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  • Amino Acid Sequence  (14)
  • Rats, Inbred Strains  (9)
  • American Association for the Advancement of Science (AAAS)  (23)
  • International Union of Crystallography (IUCr)
  • 1980-1984  (23)
  • 1984  (23)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (23)
  • International Union of Crystallography (IUCr)
Years
  • 1980-1984  (23)
Year
  • 1
    Publication Date: 1984-08-10
    Description: The gene for the circumsporozoite (CS) protein of Plasmodium falciparum has been cloned and its nucleotide sequence determined. The gene encodes a protein of 412 amino acids as deduced from the nucleotide sequence. The protein contains 41 tandem repeats of a tetrapeptide, 37 of which are Asn-Ala-Asn-Pro and four of which are Asn-Val-Asp-Pro. Monoclonal antibodies against the CS protein of Plasmodium falciparum were inhibited from binding to the protein by synthetic peptides of the repeat sequence. The CS protein of Plasmodium falciparum and the CS protein of a simian malaria parasite, Plasmodium knowlesi, have two regions of homology, one of which is present on either side of the repeat. One region contains 12 of 13 identical amino acids. Within the nucleotide sequence of this region, 25 of 27 nucleotides are conserved. The conservation of these regions in parasites widely separated in evolution suggests that they may have a function such as binding to liver cells and may represent an invariant target for immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dame, J B -- Williams, J L -- McCutchan, T F -- Weber, J L -- Wirtz, R A -- Hockmeyer, W T -- Maloy, W L -- Haynes, J D -- Schneider, I -- Roberts, D -- New York, N.Y. -- Science. 1984 Aug 10;225(4662):593-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Base Sequence ; Epitopes/genetics ; *Genes ; Humans ; Liver/parasitology ; Malaria/*immunology ; Plasmodium/genetics ; Plasmodium falciparum/*genetics/immunology ; *Protozoan Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1984-11-16
    Description: The guanosine triphosphate-binding proteins (G proteins) found in a variety of tissues transduce signals generated by ligand binding to cell surface receptors into changes in intracellular metabolism. Amino acid sequences of peptides prepared by partial proteolysis of the alpha subunit of a bovine brain G protein and the alpha subunit of rod outer-segment transducin were determined. The two proteins show regions of sequence identity as well as regions of diversity. A portion of the amino-terminal peptide sequence of each protein is highly homologous with the corresponding region in the ras protein (a protooncogene product). These similarities suggest that G proteins and ras proteins may have analogous functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J B -- Simon, M I -- Teplow, D B -- Robishaw, J D -- Gilman, A G -- GM 09731-02/GM/NIGMS NIH HHS/ -- NS 18153/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):860-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436980" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cattle ; GTP-Binding Proteins/*metabolism ; Neoplasm Proteins/*metabolism ; Oncogenes ; Protein Conformation ; Proto-Oncogene Proteins p21(ras) ; Transduction, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1984-10-05
    Description: The human T-cell leukemia viruses HTLV-I and HTLV-II are unique among the transforming retroviruses of vertebrates in their ability to transform human T cells in vitro and in their close association with human malignancies (T-cell lymphomas and leukemia). Their genomes are relatively simple, containing the genes gag, pol, env, and a 3' region termed "X." This 3' region may be responsible for the transforming potential of the viruses. The existence of proteins encoded by the 3' region has been postulated on the basis of multiple open reading frames. In the present study this region is shown to contain a gene encoding a protein of 40 kilodaltons in HTLV-I and 37 kilodaltons in HTLV-II. It is proposed that these proteins be called, respectively, p40xI and p37xII.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Slamon, D J -- Shimotohno, K -- Cline, M J -- Golde, D W -- Chen, I S -- CA 16042/CA/NCI NIH HHS/ -- CA 32737/CA/NCI NIH HHS/ -- RR 00865/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):61-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089351" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; B-Lymphocytes/microbiology ; Cell Line ; *Cell Transformation, Viral ; Deltaretrovirus/analysis/*genetics/physiology ; *Genes, Viral ; Humans ; Immune Sera ; Molecular Weight ; T-Lymphocytes/*microbiology ; Trans-Activators ; Viral Proteins/genetics/immunology/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1984-06-29
    Description: The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line. Nucleotide sequence analysis of the gene revealed that the encoded IL-2 protein has three cysteines located at amino acid residues 58, 105, and 125 of the mature protein. Site-specific mutagenesis procedures were used to modify the IL-2 gene by changing each of the cysteine codons individually to serine codons. Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge. The modified IL-2 protein containing a substitution at position 125 retained full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, A -- Lu, S D -- Mark, D F -- New York, N.Y. -- Science. 1984 Jun 29;224(4656):1431-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6427925" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Cysteine/metabolism ; DNA, Recombinant/metabolism ; Escherichia coli/genetics ; Genes ; Humans ; Interleukin-2/*genetics ; *Mutation ; Receptors, Immunologic/metabolism ; Receptors, Interleukin-2 ; Serine/metabolism ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1984-07-27
