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  • Amino Acid Sequence  (35)
  • Species Specificity
  • American Association for the Advancement of Science (AAAS)  (52)
  • Blackwell Publishing Ltd
  • 1980-1984  (52)
  • 1975-1979
  • 1925-1929
  • 1984  (52)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (52)
  • Blackwell Publishing Ltd
Years
  • 1980-1984  (52)
  • 1975-1979
  • 1925-1929
Year
  • 1
    Publication Date: 1984-02-24
    Description: The suprachiasmatic nucleus has been identified tentatively as a circadian pacemaker. To examine the functional role of peptides found within suprachiasmatic neurons, avian pancreatic polypeptide and vasopressin were microinjected into the suprachiasmatic region. Avian pancreatic polypeptide, but not vasopressin, shifted the phase of the wheelrunning rhythm as a function of the time of its injection within the circadian cycle. Avian pancreatic polypeptide or a similar peptide may be one component of the neurochemical processes underlying entrainment to the light-dark cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albers, H E -- Ferris, C F -- Leeman, S E -- Goldman, B D -- GM-31199/GM/NIGMS NIH HHS/ -- HD-18022/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):833-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6546454" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; Cerebral Ventricles/drug effects ; *Circadian Rhythm ; Cricetinae ; Motor Activity/drug effects ; Nerve Tissue Proteins/pharmacology ; Neuropeptide Y ; Pancreatic Polypeptide/*pharmacology ; Species Specificity ; Suprachiasmatic Nucleus/*drug effects ; Vasopressins/pharmacology
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  • 2
    Publication Date: 1984-11-23
    Description: Endonuclease restriction (Hind III) fragments of DNA from Chinese hamster X mouse somatic cell hybrids hybridized with proline-rich protein complementary DNA clones only when the DNA was isolated from cells containing mouse chromosome 8, or a fragment of chromosome 8. The evidence suggests that proline-rich protein genes are located at the proximal portion of chromosome 8 toward the centromere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azen, E A -- Carlson, D M -- Clements, S -- Lalley, P A -- Vanin, E -- AM 19175/AM/NIADDK NIH HHS/ -- DEO 3658-19/DE/NIDCR NIH HHS/ -- GM 20069/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):967-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095444" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; DNA Restriction Enzymes ; *Genes ; Humans ; Mice ; Mice, Inbred Strains ; Nucleic Acid Hybridization ; Peptides/*genetics ; Proline-Rich Protein Domains ; Protein Biosynthesis ; RNA, Messenger/genetics ; Salivary Proteins and Peptides/*genetics ; Species Specificity
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  • 3
    Publication Date: 1984-11-23
    Description: The elasmobranch spiracular organ is a specialized receptor associated with the first visceral pouch. The structure of the sensory epithelium of the spiracular organ and the pattern of central termination of the afferent neurons that innervate it show that the spiracular organ is a mechanoreceptor closely related to the lateral line system of sense organs. Its position and orientation within the spiracular cleft suggest that it plays a role in proprioception or equilibrium-audition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barry, M A -- Boord, R L -- NS 11272/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):990-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505680" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways/anatomy & histology ; Animals ; Fishes/*anatomy & histology ; Mechanoreceptors/*physiology/ultrastructure ; Microscopy, Electron, Scanning ; Sharks/*anatomy & histology ; Species Specificity
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-08-03
    Description: The brain has diversified and advanced in evolution more than any other organ; the variety of nervous systems and behaviors among animal species is thus available for our exploitation. Comparative neuroscience is likely to reach insights so novel as to constitute revolutions in understanding the structure, functions, ontogeny, and evolution of nervous systems. This promise requires pursuit on a wide front, in respect to disciplines and in respect to the species, stages, and states compared. It also requires deliberate concentration on the differences among animals, in addition to the prevailing concern for the basic and common. Neglect of these challenges would be costly. Without due consideration of the neural and behavioral correlates of differences between higher taxa and between closely related families, species, sexes, and stages, we cannot expect to understand our nervous systems or ourselves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bullock, T H -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):473-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6740319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Brain/*physiology ; Electrophysiology ; Humans ; Invertebrates ; Neurons/physiology ; Species Specificity ; Synapses/physiology ; Vertebrates
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  • 5
    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
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  • 6
    Publication Date: 1984-08-03
    Description: The nucleotide sequence of a human Blym-1 transforming gene activated in a Burkitt's lymphoma cell line was determined. This sequence predicts a small protein of 58 amino acids that is 33 percent identical to the predicted product of chicken Blym-1, the activated transforming gene of chicken B cell lymphomas. Both the human and chicken Blym-1 genes exhibit significant identity to an amino-terminal region of transferrins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, A -- Devine, J M -- Cooper, G M -- CA 07250/CA/NCI NIH HHS/ -- CA 28946/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):516-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330897" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Burkitt Lymphoma/*genetics ; Cell Line ; *Cell Transformation, Neoplastic ; DNA Restriction Enzymes ; Humans ; *Oncogenes ; Structure-Activity Relationship ; Transcription, Genetic ; Transferrin/genetics
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  • 7
    Publication Date: 1984-02-03
