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  • Female  (68)
  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (96)
  • 1990-1994  (96)
  • 1990  (96)
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Publisher
  • American Association for the Advancement of Science (AAAS)  (96)
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  • 1990-1994  (96)
Year
  • 1
    Publication Date: 1990-08-17
    Description: The transcription factor C/EBP uses a bipartite structural motif to bind DNA. Two protein chains dimerize through a set of amphipathic alpha helices termed the leucine zipper. Highly basic polypeptide regions emerge from the zipper to form a linked set of DNA contact surfaces. In the recently proposed a "scissors grip" model, the paired set of basic regions begin DNA contact at a central point and track in opposite directions along the major groove, forming a molecular clamp around DNA. This model predicts that C/EBP must undertake significant changes in protein conformation as it binds and releases DNA. The basic region of ligand-free C/EBP is highly sensitive to protease digestion. Pronounced resistance to proteolysis occurred when C/EBP associated with its specific DNA substrate. Sequencing of discrete proteolytic fragments showed that prominent sites for proteolysis occur at two junction points predicted by the "scissors grip" model. One junction corresponds to the cleft where the basic regions emerge from the leucine zipper. The other corresponds to a localized nonhelical segment that has been hypothesized to contain an N-cap and facilitate the sharp angulation necessary for the basic region to track continuously in the major groove of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuman, J D -- Vinson, C R -- McKnight, S L -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2202050" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; CCAAT-Enhancer-Binding Proteins ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA-Binding Proteins/metabolism ; Kinetics ; Leucine ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Peptide Fragments/metabolism ; Peptide Hydrolases/*metabolism ; Protein Conformation ; Transcription Factors/*metabolism ; Trypsin/metabolism
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wright, K -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1659.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270478" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/diagnosis/*genetics/prevention & control ; Female ; Humans ; Risk Factors
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dusheck, J -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1494-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218487" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Congresses as Topic ; Female ; Humans ; Male ; Men ; United States ; *Women
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-21
    Description: Nonobese diabetic (NOD) mice develop an autoimmune form of diabetes, becoming hyperglycemic after 3 months of age. This process was accelerated by injecting young NOD mice with CD4+ islet-specific T cell clones derived from NOD mice. Overt diabetes developed in 10 of 19 experimental animals by 7 weeks of age, with the remaining mice showing marked signs of the disease in progress. Control mice did not become diabetic and had no significant pancreatic infiltration. This work demonstrates that a CD4 T cell clone is sufficient to initiate the disease process in the diabetes-prone NOD mouse.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haskins, K -- McDuffie, M -- P01 DK40144/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1433-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Barbara Davis Center for Childhood Diabetes, University of Colorado Health Sciences Center, Denver 80262.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2205920" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/analysis/*immunology ; Clone Cells ; Diabetes Mellitus, Experimental/*immunology/pathology ; Female ; Islets of Langerhans/*immunology/pathology ; Male ; Mice ; Mice, Inbred Strains ; Mice, Mutant Strains ; T-Lymphocytes/*immunology/transplantation
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  • 5
    Publication Date: 1990-08-24
    Description: The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly alpha-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hecht, M H -- Richardson, J S -- Richardson, D C -- Ogden, R C -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):884-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2392678" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Base Sequence ; DNA/genetics ; *Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Denaturation ; *Proteins ; *Recombinant Proteins
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, D C -- He, X M -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):302-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Space Science Laboratory, NASA Marshall Space Flight Center, Huntsville, AL 35812.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374930" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; Models, Molecular ; Protein Conformation ; *Serum Albumin ; X-Ray Diffraction
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  • 7
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
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  • 8
    Publication Date: 1990-08-10
    Description: The interaction of the T cell receptor for antigen (TCR) with its antigen-major histocompatibility complex ligand is difficult to study because both are cell surface multimers. The TCR consists of two chains (alpha and beta) that are complexed to the five or more nonpolymorphic CD3 polypeptides. A soluble form of the TCR was engineered by replacing the carboxyl termini of alpha and beta with signal sequences from lipid-linked proteins, making them susceptible to enzymatic cleavage. In this manner, TCR heterodimers can be expressed independently of the CD3 polypeptides and in significant quantities (0.5 milligram per week). This technique seems generalizable to biochemical and structural studies of many other cell surface molecules as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, A Y -- Devaux, B -- Green, A -- Sagerstrom, C -- Elliott, J F -- Davis, M M -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):677-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305-5402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1696397" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaline Phosphatase/genetics ; Amino Acid Sequence ; Animals ; Antigens, CD3 ; Antigens, CD55 ; Antigens, Differentiation, T-Lymphocyte/genetics ; Cell Line ; Complement Inactivator Proteins/genetics ; Female ; Humans ; Macromolecular Substances ; Membrane Proteins/genetics ; Molecular Sequence Data ; Placenta/enzymology ; Pregnancy ; Protein Sorting Signals/genetics ; Receptors, Antigen, T-Cell/*genetics ; Transfection
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  • 9
    Publication Date: 1990-12-07
    Description: A molecular clone of the Xenopus laevis ets-2 gene was isolated from an oocyte complementary DNA library. The amount of messenger RNA (mRNA) in each oocyte or embryo was almost constant during oogenesis and was maintained until the blastula stage of embryonic development, indicating that the observed 3.2-kilobase transcript is a maternal message. The only normal adult tissue in which ets-2 mRNA was detected was the ovary. Injection of antisense oligonucleotides homologous to the ets-2 sequence into oocytes led to degradation of the mRNA and blocked hormone-induced germinal vesicle breakdown. The ets-2 product is thus required for the meiotic maturation of Xenopus oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Z Q -- Burdett, L A -- Seth, A K -- Lautenberger, J A -- Papas, T S -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1416-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Oncology, National Cancer Institute, Frederick, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255913" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; *DNA-Binding Proteins ; Embryo, Nonmammalian/physiology ; Female ; Gene Expression ; Gene Library ; Oligonucleotides, Antisense/pharmacology ; Oocytes/cytology/drug effects/*physiology ; Oogenesis ; Protein-Tyrosine Kinases/genetics ; Proto-Oncogene Protein c-ets-2 ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogenes ; RNA, Messenger/analysis/genetics ; *Repressor Proteins ; *Trans-Activators ; *Transcription Factors ; Transcription, Genetic ; Xenopus laevis
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-17
    Description: A class of transcriptional regulator proteins bind to DNA at dyad-symmetric sites through a motif consisting of (i) a "leucine zipper" sequence that associates into noncovalent, parallel, alpha-helical dimers and (ii) a covalently connected basic region necessary for binding DNA. The basic regions are predicted to be disordered in the absence of DNA and to form alpha helices when bound to DNA. These helices bind in the major groove forming multiple hydrogen-bonded and van der Waals contacts with the nucleotide bases. To test this model, two peptides were designed that were identical to natural leucine zipper proteins only at positions hypothesized to be critical for dimerization and DNA recognition. The peptides form dimers that bind specifically to DNA with their basic regions in alpha-helical conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neil, K T -- Hoess, R H -- DeGrado, W F -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):774-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research and Development Department, E.I. du Pont de Nemours & Co., Wilmington, DE 19880-0328.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2389143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chemistry, Physical ; Circular Dichroism ; Computer Simulation ; DNA/*metabolism ; DNA-Binding Proteins/*metabolism ; Hydrogen Bonding ; *Leucine ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Physicochemical Phenomena ; Protein Conformation
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  • 11
    Publication Date: 1990-07-20
    Description: Animal lines selected for differences in drug sensitivity can be used to help determine the molecular basis of drug action. Long-sleep (LS) and short-sleep (SS) mice differ markedly in their genetic sensitivity to ethanol. To investigate the molecular basis for this difference, mRNA from brains of LS and SS mice was expressed in Xenopus oocytes and the ethanol sensitivity of gamma-aminobutyric acid A (GABAA)- and N-methyl D-aspartate (NMDA)-activated ion channels was tested. Ethanol facilitated GABA responses in oocytes injected with mRNA from LS mice but antagonized responses in oocytes injected with mRNA from SS animals. Ethanol inhibited NMDA responses equally in the two lines. Thus, genes coding for the GABAA receptor or associated proteins may be critical determinants of individual differences in ethanol sensitivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wafford, K A -- Burnett, D M -- Dunwiddie, T V -- Harris, R A -- AA03527/AA/NIAAA NIH HHS/ -- AA06399/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):291-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, Denver.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1695761" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aspartic Acid/analogs & derivatives/pharmacology ; Brain/*metabolism ; Chloride Channels ; Chlorides/*physiology ; Diazepam/pharmacology ; Ethanol/*pharmacology ; Female ; Ion Channels/drug effects/physiology ; Membrane Proteins/*physiology ; Mice ; Mice, Inbred Strains ; Microinjections ; N-Methylaspartate ; Oocytes/*drug effects/*physiology ; RNA, Messenger/administration & dosage/genetics ; Receptors, GABA-A/drug effects/*genetics ; Xenopus ; gamma-Aminobutyric Acid/pharmacology
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  • 12
    Publication Date: 1990-05-04
    Description: A cell line has been established in continuous culture of human cerebral cortical neurons obtained from a patient with unilateral megalencephaly, a disorder associated with continued proliferation of immature neuronal cells. When differentiated in the presence of nerve growth factor, 1-isobutyl-3-methylxanthine, and dibutyryl adenosine 3',5'-monophosphate (cAMP), the cells display mature neuronal morphology with numerous long, extensively branched processes with spines and varicosities. The cells stain positively for neurofilament protein and neuron-specific enolase (selective neuronal markers) but are negative for glial markers, such as glial fibrillary acidic protein, S-100, and myelin basic protein. The cells also stain positively for the neurotransmitters gamma-aminobutyric acid (GABA), glutamate, somatostatin, cholecystokinin-8, and vasoactive intestinal polypeptide. These cells may facilitate characterization of neurons in the human central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ronnett, G V -- Hester, L D -- Nye, J S -- Connors, K -- Snyder, S H -- DA 00074/DA/NIDA NIH HHS/ -- DA 00266/DA/NIDA NIH HHS/ -- MH 18501/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 May 4;248(4955):603-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, 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/1692158" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Brain Diseases/*pathology ; Bucladesine/pharmacology ; Cell Differentiation/drug effects ; Cell Line ; Cerebral Cortex/*pathology ; Culture Techniques/methods ; Female ; Humans ; Infant ; Nerve Growth Factors/pharmacology ; Nerve Tissue Proteins/analysis ; Neurons/cytology/drug effects/*pathology ; Neurotransmitter Agents/analysis ; gamma-Aminobutyric Acid/analysis
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  • 13
    Publication Date: 1990-12-07
