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  • Articles  (1,913)
  • Polymer and Materials Science  (1,607)
  • Chemical Engineering  (228)
  • Amino Acid Sequence  (78)
  • 1985-1989  (1,913)
  • 1950-1954
  • 1945-1949
  • 1988  (1,913)
  • Physics  (1,913)
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  • Articles  (1,913)
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  • 1985-1989  (1,913)
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  • 1
    Publication Date: 1988-07-15
    Description: Odorant-binding protein (OBP) is found in nasal epithelium, and it selectively binds odorants. Three complementary DNAs encoding rat odorant-binding protein have now been cloned and sequenced. One clone contains an open reading frame predicted to encode an 18,091-dalton protein. RNA blot analysis confirms the localization of OBP messenger RNA in the nasal epithelium. This OBP has 33 percent amino acid identity to alpha 2-microglobulin, a secreted plasma protein. Other members of an alpha 2-microglobulin superfamily bind and transport hydrophobic ligands. Thus, OBP probably binds and carries odorants within the nasal epithelium to putative olfactory receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pevsner, J -- Reed, R R -- Feinstein, P G -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- GM-07626/GM/NIGMS NIH HHS/ -- P01 CA16519-13/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):336-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388043" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*genetics ; Cloning, Molecular ; Ligands ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nasal Mucosa/*physiology ; Rats ; *Receptors, Odorant ; Smell/*physiology
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-06-17
    Description: The alpha helix, first proposed by Pauling and co-workers, is a hallmark of protein structure, and much effort has been directed toward understanding which sequences can form helices. The helix hypothesis, introduced here, provides a tentative answer to this question. The hypothesis states that a necessary condition for helix formation is the presence of residues flanking the helix termini whose side chains can form hydrogen bonds with the initial four-helix greater than N-H groups and final four-helix greater than C-O groups; these eight groups would otherwise lack intrahelical partners. This simple hypothesis implies the existence of a stereochemical code in which certain sequences have the hydrogen-bonding capacity to function as helix boundaries and thereby enable the helix to form autonomously. The three-dimensional structure of a protein is a consequence of the genetic code, but the rules relating sequence to structure are still unknown. The ensuing analysis supports the idea that a stereochemical code for the alpha helix resides in its boundary residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Presta, L G -- Rose, G D -- AG 06084/AG/NIA NIH HHS/ -- GM 29458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1632-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Hershey Medical Center, Pennsylvania State University, Hershey 17033.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2837824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carboxypeptidases ; Carboxypeptidases A ; Cytochrome c Group ; Flavodoxin ; Humans ; Hydrogen Bonding ; Models, Chemical ; Molecular Sequence Data ; Muramidase ; Myoglobin ; Pancreatic Polypeptide ; Parvalbumins ; Plastocyanin ; *Protein Conformation ; Ribonucleases ; Scorpion Venoms ; Tetrahydrofolate Dehydrogenase ; Triose-Phosphate Isomerase ; Trypsin Inhibitors ; X-Ray Diffraction
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-08-19
    Description: The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- DeGrado, W F -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):976-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research & Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; Chromatography, Gel ; Escherichia coli/genetics ; Molecular Sequence Data ; Plasmids ; *Protein Conformation ; *Proteins/genetics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-06-17
    Description: A definition based on alpha-carbon positions and a sample of 215 alpha helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richardson, J S -- Richardson, D C -- GM-15000/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1648-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3381086" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acids ; Asparagine ; Hydrogen Bonding ; Proline ; *Protein Conformation
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  • 5
    Publication Date: 1988-07-01
    Description: A method of combinatorial cassette mutagenesis was designed to readily determine the informational content of individual residues in protein sequences. The technique consists of simultaneously randomizing two or three positions by oligonucleotide cassette mutagenesis, selecting for functional protein, and then sequencing to determine the spectrum of allowable substitutions at each position. Repeated application of this method to the dimer interface of the DNA-binding domain of lambda repressor reveals that the number and type of substitutions allowed at each position are extremely variable. At some positions only one or two residues are functionally acceptable; at other positions a wide range of residues and residue types are tolerated. The number of substitutions allowed at each position roughly correlates with the solvent accessibility of the wild-type side chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reidhaar-Olson, J F -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):53-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388019" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Codon ; DNA/genetics/metabolism ; *DNA-Binding Proteins ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Plasmids ; Protein Conformation ; Repressor Proteins/*genetics ; Structure-Activity Relationship ; Transcription Factors/*genetics ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 6
    Publication Date: 1988-08-05
    Description: The human pS2 gene is specifically expressed under estrogen transcriptional control in a subclass of estrogen receptor-containing human breast cancer cells. The pS2 gene encodes an 84-amino acid protein that is secreted after signal peptide cleavage. The distribution of pS2 protein in normal human tissues was studied with antibodies to pS2; pS2 was specifically expressed and secreted by mucosa cells of the normal stomach antrum and body of both female and male individuals. Moreover, no estrogen receptor could be detected in these cells, indicating that pS2 gene expression is estrogen-independent in the stomach. The function of the pS2 protein in the gastrointestinal tract is unknown. However, the pS2 protein is similar in sequence to a porcine pancreatic protein that has been shown to inhibit gastrointestinal motility and gastric secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rio, M C -- Bellocq, J P -- Daniel, J Y -- Tomasetto, C -- Lathe, R -- Chenard, M P -- Batzenschlager, A -- Chambon, P -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):705-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS et U. 184 de l'INSERM, Institut de Chimie Biologique, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041593" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Breast Neoplasms/*metabolism ; Estrogens/pharmacology ; Exons ; Female ; Gastric Mucosa/*metabolism ; *Gene Expression Regulation ; Histocytochemistry ; Humans ; Immunoenzyme Techniques ; Male ; Molecular Sequence Data ; Neoplasm Proteins/*biosynthesis/genetics/secretion ; *Proteins ; RNA, Messenger/metabolism ; Receptors, Estrogen/metabolism ; Sequence Homology, Nucleic Acid ; Tissue Distribution ; Tumor Cells, Cultured ; Tumor Suppressor Proteins