    Description: The nucleotide sequences of the six regions within the normal human cellular locus (c-sis) that correspond to the entire transforming region of the simian sarcoma virus (SSV) genome (v-sis) were determined. The regions are bounded by acceptor and donor splice sites and, except for region 6, resemble exons. Region 6 lacks a 3' donor splice site and terminates -5 base pairs from the 3' v-sis-helper-viral junction. This is consistent with a model proposing that SSV was generated by recombination between proviral DNA of a simian sarcoma associated virus and proto-sis and that introns were spliced out subsequently from a fused viral-sis messenger RNA. This also suggests that the 3' recombination occurred within an exon of the woolly monkey (Lagothrix) genome. The open reading frames predicting the v-sis and c-sis gene products coincide with the stop codon of c-sis located 123 nucleotides into the fifth region of homology. The overall nucleotide homology was 91 percent with substitutions mainly in the third codon positions within the open reading frame and with greatest divergence within the untranslated 3' portion of the sequences. The predicted protein products for v-sis and c-sis are 93 percent homologous. The predicted c-sis gene product is identical in 31 of 31 amino acids to one of the published sequences of platelet-derived growth factor. Thus, c-sis encodes one chain of human platelet-derived growth factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Josephs, S F -- Guo, C -- Ratner, L -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Feb 3;223(4635):487-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318322" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; Codon ; *Genes, Viral ; Humans ; *Oncogenes ; Platelet-Derived Growth Factor/*genetics ; RNA Splicing ; RNA, Messenger/genetics ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/genetics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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  • 9
    Publication Date: 1984-10-05
    Description: Antibodies in sera from patients with adult T-cell leukemia-lymphoma or from healthy carriers of type I human T-cell leukemia virus (HTLV) recognize an antigen of approximately 42 kilodaltons (p42) in cell lines infected with HTLV-I. Radiolabel sequence analysis of cyanogen bromide fragments of p42 led to the conclusion that this antigen is encoded in part by LOR, a conserved portion of the "X" region that is flanked by the envelope gene and the 3' long terminal repeat of HTLV-I. It is possible that this novel product mediates the unique transformation properties of the HTLV family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, T H -- Coligan, J E -- Sodroski, J G -- Haseltine, W A -- Salahuddin, S Z -- Wong-Staal, F -- Gallo, R C -- Essex, M -- 2-T32-CA0903/CA/NCI NIH HHS/ -- CA07094/CA/NCI NIH HHS/ -- CA13885/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):57-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089350" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Viral/*genetics ; Base Sequence ; Cell Line ; Cyanogen Bromide ; Deltaretrovirus/*genetics/immunology ; *Genes, Viral ; Humans ; Peptide Fragments ; Trans-Activators ; Viral Proteins/*genetics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):806.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Cycle ; Humans ; *Oncogenes ; Receptor, Epidermal Growth Factor ; *Receptors, Cell Surface
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  • 11
    Publication Date: 1984-08-24
    Description: Malaria parasites can be grouped evolutionarily by analysis of DNA composition and genome arrangement. Those that vary widely with regard to host range, morphology, and biological characteristics fit into only a small number of distinctive groups. The DNA of the human parasite Plasmodium falciparum fits into a group that includes rodent and avian malarias and is unlike the DNA of other primate malaria parasites. The DNA of Plasmodium vivax, which is also a human parasite, fits into a distinctly different group that includes Plasmodium cynomolgi, a parasite of monkeys. The evolutionary lines suggested here appear to be consistent with similarities seen among malaria parasites with regard to gene sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCutchan, T F -- Dame, J B -- Miller, L H -- Barnwell, J -- New York, N.Y. -- Science. 1984 Aug 24;225(4664):808-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382604" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; *Biological Evolution ; DNA/*analysis ; Deoxycytidine/analysis ; Deoxyguanosine/analysis ; Nucleic Acid Hybridization ; Plasmodium/*classification/genetics ; Plasmodium berghei/classification/genetics ; Plasmodium falciparum/classification/genetics ; Plasmodium vivax/classification/genetics ; Species Specificity
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  • 12
    Publication Date: 1984-11-30
    Description: A single recessive gene, lpr, induces an autoimmune-lymphoproliferative syndrome in several strains of mice. The lymphoid organs of lpr/lpr mice contained cells with increased amounts of myb RNA, which codes for a protein found in the nucleus. A similar human lymphoproliferative disorder also had an increase in c-myb expression. Mouse T cells induced by mitogens to proliferate did not express large amounts of myb RNA, indicating that marked myb expression is not a general feature of lymphocyte activation and proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mountz, J D -- Steinberg, A D -- Klinman, D M -- Smith, H R -- Mushinski, J F -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1087-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantibodies/*genetics ; Autoimmune Diseases/*genetics ; Female ; *Genes, Recessive ; Lymphocytes/immunology ; Lymphoproliferative Disorders/*genetics ; Mice ; Mice, Inbred Strains ; Nucleic Acid Hybridization ; *Oncogenes ; Species Specificity ; Spleen/immunology ; *Transcription, Genetic
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  • 13
    Publication Date: 1984-03-23
    Description: A gene for ribonuclease S protein, has been chemically synthesized and cloned. The gene is designed to have 25 specific restriction endonuclease sites spaced at short intervals, permitting its structure to be rapidly modified. This flexibility facilitates tests of hypotheses relating the primary structure of the enzyme to its physical and catalytic behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nambiar, K P -- Stackhouse, J -- Stauffer, D M -- Kennedy, W P -- Eldredge, J K -- Benner, S A -- 1 RO1 GM 30110-01A2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 23;223(4642):1299-301.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322300" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; DNA Restriction Enzymes ; Escherichia coli/genetics ; *Genes, Synthetic ; Oligodeoxyribonucleotides/chemical synthesis ; Peptide Fragments/*genetics ; Ribonucleases/*genetics
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  • 14
    Publication Date: 1984-01-06
