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  • Gene Expression Regulation  (20)
  • Amino Acid Sequence  (19)
  • American Association for the Advancement of Science (AAAS)  (37)
  • American Geophysical Union
  • Cambridge University Press
  • Periodicals Archive Online (PAO)
  • 1980-1984  (37)
  • 1925-1929
  • 1983  (37)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (37)
  • American Geophysical Union
  • Cambridge University Press
  • Periodicals Archive Online (PAO)
Years
  • 1980-1984  (37)
  • 1925-1929
Year
  • 1
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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    Description: Human platelet-derived growth factor (PDGF) obtained from outdated human platelets was subjected to amino-terminal amino acid sequence analysis by automated Edman degradation.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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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, J L -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):828-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6138857" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; DNA, Recombinant ; Gene Expression Regulation ; Nerve Tissue Proteins/*genetics ; Neurotransmitter Agents/*physiology ; Rats
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  • 3
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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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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-02-11
    Description: Plasmids were constructed to direct synthesis of the human interferons IFN-alpha 1, IFN-alpha 2, and IFN-gamma in the yeast Saccharomyces cerevisiae. Expression of IFN genes containing coding sequences for secretion signals resulted in the secretion of IFN activity. A large proportion of the IFN-alpha 1 and IFN-alpha 2 isolated from the yeast cell growth media had the same amino termini as the natural mature interferons, suggesting a removal of the signal sequences identical to that of human cells. These results show that a lower eukaryote, such as yeast, can utilize and process a human signal sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hitzeman, R A -- Leung, D W -- Perry, L J -- Kohr, W J -- Levine, H L -- Goeddel, D V -- New York, N.Y. -- Science. 1983 Feb 11;219(4585):620-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186023" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; Gene Expression Regulation ; Humans ; Interferons/*genetics/secretion ; Peptides/physiology ; Plasmids ; Protein Processing, Post-Translational ; Protein Sorting Signals ; RNA Processing, Post-Transcriptional ; Saccharomyces cerevisiae/genetics
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  • 5
    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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  • 6
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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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  • 7
    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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  • 8
    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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  • 9
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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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  • 10
    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
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-08-19
    Description: The structural gene for group A streptococcal M protein, the fibrillar surface molecule enabling the organism to resist phagocytosis, has been cloned into Escherichia coli. The molecule produced by Escherichia coli is slightly larger than the M protein isolated by solubilization of the streptococcal cell wall, but is similar in size to that secreted by streptococcal protoplast and L forms. Immunologically, the molecule synthesized by Escherichia coli has the same type-specific determinants as the streptococcal M protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, J R -- Fischetti, V A -- AI11822/AI/NIAID NIH HHS/ -- RR05364/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):758-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6192499" target="_blank"〉PubMed〈/a〉
    Keywords: *Antigens, Bacterial ; *Bacterial Outer Membrane Proteins ; Bacterial Proteins/*genetics/immunology ; *Carrier Proteins ; Cloning, Molecular ; Epitopes ; Escherichia coli/*genetics ; Gene Expression Regulation ; Molecular Weight
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Comparison of two closely related primate papovaviruses, simian virus 40 (SV40) and human BK virus (BKV), reveals that the only region of extensive divergence, the tandem sequences adjacent to the origins of DNA replication, is responsible in SV40 for enhancing early gene expression. This study demonstrates a similar enhancer function for the analogous repeated region in BKV. The dissimilarity in sequence of the BKV and SV40 enhancer elements suggests that they may have been acquired since SV40 and BKV diverged. A locus cloned from the human genome homologous to the BKV tandem repeats has been shown to function as low level enhancer element in mammalian cells. These data support the hypothesis that viral enhancer sequences may be evolutionarily related to host cell sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenthal, N -- Kress, M -- Gruss, P -- Khoury, G -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):749-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BK Virus/*genetics ; Base Sequence ; Biological Evolution ; DNA, Viral/*genetics ; Gene Expression Regulation ; *Genes, Regulator ; Humans ; Plasmids ; Polyomavirus/*genetics ; Repetitive Sequences, Nucleic Acid ; Species Specificity