    Description: A genetic system was developed in Escherichia coli to study leucine zippers with the amino-terminal domain of bacteriophage lambda repressor as a reporter for dimerization. This system was used to analyze the importance of the amino acid side chains at eight positions that form the hydrophobic interface of the leucine zipper dimer from the yeast transcriptional activator, GCN4. When single amino acid substitutions were analyzed, most functional variants contained hydrophobic residues at the dimer interface, while most nonfunctional sequence variants contained strongly polar or helix-breaking residues. In multiple randomization experiments, however, many combinations of hydrophobic residues were found to be nonfunctional, and leucines in the heptad repeat were shown to have a special function in leucine zipper dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, J C -- O'Shea, E K -- Kim, P S -- Sauer, R T -- AI15706/AI/NIAID NIH HHS/ -- GM11117/GM/NIGMS NIH HHS/ -- GM44162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2147779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage lambda/*genetics ; DNA-Binding Proteins/*genetics ; Escherichia coli/*genetics ; Fungal Proteins/*genetics ; Genetic Variation ; Leucine Zippers/*genetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phenotype ; Protein Conformation ; *Protein Kinases ; Random Allocation ; Recombinant Fusion Proteins/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/*genetics
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  • 14
    Publication Date: 1990-09-28
    Description: The erbB2 oncogene encodes a 185-kilodalton transmembrane protein whose sequence is similar to the epidermal growth factor receptor (EGFR). A 30-kilodalton factor (gp30) secreted from MDA-MB-231 human breast cancer cells was shown to be a ligand for p185erbB2. An antibody to EGFR abolished the tyrosine phosphorylation induced by EGF and transforming growth factor-alpha (TGF-alpha) but only partially blocked that produced by gp30 in SK-BR-3 breast cancer cells. In two cell lines that overexpress erbB2 but do not expresss EGFR (MDA-MB-453 breast cancer cells and a Chinese hamster ovary cell line that had been transfected with erbB2), phosphorylation of p185erbB2 was induced only by gp30. The gp30 specifically inhibited the growth of cells that overexpressed p185erbB2. An antibody to EGFR had no effect on the inhibition of SK-BR-3 cell colony formation obtained with gp30. Thus, it appeared that gp30 interacted directly with the EGFR and erbB2. Direct binding of gp30 to p185erbB2 was confirmed by binding competition experiments, where gp30 was found to displace the p185erbB2 binding of a specific antibody to p185erbB2. The evidence described here suggests that gp30 is a ligand for p185erbB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupu, R -- Colomer, R -- Zugmaier, G -- Sarup, J -- Shepard, M -- Slamon, D -- Lippman, M E -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1552-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vincent T. Lombardi Cancer Research Center, Georgetown University Medical Center, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218496" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Binding, Competitive ; Breast Neoplasms ; Cell Line ; Chromatography, Affinity ; Female ; Humans ; Kinetics ; Ligands ; Molecular Weight ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogenes ; Receptor, Epidermal Growth Factor/isolation & purification/*metabolism ; Transfection
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galloway, A -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2078250" target="_blank"〉PubMed〈/a〉
    Keywords: *Congresses as Topic ; Female ; Government Agencies ; Humans ; *Prejudice ; Science ; United States ; *Women
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-05-04
    Description: The amino acid sequences of three fragments of cyanogen bromide-digested human placental inositol 1,2-cyclic phosphate 2-phosphohydrolase, an enzyme of the phosphatidylinositol signaling pathway, are identical to sequences within lipocortin III, a member of a family of homologous calcium- and phospholipid-binding proteins that do not have defined physiological functions. Lipocortin III has also been previously identified as placental anticoagulant protein III (PAP III) and calcimedin 35 alpha. Antibodies to PAP III detected PAP III and inositol 1,2-cyclic phosphate 2-phosphohydrolase with identical reactivity on immunoblotting. In addition, inositol 1,2-cyclic phosphate 2-phosphohydrolase was stimulated by the same acidic phospholipids that bind lipocortins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, T S -- Tait, J F -- Majerus, P W -- HLBI 14147/HL/NHLBI NIH HHS/ -- HLBI 16634/HL/NHLBI NIH HHS/ -- HLBI 40801/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 May 4;248(4955):605-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, 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/2159184" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Annexin A3 ; Annexins ; Calcium-Binding Proteins/*genetics ; Female ; Humans ; Immunoblotting ; Kinetics ; Molecular Sequence Data ; Phosphoric Diester Hydrolases/*genetics/isolation & purification/metabolism ; Placenta/*enzymology ; Pregnancy
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  • 17
    Publication Date: 1990-08-10
    Description: Somatic mutations in a subset of growth hormone (GH)-secreting pituitary tumors convert the gene for the alpha polypeptide chain (alpha s) of Gs into a putative oncogene, termed gsp. These mutations, which activate alpha s by inhibiting its guanosine triphosphatase (GTPase) activity, are found in codons for either of two amino acids, each of which is completely conserved in all known G protein alpha chains. The likelihood that similar mutations would activate other G proteins prompted a survey of human tumors for mutations that replace either of these two amino acids in other G protein alpha chain genes. The first gene so far tested, which encodes the alpha chain of Gi2, showed mutations that replaced arginine-179 with either cysteine or histidine in 3 of 11 tumors of the adrenal cortex and 3 of 10 endocrine tumors of the ovary. The mutant alpha i2 gene is a putative oncogene, referred to as gip2. In addition, gsp mutations were found in 18 of 42 GH-secreting pituitary tumors and in an autonomously functioning thyroid adenoma. These findings suggest that human tumors may harbor oncogenic mutations in various G protein alpha chain genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyons, J -- Landis, C A -- Harsh, G -- Vallar, L -- Grunewald, K -- Feichtinger, H -- Duh, Q Y -- Clark, O H -- Kawasaki, E -- Bourne, H R -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):655-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics, Cetus Corporation, Emeryville CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2116665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Neoplasm/genetics ; Endocrine System Diseases/*genetics ; Female ; GTP Phosphohydrolases/genetics/metabolism ; GTP-Binding Proteins/*genetics/metabolism ; Humans ; Male ; Molecular Sequence Data ; *Mutation ; Neoplasms/*genetics ; Oligonucleotide Probes ; *Oncogenes ; Pituitary Neoplasms/*genetics ; Polymerase Chain Reaction
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  • 18
    Publication Date: 1990-07-20
    Description: Minor histocompatibility (H) antigens can be peptides derived from cellular proteins that are presented on the cell surface by major histocompatibility complex (MHC) class I molecules. This is similar to viral antigens, because in both cases cytotoxic T lymphocytes (CTLs) recognize artificially produced peptides loaded on target cells. Naturally processed minor H peptides were found to be similar to those artificial CTL-epitopes, as far as size and hydrophobicity is concerned. The peptides studied were isolated from a transfectant that expressed a model CTL-defined antigen, beta-galactosidase, from male cells that express H-Y, which has been known operationally since 1955, and from cells that express H-4, known since 1961.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rotzschke, O -- Falk, K -- Wallny, H J -- Faath, S -- Rammensee, H G -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):283-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biologie, Abteilung Immungenetik, Tubingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1695760" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Epitopes/isolation & purification ; Female ; H-Y Antigen/*analysis/immunology ; Male ; Mice ; Mice, Inbred Strains ; Minor Histocompatibility Antigens/*analysis/immunology ; Molecular Sequence Data ; Peptides/chemical synthesis ; Species Specificity ; Spleen/immunology ; T-Lymphocytes, Cytotoxic/*immunology
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-28
    Description: To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize the native state. Proteins in partly folded states can be used to dissect protein organizational hierarchies. A partly folded apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them by two-dimensional 1H-NMR (nuclear magnetic resonance). Protons in the A, G, and H helix regions are protected from exchange, while protons in the B and E helix regions exchange freely. On the basis of these results and the three-dimensional structure of native myoglobin, a structural model is presented for the partly folded intermediate in which a compact subdomain retains structure while the remainder of the protein is essentially unfolded.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughson, F M -- Wright, P E -- Baldwin, R L -- DK34909/DK/NIDDK NIH HHS/ -- GM19988/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1544-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Beckman Center, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218495" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apoproteins/chemistry/*metabolism ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Myoglobin/chemistry/*metabolism ; Protein Conformation ; Spectrophotometry, Ultraviolet
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  • 20
    Publication Date: 1990-08-31
    Description: The isocitrate dehydrogenase of Escherichia coli is an example of a ubiquitous class of enzymes that are regulated by covalent modification. In the three-dimensional structure of the enzyme-substrate complex, isocitrate forms a hydrogen bond with Ser113, the site of regulatory phosphorylation. The structures of Asp113 and Glu113 mutants, which mimic the inactivation of the enzyme by phosphorylation, show minimal conformational changes from wild type, as in the phosphorylated enzyme. Calculations based on observed structures suggest that the change in electrostatic potential when a negative charge is introduced either by phosporylation or site-directed mutagenesis is sufficient to inactivate the enzyme. Thus, direct interaction at a ligand binding site is an alternative mechanism to induced conformational changes from an allosteric site in the regulation of protein activity by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J H -- Dean, A M -- Sohl, J L -- Koshland, D E Jr -- Stroud, R M -- GM 24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1012-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2204109" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Homeostasis ; Isocitrate Dehydrogenase/genetics/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation
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  • 21
    Publication Date: 1990-08-03
    Description: Comparison of the 2.4 angstrom resolution crystal structures of dimeric clam hemoglobin in the deoxygenated and carbon-monoxide liganded states shows how radically different the structural basis for cooperative oxygen binding is from that operative in mammalian hemoglobins. Heme groups are in direct communication across a novel subunit interface formed by the E and F helices. The conformational changes at this interface that accompany ligand binding are more dramatic at a tertiary level but more subtle at a quaternary level than those in mammalian hemoglobins. These findings suggest a cooperative mechanism that links ligation at one subunit with potentiation of affinity at the second subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Royer, W E Jr -- Hendrickson, W A -- Chiancone, E -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382132" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carboxyhemoglobin/metabolism ; Hemoglobins/*metabolism ; Ligands ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Mollusca ; Protein Conformation
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Page, L M -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1320.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Models, Biological ; Reproduction ; Species Specificity ; Zebrafish/genetics/*physiology
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-06
    Description: A review of methodologically sound studies of the psychological responses of U.S. women after they obtained legal, nonrestrictive abortions indicates that distress is generally greatest before the abortion and that the incidence of severe negative responses is low. Factors associated with increased risk of negative response are consistent with those reported in research on other stressful life events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adler, N E -- David, H P -- Major, B N -- Roth, S H -- Russo, N F -- Wyatt, G E -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):41-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181664" target="_blank"〉PubMed〈/a〉
    Keywords: Abortion, Induced/*psychology ; Adaptation, Psychological ; Adolescent ; Emotions ; Female ; Humans ; Pregnancy ; Pregnancy Trimester, First ; *Pregnant Women ; Risk Assessment ; Social Support ; United States
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  • 24
    Publication Date: 1990-07-20
    Description: The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution. Hirudin consists of an NH2-terminal globular domain and a long (39 A) COOH-terminal extended domain. Residues Ile1 to Tyr3 of hirudin form a parallel beta-strand with Ser214 to Glu217 of thrombin with the nitrogen atom of Ile1 making a hydrogen bond with Ser195 O gamma atom of the catalytic site, but the specificity pocket of thrombin is not involved in the interaction. The COOH-terminal segment makes numerous electrostatic interactions with an anion-binding exosite of thrombin, whereas the last five residues are in a helical loop that forms many hydrophobic contacts. In all, 27 of the 65 residues of hirudin have contacts less than 4.0 A with thrombin (10 ion pairs and 23 hydrogen bonds). Such abundant interactions may account for the high affinity and specificity of hirudin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rydel, T J -- Ravichandran, K G -- Tulinsky, A -- Bode, W -- Huber, R -- Roitsch, C -- Fenton, J W 2nd -- HL13160/HL/NHLBI NIH HHS/ -- HL43229/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):277-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Michigan State University, East Lansing 48824.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Hirudins/*metabolism ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Recombinant Proteins/metabolism ; Thrombin/*metabolism ; X-Ray Diffraction