    Description: The nucleotide sequence of the region of Gardner-Rasheed feline sarcoma virus (GR-FeSV) encoding its primary translation product, p70gag-fgr, has been determined. From the nucleotide sequence, the amino acid sequence of this transforming protein was deduced. Computer analysis indicates that a portion of P70gag-fgr has extensive amino acid sequence homology with actin, a eukaryotic cytoskeletal protein. A second region of P70gag-fgr is closely related to the tyrosine-specific kinase gene family. Thus, the v-fgr oncogene appears to have arisen as a result of recombinational events involving two distinct cellular genes, one coding for a structural protein and the other for a protein kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naharro, G -- Robbins, K C -- Reddy, E P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):63-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318314" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/analysis ; Amino Acid Sequence ; Base Sequence ; Computers ; Gene Products, gag ; *Genes, Viral ; *Oncogenes ; Protein Kinases/analysis ; Protein-Tyrosine Kinases ; Recombination, Genetic ; Retroviridae/*genetics ; Sarcoma Viruses, Feline/*genetics ; Viral Proteins/analysis/*genetics
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  • 15
    Publication Date: 1984-04-27
    Description: Immunodominant, disulfide-bond independent epitopes recognized by human antibodies to hepatitis B virus (HBV) are located within the 55-residue amino terminal portion (coded for by the pre-S region of HBV DNA) of minor HBV envelope components larger than the major protein constituents encoded by the S gene. A peptide having the sequence of the first 26 amino acids from the amino terminal methionine was synthesized and elicited antibodies (at dilutions of greater than or equal to 1 to 10(5) ) to the HBV envelope. These antibodies can be utilized for diagnostic tests. The immunogenicity of the peptide was substantially increased by covalent attachment to liposomes. The disulfide bond-independent determinants on sequences coded for by the pre-S gene may be more easily mimicked by peptide analogs than "conformational" determinants on the S-gene product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, A R -- Kent, S B -- Strick, N -- 9011/PHS HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):392-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200931" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Epitopes/*analysis/genetics/immunology ; *Genes, Viral ; Hepatitis B Antibodies/biosynthesis ; Hepatitis B Surface Antigens/analysis/genetics/*immunology ; Hepatitis B virus/genetics/*immunology ; Immunization ; Liposomes ; Peptides/chemical synthesis/genetics/*immunology ; Rabbits
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  • 16
    Publication Date: 1984-08-17
    Description: Antisera to a synthetic c-myc peptide and to c-myc antigens synthesized from various portions of the human gene expressed in Escherichia coli were used in order to characterize the protein product of the human c-myc oncogene. Although the deduced molecular weight of the human c-myc protein is 49,000, these antisera precipitate a protein from human cells that migrates in sodium dodecyl sulfate-polyacrylamide gel as if its molecular weight were 65,000. In addition, the mouse c-myc protein, whether synthesized in cells or in a cell-free system directed by pure, synthetic messenger RNA, has analogous properties and is immunoprecipitated by the antiserum to the human c-myc protein. Similar proteins are immunoprecipitated from monkey, rat, hamster, and frog cells, suggesting evolutionary conservation of antigenic structure of the c-myc protein among vertebrates. In addition, and in a manner consistent with the behavior of its messenger RNA, the immunoprecipitable c-myc protein is sharply induced by the action of mitogens on resting human T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Persson, H -- Hennighausen, L -- Taub, R -- DeGrado, W -- Leder, P -- New York, N.Y. -- Science. 1984 Aug 17;225(4663):687-93.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6431612" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Neoplasm/*immunology ; Base Sequence ; *Cell Division ; Chickens ; Cricetinae ; DNA, Neoplasm/genetics ; DNA, Recombinant/metabolism ; Electrophoresis, Polyacrylamide Gel ; Haplorhini ; Humans ; Mice ; Mitogens/pharmacology ; Molecular Weight ; Neoplasm Proteins/genetics/*immunology ; *Oncogenes ; RNA, Messenger/genetics ; Rabbits ; Rats
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  • 17
    Publication Date: 1984-11-23
    Description: The tachykinins are a family of peptides with the carboxyl terminal amino acid sequence Phe-X-Gly-Leu-Met-NH2. Three major mammalian tachykinins have been identified--substance K, neuromedin K, and substance P--but only two tachykinin receptors have been postulated. Three tachykinins were labeled with radioiodinated Bolton-Hunter reagent and their binding characteristics were determined in crude membrane suspensions from several tissues. In cerebral cortex labeled eledoisin exhibited high-affinity binding that was inhibited by tachykinins in a manner indicating a definitive SP-E receptor site. In gastrointestinal smooth muscle and bladder, high-affinity binding of labeled substance P was inhibited in a pattern indicating a definitive SP-P site. In intestinal smooth muscle and bladder, however, labeled substance K and labeled eledoisin were both bound in a pattern indicating a preference for substance K itself. The results suggest the existence of three distinct types of tachykinin receptors: SP-P, SP-E, and SP-K.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buck, S H -- Burcher, E -- Shults, C W -- Lovenberg, W -- O'Donohue, T L -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):987-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Cell Membrane/metabolism ; Cerebral Cortex/*metabolism ; Duodenum/*metabolism ; Guinea Pigs ; Intestine, Small/*metabolism ; Kinetics ; Mice ; Organ Specificity ; Peptides/*metabolism ; Rats ; Receptors, Neurokinin-2 ; Receptors, Neurotransmitter/*metabolism ; *Receptors, Tachykinin ; Species Specificity ; Tachykinins ; Urinary Bladder/*metabolism
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
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  • 19
    Publication Date: 1984-01-27
    Description: The genetic relationships among molecularly cloned prototype viruses representing all of the major oncovirus genera were investigated by molecular hybridization and nucleotide sequence analysis. One of the major progenitors of the pol genes of such viruses gives rise to mammalian type C viruses and another gives rise to type A, B, D, and avian type C oncoviruses. Evidence of unusual patterns of homology among the env genes of mammalian type C and D oncoviruses illustrates that genetic interactions between their progenitors contributed to the evolution of oncoviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiu, I M -- Callahan, R -- Tronick, S R -- Schlom, J -- Aaronson, S A -- New York, N.Y. -- Science. 1984 Jan 27;223(4634):364-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6197754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Avian Sarcoma Viruses/genetics ; Base Sequence ; *Biological Evolution ; Cloning, Molecular ; DNA Restriction Enzymes ; *Genes, Viral ; Nucleic Acid Heteroduplexes ; Nucleic Acid Hybridization ; RNA-Directed DNA Polymerase/*genetics/metabolism ; Recombination, Genetic ; Retroviridae/classification/*genetics ; Viral Envelope Proteins/genetics