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  • 13
    Publication Date: 1983-06-03
    Description: In order to investigate the functions of stimulus recognition, signal transduction, and adaptation, the aspartate receptor gene for bacterial chemotaxis in Salmonella typhimurium has been sequenced and modified. A carboxyl-terminal truncated receptor was shown to bind aspartate and to transmit a signal to change motility behavior. However, the truncated receptor showed greatly reduced methyl-accepting capacity, and did not allow adaptation to the sensory stimulation. The separation of receptor functions by alteration of primary structure emphasizes that the receptor is directly involved in adaptation and is not solely a device for transmitting a signal across a membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russo, A F -- Koshland, D E Jr -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1016-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302843" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Aspartic Acid ; *Bacterial Physiological Phenomena ; Base Sequence ; *Chemotaxis ; Escherichia coli/physiology ; Methylation ; *Receptors, Amino Acid ; Receptors, Cell Surface/genetics/*physiology ; Salmonella typhimurium/physiology ; Serine
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-14
    Description: A modified cloning method designed to produce differential complementary DNA libraries permits the isolation of sequences that are present in the RNA population of any developmental stage or tissue, but are not present or are much less abundant in another stage or tissue. Selective complementary DNA cloning is especially useful when the differentially expressed RNA's are of low to moderate abundance in the cells in which they occur. A class of cytoplasmic polyadenylated RNA's differentially expressed in gastrula embryos of Xenopus laevis (DG RNA's) has been isolated. These DG RNA's occur very rarely or not at all in unfertilized eggs and blastulae, accumulate as the result of transcription before and during gastrulation, and, with some exceptions, decline in abundance as development proceeds. Many of these RNA molecules appear to be translated at the gastrula stage. Thus, DG RNA's may encode proteins that are important in the process of gastrulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sargent, T D -- Dawid, I B -- New York, N.Y. -- Science. 1983 Oct 14;222(4620):135-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6688681" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Gastrula/*physiology ; Gene Expression Regulation ; Nucleic Acid Hybridization ; Polyribosomes/metabolism ; Protein Biosynthesis ; Transcription, Genetic ; Xenopus laevis/*embryology/genetics
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  • 15
    Publication Date: 1983-08-19
    Description: A genomic clone consisting of the Moloney leukemia proviral genome with moderately repetitive mouse sequences was microinjected into the pronucleus of a mouse zygote. An animal was derived that carried multiple copies of proviral DNA in a tandem array. No evidence for homologous recombination was obtained. The viral genome was expressed in this animal and was transmitted as a single unit to its offspring. Subsequent breeding studies revealed that the proviral DNA had integrated on an X chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stewart, C -- Harbers, K -- Jahner, D -- Jaenisch, R -- New York, N.Y. -- Science. 1983 Aug 19;221(4612):760-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6683871" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/physiology ; Female ; Gene Expression Regulation ; Genes, Viral ; Mice ; Microinjections ; Moloney murine leukemia virus/*genetics ; Recombination, Genetic ; Sex Chromosomes/*physiology ; X Chromosome/*physiology
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
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  • 17
    Publication Date: 1983-10-28
    Description: Burkitt lymphoma cells carrying either a rearranged or unrearranged c-myc oncogene were examined with the use of probes from the 5' exon and for the second and third exon of the oncogene. The results indicate that the normal c-myc gene on chromosome 8 and the 5' noncoding and 3' coding segments of the c-myc oncogene separated by the chromosomal translocation are under different transcriptional control in the lymphoma cells. Burkitt lymphoma cells carrying a translocated but unrearranged c-myc oncogene express normal c-myc transcripts. In contrast, lymphoma cells carrying a c-myc gene rearranged head to head with the immunoglobulin constant mu region gene express c-myc transcripts lacking the normal untranslated leader.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉ar-Rushdi, A -- Nishikura, K -- Erikson, J -- Watt, R -- Rovera, G -- Croce, C M -- CA09171/CA/NCI NIH HHS/ -- CA10815/CA/NCI NIH HHS/ -- CA16685/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6414084" target="_blank"〉PubMed〈/a〉
