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  • Base Sequence  (204)
  • Species Specificity  (116)
  • Amino Acid Sequence  (112)
  • American Association for the Advancement of Science (AAAS)  (376)
  • Blackwell Publishing Ltd
  • 1980-1984  (306)
  • 1975-1979  (70)
  • 1925-1929
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (376)
  • Blackwell Publishing Ltd
Years
Year
  • 1
    Publication Date: 1978-06-16
    Description: Throbin-activated human platelets cause agglutination of trypsinized, formalinized bovine erythrocytes. This lectin activity of stimulated platelets was blocked by galactosamine, glucosamine, mannosamine, lysine, and arginine, but not by N-acetylated sugars, other neutral sugars, or other amino acids. Inhibitors of the thrombin-induced lectin activity also blocked thrombin-induced platelet aggregation. It appears that a membrane surface component that has lectin activity mediates platelet aggregation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gartner, T K -- Williams, D C -- Minion, F C -- Phillips, D R -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1281-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663608" target="_blank"〉PubMed〈/a〉
    Keywords: *Agglutinins ; Amino Acids/pharmacology ; Amino Sugars/pharmacology ; Animals ; Binding Sites ; Cytochalasin B/pharmacology ; *Hemagglutinins ; Humans ; Membrane Proteins/blood ; Platelet Aggregation/*drug effects ; Prostaglandins E/pharmacology ; Species Specificity ; Thrombin/*pharmacology
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-04-07
    Description: Comparative analyses of behavior have an underappreciated potential for revealing the role of ethoecological factors in the origins of higher taxa. Twenty-seven species (13 genera) in the advanced family Colubridae exhibited 19 patterns of coil application; one or two patterns were usually consistent within a genus. Forty-eight species (26 genera) in the primitive families Acrochordidae, Aniliidae, Boidae, and Xenopeltidae usually used a single pattern, despite differences in age, size, shape, habitat, and diet. This implies the shared retention of an action pattern used by their common ancestor no later than the early Paleocene. Constriction must have been used as a prey-killing tactic very early in the history of snakes and might have been a behavioral "key innovation" in the evolution of their unusual jaw mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greene, H W -- Burghardt, G M -- New York, N.Y. -- Science. 1978 Apr 7;200(4337):74-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/635575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/*physiology ; *Biological Evolution ; Predatory Behavior/physiology ; Snakes/*physiology ; Species Specificity
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guillemin, R -- New York, N.Y. -- Science. 1978 Oct 27;202(4366):390-402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/212832" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Endorphins/*history/isolation & purification/pharmacology ; Gonadotropin-Releasing Hormone/isolation & purification ; Growth Hormone-Releasing Hormone/isolation & purification ; History, 20th Century ; Hypothalamic Hormones/*history/pharmacology ; Hypothalamo-Hypophyseal System/*physiology ; *Neurosecretion ; Sheep ; Species Specificity ; Structure-Activity Relationship ; Synaptic Transmission ; Thyrotropin-Releasing Hormone/isolation & purification/physiology
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-03-03
    Description: The gymnotoid electric fish Hypopomus artedi discriminates between electric stimulus pulses with identical spectral amplitudes but different spectral phase functions. Behavioral results can be explained on the assumption that electroreception is based on a linear filter, approximately matched to the species' electric organ discharge. The impulse response of the appropriate matched filter, in fact, resembles the known impulse response of the electroreceptors involved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heiligenberg, W -- Altes, R A -- New York, N.Y. -- Science. 1978 Mar 3;199(4332):1001-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/622577" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/*physiology ; Discrimination (Psychology)/physiology ; Electric Conductivity ; Electric Organ/*physiology ; Electric Stimulation ; Electrophysiology ; Fishes/*physiology ; Sensory Receptor Cells/*physiology ; Species Specificity
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  • 5
    Publication Date: 1978-09-29
    Description: The Z variant of alpha1-antitrypsin was isolated by a new technique from the liver of a patient homozygous for the Z allele of the protease inhibitor locus. The material was homogenous and antigenically competent but had no protease inhibiting capacity. An interesting correlation was found between the subcellular localization and the carbohydrate composition of the Z variant from liver. Carbohydate analysis of this glycoprotein showed an absence of galactose and sialic acid, an appreciable decrease in N-acetylglucosamine, and an almost twofold increase in mannose residues. These data indicate a considerable slowdown in the processing of the oligosaccharides of liver Z variant. In spite of the absence of sialyl residues, the liver Z varant was microheterogeneous by analytical isoelectric focusing. The isoproteins of liver Z variant coincided with those of asialo M variant in the focusing field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hercz, A -- Katona, E -- Cutz, E -- Wilson, J R -- Barton, M -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1229-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/308696" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Metabolism ; Female ; Galactose/metabolism ; Glycoproteins/genetics ; Homozygote ; Humans ; Liver/metabolism ; Mannose/metabolism ; Middle Aged ; Mutation ; Phenotype ; Sialic Acids/metabolism ; alpha 1-Antitrypsin/*genetics/metabolism
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-10-20
    Description: Retinal growth in young Sebastes diploproa involves the succession of three distinct cone patterns. Development of the final pattern with the loss of single cones occurs in close temporal association with a permanent migration from the surface to deep water. The results suggest that loss of single cones depends upon the change in environment and that the loss occurs through fusion to double elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehlert, G W -- New York, N.Y. -- Science. 1978 Oct 20;202(4365):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694534" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Environment ; Fishes/*physiology ; Light ; Photoreceptor Cells/*physiology ; Retina/ultrastructure ; Species Specificity ; Trout/physiology
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-09-29
    Description: Honey bees were trained in two consecutive two-dimensional (color-position) problems with one dimension (color or position) relevant and the other irrelevant in each problem. As in analogous experiments on dimensional transfer in rats and monkeys, performance in the second problem was more accurate when the relevant and irrelevant dimensions were the same as in the first problem than when they were interchanged. The results of further experiments suggest that the transfer is mediated by different modes of responding that develop in color and position problems rather than by some special process of dimensional selection, such as has been assumed to operate in vertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klosterhalfen, S -- Fischer, W -- Bitterman, M E -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1241-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694513" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Attention/*physiology ; Bees/*physiology ; Behavior, Animal/physiology ; Color Perception ; Discrimination Learning/*physiology ; Rats ; Species Specificity
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  • 8
    Publication Date: 1978-10-20
    Description: Five Japanese macaques and five other Old World monkeys were trained to discriminate among field-recorded Japanese macaque vocalizations. One task required discrimination of a communicatively relevant acoustic feature ("peak"), and a second required discrimination of an orthogonal feature of the same vocalizations ("pitch"). The Japanese animals more proficiently discriminated the peak feature when stimuli were presented to the right ear (primarily left cerebral hemisphere), as opposed to the left ear (primarily right hemisphere). In discriminating the pitch feature, the Japanese animals either showed (i) a left-ear processing advantage or (ii) no ear advantage. The comparison animals, with one exception, showed no ear advantage in processing either feature of the vocalizations. The results suggest that Japanese macaques engage left-hemisphere processors for the analysis of communicatively significant sounds that are analogous to the lateralized mechanisms used by humans listening to speech.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petersen, M R -- Beecher, M D -- Zoloth, S R -- Moody, D B -- Stebbins, W C -- New York, N.Y. -- Science. 1978 Oct 20;202(4365):324-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/99817" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Auditory Perception/*physiology ; Discrimination Learning/physiology ; Female ; *Functional Laterality ; Haplorhini ; Macaca/*physiology ; Male ; Species Specificity ; Vocalization, Animal/*physiology
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  • 9
    Publication Date: 1978-05-05
    Description: The nucleotide sequence of SV40 DNA was determined, and the sequence was correlated with known genes of the virus and with the structure of viral messenger RNA's. There is a limited overlap of the coding regions for structural proteins and a complex pattern of leader sequences at the 5' end of late messenger RNA. The sequence of the early region is consistent with recent proposals that the large early polypeptide of SV40 is encoded in noncontinguous segments of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, V B -- Thimmappaya, B -- Dhar, R -- Subramanian, K N -- Zain, B S -- Pan, J -- Ghosh, P K -- Celma, M L -- Weissman, S M -- New York, N.Y. -- Science. 1978 May 5;200(4341):494-502.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/205947" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Mapping ; Codon ; DNA Replication ; DNA, Circular ; DNA, Viral ; Genes ; *Genes, Viral ; Simian virus 40/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwartz, R M -- Dayhoff, M O -- New York, N.Y. -- Science. 1978 Jan 27;199(4327):395-403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/202030" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Biological Evolution ; *Cells ; *Chloroplasts ; Computers ; Cytochrome c Group ; *Eukaryotic Cells ; Ferredoxins ; *Mitochondria ; Nucleic Acids ; *Prokaryotic Cells ; Proteins ; RNA, Ribosomal
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1978-10-06
    Description: Three important aspects of immunoglobulin gene organization and structure have emerged from studies of cloned immunoglobulin kappa chain genes. (i) Multiple variable genes are encoded separately in the genome of both immunoglobulin-producing and uncommitted (embryonic) cells, thereby establishing the evolutionary base for generating immunoglobulin diversity. (ii) These genes exist as many small, closely related families (subgroups) that share close sequence homology largely within their own subgroup. (iii) Comparison of two cloned variable gene segments derived from a single subgroup reveals a feature of their structure that distinguishes them from fixed genes (that is, globin genes) and provides, through extensive surrounding sequence homology, a large target for intergenic recombination. This last observation suggests that a simple recombination mechanism may account for their genetic instability in both germ line and somatic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seidman, J G -- Leder, A -- Nau, M -- Norman, B -- Leder, P -- New York, N.Y. -- Science. 1978 Oct 6;202(4363):11-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/99815" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibody Specificity ; Base Sequence ; Binding Sites, Antibody/*genetics ; Biological Evolution ; Cell Line ; Embryo, Mammalian/immunology ; *Genes ; Immunoglobulin Constant Regions/*genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulin kappa-Chains/*genetics ; Immunoglobulins/*genetics ; Mice ; Neoplasms, Experimental/immunology ; Plasmacytoma/immunology ; Recombination, Genetic