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  • 20
    Publication Date: 1984-11-30
    Description: Complementary DNA clones of genes induced by platelet-derived growth factor (PDGF) in BALB/c-3T3 cells were isolated; one such clone contains a domain having nucleotide sequence homology with the third exon of c-fos. This nucleotide sequence homology is reflected in the predicted amino acid sequences of the gene products. Under low stringency conditions, the mouse v-fos gene cross-hybridizes with the PDGF-inducible complementary DNA clone. However, the messenger RNA transcripts of mouse c-fos and the new fos-related gene can be distinguished by gel electrophoresis and by S1 nuclease analysis. Expression of the authentic c-fos gene is induced by PDGF and superinduced by the combination of PDGF and cycloheximide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochran, B H -- Zullo, J -- Verma, I M -- Stiles, C D -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1080-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6093261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; *Cloning, Molecular ; DNA/analysis ; DNA Restriction Enzymes ; DNA Transposable Elements ; Endonucleases ; Genes/drug effects ; Mice ; Mice, Inbred BALB C ; Nucleic Acid Hybridization ; Oncogenes/*drug effects ; Platelet-Derived Growth Factor/*pharmacology ; Single-Strand Specific DNA and RNA Endonucleases ; Transcription, Genetic/drug effects
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  • 21
    Publication Date: 1984-01-06
    Description: Mammalian cardiac atria have several biologically active peptides that exert profound effects on sodium excretion, urine volume, and smooth muscle tone. In the present study two such peptides of low molecular weight were purified and separated from each other on the basis of differences in charge, hydrophobicity, and biological profile. The first peptide, designated atriopeptin I, exhibits natriuretic and diuretic activity and selectivity relaxes intestinal smooth muscle but not vascular smooth muscle strips. The second peptide, atriopeptin II, is a potent natriuretic and diuretic that relaxes both intestinal and vascular strips. Sequence analysis of atriopeptin I indicates that it is composed of 21 amino acids, of which serine and glycine residues predominate. The amino terminal sequence of atriopeptin II up to residue 21 is the same as that of atriopeptin I, with the addition of the Phe-Arg extension at the carboxyl terminus. Both peptides appear to be derived from a common high molecular weight precursor (designated atriopeptigen); their biological selectivity and potency may be determined by the site of carboxyl terminal cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Currie, M G -- Geller, D M -- Cole, B R -- Siegel, N R -- Fok, K F -- Adams, S P -- Eubanks, S R -- Galluppi, G R -- Needleman, P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6419347" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine/analysis ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Diuresis/drug effects ; Glycine/analysis ; Heart Atria/*analysis ; Muscle Contraction/drug effects ; Muscle, Smooth/drug effects ; Muscle, Smooth, Vascular/drug effects ; Natriuresis/drug effects ; Peptides/analysis/*isolation & purification/pharmacology ; Phenylalanine/analysis ; Rats ; Serine/analysis
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  • 22
    Publication Date: 1984-08-10
    Description: A clone of complementary DNA encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium falciparum has been isolated by screening an Escherichia coli complementary DNA library with a monoclonal antibody to the CS protein. The DNA sequence of the complementary DNA insert encodes a four-amino acid sequence: proline-asparagine-alanine-asparagine, tandemly repeated 23 times. The CS beta-lactamase fusion protein specifically binds monoclonal antibodies to the CS protein and inhibits the binding of these antibodies to native Plasmodium falciparum CS protein. These findings provide a basis for the development of a vaccine against Plasmodium falciparum malaria.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enea, V -- Ellis, J -- Zavala, F -- Arnot, D E -- Asavanich, A -- Masuda, A -- Quakyi, I -- Nussenzweig, R S -- New York, N.Y. -- Science. 1984 Aug 10;225(4662):628-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6204384" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; *Cloning, Molecular ; DNA/genetics ; Epitopes/*genetics ; *Genes ; Malaria/immunology ; Plasmodium falciparum/*genetics ; *Protozoan Proteins ; *Repetitive Sequences, Nucleic Acid
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  • 23
    Publication Date: 1984-05-25
    Description: A pool of synthetic oligonucleotides was prepared based on the amino terminal amino acid sequence of tetanus toxin. This probe hybridized to plasmid DNA isolated from three toxigenic strains of Clostridium tetani but not to plasmid DNA from a nontoxigenic strain. These results show that the structural gene for the toxin is on the plasmid. The pCL1 plasmid from one of the toxigenic strains spontaneously deleted 22 kilobase pairs of DNA to form pCL2. Strains harboring this deleted plasmid are nontoxigenic. However, the probe mixture hybridized to pCL2, indicating that the DNA encoding the amino terminus of the toxin had not been deleted. Restriction endonuclease cleavage maps of pCL1 and pCL2 were constructed and indicate the approximate location and orientation of the structural gene for tetanus toxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finn, C W Jr -- Silver, R P -- Habig, W H -- Hardegree, M C -- Zon, G -- Garon, C F -- New York, N.Y. -- Science. 1984 May 25;224(4651):881-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6326263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; DNA Restriction Enzymes ; *Genes ; Nucleic Acid Hybridization ; *Plasmids ; Tetanus Toxin/*genetics
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  • 24
    Publication Date: 1984-11-02