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-10
    Description: A metalloantibody has been constructed with a coordination site for metals in the antigen binding pocket. The Zn(II) binding site from carbonic anhydrase B was used as a model. Three histidine residues have been placed in the light chain complementarity determining regions of a single chain antibody molecule. In contrast to the native protein, the mutant displayed metal-dependent fluorescence-quenching behavior. This response was interpreted as evidence for metal binding in the three-histidine site with relative affinities in the order Cu(II) greater than Zn(II) greater than Cd(II). The presence of metal cofactors in immunoglobulins should facilitate antibody catalysis of redox and hydrolytic reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iverson, B L -- Iverson, S A -- Roberts, V A -- Getzoff, E D -- Tainer, J A -- Benkovic, S J -- Lerner, R A -- F32GM-1204702/GM/NIGMS NIH HHS/ -- IGM 37684/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):659-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2116666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Binding Sites, Antibody ; Cadmium ; Carbonic Anhydrases/*immunology ; Copper ; Fluoresceins ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; Ligands ; *Metals ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Spectrometry, Fluorescence ; Zinc
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  • 26
    Publication Date: 1990-02-09
    Description: Gene mutation in vivo in human T lymphocytes appears to occur preferentially in dividing cells. Individuals with multiple sclerosis (MS) are assumed to have one or more populations of diving T cells that are being stimulated by autoantigens. Mutant T cell clones from MS patients were isolated and tested for reactivity to myelin basic protein, an antigen that is thought to participate in the induction of the disease. The hypoxanthine guanine phosphoribosyltransferase (hprt) clonal assay was used to determine mutant frequency values in MS patients with chronic progressive disease. Eleven of 258 thioguanine-resistant (hprt-) T cell clones from five of the six MS patients who were tested proliferated in response to human myelin basic protein without prior in vitro exposure to this antigen. No wild-type clones from these patients, nor any hprt- or wild-type clones from three healthy individuals responded to myelin basic protein. Thus, T cell clones that react with myelin basic protein can be isolated from the peripheral blood of MS patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allegretta, M -- Nicklas, J A -- Sriram, S -- Albertini, R J -- CA30688-07/CA/NCI NIH HHS/ -- NS00849/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 9;247(4943):718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics Laboratory, University of Vermont, Burlington 05401.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1689076" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Autoantigens/immunology ; Cell Division ; Clone Cells/immunology ; Female ; Humans ; Hypoxanthine Phosphoribosyltransferase/genetics ; Male ; Middle Aged ; Multiple Sclerosis/genetics/*immunology ; Mutation ; Myelin Basic Protein/*immunology ; T-Lymphocytes/drug effects/*immunology ; Thioguanine/pharmacology ; X Chromosome
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1990 Nov 16;250(4983):900-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237436" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Female ; Humans ; Male ; Middle Aged ; Neoplasms/*mortality ; United States
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneiderman, M -- Davis, D L -- Wagener, D K -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):228-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374921" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans ; European Continental Ancestry Group ; Female ; Humans ; Lung Neoplasms/mortality ; Male ; Prevalence ; Smoking/*epidemiology ; United States
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-09
    Description: Deletion of chromosome 11p13 in humans produces the WAGR syndrome, consisting of aniridia (an absence or malformation of the iris), Wilms tumor (nephroblastoma), genitourinary malformations, and mental retardation. An interspecies backcross between Mus musculus/domesticus and Mus spretus was made in order to map the homologous chromosomal region in the mouse genome and to define an animal model of this syndrome. Nine evolutionarily conserved DNA clones from proximal human 11p were localized on mouse chromosome 2 near Small-eyes (Sey), a semidominant mutation that is phenotypically similar to aniridia. Analysis of Dickie's Small-eye (SeyDey), a poorly viable allele that has pleiotropic effects, revealed the deletion of three clones, f3, f8, and k13, which encompass the aniridia (AN2) and Wilms tumor susceptibility genes in man. Unlike their human counterparts, SeyDey/+ mice do not develop nephroblastomas. These findings suggest that the Small-eye defect is genetically equivalent to human aniridia, but that loss of the murine homolog of the Wilms tumor gene is not sufficient for tumor initiation. A comparison among Sey alleles suggests that the AN2 gene product is required for induction of the lens and nasal placodes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glaser, T -- Lane, J -- Housman, D -- 2 T32 GMO7753-11/GM/NIGMS NIH HHS/ -- GM27882/GM/NIGMS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):823-7.〈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/2173141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aniridia/*genetics ; Blotting, Southern ; Chromosome Deletion ; Chromosome Mapping ; DNA/analysis ; *Disease Models, Animal ; Eye/embryology/pathology ; Female ; Genes, Wilms Tumor/*genetics ; Genetic Markers ; Kidney Neoplasms/*genetics ; Male ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Muridae ; Mutation ; Phenotype ; Polymorphism, Genetic ; Syndrome ; Wilms Tumor/*genetics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alper, J -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):804-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154848" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/drug therapy ; *Antiviral Agents/therapeutic use ; Capsid/ultrastructure ; Common Cold/*drug therapy ; Drug Design ; Humans ; Models, Molecular ; Protein Conformation ; Rhinovirus/ultrastructure ; Software
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  • 31
    Publication Date: 1990-01-19
    Description: The product of the yeast cell cycle control gene cdc2, and its homologs in higher eukaryotes (p34cdc2), all contain a perfectly conserved sequence of 16 amino acids that has not been found in any other protein sequence. Microinjection of this peptide triggers a specific increase in the concentration of intracellular free Ca2+ that originates from intracellular stores in both starfish and Xenopus oocytes. Thus, p34cdc2 might interact through its conserved peptide domain with some component of the Ca2(+)-regulatory system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Picard, A -- Cavadore, J C -- Lory, P -- Bernengo, J C -- Ojeda, C -- Doree, M -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):327-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS and INSERM, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2153316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *CDC2 Protein Kinase ; Calcium/*metabolism ; Chloride Channels ; Chlorides/metabolism ; Cytoplasmic Granules/physiology ; Egtazic Acid/pharmacology ; Exocytosis/drug effects ; Female ; Genes, Fungal ; Growth Substances/*genetics ; Maturation-Promoting Factor ; Membrane Proteins/metabolism ; Microinjections ; Molecular Sequence Data ; Oocytes/drug effects/*physiology ; *Peptide Fragments ; Peptides/*pharmacology ; Starfish ; Xenopus
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  • 32
    Publication Date: 1990-08-13
    Description: The three-dimensional structure of charybdotoxin, a high-affinity peptide blocker of several potassium ion channels, was determined by two-dimensional nuclear magnetic resonance (2-D NMR) spectroscopy. Unambiguous NMR assignments of backbone and side chain hydrogens were made for all 37 amino acids. The structure was determined by distance geometry and refined by nuclear Overhauser and exchange spectroscopy back calculation. The peptide is built on a foundation of three antiparallel beta strands to which other parts of the sequence are attached by three disulfide bridges. The overall shape is roughly ellipsoidal, with axes of approximately 2.5 and 1.5 nanometers. Nine of the ten charged groups are located on one side of the ellipsoid, with seven of the eight positive residues lying in a stripe 2.5 nanometers in length. The other side displays three hydrophobic residues projecting prominently into aqueous solution. The structure rationalizes several mechanistic features of charybdotoxin block of the high-conductance Ca2(+)-activated K+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Massefski, W Jr -- Redfield, A G -- Hare, D R -- Miller, C -- GM-20168/GM/NIGMS NIH HHS/ -- GM-31768/GM/NIGMS NIH HHS/ -- RR0031/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):521-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1696395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Charybdotoxin ; Disulfides/analysis ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Molecular Sequence Data ; Potassium Channels/drug effects ; Protein Conformation ; *Scorpion Venoms/pharmacology
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  • 33
    Publication Date: 1990-06-08
    Description: X-linked Alport syndrome is a hereditary glomerulonephritis in which progressive loss of kidney function is often accompanied by progressive loss of hearing. Ultrastructural defects in glomerular basement membranes (GBM) of Alport syndrome patients implicate an altered structural protein as the cause of nephritis. The product of COL4A5, the alpha 5(IV) collagen chain, is a specific component of GBM within the kidney, and the gene maps to the same X chromosomal region as does Alport syndrome. Three structural aberrations were found in COL4A5, in intragenic deletion, a Pst I site variant, and an uncharacterized abnormality, which appear to cause nephritis and deafness, with allele-specific severity, in three Alport syndrome kindreds in Utah.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, D F -- Hostikka, S L -- Zhou, J -- Chow, L T -- Oliphant, A R -- Gerken, S C -- Gregory, M C -- Skolnick, M H -- Atkin, C L -- Tryggvason, K -- DK 36200/DK/NIDDK NIH HHS/ -- DK 39497/DK/NIDDK NIH HHS/ -- M01 RR 00064/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1224-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Informatics, University of Utah School of Medicine, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2349482" target="_blank"〉PubMed〈/a〉
    Keywords: Blotting, Southern ; Cloning, Molecular ; Collagen/*genetics ; DNA/genetics/isolation & purification ; Exons ; Female ; *Genes ; Humans ; Male ; Molecular Weight ; *Mutation ; Nephritis, Hereditary/*genetics ; Pedigree ; Restriction Mapping ; X Chromosome
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  • 34
    Publication Date: 1990-12-21
    Description: Previous studies have emphasized that genetic susceptibility to breast cancer is rare and is expressed primarily as premenopausal breast cancer, bilateral breast cancer, or both. Proliferative breast disease (PBD) is a significant risk factor for the development of breast cancer and appears to be a precursor lesion. PBD and breast cancer were studied in 103 women from 20 kindreds that were selected for the presence of two first degree relatives with breast cancer and in 31 control women. Physical examination, screening mammography, and four-quadrant fine-needle breast aspirates were performed. Cytologic analysis of breast aspirates revealed PBD in 35% of clinically normal female first degree relatives of breast cancer cases and in 13% of controls. Genetic analysis suggests that genetic susceptibility causes both PBD and breast cancer in these kindreds. This study supports the hypothesis that this susceptibility is responsible for a considerable portion of breast cancer, including unilateral and postmenopausal breast cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skolnick, M H -- Cannon-Albright, L A -- Goldgar, D E -- Ward, J H -- Marshall, C J -- Schumann, G B -- Hogle, H -- McWhorter, W P -- Wright, E C -- Tran, T D -- CA-28854/CA/NCI NIH HHS/ -- CA-42014/CA/NCI NIH HHS/ -- CA-48711/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1715-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Utah Regional Cancer Center, University of Utah Medical Center, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270486" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Breast Diseases/*genetics/pathology ; Breast Neoplasms/*genetics/pathology ; Female ; Genetic Predisposition to Disease ; Humans ; Male ; Menopause ; Middle Aged ; Pedigree
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  • 35
    Publication Date: 1990-12-21
    Description: Human growth hormone (hGH) elicits a diverse set of biological activities including lactation that derives from binding to the prolactin (PRL) receptor. The binding affinity of hGH for the extracellular binding domain of the hPRL receptor (hPRLbp) was increased about 8000-fold by addition of 50 micromolar ZnCl2. Zinc was not required for binding of hGH to the hGH binding protein (hGHbp) or for binding of hPRL to the hPRLbp. Other divalent metal ions (Ca2+, Mg2+, Cu2+, Mn2+, and Co2+) at physiological concentrations did not support such strong binding. Scatchard analysis indicated a stoichiometry of one Zn2+ per hGH.hPRLbp complex. Mutational analysis showed that a cluster of three residues (His18, His21, and Glu174) in hGH and His188 from the hPRLbp (conserved in all PRL receptors but not GH receptors) are probable Zn2+ ligands. This polypeptide hormone.receptor "zinc sandwich" provides a molecular mechanism to explain why nonprimate GHs are not lactogenic and offers a molecular link between zinc deficiency and its association with altered functions of hGH.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Bass, S -- Fuh, G -- Wells, J A -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270485" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chlorides/*pharmacology ; Growth Hormone/*metabolism ; Humans ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligonucleotide Probes ; Plasmids ; Protein Conformation ; Receptors, Prolactin/drug effects/genetics/*metabolism ; Restriction Mapping ; Zinc/metabolism/*pharmacology ; *Zinc Compounds