    Keywords: Burkitt Lymphoma/*genetics ; Chromosomes, Human, 13-15 ; Chromosomes, Human, 19-20 ; Chromosomes, Human, 6-12 and X ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulin Heavy Chains/genetics ; *Oncogenes ; Operon ; Transcription, Genetic ; Translocation, Genetic
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  • 18
    Publication Date: 1983-09-23
    Description: A peptide that accumulated as the major product during the proteolysis of arginine vasopressin by rat brain synaptic membranes was isolated and its structure was shown to be the hexapeptide pGlu-Asn-Cys(Cys)-Pro-Arg-Gly-NH2. When administered intracerebroventricularly in extremely low doses, this vasopressin fragment and its desglycinamide derivative facilitated memory consolidation in a passive avoidance situation. These vasopressin metabolites, which are devoid of pressor activity, constitute highly potent neuropeptides with selective effects on memory and related processes; they are activated via proteolytic processing of vasopressin by brain peptidases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burbach, J P -- Kovacs, G L -- de Wied, D -- van Nispen, J W -- Greven, H M -- New York, N.Y. -- Science. 1983 Sep 23;221(4617):1310-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6351252" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/*metabolism/physiology ; Avoidance Learning/physiology ; Brain/*metabolism ; Dose-Response Relationship, Drug ; Male ; Memory/*physiology ; Oligopeptides/metabolism ; Peptide Hydrolases/metabolism ; Rats ; Structure-Activity Relationship
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  • 19
    Publication Date: 1983-07-15
    Description: The polymorphism of immune response genes plays a critical role in determining the immune capabilities of a particular individual. The molecular nature of this polymorphism was studied by examining the structure of the coding portions of three alleles of the I-A beta chain gene, an immune response gene whose protein product constitutes a subunit of the I-A molecule. Comparison of the I-A beta chains encoded by these alleles revealed an amino acid sequence divergence of 5 to 8 percent. The differences were found to be a series of short alterations clustered in the amino terminal half of the polypeptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, E -- McIntyre, K -- Germain, R N -- Seidman, J G -- AI18436/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):283-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6407114" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; *Genes, MHC Class II ; Histocompatibility Antigens Class II/immunology ; Humans ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; *Polymorphism, Genetic
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  • 20
    Publication Date: 1983-02-25
    Description: The locus for the cellular myc (c-myc) oncogene in humans is located on the region of chromosome 8 that is translocated to chromosome 14 in cells from most undifferentiated B-cell lymphomas. It is shown in this study that the c-myc locus is rearranged in 5 out of 15 cell lines from patients with undifferentiated B-cell lymphomas, and that the rearrangement involves a region at the 5' side of an apparently intact c-myc gene. In at least three patients, this rearranged region appears to contain immunoglobulin heavy chain mu sequences that are located on chromosome 14. The data indicate that this region contains the crossover point between chromosomes 8 and 14. The break point can occur at different positions on both chromosomes among individual cell lines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dalla-Favera, R -- Martinotti, S -- Gallo, R C -- Erikson, J -- Croce, C M -- New York, N.Y. -- Science. 1983 Feb 25;219(4587):963-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6401867" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Cell Differentiation ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Genetic Linkage ; Humans ; Immunoglobulin Constant Regions/genetics ; Immunoglobulin Heavy Chains/genetics ; Lymphoma/*genetics ; *Oncogenes ; Recombination, Genetic
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  • 21
    Publication Date: 1983-09-30
    Description: The near identity of the partial amino acid sequence of human platelet-derived growth factor (PDGF) and that predicted for p28sis, the putative transforming protein of the simian sarcoma virus (SSV), suggests expression of a growth factor activity may be central for transformation by SSV. It is now reported that SSV-transformed cells but not control cells contain a growth factor activity that is identical to PDGF in immunoassay, in mitogenic dose response, and in specific mitogenic activity. The protein immunoprecipitated by antiserum to human PDGF has an apparent molecular weight of 20,000, identical to that of p20sis, the putative intracellular degradation product of p28sis. The results support the concept that expression of a PDGF-like molecule, which appears to be the product of the viral-sis gene, is responsible for the abnormal regulation of growth is SSV-transformed cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deuel, T F -- Huang, J S -- Huang, S S -- Stroobant, P -- Waterfield, M D -- New York, N.Y. -- Science. 1983 Sep 30;221(4618):1348-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6310754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Cell Transformation, Viral ; Cross Reactions ; DNA Replication/drug effects ; *Genes, Viral ; Growth Substances/*genetics/immunology ; Mice ; Molecular Weight ; Peptides/*genetics/immunology ; Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics ; Sarcoma, Experimental/*physiopathology