    Description: Cyclophilin, a specific cytosolic binding protein responsible for the concentration of the immunosuppressant cyclosporin A by lymphoid cells, was purified to homogeneity from bovine thymocytes. Cation-exchange high-performance liquid chromatography resolved a major and minor cyclophilin species that bind cyclosporin A with a dissociation constant of about 2 X 10(-7) moles per liter and specific activities of 77 and 67 micrograms per milligram of protein, respectively. Both cyclophilin species have an apparent molecular weight of 15,000, an isoelectric point of 9.6, and nearly identical amino acid compositions. A portion of the NH2-terminal amino acid sequence of the major species was determined. The cyclosporin A-binding activity of cyclophilin is sulfhydryl dependent, unstable at 56 degrees C and at pH 4 or 9.5, and sensitive to trypsin but not to chymotrypsin digestion. Cyclophilin specifically binds a series of cyclosporin analogs in proportion to their activity in a mixed lymphocyte reaction. Isolation of cyclophilin from the cytosol of thymocytes suggests that the immunosuppressive activity of cyclosporin A is mediated by an intracellular mechanism, not by a membrane-associated mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Handschumacher, R E -- Harding, M W -- Rice, J -- Drugge, R J -- Speicher, D W -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6238408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*isolation & purification/metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Cyclosporins/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Isoelectric Point ; Kinetics ; Lymphocyte Culture Test, Mixed ; Mice ; Molecular Weight ; Peptidylprolyl Isomerase
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  • 25
    Publication Date: 1984-02-10
    Description: Data are presented suggesting a resolution to the paradox concerning the murine response subregion I-J, which encodes a suppressor T cell marker. The controversy arose when sequences corresponding to I-J DNA were not found in the central immune response region described by immunogeneticists. New evidence is presented that T cell surface I-J expression results from the action of at least two complementing genes. One gene is within the H-2 region on chromosome 17; the second gene, termed Jt, is on chromosome 4. The two recombinant mouse strains B10.A(3R) and B10.A(5R) originally used to define the I-J subregion apparently differ not within the H-2 region but elsewhere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayes, C E -- Klyczek, K K -- Krum, D P -- Whitcomb, R M -- Hullett, D A -- Cantor, H -- CA34106/CA/NCI NIH HHS/ -- T 32 CA 09106/CA/NCI NIH HHS/ -- T 32 GM 07215/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):559-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6607530" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Antigens, Surface/*genetics ; Chromosome Mapping ; *Genes ; *Major Histocompatibility Complex ; Mice ; Mice, Inbred Strains ; Species Specificity ; T-Lymphocytes/*immunology
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-10-05
    Description: Japanese macaques were trained to discriminate two forms of their coo vocalization before and after unilateral and bilateral ablation of the temporal cortex. Unilateral ablation of the left superior temporal gyrus, including auditory cortex, resulted in an initial impairment in the discrimination, but similar unilateral ablation of the right superior temporal gyrus had no effect. Bilateral temporal lesions including auditory cortex completely abolished the ability of the animals to discriminate their coos. Neither unilateral nor bilateral ablation of cortex dorsal to and sparing the auditory cortex had any effect on the discrimination. The perception of species-specific vocalizations by Japanese macaques seems to be mediated by the temporal cortex, with the left hemisphere playing a predominant role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heffner, H E -- Heffner, R S -- HD 02528/HD/NICHD NIH HHS/ -- NS 12992/NS/NINDS NIH HHS/ -- RR 07037/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 5;226(4670):75-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474192" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Auditory Cortex/*physiology ; *Auditory Perception ; Macaca/*physiology ; Species Specificity ; Speech Perception ; Temporal Lobe/*physiology ; *Vocalization, Animal
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-08-03
    Description: Ribosomes derived from the sulfur-dependent archaebacteria are structurally distinct from those types found in ribosomes from eubacteria, eukaryotes, and other archaebacteria. All four ribosome types share a common structural core, but each type also has additional independent structural features. In the smaller subunit derived from sulfur-dependent archaebacteria ("eocytes"), lobes, similar to those found at the base of the eukaryotic small subunits, and an archaebacterial bill, similar to those found on the smaller subunit of archaebacteria and eukaryotes, are present. On the larger subunit from sulfur-dependent archaebacteria, an eocytic lobe, eocytic gap, and eocytic bulge are present. These features, with the exception of the eocytic gap, are found in a slightly modified form on eukaryotic large subunits. These novel ribosomal properties are in general consistent with other molecular biological properties peculiar to these organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, E -- Oakes, M -- Clark, M W -- Lake, J A -- Matheson, A T -- Zillig, W -- GM 24034/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):510-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6429855" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/ultrastructure ; Halobacterium/ultrastructure ; Microscopy, Electron ; Models, Structural ; Ribosomes/*ultrastructure ; Species Specificity
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  • 28
    Publication Date: 1984-06-08
    Description: Most mitochondrial proteins are encoded in the nucleus and are translated on free cytoplasmic ribosomes as larger precursors containing amino-terminal "leader" sequences, which are removed after the precursors are taken up by mitochondria. We have deduced the complete primary structure of the precursor of a human mitochondrial matrix enzyme, ornithine transcarbamylase (OTC), from the nucleotide sequence of cloned complementary DNA. The amino-terminal leader peptide of OTC is 32 amino acids in length and contains four arginines but no acidic residues. Cleavage of the leader peptide from the "mature" protein occurs between glutamine and asparagine residues. The sequence of mature human OTC resembles that of the subunits of both OTC and aspartate transcarbamylase from Escherichia coli. The biological activity of the cloned OTC complementary DNA was tested by joining it with SV40 (an animal virus) regulatory elements and transfecting cultured HeLa cells, which do not normally express OTC. Both the precursor and mature forms of the OTC subunit were identified; in stable transformants, enzymatic activity was also detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horwich, A L -- Fenton, W A -- Williams, K R -- Kalousek, F -- Kraus, J P -- Doolittle, R F -- Konigsberg, W -- Rosenberg, L E -- AM 09527/AM/NIADDK NIH HHS/ -- AM 12579/AM/NIADDK NIH HHS/ -- GM 31539/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1068-74.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; DNA, Mitochondrial/*genetics ; DNA, Recombinant/metabolism ; Escherichia coli/enzymology ; HeLa Cells/metabolism ; Humans ; Mitochondria/enzymology ; Ornithine Carbamoyltransferase/*genetics ; Protein Biosynthesis ; Rats
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  • 29