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-04-06
    Description: Vascular casts of the pituitary gland have demonstrated a paucity of veins extending from the adenohypophysis to the systemic circulation and have suggested that some adenohypophyseal venous blood returns to the neurohypophysis. The neurohypophyseal capillary bed may function as a vascular switch and in this article a series of 14 questions are proposed regarding the vascular dynamics of the pituitary. Together these questions raise the larger question, namely, whether pituitary hormones are transported directly to the brain to modify brain function?〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bergland, R M -- Page, R B -- New York, N.Y. -- Science. 1979 Apr 6;204(4388):18-24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/373118" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arteriovenous Anastomosis/anatomy & histology ; Capillaries/anatomy & histology ; Cats ; *Cerebrovascular Circulation ; Dogs ; Humans ; Hypothalamo-Hypophyseal System/blood supply ; Pituitary Gland/*blood supply ; Pituitary Gland, Anterior/blood supply ; Rats ; Species Specificity
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-09-07
    Description: In the past two decades, biochemistry and molecular biology have demonstrated the existence of potentially exploitable biochemical differences between etiologic agents of disease and their hosts. Known differences between organism and host with respect to metabolism and polymer structure point to the detailed characterization of key proteins as the focus for the development of potential inhibitors. In the last decade, the methodology of the isolation, characterization, and inactivation of proteins and enzymes has been advanced. The present scientific and technological base suggests that new efforts toward the development of selective chemotherapeutic agents for infections caused by bacteria, viruses, protozoa, and higher eukaryotes should exploit the known differences in proteins or other specific biopolymers serving crucial structural or metabolic roles in the economy of the parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, S S -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):964-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/382357" target="_blank"〉PubMed〈/a〉
    Keywords: *Anti-Bacterial Agents ; *Antiviral Agents ; Communicable Diseases/*drug therapy ; Humans ; Mycobacterium leprae/metabolism ; Polysaccharides, Bacterial/metabolism ; Species Specificity ; Structure-Activity Relationship ; Trypanosomiasis/drug therapy ; Vidarabine/pharmacology ; Viral Proteins/biosynthesis ; Virus Replication/drug effects
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-06-08
    Description: Large contrasts are observed between the messenger RNA populations of different tissues and of embryos at different stages of development. Nevertheless, coding sequences for genes not expressed in a cell appear to be present in its nuclear RNA. Though many nuclear RNA transcripts of single copy DNA sequences are held in common between tissues, an additional set, probably consisting of non-message sequences, is not shared. Nuclear RNA also contains transcripts of repetitive DNA sequences. Certain repeat families are represented at high levels in the nuclear RNA of particular tissues and much lower levels in others. It is surprising that both complements of most repeat sequences are present in nuclear RNA. These observations lead to model for regulation of gene expression in which the formation of repetitive RNA-RNA duplexes controls the production of messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davidson, E H -- Britten, R J -- New York, N.Y. -- Science. 1979 Jun 8;204(4397):1052-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451548" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/physiology ; DNA/*genetics ; Genes ; *Genes, Regulator ; Hydrogen Bonding ; Mammals/embryology ; Models, Biological ; Polyribosomes/metabolism ; *RNA, Heterogeneous Nuclear/genetics ; RNA, Messenger/genetics ; Sea Urchins/embryology ; *Transcription, Genetic
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-08-31
    Description: Viroids are nucleic acid species of relatively low molecular weight and unique structure that cause several important diseases of cultivated plants. Similar nucleic acid species may be responsible for certain diseases of animals and humans. Viroids are the smallest known agents of infectious disease. Unlike viral nucleic acids, viroids are not encapsidated. Despite their small size, viroids replicate autonomously in cells of susceptible plant species. Known viroids are single-stranded, covalently closed circular, as well as linear, RNA molecules with extensive regions of intramolecular complementarity; they exist in their native state as highly base-paired rods.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diener, T O -- New York, N.Y. -- Science. 1979 Aug 31;205(4409):859-66.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472709" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Viral/genetics ; Molecular Weight ; Nucleic Acid Conformation ; Plant Viruses/*genetics/isolation & purification/ultrastructure ; RNA, Viral/*genetics ; Templates, Genetic ; Virus Replication
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  • 16
    Publication Date: 1979-03-30
    Description: The amino terminal acid sequences of several mouse leukemia virus phosphoproteins (p12) show definite homology with the amino terminal conserved region of H5 histones, the phosphorylated nuclear proteins of nucleated erythrocytes. Differences in the amino acid compositions of the two groups of proteins seem to rule out the possibility that they evolved from a single common ancestral gene. The finding of sequence homology between viral p12's and cellular histones, however, is consistent with evolution of retrovirus structural proteins by a process of differentiation from preexisting cellular genes. The conserved primary and secondary structure at the amino terminal region, common to both groups of proteins, may be related to their common function of nucleic acid binding modulated by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, L E -- Gilden, R V -- Oroszlan, S -- New York, N.Y. -- Science. 1979 Mar 30;203(4387):1346-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/218289" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins ; Cell Nucleus/analysis ; Chickens/blood ; Erythrocytes/analysis ; Geese/blood ; *Histones ; Leukemia Virus, Murine/*analysis ; Nucleic Acids/metabolism ; *Phosphoproteins ; Structure-Activity Relationship ; *Viral Proteins
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-09-07
    Description: Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of beta-endorphin and its D-alanine derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, beta-lipotropin, adrenocorticotrophic hormone, or alpha-melanocyte-stimulating hormone; this suggests the existence of a specific, non-opiate binding site (receptor) for beta-endorphin. The carboxy-terminal region of beta-endorphin is essential for this binding activity, since alpha-endorphin is not active. beta-Endorphin may be a circulating hormone with peripheral physiological effects that are not primarily mediated through interactions with opiate or enkephalin receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hazum, E -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):1033-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224457" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cells, Cultured ; Endorphins/blood/*metabolism ; Humans ; Lymphocyte Activation ; Lymphocytes/*metabolism ; Receptors, Drug/*metabolism ; Receptors, Opioid/metabolism ; Stress, Physiological/metabolism ; Structure-Activity Relationship
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-02-16
    Description: The method developed for the total synthesis of a given DNA containing biologically specific sequences consists of the following. The DNA in the double-stranded form is carefully divided into short single-stranded segments with suitable overlaps in the complementary strands. All the segments are chemically synthesized starting with protected nucleosides and mononucleotides. The 5'-OH ends of the appropriate oligonucleotides are then phosphorylated with the use of [y-32P]ATP and polynucleotide kinase. A few to several neighboring oligonucleotides are then allowed to form bihelical complexes in aqueous solution, and the latter are joined end to end by polynucleotide ligase to form covalently linked duplexes. Subsequent heat-to-tail joining of the short duplexes leads to the total DNA. The methods are described for the construction of a biologically functional suppressor transfer RNA gene. The total work involved (i) the synthesis of a 126-nucleotide-long bihelical DNA corresponding to a known precursor to the tyrosine suppressor transfer RNA, (ii) the sequencing of the promoter region and the distal region adjoining the C-C-A end, which contained a signal for the processing of the RNA transcript, (iii) total synthesis of the 207 base-pair-long DNA, which included the control elements, as well as the Eco R1 restriction endonuclease specific sequences at the two ends, and (iv) full characterization by transcription in vitro and amber suppressor activity in vivo of the synthetic gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khorana, H G -- New York, N.Y. -- Science. 1979 Feb 16;203(4381):614-25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/366749" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Recombinant ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/genetics ; *Genes ; Genes, Regulator ; Hydrogen Bonding ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemical synthesis ; Oligonucleotides/*chemical synthesis ; RNA, Transfer/*genetics ; Suppression, Genetic ; Transcription, Genetic ; Tyrosine
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-10-05
    Description: Radioimmunoassay and chromatography analyses of hypothalamic luteinizing hormone-releasing hormone (LHRH) have demonstrated the presence of LHRH-like immunoreactive peptides in a wide range of vertebrates. Contrary to previous reports, the molecule differs in various vertebrates. Avian, reptilian, and teleostean LHRH's are chemically distinct from the mammalian peptide but are in themselves indistinguishable. However, amphibian LHRH appears to be identical to the mammalian peptide. These findings have interesting evolutionary implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, J A -- Millar, R P -- New York, N.Y. -- Science. 1979 Oct 5;206(4414):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/384514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chromatography ; Gonadotropin-Releasing Hormone/*analysis/immunology ; Hypothalamus/analysis ; Radioimmunoassay ; Species Specificity ; Structure-Activity Relationship
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-04-06
    Description: Occluding junctions have been found between the lateral cell borders at the base of the rectum of Periplaneta americana. They appear as punctate membrane appositions in thin sections, and after incubation in physiological solutions containing lanthanum before fixation the inward penetration of tracer is impeded in this same basal area. Moreover, freeze-fracture studies of this region reveal simple linear ridges on fracture face P and grooves on fracture face E, which are similar to the less complex vertebrate tight junctions. The luminal clefts, which permit free inward diffusion of tracers, present no tight junctions, but do have septate junctions. These results support the contention that, contrary to earlier speculation, arthropods do possess tight junctions; these, rather than septate junctions, appear to form the morphological basis of at least some of the permeability barriers observed in invertebrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lane, N J -- New York, N.Y. -- Science. 1979 Apr 6;204(4388):91-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cockroaches/*ultrastructure ; Epithelium/physiology/ultrastructure ; Freeze Fracturing ; Intercellular Junctions/*ultrastructure ; Periplaneta/*ultrastructure ; Rectum/physiology/ultrastructure ; Species Specificity ; Water-Electrolyte Balance