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  • 36
    Publication Date: 1990-04-13
    Description: The alpha chain of the human histocompatibility antigen HLA-G was identified as an array of five 37- to 39-kilodalton isoforms by the use of two-dimensional gel electrophoresis. Both cell-associated and secreted HLA-G antigens are prominent in first trimester villous cytotrophoblasts and are greatly reduced in third trimester cytotrophoblasts. Allelic variation was not detected, an indication that HLA-G is not obviously polymorphic in cytotrophoblasts. Among the following choriocarcinoma cell lines studied, HLA-G is expressed in JEG but not in Jar or BeWo. Expression of endogenous HLA-G genes has not been found in normal lymphoid cells. Thus, HLA-G is subject to both cell type-specific and developmental regulation and is expressed in early gestation human cytotrophoblasts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kovats, S -- Main, E K -- Librach, C -- Stubblebine, M -- Fisher, S J -- DeMars, R -- AI-15586/AI/NIAID NIH HHS/ -- HD-24495/HD/NICHD NIH HHS/ -- P0I HD-24180/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):220-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Oncology, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2326636" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Cell Line ; Choriocarcinoma/immunology ; Female ; Gene Expression ; *Genes, MHC Class I ; HLA Antigens/*genetics ; HLA-G Antigens ; Histocompatibility Antigens Class I/*genetics ; Humans ; Macromolecular Substances ; Pregnancy ; Pregnancy Trimester, First ; Trophoblasts/*immunology ; Tumor Cells, Cultured/immunology ; Uterine Neoplasms/immunology
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-30
    Description: Mice have an olfactory (pheromone) recognition memory located at the first relay in the sensory system. It is acquired with one-trial learning, contingent upon norepinephrine activation at mating, and lasts for several weeks. The mechanism involves Hebbian (association-dependent) changes in synaptic efficacy at dendrodendritic synapses in the accessory olfactory bulb. As a result of this memory, males made familiar by mating are recognized by the females, thereby mitigating pregnancy block. Such a memory function is biologically important to the female, as it is required to sustain pregnancy in the presence of her stud male's odors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brennan, P -- Kaba, H -- Keverne, E B -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sub-Department of Animal Behaviour, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2147078" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/drug effects/physiology ; Animals ; Female ; Hypothalamus/physiology ; Lidocaine/pharmacology ; Male ; Memory/*physiology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred CBA ; N-Methylaspartate/antagonists & inhibitors/physiology ; Norepinephrine/physiology ; Olfactory Bulb/drug effects/physiology ; Olfactory Pathways/drug effects/physiology ; *Pheromones/urine ; Pregnancy ; Pregnancy, Animal/*physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Reproduction/physiology ; Smell/*physiology ; Synapses/physiology
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-01-19
    Description: The mevalonate-derived portion of a prenylated protein from Chinese hamster ovary cells has been established as diterpenoid (C20). This group is linked to a carboxyl-terminal cysteine as a thioether. It was removed from the protein by hydrazinolysis followed by Raney nickel desulfurization, and the resulting hydrocarbon fraction was analyzed by gas chromatography-mass spectrometry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rilling, H C -- Breunger, E -- Epstein, W W -- Crain, P F -- GM 29812/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City 84112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2296720" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Diterpenes/*metabolism ; Female ; Gas Chromatography-Mass Spectrometry ; Mevalonic Acid/metabolism ; Molecular Structure ; Ovary ; Protein Precursors/metabolism ; *Protein Processing, Post-Translational ; Proteins/*metabolism
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carson, H L -- New York, N.Y. -- Science. 1990 Oct 12;250(4978):191.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218517" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Female ; Genetic Variation ; *Genetics, Population ; Male ; Recombination, Genetic ; Selection, Genetic
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-30
    Description: Population growth in the United States and the Soviet Union is slowing. Since the 1970s, labor force growth in both countries is slowing even more than population growth, and both countries are aging. Economic effects of slowing growth can be compensated for by increased participation in the labor force and increased productivity and by adjustments in the military forces. Economic flexibility and policy choices will determine how successfully the trend to slower population growth will be accommodated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Torrey, B B -- Kingkade, W W -- New York, N.Y. -- Science. 1990 Mar 30;247(4950):1548-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for International Research, U.S. Bureau of the Census, Washington DC 20233.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321015" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Aged ; Female ; Fertility ; Humans ; Male ; Middle Aged ; *Population Dynamics ; Ussr ; United States
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  • 41
    Publication Date: 1990-06-01
    Description: An amyloid protein that precipitates in the cerebral vessel walls of Dutch patients with hereditary cerebral hemorrhage with amyloidosis is similar to the amyloid protein in vessel walls and senile plaques in brains of patients with Alzheimer's disease, Down syndrome, and sporadic cerebral amyloid angiopathy. Cloning and sequencing of the two exons that encode the amyloid protein from two patients with this amyloidosis revealed a cytosine-to-guanine transversion, a mutation that caused a single amino acid substitution (glutamine instead of glutamic acid) at position 22 of the amyloid protein. The mutation may account for the deposition of this amyloid protein in the cerebral vessel walls of these patients, leading to cerebral hemorrhages and premature death.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy, E -- Carman, M D -- Fernandez-Madrid, I J -- Power, M D -- Lieberburg, I -- van Duinen, S G -- Bots, G T -- Luyendijk, W -- Frangione, B -- AG 05891/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1124-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2111584" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Alleles ; Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; Amyloid beta-Protein Precursor ; Amyloidosis/complications/*genetics ; Base Sequence ; Brain Chemistry ; Cerebral Hemorrhage/etiology/*genetics ; Cerebrovascular Disorders/complications/*genetics ; Dna ; Deoxyribonucleases, Type II Site-Specific ; Exons ; Female ; Genes, Dominant ; Humans ; Middle Aged ; Molecular Sequence Data ; *Mutation ; Netherlands ; Polymerase Chain Reaction ; Protein Precursors/*genetics
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  • 42
    Publication Date: 1990-10-05
    Description: Rhodopsin is a member of a family of receptors that contain seven transmembrane helices and are coupled to G proteins. The nature of the interactions between rhodopsin mutants and the G protein, transduction (Gt), was investigated by flash photolysis in order to monitor directly Gt binding and dissociation. Three mutant opsins with alterations in their cytoplasmic loops bound 11-cis-retinal to yield pigments with native rhodopsin absorption spectra, but they failed to stimulate the guanosine triphosphatase activity of Gt. The opsin mutations included reversal of a charged pair conserved in all G protein-coupled receptors at the cytoplasmic border of the third transmembrane helix (mutant CD1), replacement of 13 amino acids in the second cytoplasmic loop (mutant CD2), and deletion of 13 amino acids from the third cytoplasmic loop (mutant EF1). Whereas mutant CD1 failed to bind Gt, mutants CD2 and EF1 showed normal Gt binding but failed to release Gt in the presence of guanosine triphosphate. Therefore, it appears that at least the second and third cytoplasmic loops of rhodopsin are required for activation of bound Gt.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franke, R R -- Konig, B -- Sakmar, T P -- Khorana, H G -- Hofmann, K P -- New York, N.Y. -- Science. 1990 Oct 5;250(4977):123-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218504" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/metabolism ; Chromosome Deletion ; Micelles ; Models, Molecular ; Molecular Sequence Data ; *Mutation ; Photolysis ; Protein Binding ; Protein Conformation ; Rhodopsin/genetics/*metabolism ; Transducin/*metabolism ; Transfection
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherfas, J -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1240.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2399460" target="_blank"〉PubMed〈/a〉
    Keywords: Fatigue Syndrome, Chronic/*etiology/microbiology/psychology ; Female ; Humans ; Male
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cherfas, J -- New York, N.Y. -- Science. 1990 Aug 24;249(4971):852-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2392675" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Female ; Growth Hormone/*standards ; Humans ; Milk ; Recombinant Proteins/standards ; United States ; United States Food and Drug Administration
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  • 45
    Publication Date: 1990-11-02
    Description: The ventromedial nuclei of the hypothalamus (VMN) are important for the control of feminine mating behavior, and hormone action within these nuclei has been causally related to behavior. Estradiol induces receptors for oxytocin in the VMN and in the area lateral to these nuclei over the course of 1 to 2 days, and progesterone causes, within 30 minutes of its application, a further increase in receptor binding and an expansion of the area covered by these receptors lateral to the VMN. The rapid progesterone effect appears to be a direct and specific effect of this steroid on the receptor or membrane, because it was produced in vitro as well as in vivo and was not mimicked by a variety of other steroids. The effect of progesterone occurred in the posterior part of the VMN, where oxytocin infusion facilitated feminine mating behavior; it did not take place in the anterior part of the VMN, where oxytocin infusion had no effect on mating behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schumacher, M -- Coirini, H -- Pfaff, D W -- McEwen, B S -- HD-05751/HD/NICHD NIH HHS/ -- NS-07080/NS/NINDS NIH HHS/ -- TWO4103/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 2;250(4981):691-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Neuroendocrinology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2173139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Estradiol/pharmacology ; Female ; Oxytocin/pharmacology ; Progesterone/*pharmacology ; Rats ; Receptors, Angiotensin/*drug effects/metabolism ; Receptors, Oxytocin ; Sexual Behavior, Animal/*drug effects ; Ventromedial Hypothalamic Nucleus/*drug effects
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  • 46
    Publication Date: 1990-12-14
    Description: A chemical description of the action of phospholipase A2 (PLA2) can now be inferred with confidence from three high-resolution x-ray crystal structures. The first is the structure of the PLA2 from the venom of the Chinese cobra (Naja naja atra) in a complex with a phosphonate transition-state analogue. This enzyme is typical of a large, well-studied homologous family of PLA2S. The second is a similar complex with the evolutionarily distant bee-venom PLA2. The third structure is the uninhibited PLA2 from Chinese cobra venom. Despite the different molecular architectures of the cobra and bee-venom PLA2s, the transition-state analogue interacts in a nearly identical way with the catalytic machinery of both enzymes. The disposition of the fatty-acid side chains suggests a common access route of the substrate from its position in the lipid aggregate to its productive interaction with the active site. Comparison of the cobra-venom complex with the uninhibited enzyme indicates that optimal binding and catalysis at the lipid-water interface is due to facilitated substrate diffusion from the interfacial binding surface to the catalytic site rather than an allosteric change in the enzyme's structure. However, a second bound calcium ion changes its position upon the binding of the transition-state analogue, suggesting a mechanism for augmenting the critical electrophile.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3443688/" 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/PMC3443688/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, D L -- White, S P -- Otwinowski, Z -- Yuan, W -- Gelb, M H -- Sigler, P B -- GM22324/GM/NIGMS NIH HHS/ -- HL36235/HL/NHLBI NIH HHS/ -- R01 HL036235/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1541-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2274785" target="_blank"〉PubMed〈/a〉
    Keywords: Bee Venoms/analysis ; Binding Sites ; Calcium/metabolism ; Catalysis ; Chemistry, Physical ; Cobra Venoms/analysis ; Models, Molecular ; Molecular Structure ; Organophosphonates/metabolism ; Phospholipases A/chemistry/*metabolism ; Phospholipases A2 ; Phospholipids/metabolism ; Physicochemical Phenomena ; Protein Conformation ; X-Ray Diffraction
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  • 47
    Publication Date: 1990-03-16