    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
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  • 30
    Publication Date: 1984-02-24
    Description: A common cellular sequence was independently transduced by avian carcinoma virus MH2 (v-mht) and murine sarcoma virus (MSV) 3611 (v-raf). Comparison of the nucleotide sequences of v-mht and v-raf revealed a region of homology that extends over 969 nucleotides. The homology between the corresponding amino acids was about 95 percent with only 19 of 323 amino acids being different. With this example, 5 of the 19 known different viral onc genes have been observed in viruses of different taxonomic groups. These data indicate that (i) the number of cellular proto-onc genes is limited because, like other viruses of different taxonomic groups, MH2 and MSV 3611 have transduced the same onc gene-specific sequences from different cell species and (ii) that specific deletion and linkage of the same proto-onc sequences to different viral vector elements affect the oncogenic potential of the resulting viruses. The difference in transformation capabilities of MH2 and MSV 3611 serves as an example.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kan, N C -- Flordellis, C S -- Mark, G E -- Duesberg, P H -- Papas, T S -- CA11426/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 24;223(4638):813-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320371" target="_blank"〉PubMed〈/a〉
    Keywords: Alpharetrovirus/*genetics ; Animals ; Base Sequence ; Chickens/genetics ; Genes, Viral ; Mice ; *Oncogenes ; Sarcoma Viruses, Murine/*genetics ; Species Specificity ; Transduction, Genetic
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-03-02
    Description: Anti-idiotype reagents that recognize a common idiotype associated with antibody to hepatitis B surface antigen (anti-HBs) were used to induce anti-HBs in mice. The anti-idiotype-induced anti-HBs was found to recognize the group-specific a determinant of hepatitis B surface antigen and to express an interspecies idiotype. These findings suggest that anti-idiotypes may be useful as vaccines or vaccine primers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kennedy, R C -- Melnick, J L -- Dreesman, G R -- New York, N.Y. -- Science. 1984 Mar 2;223(4639):930-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6198721" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cross Reactions ; Epitopes/immunology ; Hepatitis B Antibodies/*biosynthesis/immunology ; Hepatitis B Surface Antigens/classification/*immunology ; Immunization, Passive ; Immunoglobulin Idiotypes/*immunology ; Mice ; Mice, Inbred BALB C ; Species Specificity
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  • 32
    Publication Date: 1984-11-16
    Description: Evidence was presented earlier that a host-cell receptor for the highly neurotropic rabies virus might be the acetylcholine receptor. The amino acid sequence of the glycoprotein of rabies virus was compared by computer analysis with that of snake venom curaremimetic neurotoxins, potent ligands of the acetylcholine receptor. A statistically significant sequence relation was found between a segment of the rabies glycoprotein and the entire sequence of long neurotoxins. The greatest identity occurs with residues considered most important in neurotoxicity, including those interacting with the acetylcholine binding site of the acetylcholine receptor. Because of the similarity between the glycoprotein and the receptor-binding region of the neurotoxins, this region of the viral glycoprotein may function as a recognition site for the acetylcholine receptor. Direct binding of the rabies virus glycoprotein to the acetylcholine receptor could contribute to the neurotropism of this virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lentz, T L -- Wilson, P T -- Hawrot, E -- Speicher, D W -- GM 32629/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):847-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494916" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Glycoproteins/*genetics ; Neurotoxins/*genetics ; Rabies virus/*genetics ; Receptors, Cholinergic/metabolism ; Snake Venoms/*genetics ; Snakes ; Viral Proteins/*genetics
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-11-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):955.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505675" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Mitochondrial/genetics ; Female ; *Genes ; Male ; Mice/*genetics ; Ranidae/*genetics ; Species Specificity
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  • 34
    Publication Date: 1984-03-09
    Description: The complete amino acid sequence of rat transforming growth factor type 1 has been determined. This growth factor, obtained from retrovirus-transformed fibroblasts, is structurally and functionally related to mouse epidermal growth factor and human urogastrone. Production of this polypeptide by various neoplastic cells might contribute to the continued expression of the transformed phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marquardt, H -- Hunkapiller, M W -- Hood, L E -- Todaro, G J -- New York, N.Y. -- Science. 1984 Mar 9;223(4640):1079-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320373" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; *Cell Transformation, Neoplastic ; DNA/biosynthesis ; Epidermal Growth Factor/*metabolism/pharmacology ; Humans ; Idoxuridine/metabolism ; Mice ; Peptide Biosynthesis ; Peptides/*metabolism/pharmacology ; Rats ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/metabolism ; Structure-Activity Relationship ; Transforming Growth Factors
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: A replication-defective, acute transforming retrovirus (murine sarcoma virus 3611) was isolated from mouse and molecularly cloned. The nucleotide sequence of 1.5 kilobases encompassing the transforming gene (v-raf) was determined. This sequence, which predicts the amino acid sequence of a gag-raf fusion protein, terminates 180 nucleotides from the 3' end of the acquired cellular sequence. Comparison of the predicted amino acid sequence of v-raf with the predicted amino acid sequences of other oncogenes reveals significant homologies to the src family of oncogenes. There is a lack of homology within the sequence of the tyrosine acceptor domain described for the phosphotyrosine kinase members of the src family of transforming proteins. Phylogenetic arrangement of this family of oncogenes suggests that tyrosine-specific phosphorylation may be a recently acquired activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mark, G E -- Rapp, U R -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):285-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Biological Evolution ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; DNA Restriction Enzymes ; Gene Products, gag ; *Genes, Viral ; Mice ; *Oncogenes ; Protein Biosynthesis ; Protein Kinases/metabolism ; Protein-Tyrosine Kinases ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Tyrosine/metabolism ; Viral Proteins/analysis/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 May 25;224(4651):859-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6426056" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Cloning, Molecular ; Dna ; *Genes, MHC Class II ; Humans ; Mice ; Receptors, Antigen, T-Cell/*genetics