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  • 21
    Publication Date: 1979-06-08
    Description: The organism Methanobacterium thermoautotrophicum, an archaebacterium, is envolutionarily very distant from both traditional prokaryotes and eukaryotes. Its genome (DNA) has physical characteristics typical of most prokaryotes except that it is quite small (about 10(9) daltons, less than half the size of the genome of Escherichia coli) and contains a significant amount (6 percent) DNA which renatures extremely rapidly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitchell, R M -- Loeblich, L A -- Klotz, L C -- Loeblich, A R 3rd -- New York, N.Y. -- Science. 1979 Jun 8;204(4397):1082-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/377486" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Biological Evolution ; DNA, Bacterial/*genetics ; Escherichia coli/genetics ; Euryarchaeota/classification/*genetics ; Nucleic Acid Renaturation
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-04-13
    Description: Removal of fibrinopeptide B from human fibrinogen by reaction with the procoagulant enzyme from copperhead snake venom below 25 degrees C resulted in tight aggregation of the fibrinogen, which, in turn, progressively blocked a concomitant but sluggish release of fibrinopeptide A by the enzyme. When the clots obtained at less than 25 degrees C were warmed, they dissociated into soluble aggregates and monomers. Release of fibrinopeptide A then resumed, and a secondary coagulation followed. The aggregation induced by release of fibrinopeptide B itself involves a plasmin-susceptible segment located just distal to B in the B beta chain of fibrinogen, a segment previously shown to be of little importance in the aggregation induced by release of fibrinopeptide A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shainoff, J R -- Dardik, B N -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):200-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/155308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crotalid Venoms/*metabolism ; Fibrinogen/*metabolism ; Fibrinolysin/metabolism ; Fibrinopeptide A/metabolism ; Fibrinopeptide B/*metabolism ; Humans ; Molecular Weight ; Protein Binding ; Temperature
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1979-08-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, H O -- New York, N.Y. -- Science. 1979 Aug 3;205(4405):455-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/377492" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Sequence ; DNA Restriction Enzymes/*metabolism ; DNA, Bacterial ; Escherichia coli/enzymology ; Haemophilus influenzae/enzymology ; Species Specificity ; Substrate Specificity
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  • 24
    Publication Date: 1979-12-14
    Description: The complete coding sequence for the constant region of the mouse gamma 2b immunoglobulin heavy chain and the 3' untranslated region has been determined. The coding portion of the sequence is 1008 nucleotides long (amino acid residues 114 to 449), and the 3' noncoding region contains 102 nucleotides preceeding the polyadenylate. An extra carboxyl-terminal lysine residue which had not been observed in the gamma 2b or other gamma subclass protein sequences occurs in the nucleotide sequence and is probably processed posttranslationally. A 17-nucleotide sequence occurs with slight variation twice in CH1 and once in CH2 domains in the same relative location but with different translational phase. This sequence may be the site of crossover in a gamma 2b . gamma 2a heavy chain variant, an indication of possible recombinational activity of some kind.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tucker, P W -- Marcu, K B -- Slightom, J L -- Blattner, F R -- New York, N.Y. -- Science. 1979 Dec 14;206(4424):1299-303.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/117548" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; Codon ; DNA, Recombinant ; Immunoglobulin Constant Regions/*genetics ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin gamma-Chains/*genetics ; Immunoglobulins/*genetics ; Mice ; *Protein Biosynthesis ; RNA, Messenger/*genetics
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  • 25
    Publication Date: 1979-05-25
    Description: Monkeys of four species were trained to discriminate between sets of natural tonal calls of Japanese macaques (Macaca fuscata) by the position of a frequency-inflection peak or by initial pitch. The Japanese macaques consistently performed best on peak position and the other species on pitch. The results imply special strategies for perceptional processing of vocal sounds and suggest parallels with human speech perception.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zoloth, S R -- Petersen, M R -- Beecher, M D -- Green, S -- Marler, P -- Moody, D B -- Stebbins, W -- New York, N.Y. -- Science. 1979 May 25;204(4395):870-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/108805" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Auditory Perception/*physiology ; Haplorhini ; Macaca/*physiology ; Species Specificity ; Speech Perception/*physiology ; Vocalization, Animal/*physiology
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-09-12
    Description: In the report by T. Kakunaga and J. D. Crow (25 July, p. 505), Fig. 1 on page 506 should have been printed as follows: [See figure in the PDF file]〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dayhoff, M O -- Schwartz, R M -- Chen, H R -- Hunt, L T -- Barker, W C -- Orcutt, B C -- New York, N.Y. -- Science. 1980 Sep 12;209(4462):1182.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7403878" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Information Systems ; *Nucleic Acids
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  • 27
    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-03-21
    Description: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-02-08
    Description: The distribution of active polyadenylate-messenger RNA sequences in fractionated chicken liver chromatin was examined. A portion of these active gene sequences is concentrated in a DNA fraction retained by tightly bound nonhistone chromosomal proteins, while the nonretained DNA fraction is substantially depleted of a portion of these sequences. These findings suggest that the tightly bound nonhistones are physically associated with a subset of active gene sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gates, D M -- Bekhor, I -- New York, N.Y. -- Science. 1980 Feb 8;207(4431):661-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7352280" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chickens ; Chromatin/ultrastructure ; Chromosomal Proteins, Non-Histone/*metabolism ; DNA/*metabolism ; *Genes ; Liver/*metabolism ; Nucleic Acid Hybridization ; Protein Binding ; RNA, Messenger/genetics ; Sodium Chloride
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  • 30
    Publication Date: 1980-05-02
    Description: Amphibians of the family Bufonidae contain high levels of skin compounds that both inhibit Na+- and K+-dependent adenosinetriphosphatase and antagonize the binding of ouabain to the enzyme. In species of Bufo and Atelopus, these compounds are relatively nonpolar bufodienolides, whereas Dendrophryniscus and Melanophryniscus contain more polar compounds of unknown structure. Skin extracts from 30 of 48 species of frogs representing an additional eight families contained relatively low levels of compounds that inhibit binding of ouabain to Na+,K+-adenosinetriphosphatase. The widespread occurrence of low levels of inhibitory compounds is consonant with the role for these compounds as physiological regulators of Na+,K+-adenosinetriphosphatase in amphibian skin; high levels in the Bufonidae probably also serve as a defense against some predators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flier, J -- Edwards, M W -- Daly, J W -- Myers, C W -- New York, N.Y. -- Science. 1980 May 2;208(4443):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6245447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/*metabolism ; Binding Sites ; Bufanolides/pharmacology ; Ouabain/antagonists & inhibitors/*metabolism ; Skin/analysis/enzymology/*metabolism ; Sodium-Potassium-Exchanging ATPase/*metabolism ; Species Specificity ; Tissue Extracts/pharmacology
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  • 31
    Publication Date: 1980-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, G E -- Stackebrandt, E -- Hespell, R B -- Gibson, J -- Maniloff, J -- Dyer, T A -- Wolfe, R S -- Balch, W E -- Tanner, R S -- Magrum, L J -- Zablen, L B -- Blakemore, R -- Gupta, R -- Bonen, L -- Lewis, B J -- Stahl, D A -- Luehrsen, K R -- Chen, K N -- Woese, C R -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):457-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6771870" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*classification ; Base Sequence ; Biological Evolution ; Chloroplasts/analysis ; Clostridium/classification ; Cyanobacteria/classification ; DNA/analysis ; *Phylogeny ; RNA, Ribosomal/*analysis ; Species Specificity
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  • 32
    Publication Date: 1980-05-02
    Description: Analysis of extracts of the bloodstream forms of Trypanosoma brucei showed that both DNA polymerase-alpha and DNA polymerase-beta activities were present. The detection of DNA polymerase-beta in T. brucei demonstrates the presence of this enzyme in unicellular organisms. DNA polymerase-beta is present also in Leishmania mexicana. The DNA polymerases in T. brucei are immunologically distinct from the host enzymes. The structural differences between the parasite and the host enzymes could be exploited for the development of agents to combat parasitic diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, L M -- Cheriathundam, E -- Mahoney, E M -- Cerami, A -- New York, N.Y. -- Science. 1980 May 2;208(4443):510-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367875" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centrifugation, Density Gradient ; Chickens ; DNA Polymerase I/analysis ; DNA Polymerase II/analysis ; DNA Polymerase III/analysis ; DNA-Directed DNA Polymerase/*analysis ; Fishes ; Immune Sera ; Leishmania/*enzymology ; Molecular Weight ; Rabbits ; Rats ; Species Specificity ; Trypanosoma brucei brucei/*enzymology
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  • 33
    Publication Date: 1980-03-21
    Description: The indirect method of immunofluorescence was used to demonstrate the presence of amelogenins in the enameloid of teeth and dermal denticles of Chondrichthyes; in the enameloid of Teleostei and Amphibia; and in the enamel of Reptilia. Nonmammalian amelogenins are formed in the ectodermal cells of tooth organs and chemically are so similar to mammalian amelogenins that they interact with antiserum prepared from bovine enamel matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herold, R C -- Graver, H T -- Christner, P -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1357-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6986656" target="_blank"〉PubMed〈/a〉
    Keywords: Amelogenesis ; Animals ; Dental Enamel Proteins/immunology/*metabolism ; Fluorescent Antibody Technique ; Species Specificity ; Tooth/*anatomy & histology ; Vertebrates/*anatomy & histology
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  • 34
    Publication Date: 1980-12-19
    Description: Anglerfish (Lophius americanus) insulin complementary DNA was cloned in bacterial plasmids, and its sequence was determined. Fish insulin messenger RNA is larger (1.5 times) than the messenger RNA encoding mammalian (rat and human) insulin, in part because of a larger C peptide (an additional six amino acids or 18 nucleotides in length) but mainly because of increases in the 5' and 3' untranslated regions. Comparison of the fish, rat, and human insulin messenger RNA (from the complementary DNA) reveals that, in addition to the regions coding for the A and B peptides, sequence conservation is limited to a segment within the 5' untranslated region which may be involved in ribosomal binding, two small segments of the signal peptide, and two stretches of sequence in the 3' untranslated region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobart, P M -- Shen, L P -- Crawford, R -- Pictet, R L -- Rutter, W J -- AM 21344/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1980 Dec 19;210(4476):1360-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001633" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Cloning, Molecular ; Codon ; Fishes/*genetics ; Insulin/*genetics ; Nucleic Acid Conformation ; Proinsulin/genetics ; Protein Biosynthesis ; Protein Precursors/genetics ; RNA, Messenger/*genetics