    Description: An amino acid sequence encodes a message that determines the shape and function of a protein. This message is highly degenerate in that many different sequences can code for proteins with essentially the same structure and activity. Comparison of different sequences with similar messages can reveal key features of the code and improve understanding of how a protein folds and how it performs its function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, J U -- Reidhaar-Olson, J F -- Lim, W A -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315699" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Computer Graphics ; *DNA-Binding Proteins ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Proteins/*physiology/ultrastructure ; Repressor Proteins ; Structure-Activity Relationship ; Surface Properties ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-01-19
    Description: In a pedigree derived from a mouse treated with the mutagen ethylnitrosourea, a mutation has been identified that predisposes to spontaneous intestinal cancer. The mutant gene was found to be dominantly expressed and fully penetrant. Affected mice developed multiple adenomas throughout the entire intestinal tract at an early age.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moser, A R -- Pitot, H C -- Dove, W F -- CA07175/CA/NCI NIH HHS/ -- CA50585/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):322-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉McArdle Laboratory for Cancer Research, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2296722" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/complications/*genetics ; Alleles ; Anemia/complications/genetics ; Animals ; Ethylnitrosourea ; Female ; Intestinal Neoplasms/complications/*genetics/pathology ; Male ; Mice ; Mice, Inbred AKR ; Mice, Inbred C57BL ; Mice, Mutant Strains ; *Mutation
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Feb 9;247(4943):620-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300818" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Male ; Neoplasms, Radiation-Induced/*epidemiology ; Occupational Diseases/*epidemiology ; Radiation Injuries/*epidemiology ; Risk Factors
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  • 50
    Publication Date: 1990-12-21
    Description: lambda Cro is a dimeric DNA binding protein. Random mutagenesis and a selection for Cro activity have been used to identify the contacts between Cro subunits that are crucial for maintenance of a stably folded structure. To obtain equivalent contacts in a monomeric system, a Cro variant was designed and constructed in which the antiparallel beta-ribbon that forms the dimer interface was replaced by a beta-hairpin. The engineered monomer has a folded structure similar to wild type, is significantly more stable than wild type, and exhibits novel half-operator binding activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mossing, M C -- Sauer, R T -- AI-16982/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1712-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2148648" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophage lambda/*genetics ; Circular Dichroism ; *DNA-Binding Proteins ; Escherichia coli/genetics ; *Genetic Variation ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; Repressor Proteins/*genetics/metabolism ; Thermodynamics ; Transcription Factors/*genetics ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 51
    Publication Date: 1990-07-13
    Description: The three-dimensional structure of the DNA-binding domain (DBD) of the glucocorticoid receptor has been determined by nuclear magnetic resonance spectroscopy and distance geometry. The structure of a 71-residue protein fragment containing two "zinc finger" domains is based on a large set of proton-proton distances derived from nuclear Overhauser enhancement spectra, hydrogen bonds in previously identified secondary structure elements, and coordination of two zinc atoms by conserved cysteine residues. The DBD is found to consist of a globular body from which the finger regions extend. A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed. The model is consistent with previous results indicating that specific amino acid residues of the DBD are involved in protein-DNA and protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hard, T -- Kellenbach, E -- Boelens, R -- Maler, B A -- Dahlman, K -- Freedman, L P -- Carlstedt-Duke, J -- Yamamoto, K R -- Gustafsson, J A -- Kaptein, R -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):157-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utrecht, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115209" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/*metabolism ; DNA-Binding Proteins/analysis/*metabolism ; Humans ; Magnetic Resonance Spectroscopy ; Metalloproteins/analysis ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/analysis/metabolism ; Protein Conformation ; Rats ; Receptors, Glucocorticoid/*analysis/metabolism ; Regulatory Sequences, Nucleic Acid ; Zinc/analysis
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-16
    Description: Activin, a member of the transforming growth factor beta protein family, was originally isolated from gonadal fluids and stimulates the release of pituitary follicle-stimulating hormone (FSH). Activin has numerous functions in both normal and neoplastic cells. Various cells synthesize activin and have a specific binding site for this peptide. However, the molecular basis for its actions is unknown. A binding protein for activin was purified from rat ovary and was identical to follistatin, a specific inhibitor of FSH release. It is likely that the binding protein participates in the diverse regulatory actions of activin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, T -- Takio, K -- Eto, Y -- Shibai, H -- Titani, K -- Sugino, H -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):836-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2106159" target="_blank"〉PubMed〈/a〉
    Keywords: Activins ; Animals ; *Carrier Proteins ; Cells, Cultured ; Female ; Follicle Stimulating Hormone/secretion ; Inhibins/isolation & purification/*metabolism/pharmacology ; Kinetics ; Molecular Weight ; Ovary/*metabolism ; Pituitary Gland/drug effects/secretion ; Protein Binding ; Rats
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-17
    Description: The major small nuclear ribonucleoprotein particles (snRNPs) U1, U2, U4 + U6, and U5 have to be transported from the cytoplasm, where they are synthesized, to the nucleus, where they splice pre-messenger RNAs. Since the free core snRNP proteins in the cytoplasm do not enter the nucleus on their own, the nuclear location signal must either reside on the snRNA or be created as a result of snRNA-protein interaction. Here the involvement by the 5'-terminal cap of snRNA molecules in the nucleo-cytoplasmic transport of UsnRNPs has been studied by microinjection of synthetic U1 RNA molecules into frog oocytes; the U1 RNA bore either the normal cap (m3G) or a chemical derivative. Antibodies in the cytoplasm against the m3G cap inhibited the nuclear uptake of U1 snRNP. U1 RNA that was uncapped or contained an unnatural ApppG cap did not enter the nucleus, even though it carried a normal complement of protein molecules. When the ribose ring of the m3G cap was oxidized with periodate, nuclear transport of U1 snRNPs was severely inhibited. Finally, microinjection of m3G cap alone (but not m7G cap) into oocytes severely inhibited the transport of U1 snRNPs to the nucleus. These data suggest that one step in the nuclear uptake of U1 snRNPs involves the m3G cap structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, U -- Luhrmann, R -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):786-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Tumorforschung, Phillipps-Universitat Marburg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2143847" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Cell Nucleus/*metabolism ; Cytoplasm/metabolism ; Female ; Guanosine/*analogs & derivatives/physiology ; Kinetics ; Mutation ; Oocytes/*ultrastructure ; RNA Caps/*physiology ; Ribonucleoproteins/genetics/*metabolism ; Ribonucleoproteins, Small Nuclear ; Signal Transduction/*physiology ; Xenopus laevis
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  • 54
    Publication Date: 1990-06-01
    Description: Human hereditary cerebral hemorrhage with amyloidosis of the Dutch type (HCHWA-D), an autosomal dominant form of cerebral amyloid angiopathy (CAA), is characterized by extensive amyloid deposition in the small leptomeningeal arteries and cortical arterioles, which lead to an early death of those afflicted in their fifth or sixth decade. Immunohistochemical and biochemical studies have indicated that the amyloid subunit in HCHWA-D is antigenically related to and homologous in sequence with the amyloid beta protein isolated from brains of patients with Alzheimer's disease and Down syndrome. The amyloid beta protein is encoded by the amyloid beta protein precursor (APP) gene located on chromosome 21. Restriction fragment length polymorphisms detected by the APP gene were used to examine whether this gene is a candidate for the genetic defect in HCHWA-D. The data indicate that the APP gene is tightly linked to HCHWA-D and therefore, in contrast to familial Alzheimer's disease, cannot be excluded as the site of mutation in HCHWA-D.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Broeckhoven, C -- Haan, J -- Bakker, E -- Hardy, J A -- Van Hul, W -- Wehnert, A -- Vegter-Van der Vlis, M -- Roos, R A -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Born Bunge Foundation, Department of Biochemistry, University of Antwerp, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1971458" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Amyloid/*genetics ; Amyloid beta-Protein Precursor ; Amyloidosis/complications/*genetics ; Cerebral Hemorrhage/etiology/*genetics ; Cerebrovascular Disorders/complications/*genetics ; Female ; Genes, Dominant ; Genetic Linkage ; Humans ; Lod Score ; Male ; Middle Aged ; Netherlands ; Pedigree ; Polymorphism, Restriction Fragment Length ; Protein Precursors/*genetics
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):909.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305259" target="_blank"〉PubMed〈/a〉
    Keywords: Contraceptive Agents ; Contraceptive Devices ; Family Planning Services/*legislation & jurisprudence/trends ; Female ; Humans ; Male ; Sterilization, Reproductive ; United States
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-15
    Description: The alpha beta T cell receptor (TCR) recognizes antigens that are presented by major histocompatibility complex (MHC)-encoded cell surface molecules by binding to both the antigen and the MHC molecules. Discrimination of self from nonself antigens and MHC molecules is achieved by negative and positive selection of T cells in the thymus: potentially harmful T cells with receptors that bind to self antigens plus self MHC molecules are deleted before they can mount immune responses. In contrast, the maturation of useful T cells with receptors that bind foreign antigens plus self MHC molecules requires the binding of their receptor to MHC molecules on thymic epithelium in the absence of foreign antigen. The binding of the TCR to either class I or class II MHC molecules directs differentiation of the selected cells into either CD4-8+ (killer) or CD4+8- (helper) T cells, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Boehmer, H -- Kisielow, P -- New York, N.Y. -- Science. 1990 Jun 15;248(4961):1369-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Basel Institute for Immunology, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1972594" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/immunology ; Cell Differentiation ; Cell Survival ; Female ; H-2 Antigens/immunology ; Histocompatibility Antigens/immunology ; *Immune Tolerance ; Killer Cells, Natural/immunology ; Male ; Mice ; Mice, Transgenic ; Phenotype ; Receptors, Antigen, T-Cell/genetics/immunology ; T-Lymphocytes/*immunology ; T-Lymphocytes, Helper-Inducer/immunology ; T-Lymphocytes, Regulatory/immunology
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, C K -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):612.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2382137" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Male ; National Institutes of Health (U.S.) ; *Physicians, Women ; *Research Support as Topic ; United States
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  • 58
    Publication Date: 1990-10-26
    Description: The role of defective glucose transport in the pathogenesis of noninsulin-dependent diabetes (NIDDM) was examined in Zucker diabetic fatty rats, a model of NIDDM. As in human NIDDM, insulin secretion was unresponsive to 20 mM glucose. Uptake of 3-O-methylglucose by islet cells was less than 19% of controls. The beta cell glucose transporter (GLUT-2) immunoreactivity and amount of GLUT-2 messenger RNA were profoundly reduced. Whenever fewer than 60% of beta cells were GLUT-2-positive, the response to glucose was absent and hyperglycemia exceeded 11 mM plasma glucose. We conclude that in NIDDM underexpression of GLUT-2 messenger RNA lowers high Km glucose transport in beta cells, and thereby impairs glucose-stimulated insulin secretion and prevents correction of hyperglycemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, J H -- Ogawa, A -- Chen, L -- Orci, L -- Newgard, C B -- Alam, T -- Unger, R H -- DK02700-30/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):546-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Diabetes Research, University of Texas, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237405" target="_blank"〉PubMed〈/a〉
    Keywords: 3-O-Methylglucose ; Animals ; Biological Transport ; Diabetes Mellitus/metabolism ; Diabetes Mellitus, Experimental/*metabolism ; Diabetes Mellitus, Type 2/*metabolism ; Female ; *Gene Expression ; Glucose/pharmacology ; Immunoblotting ; Insulin/secretion ; Islets of Langerhans/drug effects/*metabolism ; Kinetics ; Male ; Methylglucosides/metabolism ; Monosaccharide Transport Proteins/*genetics/metabolism ; Obesity ; RNA, Messenger/metabolism ; Rats ; Rats, Inbred Strains ; Rats, Zucker
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  • 59
    Publication Date: 1990-02-16