    Description: The sequence of the envelope glycoprotein gene of type II human T lymphotropic virus (HTLV) is presented. The predicted amino acid sequence is similar to that of the corresponding protein of HTLV type I, in that the proteins share the same amino acids at 336 of 488 residues, and 68 of the 152 differences are of a conservative nature. The overall structural similarity of these proteins provides an explanation for the antigenic cross-reactivity observed among diverse members of the HTLV retrovirus family by procedures that assay for the viral envelope glycoprotein, for example, membrane immunofluorescence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodroski, J -- Patarca, R -- Perkins, D -- Briggs, D -- Lee, T H -- Essex, M -- Coligan, J -- Wong-Staal, F -- Gallo, R C -- Haseltine, W A -- CA-18216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jul 27;225(4660):421-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204380" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Base Sequence ; Cross Reactions ; Cysteine/metabolism ; Deltaretrovirus/*genetics ; Epitopes/immunology ; *Genes, Viral ; Glycoproteins/*genetics ; Humans ; Viral Envelope Proteins/*genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1984-07-20
    Description: Adult rats with bilateral lesions of the caudate nucleus were treated with GM1 ganglioside. Although animals injected with a control solution were severely impaired in their ability to learn a complex spatial task, those treated with ganglioside were able to learn spatial reversals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabel, B A -- Slavin, M D -- Stein, D G -- New York, N.Y. -- Science. 1984 Jul 20;225(4659):340-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6740316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/*drug effects ; Brain Injuries/*drug therapy/psychology ; Caudate Nucleus/drug effects/injuries ; G(M1) Ganglioside/pharmacology/*therapeutic use ; Gangliosides/*therapeutic use ; Humans ; Learning/drug effects ; Male ; Rats ; Rats, Inbred Strains
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-11-16
    Description: The magnetic fields associated with penicillin-induced focal epilepsy were measured in laboratory rats. Interictal magnetic spikes were similar to those previously observed in humans with focal seizure disorders. The magnetic fields of the seizure itself displayed both slow and fast phenomena, reversing in direction on opposite sides of the head.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barth, D S -- Sutherling, W -- Beatty, J -- 1-R01-NS20806-01/NS/NINDS NIH HHS/ -- 1K07NS00678-01A1/NS/NINDS NIH HHS/ -- 5-S07 RR07009/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):855-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436979" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electroencephalography ; *Electromagnetic Fields ; *Electromagnetic Phenomena ; Electrophysiology ; Epilepsies, Partial/*physiopathology ; Humans ; Penicillins/pharmacology ; Rats ; Rats, Inbred Strains ; Seizures/physiopathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-06-22
    Description: The pathophysiology of brain dysfunction was studied with an animal model of chronic alcoholism. Rats were fed a liquid diet with or without ethanol for 20 weeks and then the diet without ethanol for three more weeks. Hippocampal slices were prepared and intracellular recordings were obtained from dentate granule and CA1 cells. Significant depression of orthodromically elicited inhibitory postsynaptic potentials and postspike afterhyperpolarizations was observed in neurons from ethanol-exposed animals. No differences were observed in other active or passive membrane characteristics. These results suggest that a loss of neuronal inhibition could contribute to brain dysfunction in chronic alcoholism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Durand, D -- Carlen, P L -- New York, N.Y. -- Science. 1984 Jun 22;224(4655):1359-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6328654" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Alcoholism/physiopathology ; Animals ; Calcium/physiology ; Ethanol/*pharmacology ; Humans ; Ion Channels/drug effects ; Male ; Membrane Potentials/drug effects ; Neurons/*drug effects ; Rats ; Rats, Inbred Strains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 1984-11-02
    Description: Smooth muscle cells with 4C (double diploid) DNA content have been found in major arteries. The proportion of 4C cells increases with normal aging and with hypertension. These cells may represent a state of arrest at the G2 phase of the cell cycle or may be examples of true tetraploidy. Flow cytometric cell sorting was used to isolate 4C smooth muscle cells from the rat aorta, and the cells were cultured. Flow cytometry, Feulgen microdensitometry, and karyotyping of the progeny of the 4C cells established the presence of true tetraploid cells. These findings demonstrate the presence of reproductively viable tetraploid cells in a normal mammalian tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, I D -- Rosen, E M -- Shapiro, H M -- Zoller, L C -- Myrick, K -- Levenson, S E -- Christenson, L -- 5-P01-CA-12662/CA/NCI NIH HHS/ -- AG00599/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):559-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta, Thoracic/analysis/*cytology ; Cells, Cultured ; DNA/analysis ; Flow Cytometry ; Humans ; Karyotyping ; Muscle, Smooth, Vascular/analysis/*cytology ; *Polyploidy ; Rats ; Rats, Inbred Strains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 1984-08-17
    Description: Leukotriene B4, at the same intracutaneous doses as bradykinin, reduced the nociceptive threshold in the rat paw. The mechanism of leukotriene B4-induced hyperalgesia was distinguished from that of the hyperalgesia elicited by prostaglandin E2 and bradykinin by its dependence on polymorphonuclear leukocytes and independence of the cyclooxygenation of arachidonic acid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levine, J D -- Lau, W -- Kwiat, G -- Goetzl, E J -- AM 32634/AM/NIADDK NIH HHS/ -- DE 05369/DE/NIDCR NIH HHS/ -- HL 31809/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Aug 17;225(4663):743-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6087456" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/*pharmacology ; Animals ; Bradykinin/pharmacology ; Dinoprostone ; Indomethacin/pharmacology ; Leukotriene B4/analogs & derivatives/*pharmacology ; Male ; Neutrophils/*drug effects/physiology ; Prostaglandin-Endoperoxide Synthases/metabolism ; Prostaglandins E/pharmacology ; Rats ; Rats, Inbred Strains ; SRS-A/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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