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  • 35
    Publication Date: 1980-04-11
    Description: A high-molecular-weight protein with beta-endorphin- and adrenocorticotropin-immunoreactivities was isolated from extracts of human placenta after several purification steps, including immunoadsorption with a well-characterized antiserum raised to beta-endorphin. This protein was identified as the heavy chain of the human immunoglobulin class IgG1. These results have led to the recognition of homologies in the amino acid sequences of these physiologically unrelated molecules. They also suggest caution in accepting immunological competence as the sole criterion of the chemical identity of a ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julliard, J H -- Shibasaki, T -- Ling, N -- Guillemin, R -- New York, N.Y. -- Science. 1980 Apr 11;208(4440):183-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6244620" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electrophoresis, Polyacrylamide Gel ; Endorphins/*analysis ; Female ; Humans ; Immunoglobulin G/*analysis ; Placental Extracts/*analysis ; Pregnancy ; Radioimmunoassay ; beta-Endorphin
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  • 36
    Publication Date: 1980-06-27
    Description: Gas deposition rates in the swim bladders of postmetamorphic (silver) Anguilla rostrata eels are about five times greater than those of premetamorphic (yellow) individuals. This extends the maximum depth at which silver eels can maintain swim bladder volume and prepares them for their spawning migration to the Sargasso Sea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleckner, R C -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1481-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384792" target="_blank"〉PubMed〈/a〉
    Keywords: Acclimatization ; Air Sacs/*physiology ; Anguilla/*physiology ; Animals ; Species Specificity
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-11-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):887-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001629" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chemistry/history ; DNA/genetics ; DNA, Recombinant ; History, 20th Century ; Molecular Biology/*history ; *Nobel Prize
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  • 38
    Publication Date: 1980-07-11
    Description: During viral development bacteriophage T4 modifies the valyl-transfer RNA synthetase of its host Escherichia coli, but the function of the modification has remained elusive. A strain of Escherichia coli has now been identified which is nonpermissive for wild-type bacteriophage T4, but permissive for bacteriophage mutants impaired in the modification reaction. A comparison with other bacteria suggests that nonpermissiveness is due to synthesis of a thermolabile valyl-transfer RNA synthetase and relaxed control of RNA accumulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marchin, G L -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):294-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6992274" target="_blank"〉PubMed〈/a〉
    Keywords: Escherichia coli/*genetics ; *Genes, Viral ; *Mutation ; Species Specificity ; T-Phages/*genetics ; Viral Plaque Assay
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  • 39
    Publication Date: 1980-05-30
    Description: DNA containing the herpes simplex virus thymidine kinase (HSVtk) gene was used to transform wild-type tk+ mouse L cells to a tk++ status in vitro using methotrexate as a selective agent. HSVtk DNA was also used to transform mouse bone marrow cells in vitro. Transformed marrow cells injected into irradiated and methotrexate-treated recipient mice gave rise to proliferating cells which in some cases dominated the marrow population and which contained HSVtk gene sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, K E -- Stang, H D -- Browne, J -- Salser, W -- Cline, M J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1033-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6246577" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow/*enzymology ; Bone Marrow Transplantation ; DNA, Viral/analysis ; Drug Resistance ; *Genes, Viral ; L Cells (Cell Line) ; Methotrexate/pharmacology ; Mice ; Simplexvirus/enzymology/*genetics ; Species Specificity ; Thymidine Kinase/*genetics ; *Transformation, Genetic
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  • 40
    Publication Date: 1980-05-30
    Description: Cloned repetitive DNA sequences were used to determine the number of homologous RNA transcripts in the eggs of two sea urchin species, Strongylocentrotus purpuratus and S. franciscanus. The eggs of these species contain different amounts of RNA, and their genomes contain different numbers of copies of the cloned repeats. The specific pattern of repetitive sequence representation in the two egg RNA's is nonetheless quantitatively similar. The evolutionary conservation of this pattern suggests the functional importance of repeat sequence expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, G P -- Costantini, F D -- Posakony, J W -- Davidson, E H -- Britten, R J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1046-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA, Recombinant ; Female ; Nucleic Acid Hybridization ; Ovum/physiology ; Plasmids ; RNA/*genetics ; Sea Urchins/*genetics ; Species Specificity ; Transcription, Genetic
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  • 41
    Publication Date: 1980-08-22
    Description: A 27-kilodalton tryptic fragment, derived from the amino terminus of the 200-kilodalton fibronectin subunit, inhibited binding of intact fibronectin to Staphylococcus aureus and could be cross-linked to Staphylococcus aureus by blood coagulation Factor XIIIa. Interactions of fibronectin with Staphylococcus aureus via this fragment may be important for bacterial opsonization and attachment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mosher, D F -- Proctor, R A -- New York, N.Y. -- Science. 1980 Aug 22;209(4459):927-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7403857" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Factor XIII/*metabolism ; Fibronectins/*metabolism ; Humans ; Molecular Weight ; Opsonin Proteins ; Peptide Fragments ; Protein Binding ; Staphylococcus aureus/immunology/*metabolism ; Trypsin/metabolism
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-06-06
    Description: Dissociated embryonic rat myocardial cells and chick myocardial cells labeled with radioactive isotope coaggregate and establish intercellular junctions. These bispecific cells reconstruct synchronously beating myocardial tissue within 24 hours of culture.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nag, A C -- Cheng, M -- New York, N.Y. -- Science. 1980 Jun 6;208(4448):1150-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375923" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion ; *Cell Aggregation ; Cells, Cultured ; Chickens ; Heart/*embryology ; Intercellular Junctions/ultrastructure ; Mosaicism ; Myocardial Contraction ; Myocardium/*cytology ; Rats ; Species Specificity
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-09-05
    Description: A 15,8-kilobase pair fragment of BALB/c mouse liver DNA, cloned in the Charon 4A lambda phage vector system, was shown to contain the mu heavy chain constant region (CHmu) gene for the mouse immunoglobulin M. In addition, this fragment of DNA contains at least two J genes, used to code for the carboxyl terminal portion of heavy chain variable regions. These genes are located in genomic DNA about eight kilobase pairs to the 5' side of the CHmu gene. The complete nucleotide sequence of a 1120-base pair stretch of DNA that includes the two J genes has been determined.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newell, N -- Richards, J E -- Tucker, P W -- Blattner, F R -- New York, N.Y. -- Science. 1980 Sep 5;209(4461):1128-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6250219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; Genes ; Genetic Linkage ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulin mu-Chains/*genetics ; Mice
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-07-25
    Description: Disposal of industrial waste resulted in massive DDT contamination at Wheeler National Wildlife Refuge, Alabama. Nearly a decade after the cessation of DDT manufacturing at the facility responsible, concentrations of DDT residues in the local fauna are still high enough to suggest avian reproductive impairment and mortality. Populations of fish-eating birds are low, endangered species are being exposed, and muscle lipids of game birds contain up to 6900 parts of DDT (isomers and metabolites) per million.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Shea, T J -- Fleming, W J -- Cromartie, E -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):509-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7394517" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; DDT/*analysis ; Ducks ; *Industrial Waste ; Lipids/analysis ; Muscles/analysis ; Rabbits ; Species Specificity
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  • 45
    Publication Date: 1980-03-14
    Description: A 15.0-kilobase (kb) Eco RI DNA fragment from normal mouse Balb/c genomic DNA that contains sequences (sarc) homologous to the acquired cell sequences (src) of Moloney sarcoma virus (MSV) has been cloned in phage lambda. The sarc region (1.2 to 1.3 kb) of the 15.0-kb cell fragment is indistinguishable from the src region of two isolates of MSV as judged by heteroduplex and restriction endonuclease analyses. The cellular sequences flanking sarc show no homology to other MSV sequences. Whereas cloned subgenomic portions of MSV that contain src transformed NIH-3T3 cells in vitro, the cloned sarc fragment is inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oskarsson, M -- McClements, W L -- Blair, D G -- Maizel, J V -- Vande Woude, G F -- New York, N.Y. -- Science. 1980 Mar 14;207(4436):1222-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6243788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; DNA Restriction Enzymes ; *Genes ; *Genes, Viral ; Mice ; Mice, Inbred BALB C/*genetics ; Moloney murine leukemia virus/*genetics ; Nucleic Acid Hybridization
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  • 46
    Publication Date: 1980-07-11
    Description: The human genes for growth hormone (GH), chorionic somatomammotropin (CSH), and a third growth hormone-like gene (GHL) have been located on chromosome 17 in humans. DNA fragments of 2.6, 2.8, and 9.5 kilobase pairs containing GH, CSH, and GHL, respectively, were identified in human genomic DNA, and a 7.5-kilobase DNA fragment related to growth hormone DNA sequences was found in mouse cells. In somatic hybrids of human and mouse cells containing reduced numbers of human chromosomes, but a normal complement of mouse chromosomes, the mouse, 7.5-kolobase DNA fragment was always present, whereas the 2.6-, 2.8-, and 9.5-kilobase human fragments were present only when human chromosome 17 was also present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owerbach, D -- Rutter, W J -- Martial, J A -- Baxter, J D -- Shows, T B -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):289-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384802" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; *Chromosomes, Human, 16-18 ; *DNA/metabolism ; *Genes ; Growth Hormone/*biosynthesis ; Humans ; Hybrid Cells/metabolism ; Mice ; Placental Lactogen/*biosynthesis ; Translocation, Genetic
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  • 47
    Publication Date: 1980-01-04