    Description: Transfection of Chinese hamster ovary cells with complementary DNA encoding the RIIA sodium channel alpha subunit from rat brain led to expression of functional sodium channels with the rapid, voltage-dependent activation and inactivation characteristic of sodium channels in brain neurons. The sodium currents mediated by these transfected channels were inhibited by tetrodotoxin, persistently activated by veratridine, and prolonged by Leiurus alpha-scorpion toxin, indicating that neurotoxin receptor sites 1 through 3 were present in functional form. The RIIA sodium channel alpha subunit cDNA alone is sufficient for stable expression of functional sodium channels with the expected kinetic and pharmacological properties in mammalian somatic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheuer, T -- Auld, V J -- Boyd, S -- Offord, J -- Dunn, R -- Catterall, W A -- NS 15751/NS/NINDS NIH HHS/ -- NS 25704/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 16;247(4944):854-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2154850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; Cell Line ; Cricetinae ; Cricetulus ; Electric Conductivity ; Female ; Membrane Potentials/drug effects ; Membrane Proteins/genetics/*physiology ; Ovary ; Rats ; Sodium Channels/drug effects/*physiology ; Tetrodotoxin/pharmacology ; *Transfection
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  • 60
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1990 Dec 14;250(4987):1503-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2274777" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Breast Neoplasms/*prevention & control ; Dietary Fats/administration & dosage ; Ethics ; Female ; Humans ; Middle Aged ; *National Institutes of Health (U.S.) ; Patient Compliance ; Research Support as Topic/economics ; United States ; *Women's Health
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  • 61
    Publication Date: 1990-07-20
    Description: Angiotensin II (AII) stimulates rapid increases in the concentration of cytosolic calcium in follicular oocytes from Xenopus laevis. This calcium response was not present in denuded oocytes, indicating that it is mediated by AII receptors on the adherent follicular cells. The endogenous AII receptors differed in their binding properties from mammalian AII receptors expressed on the oocyte surface after injection of rat adrenal messenger RNA. Also, the calcium responses to activation of the amphibian AII receptor, but not the expressed mammalian AII receptor, were blocked reversibly by octanol and intracellular acidification, treatments that inhibit cell coupling through gap junctions. In addition, AII increased the rate of progesterone-induced maturation. Thus, an AII-induced calcium-mobilizing signal is transferred from follicle cells to the oocyte through gap junctions and may play a physiological role in oocyte maturation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sandberg, K -- Bor, M -- Ji, H -- Markwick, A -- Millan, M A -- Catt, K J -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):298-301.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374929" target="_blank"〉PubMed〈/a〉
    Keywords: Aequorin ; Angiotensin II/*analogs & derivatives/metabolism/*pharmacology ; Animals ; Calcium/*metabolism ; Cytosol/drug effects/metabolism ; Female ; Intercellular Junctions/drug effects/*physiology ; Kinetics ; Luminescence ; Oocytes/drug effects/*physiology ; Progesterone/pharmacology ; Receptors, Angiotensin/metabolism ; *Signal Transduction/drug effects ; Structure-Activity Relationship ; Xenopus laevis
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-12-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1657-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/immunology ; Histocompatibility Antigens Class I/genetics/*immunology ; Humans ; *Immunity, Cellular ; *Major Histocompatibility Complex ; Models, Molecular ; Protein Conformation
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  • 63
    Publication Date: 1990-08-31
    Description: Visual presentation of words activates extrastriate regions of the occipital lobes of the brain. When analyzed by positron emission tomography (PET), certain areas in the left, medial extrastriate visual cortex were activated by visually presented pseudowords that obey English spelling rules, as well as by actual words. These areas were not activated by nonsense strings of letters or letter-like forms. Thus visual word form computations are based on learned distinctions between words and nonwords. In addition, during passive presentation of words, but not pseudowords, activation occurred in a left frontal area that is related to semantic processing. These findings support distinctions made in cognitive psychology and computational modeling between high-level visual and semantic computations on single words and describe the anatomy that may underlie these distinctions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petersen, S E -- Fox, P T -- Snyder, A Z -- Raichle, M E -- HL 13851/HL/NHLBI NIH HHS/ -- NS 06833/NS/NINDS NIH HHS/ -- NS 25233/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1041-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology and Neurological Surgery, 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/2396097" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cerebral Cortex/*physiology/radionuclide imaging ; Cerebrovascular Circulation ; Female ; Humans ; *Language ; Male ; Middle Aged ; Oxygen Radioisotopes ; Tomography, Emission-Computed ; *Vision, Ocular ; Visual Cortex/*physiology/radionuclide imaging
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  • 64
    Publication Date: 1990-09-07
    Description: A protein crystal structure is usually described by one single structure, which largely omits the dynamical behavior of the molecule. A molecular dynamics method with a time-averaged crystallographic restraint was used to overcome this limitation. This method yields an ensemble of structures in which all possible thermal motions are allowed, that is, in additional to isotropic distributions, anisotropic and anharmonic positional distributions occur as well. In the case of bovine pancreatic phospholipase A2, this description markedly improves agreement with the observed x-ray diffraction data compared to the results of the classical one-model structure description. Time-averaged crystallographically restrained molecular dynamics reveals large mobilities in the loops involved in lipid bilayer association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gros, P -- van Gunsteren, W F -- Hol, W G -- New York, N.Y. -- Science. 1990 Sep 7;249(4973):1149-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BIOSON Research Institute, University of Groningen, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2396108" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Crystallography ; Hot Temperature ; Models, Molecular ; Motion ; *Phospholipases ; *Phospholipases A ; Phospholipases A2 ; Protein Conformation ; X-Ray Diffraction
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  • 65
    Publication Date: 1990-07-20
    Description: The 70-residue carboxyl-terminal domain of the muscle contractile protein troponin-C contains two helix-loop-helix calcium (Ca)-binding sites that are related to each other by approximate twofold rotational symmetry. Hydrophobic residues from the helices and a short three residue beta sheet at the interface of the two sites act to stabilize the protein domain in the presence of Ca. A synthetic 34-residue peptide representing one of these sites (site III) has been synthesized and studied by H-1 nuclear magnetic resonance (NMR) spectroscopy. In solution this peptide undergoes a Ca-induced conformational change to form the helix-loop-helix Ca-binding motif. Two-dimensional nuclear Overhauser effect spectra have provided evidence for the formation of a beta sheet and interactions between several hydrophobic residues from opposing helices as found in troponin-C. It is proposed that a symmetric two-site dimer similar in tertiary structure to the carboxyl-terminal domain of troponin-C forms from the assembly of two site III peptides in the Ca-bound form.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, G S -- Hodges, R S -- Sykes, B D -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):280-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Calcium/*metabolism/pharmacology ; Hydrogen ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemical synthesis/*metabolism ; Protein Conformation ; Troponin/chemical synthesis/*metabolism ; Troponin C ; Turkeys
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-09-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culliton, B J -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1372.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2402633" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Deaminase/*deficiency/genetics ; Child, Preschool ; Female ; *Genetic Therapy ; Humans ; National Institutes of Health (U.S.) ; Nucleoside Deaminases/*deficiency ; United States
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  • 67
    Publication Date: 1990-08-03
    Description: Chronic endobronchial infection with mucoid Pseudomonas aeruginosa accounts for much of the morbidity and mortality in patients with cystic fibrosis (CF). Reduced morbidity is observed when infection is absent. Clinical investigations have implicated opsonizing antibody specific for the mucoid exopolysaccharide (MEP) surrounding these bacteria as a potential immunologic protective mechanism, whereas nonopsonizing antibody to MEP is not protective. Mice and rats immunized with doses of MEP that elicited opsonizing antibody had reduced levels of infection compared with nonimmune controls after intratracheal challenge with mucoid P. aeruginosa enmeshed in agar beads. Doses of MEP that elicited nonopsonizing antibody were not protective. Parallel experiments in which passive transfer of polyclonal and monoclonal opsonizing and nonopsonizing antibody were used yielded similar results. These data indicate that MEP-specific opsonizing antibody can protect against chronic P. aeruginosa infection in this model of disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pier, G B -- Small, G J -- Warren, H B -- AI 22534/AI/NIAID NIH HHS/ -- AI 22806/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Channing Laboratory, Department of Medicine, Brigham and Women's Hospital and Animal Resource Center, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2116663" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/*therapeutic use ; Cystic Fibrosis/complications ; Disease Models, Animal ; Female ; Immunization, Passive ; Lung/pathology ; Polysaccharides, Bacterial/*immunology ; Pseudomonas Infections/*immunology/pathology/prevention & control ; Pseudomonas aeruginosa/immunology ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-09
    Description: Immunoglobulin rearrangement is central to generating antibody diversity because of heterogeneity generated during recombination by deletion or addition of nucleotides at coding joints by the recombinase machinery. Examination of these junctional modifications revealed that the addition of nongermline-encoded nucleotides was more prevalent in adult versus fetal B cells, thus partially limiting the fetal antibody repertoire. In contrast, deletion of nucleotides occurs equivalently in B cells at different stages of development and at different points in B cell ontogeny. Finally, the bias in murine immunoglobulins for one DH segment reading frame occurs at the DHJH intermediate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meek, K -- New York, N.Y. -- Science. 1990 Nov 9;250(4982):820-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, 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/2237433" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics/immunology ; Animals ; Animals, Newborn ; *Antibody Diversity ; B-Lymphocytes/*immunology ; Blotting, Southern ; Electrophoresis, Polyacrylamide Gel ; Female ; *Gene Rearrangement, B-Lymphocyte ; Immunoglobulin Joining Region/*genetics ; Mice ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Pregnancy ; Restriction Mapping
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  • 69
    Publication Date: 1990-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Y C -- Grable, J C -- Love, R -- Greene, P J -- Rosenberg, J M -- GM25671/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 14;249(4974):1307-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Pittsburgh, PA 15260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2399465" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Computer Graphics ; Crystallization ; DNA-Binding Proteins ; *Deoxyribonuclease EcoRI ; Methods ; Models, Molecular ; Molecular Sequence Data ; Oligonucleotides ; Protein Conformation ; X-Ray Diffraction
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  • 70
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-23
    Description: A founder transgenic mouse harbored two different integration patterns of a transgene at the same locus, each of which gave rise to a similar autosomal recessive mutation. Mice of the mutant phenotype were of small stature but had normal levels of growth hormone. The disrupted locus was cloned, and a genetic and molecular analysis showed that the insertional mutants were allelic to a spontaneous mutant, pygmy. The mice should be a useful model for the growth hormone-resistant human dwarf syndromes and could lead to a greater understanding of the pathways involved in growth and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiang, X -- Benson, K F -- Chada, K -- GM38731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):967-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305264" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Disease Models, Animal ; Dwarfism/*genetics ; Female ; Growth Hormone/blood ; Male ; Mice ; Mice, Mutant Strains ; Mice, Transgenic ; Mutation ; Nucleic Acid Hybridization ; Pedigree ; Restriction Mapping
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  • 71
    Publication Date: 1990-05-11
    Description: Female green turtles exhibit strong nest-site fidelity as adults, but whether the nesting beach is the natal site is not known. Under the natal homing hypothesis, females return to their natal beach to nest, whereas under the social facilitation model, virgin females follow experienced breeders to nesting beaches and after a "favorable" nesting experience, fix on that site for future nestings. Differences shown in mitochondrial DNA genotype frequency among green turtle colonies in the Caribbean Sea and Atlantic Ocean are consistent with natal homing expectations and indicate that social facilitation to nonnatal sites is rare.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meylan, A B -- Bowen, B W -- Avise, J C -- New York, N.Y. -- Science. 1990 May 11;248(4956):724-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Natural Resources, Florida Marine Research Institute, Petersburgh 33701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2333522" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Mitochondrial/*genetics ; Female ; Genotype ; Models, Psychological ; *Orientation ; *Social Facilitation ; Turtles/genetics/*physiology
