF2 Transcription Factors ; Mice ; Molecular Sequence Data ; Muscle, Skeletal/*cytology/metabolism ; MyoD Protein/biosynthesis/*metabolism ; Myogenic Regulatory Factors ; Myogenin/biosynthesis/genetics/metabolism ; Transcription Factors/genetics/*metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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