    Description: Freshly ejaculated, noncapacitated boar sperm bind rapidly and in large numbers to pig egg zona pellucida in vitro. In the present study, the number of sperm bound decreased sharply when sperm motility was lowered by energy poisons or by reducing the temperature. Highly motile sperm from humans, guinea pigs, and rats, added at concentrations ten times higher than control sperm, did not bind to the porcine zona. At the same high concentration, a small number of hamster and bull sperm bound to the zona. Binding of boar sperm to the zona pellucida was blocked almost completely by diluted whole antiserum to sperm plasma membranes and by univalent (Fab) antibody to these membranes. When antibody to sperm plasma membrane was first absorbed with plasma membrane vesicles, sperm binding was not inhibited. These results provide direct evidence for the existence of sperm plasma membrane receptors for the zona pellucida of the pig.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peterson, R N -- Russell, L -- Bundman, D -- Freund, M -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):73-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7188647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Membrane/metabolism ; Female ; *Fertilization ; Guinea Pigs ; Humans ; Immunoglobulin Fab Fragments ; Male ; Ovum/*metabolism ; Rats ; Receptors, Drug/metabolism ; Species Specificity ; *Sperm-Ovum Interactions ; Spermatozoa/*metabolism ; Swine ; Zona Pellucida/*metabolism
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-09-19
    Description: Two unstable mutations at the his4 locus of yeast are due to the insertion of the transposable elements Ty912 and Ty917 into the his4 regulatory region. The two transposons are related, one being derived from the other by a substitution of 4000 base pairs of DNA. Element Ty912 includes identical terminal repeats, whereas the terminal repeats of Ty917 are not identical. Transposition of Ty912 or Ty917 generates 5-base-pair duplications of the target DNA at either end of the element. Expression and reversion of a his4 gene containing Ty912 or Ty917 is controlled by three unlinked regulatory genes. The properties of these regulatory genes are similar to those described for the controlling elements in maize.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roeder, G S -- Farabaugh, P J -- Chaleff, D T -- Fink, G R -- CA23441/CA/NCI NIH HHS/ -- GM07617/GM/NIGMS NIH HHS/ -- GM15408/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1375-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251544" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular/methods ; *DNA Transposable Elements ; DNA, Fungal/genetics ; Genes, Regulator ; Genetic Linkage ; Histidine/*genetics ; Saccharomyces cerevisiae/*genetics ; Suppression, Genetic
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  • 49
    Publication Date: 1980-09-19
    Description: Many eukaryotic genes contain intevening sequences, segments of DNA that interrupt the continuity of the gene. They are removed from RNA transcripts of the gene by a process known as splicing. The intervening sequence in a yeast tyrosine transfer RNA (tRNA Tyr) suppressor gene was deleted in order to test its role in the expression of the gene. The altered gene and its parent were introduced into yeast by transformation. Both genes exhibited suppressor function, showing that the intervening sequence is not absolutely essential for the expression of this gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, R B -- Johnson, P F -- Tanaka, S -- Schold, M -- Itakura, K -- Abelson, J -- CA10984/CA/NCI NIH HHS/ -- GM 26391/GM/NIGMS NIH HHS/ -- GM 35658/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1396-400.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6997991" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; DNA, Recombinant ; Genes ; Mutation ; Nucleic Acid Precursors/genetics ; Plasmids ; RNA, Fungal/*genetics ; RNA, Transfer/*genetics ; Saccharomyces cerevisiae/genetics ; Suppression, Genetic ; Tyrosine
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  • 50
    Publication Date: 1980-04-18
    Description: The levels of gluatmine synthetase specific activity in hepatic and renal tissue are higher in fish that are ureosmoregulators than in those that are not. Enzyme activities in the liver and kidney of 18 species of fish correlated directly with the ureosmoregulatory adaptation of each species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Webb, J T -- Brown, G W Jr -- New York, N.Y. -- Science. 1980 Apr 18;208(4441):293-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6102799" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonia/metabolism ; Animals ; Brain/enzymology ; Fishes/*metabolism ; Glutamate-Ammonia Ligase/*metabolism ; Kidney/enzymology ; Liver/enzymology ; Species Specificity ; Urea/*metabolism ; Water-Electrolyte Balance
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-10-09
    Description: The systemic comparison of every newly determined amino acid sequence with all other known sequences may allow a complete reconstruction of the evolutionary events leading to contemporary proteins. But sometimes the surviving similarities are so vague that even computer-based sequence comparisons procedures are unable to validate relationships. In other cases similar sequences may appear in totally alien proteins as a result of mere chance or, occasionally, by the convergent evolution of sequences with special properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- New York, N.Y. -- Science. 1981 Oct 9;214(4517):149-59.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280687" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Animals ; *Biological Evolution ; Carrier Proteins/genetics ; Humans ; Proteins/classification/*genetics ; RNA Splicing ; RNA, Messenger/genetics ; Species Specificity
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G B -- New York, N.Y. -- Science. 1981 Nov 13;214(4522):775-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7292010" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromatin/*ultrastructure ; Deoxyribonucleases/metabolism ; *Gene Expression Regulation ; Humans ; Nucleic Acid Conformation
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  • 53
    Publication Date: 1981-12-04
    Description: A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleid, D G -- Yansura, D -- Small, B -- Dowbenko, D -- Moore, D M -- Grubman, M J -- McKercher, P D -- Morgan, D O -- Robertson, B H -- Bachrach, H L -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6272395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Base Sequence ; Cattle ; Cattle Diseases/*prevention & control ; *Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; Foot-and-Mouth Disease/*prevention & control ; Immunity, Cellular ; Protein Biosynthesis ; Swine ; Swine Diseases/*prevention & control ; Transcription, Genetic ; *Vaccines ; Viral Proteins/genetics/*therapeutic use
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-08-21
    Description: Studies of the length of DNA fragments produced upon decay of iodine-125-labeled deoxycytidine that was located at a single position within a DNA fragment of defined sequence demonstrate that most radiochemical damage occurs within 15 to 20 angstroms of the site of iodine-125 decay. However, DNA strand breakage was detectable up to 70 angstroms from the site of iodine-125 decay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, R F -- Haseltine, W A -- CA 19589/CA/NCI NIH HHS/ -- CA 25118/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Aug 21;213(4510):896-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256283" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*radiation effects ; Hydrolysis ; *Iodine Radioisotopes
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  • 55
    Publication Date: 1981-07-24
    Description: Recombinant DNA techniques were used to analyze the structure of the messenger RNA encoding a precursor of calcitonin, a small calcium-regulating hormone of 32 amino acids. Analyses of the nucleotide sequences of cloned complementary DNA's comprising the entire coding sequence of the messenger RNA revealed that calcitonin is flanked at both its amino and carboxyl termini by peptide extensions linked to the hormone by short sequences of basic amino acids. The location of glycine next to the carboxyl terminal prolinamide of calcitonin is consistent with indications that glycine is required for the enzymatic amidation of proline to the prolinamide. During cellular biosynthesis, calcitonin arises from a large precursor protein by cleavages at both amino and carboxyl terminal residues of the hormone. These findings raise questions concerning the regulation of these cleavages and the potential biological functions of the precursor extensions derived from these cleavages.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, J W -- Goodman, R H -- Chin, W W -- Dee, P C -- Habener, J F -- Bell, N H -- Potts, J T Jr -- AM 27781-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 24;213(4506):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcitonin/*genetics ; Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/*metabolism ; Macromolecular Substances ; Neoplasms, Experimental/metabolism ; Nucleic Acid Hybridization ; Peptide Biosynthesis ; Plants/metabolism ; Protein Biosynthesis ; RNA, Messenger/*genetics ; Rats ; Thyroid Neoplasms/metabolism ; Triticum/metabolism
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  • 56
    Publication Date: 1981-10-30
    Description: The complement system of the nurse shark was investigated. Six functionally pure components were isolated from a single serum sample. Sequential reactions of the components with sensitized sheep erythrocytes resulted in membrane lesions indistinguishable from the "holes" caused by guinea pig complement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jensen, J A -- Festa, E -- Smith, D S -- Cayer, M -- New York, N.Y. -- Science. 1981 Oct 30;214(4520):566-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7291995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Complement System Proteins/*physiology ; Erythrocyte Membrane/immunology ; Hemolysis ; Sharks/*immunology ; Sheep ; Species Specificity
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-05-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1981 May 29;212(4498):1015-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6785883" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*genetics ; Base Sequence ; *Genes ; Humans ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Light Chains/genetics ; Immunoglobulins/*genetics ; Transcription, Genetic
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  • 58
    Publication Date: 1981-10-23
    Description: The complete nucleotide sequence of a mammalian transforming retrovirus. Moloney murine sarcoma virus, has been determined. MSV, recombinant virus derived of helper viral and cellular sequences, possesses termini resembling prokaryotic transposable elements. The viral genome has the coding capacity for the Moloney murine leukemia virus gag gene product and contains large deletions in pol and env genes. A large open reading frame encompassing its cell-derived sequences codes for its putative transforming protein. The nature of some of the important domains in the viral genome has been established, and their structure is discussed in relation to their function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- Smith, M J -- Aaronson, S A -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):445-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6170110" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/genetics ; Base Sequence ; Binding Sites ; Cell Transformation, Viral ; DNA, Viral/*genetics ; Defective Viruses/genetics ; Gene Products, gag ; *Genes, Viral ; Moloney murine leukemia virus/*genetics ; RNA, Transfer/genetics ; RNA-Directed DNA Polymerase/genetics ; Repetitive Sequences, Nucleic Acid ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-12-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanger, F -- New York, N.Y. -- Science. 1981 Dec 11;214(4526):1205-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7302589" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages/genetics ; *Base Sequence ; Cloning, Molecular ; DNA/*genetics ; DNA, Mitochondrial/genetics ; DNA, Single-Stranded/genetics ; DNA-Directed DNA Polymerase ; Humans ; Protein Biosynthesis ; Templates, Genetic
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  • 60