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  • 72
    Publication Date: 1990-02-23
    Description: Ras proteins participate as a molecular switch in the early steps of the signal transduction pathway that is associated with cell growth and differentiation. When the protein is in its GTP complexed form it is active in signal transduction, whereas it is inactive in its GDP complexed form. A comparison of eight three-dimensional structures of ras proteins in four different crystal lattices, five with a nonhydrolyzable GTP analog and three with GDP, reveals that the "on" and "off" states of the switch are distinguished by conformational differences that span a length of more than 40 A, and are induced by the gamma-phosphate. The most significant differences are localized in two regions: residues 30 to 38 (the switch I region) in the second loop and residues 60 to 76 (the switch II region) consisting of the fourth loop and the short alpha-helix that follows the loop. Both regions are highly exposed and form a continuous strip on the molecular surface most likely to be the recognition sites for the effector and receptor molecule(or molecules). The conformational differences also provide a structural basis for understanding the biological and biochemical changes of the proteins due to oncogenic mutations, autophosphorylation, and GTP hydrolysis, and for understanding the interactions with other proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milburn, M V -- Tong, L -- deVos, A M -- Brunger, A -- Yamaizumi, Z -- Nishimura, S -- Kim, S H -- CA45593/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):939-45.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2406906" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Models, Molecular ; Molecular Structure ; Protein Conformation ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins p21(ras) ; *Signal Transduction ; Structure-Activity Relationship
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  • 73
    Publication Date: 1990-09-21
    Description: Ribonuclease H digests the RNA strand of duplex RNA.DNA hybrids into oligonucleotides. This activity is indispensable for retroviral infection and is involved in bacterial replication. The ribonuclease H from Escherichia coli is homologous with the retroviral proteins. The crystal structure of the E. coli enzyme reveals a distinctive alpha-beta tertiary fold. Analysis of the molecular model implicates a carboxyl triad in the catalytic mechanism and suggests a likely mode for the binding of RNA.DNA substrates. The structure was determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the recombinant selenomethionyl protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, W -- Hendrickson, W A -- Crouch, R J -- Satow, Y -- GM 34102/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1398-405.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2169648" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Computer Graphics ; *Endoribonucleases/genetics ; Escherichia coli/enzymology ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Recombinant Proteins ; Ribonuclease H ; *Selenium ; *Selenomethionine ; Sequence Homology, Nucleic Acid ; X-Ray Diffraction/methods
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  • 74
    Publication Date: 1990-08-17
    Description: In 1988 to 1989, 698 adult cadavers in Abidjan's two largest morgues were studied, representing 38 to 43% of all adult deaths in the city over the study period, and 6 to 7% of annual deaths. Forty-one percent of male and 32% of female cadavers were infected with human immunodeficiency virus (HIV). Fifteen percent of adult male and 13% of adult female annual deaths are due to acquired immunodeficiency syndrome (AIDS). In Abidjan, AIDS is the leading cause of death and years of potential life lost in adult men, followed by unintentional injuries and tuberculosis. In women, AIDS is the second leading cause of death and premature mortality, after deaths related to pregnancy and abortion. AIDS-specific and AIDS-proportional mortality rates may be higher in other African cities where AIDS has been found for a longer time than in Abidjan.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Cock, K M -- Barrere, B -- Diaby, L -- Lafontaine, M F -- Gnaore, E -- Porter, A -- Pantobe, D -- Lafontant, G C -- Dago-Akribi, A -- Ette, M -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Infectious Diseases, Centers for Disease Control, Atlanta, GA 30333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2167515" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/*mortality ; Adolescent ; Adult ; Africa ; Cause of Death ; Cote d'Ivoire ; Female ; HIV Seropositivity ; HIV-1/immunology ; HIV-2/immunology ; Humans ; Male
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  • 75
    Publication Date: 1990-08-31
    Description: The isocitrate dehydrogenase of Escherichia coli is regulated by covalent modification at the active site rather than, as expected, at an allosteric site. As a means of evaluating the mechanism of regulation, the kinetics of the substrate, 2R,3S-isocitrate, and a substrate analog, 2R-malate, were compared for the native, phosphorylated, and mutant enzymes. Phosphorylation decreases activity by more than a factor of 10(6) for the true substrate, but causes minor changes in the activity of the substrate analog. The kinetic results indicate that electrostatic repulsion and steric hindrance between the phosphoryl moiety and the gamma carboxyl group of 2R,3S-isocitrate are the major causes of the inactivation, with a lesser contribution from the loss of a hydrogen bond.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dean, A M -- Koshland, D E Jr -- New York, N.Y. -- Science. 1990 Aug 31;249(4972):1044-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2204110" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Site ; Amino Acid Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Isocitrate Dehydrogenase/genetics/*metabolism ; Models, Molecular ; Mutation ; Protein Conformation
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pool, R -- New York, N.Y. -- Science. 1990 Apr 6;248(4951):29-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2321025" target="_blank"〉PubMed〈/a〉
    Keywords: *Cells/ultrastructure ; Female ; Fertilization in Vitro ; Humans ; Infertility/surgery ; *Laser Therapy ; Male
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, R W -- Brent, R L -- New York, N.Y. -- Science. 1990 Mar 9;247(4947):1166.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315688" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Intellectual Disability/*etiology ; Pregnancy ; *Prenatal Exposure Delayed Effects ; Radiation Dosage ; *Radiation Injuries
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  • 78
    Publication Date: 1990-01-19
    Description: Target cells are thought to regulate the survival of afferent neurons during development by supplying limiting amounts of neurotrophic factors, but the degree to which afferent neurons remain dependent on target-derived support in the adult is uncertain. In this study, uninjured basal forebrain cholinergic neurons did not die after excitotoxic ablation of their target neurons in young adult rats, indicating that they are either not dependent on neurotrophic factors for survival or can obtain trophic support from other sources after target neurons are lost. This finding suggests that cholinergic cell death in neurodegenerative conditions such as Alzheimer's disease is not due solely to a loss of target neurons or factors provided by them.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sofroniew, M V -- Galletly, N P -- Isacson, O -- Svendsen, C N -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1990 Jan 19;247(4940):338-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of Cambridge, England.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1688664" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholinesterase/analysis ; Animals ; Aspartic Acid/analogs & derivatives/pharmacology ; Axonal Transport ; Cell Survival ; Choline/*physiology ; Diencephalon/*cytology ; Female ; Hippocampus/cytology/drug effects ; Immunohistochemistry ; N-Methylaspartate ; Nerve Growth Factors/physiology ; Neurons, Afferent/*physiology ; Rats ; Septal Nuclei/cytology ; Telencephalon/*cytology
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-03-23
    Description: Estrogen and luteinizing hormone-releasing hormone (LH-RH) interact to influence both behavior and gonadotropin release. However, little is known about the biochemical mechanisms that mediate the effects of these hormones or their interactions. The most prominent protein induced by estrogen in the ventromedial hypothalamus has the same amino-terminal sequence as the most prominent protein induced by LH-RH in the pituitary in vitro and in vivo; these proteins comigrate on two-dimensional gels. Furthermore, the hormonal induction may be caused by modification of a constitutive protein with the same molecular weight (70,000) but a slightly more acidic isoelectric point, whose level is inversely related to the level of the induced form after estrogen treatment. Thus estrogen and LH-RH may interact by additively or synergistically inducing this protein, which is called HIP-70.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mobbs, C V -- Fink, G -- Pfaff, D W -- New York, N.Y. -- Science. 1990 Mar 23;247(4949 Pt 1):1477-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Behavior, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2181662" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Electrophoresis, Gel, Two-Dimensional ; Estrogens/*pharmacology ; Female ; Gonadotropin-Releasing Hormone/*pharmacology ; Hypothalamus/drug effects/*metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/*biosynthesis ; Ovariectomy ; Pituitary Gland/drug effects/*metabolism ; *Protein Biosynthesis ; Rats
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  • 80
    Publication Date: 1990-12-21
    Description: The progesterone receptor (PR) in the chicken oviduct is a phosphoprotein that regulates gene transcription in the presence of progesterone. Treatment with progesterone in vivo stimulates phosphorylation of the progesterone receptor. With transient transfection assays, the present work has tested whether phosphorylation participates in the regulation of PR-mediated transcription. Treatment with 8-bromo-cyclic adenosine monophosphate (8-Br cAMP), a stimulator of cAMP-dependent protein kinase [protein kinase A (PKA)], mimicked progesterone-dependent, receptor-mediated transcription in the absence of progesterone. Inhibition of PKA blocked hormone action. Treatment with okadaic acid, an inhibitor of protein phosphatases 1 and 2A, stimulated transcription in a manner similar to that of progesterone. These observations suggest that phosphorylation of the PR or other proteins in the transcription complex can modulate PR-mediated transcription in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Denner, L A -- Weigel, N L -- Maxwell, B L -- Schrader, W T -- O'Malley, B W -- HD-07857/HD/NICHD NIH HHS/ -- HD-22061/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1740-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176746" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Cell Line ; Chickens ; Female ; Gene Expression Regulation ; Kinetics ; Oviducts/metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphorylation ; Progesterone/*pharmacology ; Receptors, Progesterone/*metabolism ; *Transcription, Genetic/drug effects ; Transfection
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  • 81
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, D P -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):469.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200119" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; Female ; Health Services/*legislation & jurisprudence ; Health Services Administration ; Humans ; Medicaid ; Oregon ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-01
    Description: The identification of ras oncogenes in human and animal cancers including precancerous lesions indicates that these genes participate in the early stages of neoplastic development. Yet, these observations do not define the timing of ras oncogene activation in the multistep process of carcinogenesis. To ascertain the timing of ras oncogene activation, an animal model system was devised that involves the induction of mammary carcinomas in rats exposed at birth to the carcinogen nitrosomethylurea. High-resolution restriction fragment length polymorphism analysis of polymerase chain reaction-amplified ras sequences revealed the presence of both H-ras and K-ras oncogenes in normal mammary glands 2 weeks after carcinogen treatment and at least 2 months before the onset of neoplasia. These ras oncogenes can remain latent within the mammary gland until exposure to estrogens, demonstrating that activation of ras oncogenes can precede the onset of neoplasia and suggesting that normal physiological proliferative processes such as estrogen-induced mammary gland development may lead to neoplasia if the targeted cells harbor latent ras oncogenes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumar, R -- Sukumar, S -- Barbacid, M -- 1-RO1-CA48943/CA/NCI NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Squibb Institute for Medical Research, Princeton, NJ 08543.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2188364" target="_blank"〉PubMed〈/a〉
    Keywords: Adenofibroma/genetics ; Animals ; Animals, Newborn ; Base Sequence ; Carcinoma/genetics ; Cell Transformation, Neoplastic/*genetics ; Estrogens/physiology ; Female ; Gene Expression Regulation, Neoplastic/*physiology ; Genes, ras/*physiology ; Mammary Glands, Animal/growth & development ; Mammary Neoplasms, Experimental/chemically induced/*genetics ; Methylnitrosourea ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; Rats ; Rats, Inbred Strains ; Sexual Maturation ; Time Factors
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  • 83
    Publication Date: 1990-08-03