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1984 Nov 30;226(4678):1065.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494924" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; Genes ; Humans ; Receptors, Antigen, T-Cell/*genetics
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):269-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biochemistry/*methods ; Catalysis ; *Cloning, Molecular ; Enzymes/genetics/*metabolism ; Mutation ; Structure-Activity Relationship ; Substrate Specificity ; Tetrahydrofolate Dehydrogenase/metabolism ; Tyrosine-tRNA Ligase/metabolism ; beta-Lactamases/metabolism
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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  • 40
    Publication Date: 1984-11-09
    Description: Antisera to synthetic peptides representing sequences of both chains of platelet-derived growth factor (PDGF) were used to structurally analyze PDGF isolated from outdated human platelets and PDGF-like proteins in normal and transformed cells. Most PDGF isolated from platelets did not contain the carboxyl portion of PDGF-2 in contrast to p20sis, the major form of p28sis detected in simian sarcoma virus-transformed cells. In addition, higher molecular weight forms of molecules containing PDGF-1 and PDGF-2 sequences were detected in all cell lines tested. These lines were heterogeneous with respect to species, cell type, and transforming agent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niman, H L -- Houghten, R A -- Bowen-Pope, D F -- CA 25803/CA/NCI NIH HHS/ -- HL 18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 9;226(4675):701-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Humans ; Immune Sera/immunology ; Molecular Weight ; Platelet-Derived Growth Factor/*immunology/isolation & purification ; Rats
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  • 41
    Publication Date: 1984-03-16
    Description: A basic peptide isolated from pooled human seminal plasma exhibited inhibin-like activity by suppressing pituitary follicle-stimulating hormone secretion in vitro and in vivo. The peptide has been characterized and sequenced, and a 31-amino-acid synthetic replicate showed full biological activity in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramasharma, K -- Sairam, M R -- Seidah, N G -- Chretien, M -- Manjunath, P -- Schiller, P W -- Yamashiro, D -- Li, C H -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1199-202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6422553" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Follicle Stimulating Hormone/secretion ; Gonadotropin-Releasing Hormone/antagonists & inhibitors ; Humans ; Inhibins/*isolation & purification/pharmacology ; Luteinizing Hormone/secretion ; Male ; Mice ; Molecular Weight ; Peptides/chemical synthesis/isolation & purification ; Pituitary Gland/secretion ; *Prostatic Secretory Proteins ; Proteins/chemical synthesis/*isolation & purification/pharmacology ; Rats ; Semen/*analysis ; Seminal Plasma Proteins
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  • 42
    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
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-08-03
    Description: Striated skeletal muscles from the planktonic arrowworm Sagitta elegans (phylum Chaetognatha) were voltage-clamped. The muscles displayed classical voltage-dependent sodium channels that (i) showed peak transient currents when the membrane was depolarized 90 millivolts from rest, (ii) opened rapidly with peak currents flowing within 0.4 milliseconds at 4 degrees C, (iii) showed voltage-dependent inactivation with 50 percent inactivation at +25 millivolts from rest, and (iv) were blocked by 500 nanomolar tetrodotoxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, L M -- Stuhmer, W -- AM17803/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):523-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6330898" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; Annelida/physiology ; Ion Channels/drug effects/*physiology ; Moths ; Muscles/*physiology ; Rana temporaria ; Sodium/*metabolism ; Species Specificity ; Tetrodotoxin/toxicity
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: Human epidermoid carcinoma A431 cells in culture produce a soluble 105-kilodalton protein which, by the criteria of epidermal growth factor (EGF) binding, recognition by monoclonal and polyclonal antibodies to the EGF receptor, amino-terminal sequence analysis and carbohydrate content, is related to the cell surface domain of the EGF receptor. The high rate of production and the finding that with biosynthetic labeling the specific activity of this 105-kilodalton protein exceeds that of the intact receptor indicate that it is not derived from membrane-bound mature receptor but is separately produced by the cell. These cells thus separately synthesize an EGF receptor that is inserted into the membrane and an EGF receptor-related protein that is secreted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, W -- Gill, G N -- Spiess, J -- AM13149/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):294-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Carbohydrates/analysis ; Carcinoma, Squamous Cell/*metabolism ; Cell Line ; Epidermal Growth Factor/metabolism ; Glycoproteins/analysis/*biosynthesis ; Humans ; Kinetics ; Molecular Weight ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/analysis/immunology/metabolism
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  • 45
    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
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  • 46
    Publication Date: 1984-11-23
    Description: The antidepressant compounds clomipramine and nitroimipramine were cidal to extracellular promastigotes of both human protozoan parasites Leishmania donovani and Leishmania major. Clomipramine also killed amastigotes of both species within murine macrophages with no apparent toxicity to the host cells. Further, amastigotes were more sensitive than promastigotes to clomipramine. Clomipramine (100 micromoles per liter or 0.2 nanomole per 1 X 10(6) cells) inhibited L-proline transport in promastigotes. Synergistic inhibition of L-proline transport was observed with clomipramine after addition of either of the ionophores valinomycin or nigericin. These observations suggest that the cytotoxic effects of clomipramine result from its disruption of the proton electrochemical gradient of the parasite surface membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zilberstein, D -- Dwyer, D M -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):977-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505677" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/drug effects/physiology/ultrastructure ; Clomipramine/*toxicity ; Humans ; Imipramine/analogs & derivatives/*toxicity ; Leishmania/cytology/*drug effects/physiology ; Mice ; Mice, Inbred BALB C ; Proline/metabolism ; Species Specificity