    Publication Date: 1981-07-31
    Description: The cell-to-cell channels in the junctions of an insect salivary gland and of insect and mammalian cells in culture were probed with fluorescent molecules-neutral linear oligosaccharides, neutral branched glycopeptides, and charged linear peptides. From the molecular dimensions of the largest permeants and smallest impermeants the permeation-limiting channel diameter was obtained: 16 to 20 angstroms for the mammalian cells and 20 to 30 angstroms for the insect cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzmann, G -- Wiegandt, H -- Rose, B -- Zimmerman, A -- Ben-Haim, D -- Loewenstein, W R -- CA 14464/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):551-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chironomidae ; Fluorescent Dyes ; Glycopeptides/*metabolism ; Intercellular Junctions/*ultrastructure ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oligosaccharides/*metabolism ; Protein Conformation ; Salivary Glands/*ultrastructure ; Species Specificity
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-08-14
    Description: The aorta of the octopus, Octopus dofleini, is a highly distensible, elastic tube. The circumferential elastic modulus increases with inflation in the physiological range from abut 10(4) to 10(5) newtons per square meter. Rubber-like fibers have been isolated, apparently for the first time, from the aorta of an invertebrate. These fibers have an elastic modulus, like elastin, of about 4 x 10(5) newtons per square meter and are present in sufficient quantity to account for the elastic properties of the intact vessel under physiological conditions. Thus the circulatory system of an invertebrate animal provides an "elastic reservoir" (much like that of the vertebrate system), which increases the efficiency of the circulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shadwick, R E -- Gosline, J M -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):759-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/anatomy & histology/*physiology ; Elasticity ; Octopodiformes/*physiology ; Proteins/physiology ; Species Specificity
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-07-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snell, G D -- New York, N.Y. -- Science. 1981 Jul 10;213(4504):172-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7017931" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Antigens, Neoplasm/genetics ; Antigens, Viral/genetics ; Antigens, Viral, Tumor ; Female ; Genetic Linkage ; Genotype ; H-2 Antigens/genetics ; Heterozygote ; *Major Histocompatibility Complex ; Male ; Mice ; Mice, Inbred Strains ; Neoplasms, Experimental/genetics/*immunology ; Pedigree ; Rats ; Species Specificity
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-04-17
    Description: Vitellogenin is synthesized under estrogen control in the liver, extensively modified, transported to the ovary, and there processed to the yolk proteins lipovitellin and phosvitin. In the frog Xenopus laevis there are at least four distinct but related vitellogenin genes. The two genes A1 and A2 have a 95 percent sequence homology in their messenger RNA coding regions, and contain 33 introns that interrupt the coding region (exons) at homologous positions. Sequences and lengths of analogous introns differ, and many introns contain repetitive DNA elements. The introns in these two genes that have apparently arisen by duplication have diverged extensively by events that include deletions, insertions, and probably duplications. Rapid evolutionary change involving rearrangements and the presence of repeated DNA suggests that the bulk of the sequences within introns may not have any specific function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wahli, W -- Dawid, I B -- Ryffel, G U -- Weber, R -- New York, N.Y. -- Science. 1981 Apr 17;212(4492):298-304.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Estrogens/physiology ; Female ; *Genes ; Lipoproteins/*genetics ; Liver/secretion ; Male ; Oocytes/metabolism ; RNA, Messenger/metabolism ; Receptors, Estrogen/metabolism ; Repetitive Sequences, Nucleic Acid ; Vitellogenins/biosynthesis/*genetics ; Xenopus laevis/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-01-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wade, N -- New York, N.Y. -- Science. 1981 Jan 2;211(4477):33-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444446" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; Humans ; Isoelectric Point ; Molecular Weight ; Proteins/analysis/*genetics
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  • 65
    Publication Date: 1981-07-10
    Description: Southern blot hybridization was used to identify human and other vertebrate DNA sequences that were homologous to cloned DNA fragments containing the oncogenic nucleic acid sequences of three different type C mammalian retroviruses (simian sarcoma virus, the Snyder-Theilen strain of feline sarcoma virus, and the Harvey strain of murine sarcoma virus). Each onc gene counterpart has a single genetic locus, which probably contains non-onc intervening sequences. The human DNA sequences may represent genes important to cell growth or cell differentiation, or both. Their identification and isolation may allow elucidation of their role in these processes and in neoplasias.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong-Staal, F -- Dalla-Favera, R -- Franchini, G -- Gelmann, E P -- Gallo, R C -- New York, N.Y. -- Science. 1981 Jul 10;213(4504):226-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264598" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Cell Transformation, Viral ; *Cloning, Molecular ; DNA/*genetics ; DNA, Viral/*genetics ; *Genes ; Humans ; Nucleic Acid Hybridization ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/genetics ; Sarcoma Viruses, Murine/genetics ; Species Specificity
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  • 66
    Publication Date: 1982-02-19
    Description: The 14S messenger RNA (1300 to 1500 nucleotides) for the alpha A chain of alpha-crystallin of the mammalian lens is nearly three times larger than required to code for the polypeptide that contains 173 amino acids. As a means of accounting for this anomaly, a complementary DNA clone for the mouse alpha A-crystallin messenger RNA was constructed in pBR322 and sequenced. Derivation of the protein sequence from the nucleic acid sequence showed that mouse alpha A-crystallin is similar to that of other organisms. The messenger RNA contains 536 nucleotides located on the 3' side of the coding region, excluding the polyadenylate stretch. This 3' sequence does not encode any other crystallin and has multiple termination codons in the three possible reading frames.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, C R -- Shinohara, T -- Piatigorsky, J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):985-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7156978" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Crystallins/*genetics ; Mice ; RNA, Messenger/*genetics
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  • 67
    Publication Date: 1982-10-08
    Description: Urotensin I, purified from extracts of the urophysis of a teleost fish (Catostomus commersoni), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met-Ile-Glu - Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu -Val-NH2. Extraction with 0.1N HCl at 100 degrees C cleaves the amino-terminal tripeptide, yeilding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lederis, K -- Letter, A -- McMaster, D -- Moore, G -- Schlesinger, D -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6981844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Corticotropin-Releasing Hormone ; Fishes ; Peptides/*isolation & purification ; Species Specificity ; Urotensins/*isolation & purification
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):817-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100925" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA/*analysis ; *Information Systems
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-08-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1982 Aug 13;217(4560):621-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283639" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; DNA Transposable Elements ; DNA, Satellite/genetics ; *Repetitive Sequences, Nucleic Acid ; Species Specificity
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  • 70
    Publication Date: 1982-06-25
    Description: Avian myeloblastosis virus is defective in reproductive capacity, requiring a helper virus to provide the viral proteins essential for synthesis of new infectious virus. This virus arose by recombination of the nondefective helper virus and host cellular sequences present within the normal avian genome. These latter sequences are essential for leukemogenic activity. The complete nucleotide sequence of this region is reported. Within the acquired cellular sequences there is an open reading frame of 795 nucleotides starting with the initiation codon ATG (adenine, thymine, guanine) and terminating with the triplet TAG. This open reading frame could code for the putative transforming protein of 265 amino acids with a molecular weight of approximately 30,000.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rushlow, K E -- Lautenberger, J A -- Papas, T S -- Baluda, M A -- Perbal, B -- Chirikjian, J G -- Reddy, E P -- New York, N.Y. -- Science. 1982 Jun 25;216(4553):1421-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Leukosis Virus/*genetics ; Avian Myeloblastosis Virus/*genetics ; Avian Sarcoma Viruses/genetics ; Base Sequence ; Cell Transformation, Viral ; Chickens/genetics ; DNA Restriction Enzymes ; Gene Expression Regulation ; *Genes, Viral ; RNA, Viral/analysis ; Viral Proteins/biosynthesis
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  • 71
    Publication Date: 1982-04-16
    Description: The size of the gene pool potentially encoding antibodies to p-azophenyl arsonate has been examined. A heavy chain-specific full-length complementary DNA clone has been constructed with the use of messenger RNA from a hybridoma that produces antibodies to the arsonate hapten and bears nearly a full complement of the determinants comprising the cross-reactive idiotype (CRI). The sequences of both the complementary DNA clone and the corresponding immunoglobulin heavy chain have been independently determined. A probe for the variable region gene was prepared from the original heavy chain complementary DNA clone and used to analyze, by Southern filter hybridization, genomic DNA from both A/J (CRI positive) and BALB/c (CRI negative) mice. Approximately 20 to 25 restriction fragments containing "germline" variable region gene segments were detected in both strains, and many are shared by both, Since 35 CRI-positive heavy chains have been partially sequenced thus far and 31 are different, the results of the hybridization analysis suggest that somatic mutation events involving the variable region gene segments of the heavy chain play a role in the origin of the amino acid sequence diversity seen in this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J -- Rabbitts, T H -- Estess, P -- Slaughter, C -- Tucker, P W -- Capra, J D -- A112127/PHS HHS/ -- AI-06020/AI/NIAID NIH HHS/ -- AI18016/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Apr 16;216(4543):309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6801765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites, Antibody/*genetics ; Genes ; Haptens ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Idiotypes/genetics ; Immunoglobulin Variable Region/*genetics ; Mice ; *Mutation
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  • 72
    Publication Date: 1982-12-10