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-28
    Description: The recently reported amino acid sequence of rat angiotensinogen was subjected to a computer-assisted search for homology with known sequences stored in a data bank and found to be significantly related to that of plasma alpha 1-antitrypsin, itself a member of a family that includes antithrombin III and ovalbumin. An alignment of the four sequences shows indisputably the common ancestry of all four proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- RR 00757/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):417-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6604942" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiotensinogen/*genetics ; Angiotensins/*genetics ; Animals ; Antithrombins/genetics ; *Biological Evolution ; Macromolecular Substances ; Ovalbumin/genetics ; Rats ; alpha 1-Antitrypsin/genetics
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  • 23
    Publication Date: 1983-10-28
    Description: Antiserum to a synthetic peptide corresponding to the carboxyl-terminus of the human c-myc protein immunoprecipitated a 48,000-dalton protein from a number of normal and malignant human and mouse cells. The size of the protein is consistent with the potential coding region predicted from the c-myc nucleotide sequence, and is the same for malignant cells carrying either a rearranged or an unrearranged c-myc oncogene. Because c-myc transcripts are expressed at higher levels in malignant than in normal B cells, it appears that an increased level of the c-myc protein rather than a change in the gene product is the relevant factor in determining transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giallongo, A -- Appella, E -- Ricciardi, R -- Rovera, G -- Croce, C M -- CA10815/CA/NCI NIH HHS/ -- CA16685/CA/NCI NIH HHS/ -- CA25685/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Oct 28;222(4622):430-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6604943" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/*physiology ; Burkitt Lymphoma/*genetics ; Gene Expression Regulation ; Humans ; *Oncogenes ; Peptide Fragments/immunology ; Proteins/immunology/*isolation & purification ; Transformation, Genetic
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Class III genes require multiple cellular factors for transcription by RNA polymerase III; these genes form stable transcription complexes, which in the case of Xenopus 5S genes are correlated with differential expression in vivo. The minimal number and identity of the factors required to form both stable and metastable complexes on three class III genes (encoding, respectively, 5S RNA, transfer RNA, and adenovirus VA RNA species) were determined. Stable complex formation requires one common factor, whose recognition site was analyzed, and either no additional factors (the VA gene), a second common factor (the transfer RNA gene), or a third gene-specific factor (the 5S gene). The mechanism of stable complex formation and its relevance to transcriptional regulation were examined in light of the various factors and the promoter sequences recognized by these factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lassar, A B -- Martin, P L -- Roeder, R G -- CA 24223/CA/NCI NIH HHS/ -- CA 24891/CA/NCI NIH HHS/ -- GM07200/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):740-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA-Directed RNA Polymerases/*genetics ; Eukaryotic Cells/physiology ; Gene Expression Regulation ; Genes ; Humans ; Operon ; RNA Polymerase III/*genetics ; RNA, Ribosomal/genetics ; RNA, Transfer/genetics ; RNA, Viral/genetics ; Transcription Factors/genetics ; *Transcription, Genetic
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-09-02
    Description: Development proceeds by way of a discrete yet overlapping series of biosynthetic and restructuring events that result in the continued molding of tissues and organs into highly restricted and specialized states required for adult function. Individual molecules and cells are replaced by molecular and cellular variants, called isoforms; these arise and function during embryonic development or later life. Isoforms, whether molecular or cellular, have been identified by their structural differences, which allow separation and characterization of each variant. These isoforms play a central and controlling role in the continued and dynamic remodeling that takes place during development. Descriptions of the individual phases of the orderly replacement of one isoform for another provides an experimental context in which the process of development can be better understood.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caplan, A I -- Fiszman, M Y -- Eppenberger, H M -- New York, N.Y. -- Science. 1983 Sep 2;221(4614):921-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348946" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Animals ; Bone Development ; Cartilage/*embryology ; Cell Differentiation ; Creatine Kinase/physiology ; Extracellular Space/physiology ; Gene Expression Regulation ; Humans ; Muscle Contraction ; Muscles/cytology/*embryology ; Myosins/physiology ; Phosphoproteins/physiology ; Proteoglycans/physiology