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  • 47
    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
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  • 48
    Publication Date: 1984-11-16
    Description: The Streptococcus faecalis sex pheromone cPD1, which induces a mating response in cells harboring the conjugative plasmid pPD1, has been isolated and its structure determined. It was found to have a molecular weight of 912, and its amino acid sequence was H-Phe-Leu-Val-Met-Phe-Leu-Ser-Gly-OH. A synthetic octapeptide showed the same biological activity and chromatographic behavior as the isolated cPD1. Pheromone activity was detectable at a concentration of approximately 4 X 10(-11)M.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suzuki, A -- Mori, M -- Sakagami, Y -- Isogai, A -- Fujino, M -- Kitada, C -- Craig, R A -- Clewell, D B -- AI10318/AI/NIAID NIH HHS/ -- DE02731/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):849-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6436978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Enterococcus faecalis/*physiology ; Oligopeptides/*isolation & purification ; Pheromones/*isolation & purification ; Plasmids ; Sex Attractants/*isolation & purification
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-10-19
    Description: Techniques for on-line coupling of high-performance liquid chromatography with mass spectrometry are reviewed with particular emphasis on those suitable for application to nonvolatile samples. The present status of various techniques is summarized and the strengths and weaknesses of the various approaches are assessed. The potential for future application of recently developed techniques for combined liquid chromatography and mass spectrometry is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vestal, M L -- GM24031/GM/NIGMS NIH HHS/ -- GM28291/GM/NIGMS NIH HHS/ -- GM29451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 19;226(4672):275-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6385251" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Chromatography, High Pressure Liquid/instrumentation/methods ; Computers ; Ions ; Lasers ; *Mass Spectrometry/instrumentation/methods ; Peptides
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  • 50
    Publication Date: 1984-02-17
    Description: Ribose is cardioprotective in the rat in a variety of pathophysiological conditions. The metabolic basis for this effect is the low capacity of the oxidative pentose phosphate pathway in the myocardium. Ribose bypasses this pathway, elevates the available pool of 5-phosphoribosyl-l-pyrophosphate, and thus stimulates the biosynthesis of adenine nucleotides. In this study reported here the activity of glucose-6-phosphate dehydrogenase, the first and rate-limiting enzyme of the oxidative pentose phosphate shunt, was very low in the human heart and was of the same order of magnitude in the myocardium of various animal species. Furthermore, ribose had a similar stimulating effect on myocardial adenine nucleotide biosynthesis in the guinea pig, in which hemodynamic parameters are different from those in the rat. It is concluded that the metabolic basis for the effectiveness of ribose is similar in all species investigated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmer, H G -- Ibel, H -- Suchner, U -- Schad, H -- New York, N.Y. -- Science. 1984 Feb 17;223(4637):712-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420889" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/metabolism ; Animals ; Cattle ; Dogs ; Glucosephosphate Dehydrogenase/metabolism ; Guinea Pigs ; Haplorhini ; Heart/drug effects/*physiology ; Heart Rate ; Humans ; Myocardium/*metabolism ; Oxidation-Reduction ; Pentosephosphates/*metabolism ; Phosphogluconate Dehydrogenase/metabolism ; Rabbits ; Rats ; Ribose/*pharmacology ; Species Specificity
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  • 51
    Publication Date: 1984-12-14
    Description: Few and limited amino acid sequence homologies have been found among eight bacterial aminoacyl transfer RNA (tRNA) synthetases whose primary structures are known. The entire 939-amino acid primary structure of Escherichia coli isoleucyl-tRNA synthetase is now reported. In a sequence of 11 consecutive amino acids matching a sequence in E. coli methionyl-tRNA synthetase, there are ten identical residues and one conservative change. This is the strongest homology recorded between any two aminoacyl tRNA synthetases. This part of the methionine enzyme's three-dimensional structure has been determined, and it occurs in a mononucleotide binding fold; a close three-dimensional structural homology of this part of the enzyme with Bacillus stearothermophilus tyrosyl-tRNA synthetase has also been reported. The three synthetases probably fold identically in this region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Webster, T -- Tsai, H -- Kula, M -- Mackie, G A -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 14;226(4680):1315-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6390679" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acyl-tRNA Synthetases ; Escherichia coli/enzymology ; Geobacillus stearothermophilus/enzymology ; Isoleucine-tRNA Ligase ; Methionine-tRNA Ligase ; Protein Conformation
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-02-10
    Description: The resistance of the infectious agent of scrapie disease to sterilization at 100 degrees or 121 degrees C is reputed to be inconsistent with the structure of conventional viruses. However, in kinetic studies the majority of hamster scrapie strain 263K infectivity was (like that of previously characterized viruses) rapidly inactivated at temperatures of 100 degrees C or greater. Small resistant subpopulations remained. Similar heat-resistant subpopulations were observed at 60 degrees C for phage lambda but only in the presence of brain homogenate. Brain homogenate may also confer stability to small subfractions of scrapie infectivity. Such refractory subpopulations cannot be used to make structural inferences that are properly obtained from the behavior of the majority population as revealed in the initial inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohwer, R G -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):600-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420887" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/microbiology ; Cricetinae ; *Hot Temperature ; Kinetics ; Prions/*growth & development ; Species Specificity ; Sterilization/methods
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