    Description: Simian sarcoma virus (SSV) deletion mutants were constructed from a molecular clone containing the entire infectious provirus. Transfection analysis of these mutants localized the SSV transforming gene to a small region of the viral genome encompassing its cell-derived sequence (v-sis). Antiserum to a peptide synthesized on the basis of the predicted amino acid sequence of the SSV transforming gene detected a 28,000-dalton protein that was specifically expressed in SSV transformed cells and that corresponded in size to that predicted from the v-sis coding sequence. The v-sis gene product designated p28sis was not a phosphoprotein, nor did it possess detectable protein kinase activity. These findings distinguish p28sis from a number of other retroviral onc proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robbins, K C -- Devare, S G -- Reddy, E P -- Aaronson, S A -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1131-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6293053" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Viral ; Base Sequence ; *Cell Transformation, Viral ; *Genes, Viral ; Mice ; Molecular Weight ; *Oncogenes ; Phosphoproteins/genetics ; Protein Kinases/genetics ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Viral Proteins/*genetics/immunology
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  • 73
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-06-04
    Description: A family of related sequences that includes approximately 500,000 members is the most prominent short dispersed repeat family in primate and rodent DNA's. The primate sequence is approximately 300 base pairs in length and is composed of two imperfectly repeated monomer units, whereas the rodent repeat consists of only a single monomer. Properties of this repeat sequence, its flanking sequences in chromosomal DNA, and RNA's transcribed from it suggest that it may be a mobile DNA element inserted at hundreds of thousands of different chromosomal locations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmid, C W -- Jelinek, W R -- New York, N.Y. -- Science. 1982 Jun 4;216(4550):1065-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6281889" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA/*genetics ; *DNA Transposable Elements ; Genetic Linkage ; Muridae/genetics ; Primates/genetics ; RNA Polymerase III/metabolism ; RNA, Heterogeneous Nuclear/genetics ; *Repetitive Sequences, Nucleic Acid ; Transcription, Genetic
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  • 74
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-05-14
    Description: The amino acid sequences of mouse brain Thy-1 glycoproteins are shown to be homologous to those of variable-region immunoglobulin domains. There is also good homology with constant domains and beta 2-microglobulin; overall the results suggest that Thy-1 may be like the primordial immunoglobulin domain. Preliminary evidence for an invertebrate Thy-1 homolog supports this possibility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A F -- Gagnon, J -- New York, N.Y. -- Science. 1982 May 14;216(4547):696-703.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6177036" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*immunology ; Antigens, Thy-1 ; Biological Evolution ; Epitopes ; Glycoproteins/*immunology ; Immunoglobulin Constant Regions/immunology ; Immunoglobulin Variable Region/immunology ; Immunoglobulins/*immunology ; Isoantibodies/biosynthesis ; Protein Conformation
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1982-11-12
    Description: Transfer RNA's are probably very strongly selected for translational efficiency. In this article, the argument is presented that the coding performance of the triplet anticodon is enhanced by selection of a matching anticodon loop and stem sequence. the anticodon plus these nearby sequence features (the extended anticodon) therefore contains more coding information than the anticodon alone and can perform more efficiently and accurately at the ribosome. This idea successfully accounts for the relative efficiencies of many transfer RNA's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarus, M -- New York, N.Y. -- Science. 1982 Nov 12;218(4573):646-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6753149" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli/genetics ; Kinetics ; Nucleic Acid Conformation ; *Protein Biosynthesis ; RNA, Transfer/*genetics ; Ribosomes/metabolism ; Structure-Activity Relationship ; Suppression, Genetic
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-05-27
    Description: Human platelet-derived growth factor (PDGF) obtained from outdated human platelets was subjected to amino-terminal amino acid sequence analysis by automated Edman degradation. Despite the apparent presence of limited proteolytic degradation of the protein derived from this method, the sequence analysis reveals two primary peptide sequences and suggests that active PDGF is composed of two, possibly homologous, peptides linked by a disulfide bond or bonds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Antoniades, H N -- Hunkapiller, M W -- CA30101/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 27;220(4600):963-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844921" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electrophoresis, Polyacrylamide Gel ; Growth Substances/genetics/*metabolism ; Humans ; Molecular Weight ; Peptides/genetics/*metabolism ; Platelet-Derived Growth Factor
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: A comparison between eukaryotic gene sequences and protein sequences of homologous enzymes from bacterial and mammalian organisms shows that intron-exon junctions frequently coincide with variable surface loops of the protein structures. The altered surface structures can account for functional differences among the members of a family. Sliding of the intron-exon junctions may constitute one mechanism for generating length polymorphisms and divergent sequences found in protein families. Since intron-exon junctions map to protein surfaces, the alterations mediated by sliding of these junctions can be effected without disrupting the stability of the protein core.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Craik, C S -- Rutter, W J -- Fletterick, R -- AM21344/AM/NIADDK NIH HHS/ -- AM26081/AM/NIADDK NIH HHS/ -- GM28520/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344214" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins ; Base Sequence ; Biological Evolution ; DNA/genetics ; Endopeptidases/genetics ; Eukaryotic Cells/metabolism ; Genes ; Genes, Bacterial ; Protein Conformation ; Proteins/*genetics ; *Serine Endopeptidases ; Tetrahydrofolate Dehydrogenase/genetics
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-10
    Description: An important question concerning the mechanism of somatic mutation of immunoglobulin variable (V) genes is whether it involves all of the numerous V genes in a differentiated B cell, independent of location, or if it is restricted to a particular chromosomal site. Comparison of the sequence of two alleles of a given V gene shows that the mutations are limited to the rearranged V gene, while the same V gene on the other chromosome has not undergone mutation. This indicates that a V gene sequence alone is not sufficient for somatic mutation to take place. The mutation is therefore restricted to the rearranged V gene and consequently does not occur before rearrangement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorski, J -- Rollini, P -- Mach, B -- New York, N.Y. -- Science. 1983 Jun 10;220(4602):1179-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6857243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites, Antibody/*genetics ; Chromosomes/physiology ; DNA/genetics ; *Genes ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Variable Region/*genetics ; Immunoglobulins/genetics ; Lymphocytes/metabolism ; Mice ; *Mutation
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  • 79
    Publication Date: 1983-06-24
    Description: The size of the Epstein-Barr virus (EBV) nuclear antigen (EBNA) in cells infected with different EBV isolates varies directly with the size of the EBV triplet repeat array, IR3. The isolate with the largest IR3 fragment has approximately 170 more codons than the isolates with the smallest IR3 fragment; it encodes an EBNA which is approximately 17,000 daltons larger than the smallest EBNA. The EBV IR3 encodes part of a 2-kilobase exon of a latently infected cell messenger RNA which must be translated into a repetitive amino acid domain of EBNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hennessy, K -- Heller, M -- van Santen, V -- Kieff, E -- CA 17281/CA/NCI NIH HHS/ -- CA 19264/CA/NCI NIH HHS/ -- GM 07183/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Jun 24;220(4604):1396-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304878" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/*genetics ; Base Sequence ; Cell Nucleus/immunology ; DNA, Viral/*genetics ; Epstein-Barr Virus Nuclear Antigens ; Herpesvirus 4, Human/*genetics/immunology ; Humans ; Mice ; RNA, Viral/genetics
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-03-25
    Description: During oxygen limitation in animals, glucose can be fermented via several metabolic pathways varying in energetic efficiency and leading to various end products (such as lactate, alanopine, octopine, succinate, or propionate). Because of opposite pH dependencies of proton production by fermentation and by hydrolysis of adenosine triphosphate formed in the fermentation, the total number of moles of protons generated is always two per mole of the fermentable substrate. However, two and three times more adenosine triphosphate can be turned over per mole of protons produced in succinate and propionate fermentations, respectively, than in lactate fermentation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hochachka, P W -- Mommsen, T P -- New York, N.Y. -- Science. 1983 Mar 25;219(4591):1391-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6298937" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Aerobiosis ; Anaerobiosis ; Animals ; Fermentation ; Glucose/*metabolism ; *Glycolysis ; Lactates/metabolism ; Mollusca/metabolism ; *Protons ; Species Specificity
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  • 81
    Publication Date: 1983-06-03
    Description: A synthetic analog of bovine parathyroid hormone (bPTH), [tyrosine-34] bPTH-(7-34)NH2, was found to inhibit parathyroid hormone action in vivo. When the analog and parathyroid hormone were infused simultaneously to rats at a molar ratio of 200 to 1, the analog inhibited the excretion of urinary phosphate and adenosine 3',5'-monophosphate. When infused alone at the same dose rate, the analog was devoid of agonist activity. The compound was prepared by following design principles developed for inhibitors of parathyroid hormone, and is believed to be the first antagonist of parathyroid hormone that is effective in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horiuchi, N -- Holick, M F -- Potts, J T Jr -- Rosenblatt, M -- AM11749/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1053-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cyclic AMP/urine ; Dose-Response Relationship, Drug ; Male ; Parathyroid Hormone/*antagonists & inhibitors/*pharmacology ; Peptide Fragments/*pharmacology ; Phosphates/urine ; Rats
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-18
    Description: Polynucleotide templates containing C (cytidine) as the major component facilitate the synthesis of oligonucleotides from mixtures of the activated mononucleotide derivatives (as indicated by structure 1 in the text). A nucleotide is incorporated into oligomeric products if and only if its complement is present in the template. The reaction has a high fidelity and produces products with mean chain lengths of six to ten nucleotides. Bases other than guanosine are incorporated within oligomers or at their 3' termini, but rarely at their 5' termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inoue, T -- Orgel, L E -- GM-13435/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Feb 18;219(4586):859-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186026" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/*metabolism ; Hydrogen Bonding ; Models, Chemical ; RNA/*chemical synthesis ; Templates, Genetic
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-01
    Description: Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Hsu, C P -- Itakura, K -- Inouye, M -- GM19043/GM/NIGMS NIH HHS/ -- GM30395/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Base Sequence ; DNA, Bacterial/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Lipoproteins/*biosynthesis ; Membrane Proteins/biosynthesis ; Mutation ; Protein Precursors/*biosynthesis
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-01-07