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  • 26
    Publication Date: 1983-08-26
    Description: The complete nucleotide sequence of the diphtheria tox228 gene encoding the nontoxic serologically related protein CRM228 has been determined. A comparison of the predicted amino acid sequence with the available amino acid sequences from the wild-type toxin made it possible to deduce essentially the entire nucleotide sequence of the wild-type tox gene. The signal peptide of pro-diphtheria toxin and the putative tox promoter have been identified, a highly symmetrical nucleotide sequence downstream of the toxin gene has been detected; this region may be the corynebacteriophage beta attachment site (attP). The cloned toxin gene was expressed at a low level in Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaczorek, M -- Delpeyroux, F -- Chenciner, N -- Streeck, R E -- Murphy, J R -- Boquet, P -- Tiollais, P -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):855-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348945" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; Diphtheria Toxin/*genetics ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; Nucleic Acid Conformation ; Operon
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-11-18
    Description: Two dozen cellular proto-oncogenes have been discovered to date through the study of retroviruses and the use of gene transfer. They form a structurally and functionally heterogeneous group. At least five distinct mechanisms are responsible for their conversion to active oncogenes. Recent work provides experimental strategies by which many of these oncogenes, as well as oncogenes of DNA tumor viruses, may be placed into functional categories. These procedures may lead to definition of a small number of common pathways through which the various oncogenes act to transform cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Land, H -- Parada, L F -- Weinberg, R A -- CA14051/CA/NCI NIH HHS/ -- CA26717/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):771-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356358" target="_blank"〉PubMed〈/a〉
    Keywords: Gene Expression Regulation ; Genes, Viral ; Humans ; Neoplasms/*etiology/genetics ; *Oncogenes ; Retroviridae/*genetics ; Tissue Distribution ; Transfection
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-07-08
    Description: The nucleotide sequence of the oncogene of the Rasheed strain of rat sarcoma virus was determined. The oncogene (Ra-v-ras) encodes a 29,000-dalton (p29) transforming protein. This protein is distinct from the immunologically related 21,000-dalton protein (p21) of the Harvey murine sarcoma virus in its amino terminus and in having additional mutations in its carboxyl terminus. Although the functional significance of these changes is unknown, they appear to occur only in rat sarcoma virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasheed, S -- Norman, G L -- Heidecker, G -- CA 27246/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 8;221(4606):155-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344220" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Proto-Oncogene Proteins p21(ras) ; Rats ; Retroviridae/*genetics
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-06-03
    Description: The nucleotide sequence of the T24 human bladder carcinoma oncogene was determined, and the coding and noncoding sequences of the genome were identified. The amino acid sequence of p21, the translational product of the T24 oncogene, was predicted from the nucleotide sequence of the oncogene. Comparison of this sequence with that of the normal cellular homolog showed that a single point mutation in the coding sequences of the T24 oncogene resulted in the acquisition of transforming properties. Other differences between the T24 oncogene and its normal cellular homolog were found in the 5' noncoding and 3' noncoding sequences, but these differences appear to be due to polymorphism and do not play a significant role in the transformation process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- New York, N.Y. -- Science. 1983 Jun 3;220(4601):1061-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6844927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma/*genetics ; Cell Transformation, Neoplastic/metabolism ; Humans ; Mice ; Neoplasm Proteins/genetics ; *Oncogenes ; Oncogenic Viruses/genetics ; Rats ; Urinary Bladder Neoplasms/*genetics
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  • 30
    Publication Date: 1983-05-13