    Description: A two-fold (C2) symmetric inhibitor of the protease of human immunodeficiency virus type-1 (HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the enzyme in a highly symmetric fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J -- Neidhart, D J -- VanDrie, J -- Kempf, D J -- Wang, X C -- Norbeck, D W -- Plattner, J J -- Rittenhouse, J W -- Turon, M -- Wideburg, N -- AI 27220/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer-Assisted Molecular Design, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Drug Design ; Endopeptidases/*metabolism ; Gene Products, pol/*metabolism ; HIV Protease ; HIV-1/*enzymology ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Protease Inhibitors/*pharmacology ; Protein Conformation ; Sugar Alcohols/*pharmacology ; Valine/*analogs & derivatives/pharmacology
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  • 84
    Publication Date: 1990-10-19
    Description: U6 is one of the five small nuclear RNA's (snRNA's) that are required for splicing of nuclear precursor messenger RNA (pre-mRNA). The size and sequence of U6 RNA are conserved among organisms as diverse as yeast and man, and so it has been proposed that U6 RNA functions as a catalytic element in splicing. A procedure for in vitro reconstitution of functional yeast U6 small nuclear ribonucleoproteins (snRNP's) with synthetic U6 RNA was applied in an attempt to elucidate the function of yeast U6 RNA. Two domains in U6 RNA were identified, each of which is required for in vitro splicing. Single nucleotide substitutions in these two domains block splicing either at the first or the second step. Invariably, U6 RNA mutants that block the first step of splicing do not enter the spliceosome. On the other hand, those that block the second step of splicing form a spliceosome but block cleavage at the 3' splice site of the intron. In both domains, the positions of base changes that block the second step of splicing correspond exactly to the site of insertion of pre-mRNA-type introns into the U6 gene of two yeast species, providing a possible explanation for the mechanism of how these introns originated and adding further evidence for the proposed catalytic role of U6 RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fabrizio, P -- Abelson, J -- GM 32637/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 19;250(4979):404-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Division of Biology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2145630" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Nucleus/*metabolism ; Introns ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; RNA Precursors/*genetics ; *RNA Splicing ; RNA, Small Nuclear/*genetics/metabolism ; Ribonucleoproteins/metabolism ; Ribonucleoproteins, Small Nuclear ; Saccharomyces cerevisiae/genetics ; Schizosaccharomyces/*genetics
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1990 Jul 20;249(4966):228.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2374920" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens/*physiology ; *Eggs ; Energy Metabolism ; Female ; Thermodynamics
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  • 86
    Publication Date: 1990-12-21
    Description: Human breast cancer is usually caused by genetic alterations of somatic cells of the breast, but occasionally, susceptibility to the disease is inherited. Mapping the genes responsible for inherited breast cancer may also allow the identification of early lesions that are critical for the development of breast cancer in the general population. Chromosome 17q21 appears to be the locale of a gene for inherited susceptibility to breast cancer in families with early-onset disease. Genetic analysis yields a lod score (logarithm of the likelihood ratio for linkage) of 5.98 for linkage of breast cancer susceptibility to D17S74 in early-onset families and negative lod scores in families with late-onset disease. Likelihood ratios in favor of linkage heterogeneity among families ranged between 2000:1 and greater than 10(6):1 on the basis of multipoint analysis of four loci in the region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, J M -- Lee, M K -- Newman, B -- Morrow, J E -- Anderson, L A -- Huey, B -- King, M C -- CA27632/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1684-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Public Health, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2270482" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/diagnosis/etiology/*genetics ; Chromosome Mapping ; *Chromosomes, Human, Pair 17 ; Female ; Humans ; Male ; Pedigree ; Polymorphism, Genetic ; Pregnancy ; Risk Factors
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  • 87
    Publication Date: 1990-06-29
    Description: The presence of endothelin, a vasoconstrictor peptide, in the hypothalamus and posterior pituitary suggests that it also regulates neural and other nonvascular target cells. In pituitary gonadotrophs, low doses of endothelin evoked oscillations in the intracellular calcium concentration, and high doses induced a biphasic calcium response. Mobilization of intracellular calcium predominated during the spike phase of the calcium response to endothelin, whereas calcium entry through dihydropyridine-sensitive channels contributed to both the spike and plateau phases of the calcium response. Endothelin was a potent as hypothalamic gonadotropin-releasing hormone (GnRH) in stimulation of gonadotropin release in perifused pituitary cells. Endothelin bound specifically to pituitary cells with a dissociation constant of 70 picomolar, and induced rapid formation of inositol trisphosphate and diacyglycerol. Although intracellular calcium concentration and gonadotropin secretory responses to endothelin were independent to the GnRH receptor, endothelin and GnRH appeared to have a common signal transduction mechanism. These observations suggest that endothelin can act as a neuropeptide to regulate anterior pituitary function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stojilkovic, S S -- Merelli, F -- Iida, T -- Krsmanovic, L Z -- Catt, K J -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Endocrinology and Reproduction Research Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163546" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cells, Cultured ; Cytosol/metabolism ; Endothelins ; Endothelium, Vascular ; Female ; Follicle Stimulating Hormone/*secretion ; Gonadotropin-Releasing Hormone/pharmacology ; Kinetics ; Luteinizing Hormone/*secretion ; Male ; Nifedipine/pharmacology ; Orchiectomy ; Peptides/metabolism/*pharmacology ; Pituitary Gland, Anterior/drug effects/*metabolism/secretion ; Rats ; Rats, Inbred Strains ; Receptors, Cell Surface/metabolism ; Receptors, Endothelin ; Reference Values
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Djerassi, C -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1061-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2343313" target="_blank"〉PubMed〈/a〉
    Keywords: Biomarkers/analysis ; Estradiol/analysis ; Female ; Humans ; Menstrual Cycle/physiology ; *Natural Family Planning Methods ; Ovulation Detection/*methods ; Progesterone/analysis ; Reagent Strips
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, C -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1602.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2363048" target="_blank"〉PubMed〈/a〉
    Keywords: Breast Neoplasms/*therapy ; Female ; Humans ; National Institutes of Health (U.S.) ; Prognosis ; Recurrence ; Risk Factors ; United States
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-11-02
    Description: Estimates of the upper limits to human longevity have important policy implications that directly affect forecasts of life expectancy, active life expectancy, population aging, and social and medical programs tied to the size and health status of the elderly population. In the past, investigators have based speculations about the upper limits of human longevity on observations of past trends in mortality. Here the estimate of the upper bound is based on hypothesized reductions in current mortality rates necessary to achieve a life expectancy at birth from 80 to 120 years and an expectation of life at age 50 from 30 to 70 years. With the use of conditional probabilities of death from complete life tables for the United States, reductions in mortality required to achieve extreme longevity (that is, 80 to 120 years) were compared with those resulting from hypothetical cures for all cardiovascular diseases, ischemic heart disease, diabetes, and cancer. Results indicate that in order for life expectancy at birth to increase from present levels to what has been referred to as the average biological limit to life (age 85), mortality rates from all causes of death would need to decline at all ages by 55%, and at ages 50 and over by 60%. Given that hypothetical cures for major degenerative diseases would reduce overall mortality by 75%, it seems highly unlikely that life expectancy at birth will exceed the age of 85.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olshansky, S J -- Carnes, B A -- Cassel, C -- AG06996-01/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 2;250(4981):634-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2237414" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Life Expectancy ; *Longevity ; Male ; Mortality ; Survival Rate ; Terminology as Topic
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-06-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1484.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360043" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*transmission ; Female ; Humans ; Male ; *Prostitution ; Substance Abuse, Intravenous/*complications
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  • 92
    Publication Date: 1990-09-21
    Description: Triosephosphate isomerase (TIM) is used as a model system for the study of how a localized conformational change in a protein structure is produced and related to enzyme reactivity. An 11-residue loop region moves more than 7 angstroms and closes over the active site when substrate binds. The loop acts like a "lid" in that it moves rigidly and is attached by two hinges to the remainder of the protein. The nature of the motion appears to be built into the loop by conserved residues; the hinge regions, in contrast, are not conserved. Results of molecular dynamics calculations confirm the structural analysis and suggest a possible ligand-induced mechanism for loop closure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joseph, D -- Petsko, G A -- Karplus, M -- New York, N.Y. -- Science. 1990 Sep 21;249(4975):1425-8.〈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/2402636" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Carbohydrate Epimerases/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; *Protein Conformation ; Software ; Triose-Phosphate Isomerase/*metabolism
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  • 93
    Publication Date: 1990-05-04
    Description: The Drosophila Shaker gene on the X chromosome has three sister genes, Shal, Shab, and Shaw, which map to the second and third chromosomes. This extended gene family encodes voltage-gated potassium channels with widely varying kinetics (rate of macroscopic current activation and inactivation) and voltage sensitivity of steady-state inactivation. The differences in the currents of the various gene products are greater than the differences produced by alternative splicing of the Shaker gene. In Drosophila, the transient (A current) subtype of the potassium channel (Shaker and Shal) and the delayed-rectifier subtype (Shab and Shaw) are encoded by homologous genes, and there is more than one gene for each subtype of channel. Homologs of Shaker, Shal, Shab, and Shaw are present in mammals; each Drosophila potassium-channel gene may be represented as a multigene subfamily in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wei, A -- Covarrubias, M -- Butler, A -- Baker, K -- Pak, M -- Salkoff, L -- 1 RO1-NS24785-01/NS/NINDS NIH HHS/ -- GMO 7200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 May 4;248(4955):599-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Neurobiology, 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/2333511" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Chromosome Mapping ; Drosophila/*genetics ; Drosophila Proteins ; Female ; Membrane Proteins/*genetics/physiology ; Mice/*genetics ; Molecular Sequence Data ; *Multigene Family ; Oocytes/physiology ; Potassium Channels/*physiology ; Sequence Homology, Nucleic Acid ; Shab Potassium Channels ; Transcription, Genetic ; *X Chromosome ; Xenopus
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  • 94
    Publication Date: 1990-04-27
    Description: In Drosophila three maternal pattern organizing activities, the anterior, the posterior, and the terminal, establish the anterior-posterior body pattern of the embryo by initiating the spatially restricted activities of the gap class of zygotic segmentation genes. The activities of tailless (tll) and the newly identified gap gene huckebein (hkb) are specifically involved in mediating the maternal terminal information at the posterior end of the blastoderm embryo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weigel, D -- Jurgens, G -- Klingler, M -- Jackle, H -- New York, N.Y. -- Science. 1990 Apr 27;248(4954):495-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universitat Munchen, Institut fur Genetik und Mikrobiologie, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2158673" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blastoderm/*physiology ; Cell Differentiation ; Drosophila/embryology/*genetics ; Female ; Gene Expression ; Genes/*physiology ; Genotype ; Mutation ; Phenotype ; Protein-Tyrosine Kinases/genetics ; Receptors, Cell Surface/genetics ; Suppression, Genetic
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palca, J -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):117-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2371558" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Diptera ; Female ; Government Agencies ; Libya ; Male ; Myiasis/*prevention & control ; *Pest Control, Biological ; Screw Worm Infection/*prevention & control ; United States
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1990-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1990 Feb 2;247(4942):522.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2300810" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Child ; Female ; *Government Agencies ; Humans ; Infant ; *Nutritional Physiological Phenomena ; *Public Assistance ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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