    Description: The illustration that accompanied the review by C. C. Albritton, Jr., of W. H. Goetzmann and K. Sloan's Looking Far North (Viking, New York, 1982) in the issue of 10 December, page 1109, should have been credited to the Bancroft Library, University of California, Berkeley, as well as to the book under review.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lerman, L S -- New York, N.Y. -- Science. 1983 Jan 7;219(4580):10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6184778" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; RNA/*physiology ; RNA, Small Nuclear
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-03-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1052-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/physiology ; DNA/*genetics ; Humans ; Poly A/genetics ; RNA/*genetics ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic
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  • 86
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):495-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623088" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Dna ; Eukaryota/genetics ; Humans ; *Nucleic Acid Conformation ; Species Specificity ; Structure-Activity Relationship
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  • 87
    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; Structure-Activity Relationship
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: The prospects for protein engineering, including the roles of x-ray crystallography, chemical synthesis of DNA, and computer modelling of protein structure and folding, are discussed. It is now possible to attempt to modify many different properties of proteins by combining information on crystal structure and protein chemistry with artificial gene synthesis. Such techniques offer the potential for altering protein structure and function in ways not possible by any other method.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmer, K M -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):666-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6572017" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Crystallography ; Genes ; *Genetic Engineering ; Models, Molecular ; Molecular Biology/trends ; Protein Conformation ; Proteins/*genetics ; X-Ray Diffraction
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Enhancers, or activators, dramatically increase the transcriptional activity of certain eukaryotic genes. A series of multiple point mutations affecting the simian virus 40 (SV40) enhancer-activator region were generated in order to define the nucleotide sequence required for this function. Three independent assays provided information leading to the identification of nucleotides essential for enhancer function. One class leads to a decrease in gene expression, while the second completely abolishes functional activity. One critical replacement appears to be the first G (guanine) in a sequence TGGAAAG (T, thymine, A, adenine) located in the 5' region of the 72 base-pair repeat of SV40. Comparison of this sequence with nucleotide sequences in other known enhancers leads to the identification of potential related core elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiher, H -- Konig, M -- Gruss, P -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):626-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297005" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Replication ; *Gene Expression Regulation ; Mutation ; *Operon ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Simian virus 40/*genetics ; Virus Replication
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  • 90
    Publication Date: 1983-02-11
    Description: The surface of rabies virus is composed of an approximately 60,000 dalton glycoprotein, in which most of the antigenic and immunogenic determinants of the virus reside. We have constructed plasmids for the direct expression in Escherichia coli of the mature full length rabies glycoprotein gene and also for the expression of a glycoprotein gene which has been truncated to exclude the coding region for a hydrophobic, possibly transmembrane, domain of the protein. Escherichia coli harboring the plasmids synthesize analog proteins which conform by several biochemical and antigenic criteria to rabies glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yelverton, E -- Norton, S -- Obijeski, J F -- Goeddel, D V -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):614-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6297004" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Escherichia coli ; Genes, Viral ; Genetic Vectors ; Glycoproteins/*genetics/immunology ; Plasmids ; Rabies virus/*genetics/immunology ; Viral Proteins/immunology
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  • 91
    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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  • 92
    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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  • 93
    Publication Date: 1984-08-31
    Description: A T lymphotropic virus found in patients with the acquired immune deficiency syndrome (AIDS) or lymphadenopathy syndrome has been postulated to be the cause of AIDS. Immunological analysis of this retrovirus and its biological properties suggest that it is a member of the family of human T-lymphotropic retroviruses known as HTLV. Accordingly, it has been named HTLV-III. In the present report it is shown by nucleic acid hybridization that sequences of the genome of HTLV-III are homologous to the structural genes (gag, pol, and env) of both HTLV-I and HTLV-II and to a potential coding region called pX located between the env gene and the long terminal repeating sequence that is unique to the HTLV family of retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Gallo, R C -- Hahn, B H -- Shaw, G M -- Popovic, M -- Salahuddin, S Z -- Wong-Staal, F -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):927-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089333" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; Cloning, Molecular ; Dna ; DNA, Viral ; Deltaretrovirus/classification/*genetics ; Genes ; *Genes, Viral ; Humans ; *Nucleic Acid Hybridization ; RNA, Viral ; Repetitive Sequences, Nucleic Acid
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  • 94
    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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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Prokaryotic gene control signals can be isolated, compared, and characterized by precise fusion in vitro to the Escherichia coli galactokinase gene (galK), which provides both a simple assay and genetic selection. This recombinant galK fusion vector system was applied to the study of promoters and terminators recognized by the Escherichia coli RNA polymerase. Three promoters created by mutation from DNA sequences having no promoter function were characterized. Mutations that inactivate promoter function were selected, structurally defined, and functionally analyzed. Similarly, transcription termination was examined, and mutations affecting terminator function were isolated and characterized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, M -- Chepelinsky, A B -- McKenney, K -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):734-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356355" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Bacterial/*genetics ; DNA, Recombinant ; DNA-Directed RNA Polymerases/genetics ; Escherichia coli/genetics ; Galactokinase/genetics ; Gene Expression Regulation ; Mutation ; Nucleic Acid Conformation ; *Operon ; *Transcription, Genetic
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  • 96
    Publication Date: 1984-08-31
    Description: Bromodeoxyuridine (BrdUrd) treatment of the prolactin nonproducing subclone of GH cells (rat pituitary tumor cells) induces amplification of a 20-kilobase DNA fragment including all of the prolactin gene coding sequences. This amplified DNA segment, which is flanked by two unamplified regions, thus designates a unit of BrdUrd-induced amplified sequence. Cloned DNA segments, 10.3 kilobases long, from the 5' end of the rat prolactin gene of BrdUrd-responsive and -nonresponsive cells, were ligated to the thymidine kinase gene of herpes simplex virus type 1 (HSV1TK), and the hybrid DNA was transferred to thymidine kinase-deficient mouse fibroblast cells by transfection. The HSV1TK gene and the rat prolactin gene were amplified together in drug-treated transfectants carrying the hybrid DNA HSV1TK gene and rat prolactin gene of BrdUrd-responsive GH cells. These results suggest that the 10.3-kilobase DNA segment at the 5' end of the rat prolactin gene of BrdUrd-responsive GH cells carries the information for drug-induced gene amplification (amplicon) and that another gene, such as the HSV1TK gene, is also amplified when the latter is placed adjacent to this segment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biswas, D K -- Hartigan, J A -- Pichler, M H -- CA28218/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):941-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089335" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Bromodeoxyuridine/*pharmacology ; Cell Line ; Cloning, Molecular ; DNA/*genetics ; DNA, Recombinant ; *Gene Amplification ; Genes, Viral ; Mice ; Prolactin/genetics ; Rats ; Simplexvirus/genetics ; Thymidine Kinase/genetics ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 1983-07-15
    Description: The structure of the messenger RNA (mRNA) encoding the precursor to mouse submaxillary epidermal growth factor (EGF) was determined from the sequence of a set of overlapping complementary DNA's (cDNA). The mRNA is unexpectedly large, about 4750 nucleotide bases, and predicts the sequence of preproEGF, a protein of 1217 amino acids (133,000 molecular weight). The EGF moiety (53 amino acids) is flanked by polypeptide segments of 976 and 188 amino acids at its amino and carboyxl termini, respectively. The amino terminal segment of the precursor contains seven peptides with sequences that are similar but not identical to EGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J -- Urdea, M -- Quiroga, M -- Sanchez-Pescador, R -- Fong, N -- Selby, M -- Rutter, W J -- Bell, G I -- 21344/PHS HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):236-40.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6602382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Epidermal Growth Factor/biosynthesis/*genetics ; Humans ; Male ; Mice ; RNA, Messenger/*genetics ; Submandibular Gland/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-04
    Description: The strongly paedomorphic skull form in the pygmy chimpanzee results from the heterochronic process of neoteny. This cranial paedomorphosis and neoteny in Pan paniscus may be related to reduced sexual dimorphism in morphology and behavior. The interspecific differences in form result from shifts in the rate and timing of similar patterns of development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shea, B T -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):521-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623093" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Biological Evolution ; Biometry ; Bone Development ; Bone and Bones/anatomy & histology ; Pan troglodytes/*anatomy & histology ; Skull/*anatomy & histology/growth & development ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-01-14
    Description: Two plasmids containing nonoverlapping deletions of the herpes simplex virus thymidine kinase gene were introduced into thymidine kinase-deficient mouse L cells by DNA-mediated gene transfer. Thymidine kinase-producing transformants were generated by a mixture of the two plasmids at a frequency significantly greater than that generated by either plasmid alone. Southern blot analyses demonstrated that functional thymidine kinase genes were generated by homologous recombination between the two deletion mutants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Small, J -- Scangos, G -- New York, N.Y. -- Science. 1983 Jan 14;219(4581):174-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294829" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Chromosome Deletion ; *Genetic Engineering ; Mice ; Mutation ; *Plasmids ; *Recombination, Genetic ; Simplexvirus ; Thymidine Kinase/*genetics
    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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