    Description: A recombinant bacterial plasmid, pMS1, was constructed that contains 318 nucleotides complementary to a portion of pro-opiolipomelanocortin (proOLMC) messenger RNA from an ectopic adrenocorticotropin-producing tumor. The cloned complementary DNA insert, which contains the sequence that codes for all of the beta-melanocyte-stimulating hormone and beta-endorphin portions of proOLMC, as well as the 3' nontranslated section, is identical to the genomic sequence. Hybridization of tumor proOLMC complementary DNA to RNA subjected to electrophoresis and transferred to a nitrocellulose filter revealed two proOLMC messenger RNA species in the tumor polyadenylated RNA, but only one in pituitary polyadenylated RNA. At least one of the tumor proOLMC messenger RNA's is similar, if not identical, to human pituitary proOLMC messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeBold, C R -- Schworer, M E -- Connor, T B -- Bird, R E -- Orth, D N -- 2-R01-GM25526/GM/NIGMS NIH HHS/ -- 5-R01-CA11685/CA/NCI NIH HHS/ -- 5-R25-CA19429/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 May 13;220(4598):721-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6301015" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carcinoid Tumor/physiopathology ; Cloning, Molecular ; DNA, Neoplasm/genetics ; DNA, Recombinant/*metabolism ; Endorphins/*genetics ; Hormones, Ectopic/*genetics ; Humans ; Male ; Melanocyte-Stimulating Hormones/*genetics ; Middle Aged ; Pancreatic Neoplasms/physiopathology ; Pituitary Hormones, Anterior/*genetics ; Pro-Opiomelanocortin ; Protein Precursors/*genetics ; RNA, Messenger/genetics ; beta-Endorphin
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  • 31
    Publication Date: 1983-07-15
    Description: The transforming protein of a primate sarcoma virus and a platelet-derived growth factor are derived from the same or closely related cellular genes. This conclusion is based on the demonstration of extensive sequence similarity between the transforming protein derived from the simian sarcoma virus onc gene, v-sis, and a human platelet-derived growth factor. The mechanism by which v-sis transforms cells could involve the constitutive expression of a protein with functions similar or identical to those of a factor active transiently during normal cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doolittle, R F -- Hunkapiller, M W -- Hood, L E -- Devare, S G -- Robbins, K C -- Aaronson, S A -- Antoniades, H N -- CA30101/CA/NCI NIH HHS/ -- RR00757/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 15;221(4607):275-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6304883" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cebidae ; Cell Transformation, Neoplastic/metabolism ; Genes ; Growth Substances/*genetics/physiology ; Humans ; *Oncogenes ; Peptides/*genetics/physiology ; Platelet-Derived Growth Factor ; Retroviridae/*genetics ; Sarcoma Virus, Woolly Monkey/*genetics
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  • 32
    Publication Date: 1983-08-26
    Description: The gene for the Harvey murine sarcoma virus (Ha-MuSV) p21ras protein was fused to the amino-terminal portion of the bacteriophage lambda cII gene on the expression vector pJL6. The fusion was such that transcription was controlled by the well-regulated phage lambda pL promoter, and translation initiated in the cII gene continued in frame into the ras gene sequences that code for p21. When the pL promoter was derepressed, the Escherichia coli cells harboring the fusion plasmid synthesized 23,000-dalton protein, which represented more than 10 percent of the total cellular protein. This protein was chimeric and contained 14 residues, which were specified by the vector; these residues were followed by all of the amino acids that make up Ha-MuSV p21ras except for four residues at the amino-terminal end. The protein appears similar to Ha-MuSV p21ras in that it undergoes immunoprecipitation by monoclonal antibodies directed toward that protein, binds guanosine diphosphate, and is capable of autophosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lautenberger, J A -- Ulsh, L -- Shih, T Y -- Papas, T S -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):858-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308763" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Transformation, Viral ; Escherichia coli/genetics ; Gene Expression Regulation ; Molecular Weight ; *Oncogenes ; Plasmids ; Sarcoma Viruses, Murine/enzymology/*genetics ; Viral Proteins/*genetics
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  • 33
    Publication Date: 1983-11-18
    Description: The characteristic chromosomal translocations that occur in certain human malignancies offer opportunities to understand how two gene systems can affect one another when they are accidentally juxtaposed. In the case of Burkitt lymphoma, such a translocation joins the cellular oncogene, c-myc, to a region encoding one of the immunoglobulin genes. In at least one example, the coding sequence of the rearranged c-myc gene is identical to that of the normal gene, implying that the gene must be quantitatively, rather than qualitatively, altered in its expression if it is to play a role in transformation. One might expect to find the rearranged c-myc gene in a configuration that would allow it to take advantage of one of the known immunoglobulin promoters or enhancer elements. However, the rearranged c-myc gene is often placed so that it can utilize neither of these structures. Since the level of c-myc messenger RNA is often elevated in Burkitt cells, the translocation may lead to a deregulation of the c-myc gene. Further, since the normal allele in a Burkitt cell is often transcriptionally silent in the presence of a rearranged allele, a model for c-myc regulation is suggested that involves a trans-acting negative control element that might use as its target a highly conserved portion of the c-myc gene encoding two discrete transcriptional promoters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leder, P -- Battey, J -- Lenoir, G -- Moulding, C -- Murphy, W -- Potter, H -- Stewart, T -- Taub, R -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):765-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356357" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Burkitt Lymphoma/*genetics ; Cell Transformation, Neoplastic/etiology ; Chromosome Aberrations/*genetics ; Chromosome Disorders ; Chromosome Mapping ; Gene Expression Regulation ; Genes ; Humans ; Immunoglobulins/genetics ; Models, Biological ; Neoplasms/*genetics ; *Oncogenes ; *Translocation, Genetic
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  • 34
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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〉Marx, J L -- New York, N.Y. -- Science. 1983 Mar 4;219(4588):1055-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6823566" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Genes ; Receptors, Cholinergic/*genetics ; Torpedo
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  • 35
    Publication Date: 1983-11-18
    Description: Synapses between neuroblastoma-hybrid cells and myotubes exhibit a high degree of plasticity. Increase of cyclic adenosine monophosphate (AMP) levels of the hybrid cells for several days results in the appearance of functional voltage-sensitive Ca2+ channels, which are required for evoked secretion of acetylcholine. The results show that cyclic AMP regulates synaptogenesis by regulating the expression of voltage-sensitive Ca2+ channels, and suggest that cyclic AMP affects posttranslational modifications of some glycoproteins and cellular levels of certain proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nirenberg, M -- Wilson, S -- Higashida, H -- Rotter, A -- Krueger, K -- Busis, N -- Ray, R -- Kenimer, J G -- Adler, M -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):794-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6314503" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Calcium/physiology ; Cell Adhesion ; Cells, Cultured ; Cyclic AMP/*physiology ; Gene Expression Regulation ; Humans ; Membrane Potentials ; Nerve Tissue Proteins/physiology ; Neuromuscular Junction/*physiology ; Neuronal Plasticity ; Receptors, Cell Surface/physiology ; Retina/*physiology ; Synapses/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 36
    Publication Date: 1983-09-02
    Description: Human fetal muscles at ages 110, 125, and 132 days contain a fetal-specific myosin light chain. This light chain is absent in adult human muscle, copurifies with myosin, and is identified as a slow light chain because it reacts with purified antibody to chicken slow muscle light chains and does not react strongly with antibody to fast myosin light chains. This light chain is synthesized in cultures of fetal muscle along with normal myosin light chains. The presence of a fetal light chain in culture provides a marker for studies of human muscle disease in which it is important to know when or if the muscle makes a transition from embryonic or fetal expression to true adult phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strohman, R C -- Micou-Eastwood, J -- Glass, C A -- Matsuda, R -- New York, N.Y. -- Science. 1983 Sep 2;221(4614):955-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6879193" target="_blank"〉PubMed〈/a〉
    Keywords: Fetus/physiology ; Gene Expression Regulation ; Humans ; Muscles/*embryology ; Myosins/*biosynthesis/genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 37
    Publication Date: 1983-11-18
    Description: Three mutations of the enzyme dihydrofolate reductase were constructed by oligonucleotide-directed mutagenesis of the cloned Escherichia coli gene. The mutations--at residue 27, aspartic acid replaced with asparagine; at residue 39, proline replaced with cysteine; and at residue 95, glycine replaced with alanine--were designed to answer questions about the relations between molecular structure and function that were raised by the x-ray crystal structures. Properties of the mutant proteins show that Asp-27 is important for catalysis and that perturbation of the local structure at a conserved cis peptide bond following Gly-95 abolishes activity. Substitution of cysteine for proline at residue 39 results in the appearance of new forms of the enzyme that correspond to various oxidation states of the cysteine. One of these forms probably represents a species cross-linked by an intrachain disulfide bridge between the cysteine at position 85 and the new cysteine at position 39.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Villafranca, J E -- Howell, E E -- Voet, D H -- Strobel, M S -- Ogden, R C -- Abelson, J N -- Kraut, J -- CA17374/CA/NCI NIH HHS/ -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):782-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356360" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Disulfides ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/*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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