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-11-18
    Description: A rat kidney messenger RNA that induces a slowly activating, voltage-dependent potassium current on its expression in Xenopus oocytes was identified by combining molecular cloning with an electrophysiological assay. The cloned complementary DNA encodes a novel membrane protein that consists of 130 amino acids with a single putative transmembrane domain. This protein differs from the known ion channel proteins but is involved in the induction of selective permeation of potassium ions by membrane depolarization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takumi, T -- Ohkubo, H -- Nakanishi, S -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Immunology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Electric Conductivity ; Membrane Potentials ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Potassium Channels/*physiology ; Rats ; Xenopus laevis
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  • 8
    Publication Date: 1988-05-20
    Description: Class II major histocompatibility (MHC) molecules have an immunoregulatory role. These cell-surface glycoproteins present fragments of protein antigens (or peptides) to thymus-derived lymphocytes (T cells). Nucleotide sequence polymorphism in the genes that encode the class II MHC products determines the specificity of the immune response and is correlated with the development of autoimmune diseases. This study identifies certain class II polymorphic amino acid residues that are strongly associated with susceptibility to insulin-dependent diabetes mellitus, rheumatoid arthritis, and pemphigus vulgaris. These findings implicate particular class II MHC isotypes in susceptibility to each disease and suggest new prophylactic and therapeutic strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todd, J A -- Acha-Orbea, H -- Bell, J I -- Chao, N -- Fronek, Z -- Jacob, C O -- McDermott, M -- Sinha, A A -- Timmerman, L -- Steinman, L -- New York, N.Y. -- Science. 1988 May 20;240(4855):1003-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3368786" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arthritis, Rheumatoid/immunology ; Autoantibodies/*genetics ; Autoimmune Diseases/*genetics ; Diabetes Mellitus, Type 1/immunology ; HLA-D Antigens/*genetics ; Humans ; Major Histocompatibility Complex ; Molecular Sequence Data ; Pemphigus/immunology
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  • 9
    Publication Date: 1988-09-23
    Description: Antibodies directed against a conserved intracellular segment of the sodium channel alpha subunit slow the inactivation of sodium channels in rat muscle cells. Of four site-directed antibodies tested, only antibodies against the short intracellular segment between homologous transmembrane domains III and IV slowed inactivation, and their effects were blocked by the corresponding peptide antigen. No effects on the voltage dependence of sodium channel activation or of steady-state inactivation were observed, but the rate of onset of the antibody effect and the extent of slowing of inactivation were voltage-dependent. Antibody binding was more rapid at negative potentials, at which sodium channels are not inactivated; antibody-induced slowing of inactivation was greater during depolarizations to more positive membrane potentials. The peptide segment recognized by this antibody appears to participate directly in rapid sodium channel inactivation during large depolarizations and to undergo a conformational change that reduces its accessibility to antibodies as the channel inactivates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vassilev, P M -- Scheuer, T -- Catterall, W A -- NS 15751/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458625" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies ; Cytoplasm/analysis ; In Vitro Techniques ; Ion Channels/*metabolism ; Membrane Potentials ; Molecular Sequence Data ; Peptides/*metabolism ; Rats ; Sodium/*metabolism
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  • 10
    Publication Date: 1988-12-23
    Description: The ras p21 GTPase-activating protein (GAP) was purified from human placental tissue. Internal amino acid sequence was obtained from this 120,000-dalton protein and, by means of this sequence, two types of complementary DNA clones were isolated and characterized. One type encoded GAP with a predicted molecular mass of 116,000 daltons and 96% identity with bovine GAP. The messenger RNA of this GAP was detected in human lung, brain, liver, leukocytes, and placenta. The second type appeared to be generated by a differential splicing mechanism and encoded a novel form of GAP with a predicted molecular mass of 100,400 daltons. This protein lacks the hydrophobic amino terminus characteristic of the larger species, but retains GAP activity. The messenger RNA of this type was abundantly expressed in placenta and in several human cell lines, but not in adult tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trahey, M -- Wong, G -- Halenbeck, R -- Rubinfeld, B -- Martin, G A -- Ladner, M -- Long, C M -- Crosier, W J -- Watt, K -- Koths, K -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1697-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corp., Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Brain Chemistry ; *Cloning, Molecular ; DNA/*genetics/isolation & purification ; Female ; GTPase-Activating Proteins ; Gene Expression Regulation ; Humans ; Leukocytes/analysis ; Liver/analysis ; Lung/analysis ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Placenta/*analysis ; Pregnancy ; Proteins/*genetics/isolation & purification ; RNA, Messenger/analysis/genetics ; Sequence Homology, Nucleic Acid ; ras GTPase-Activating Proteins
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  • 11
    Publication Date: 1988-04-15
    Description: A new type of agonist-binding subunit of rat neuronal nicotinic acetylcholine receptors (nAChRs) was identified. Rat genomic DNA and complementary DNA encoding this subunit (alpha 2) were cloned and analyzed. Complementary DNA expression studies in Xenopus oocytes revealed that the injection of messenger RNAs (mRNAs) for alpha 2 and beta 2 (a neuronal nAChR subunit) led to the generation of a functional nAChR. In contrast to the other known neuronal nAChRs, the receptor produced by the injection of alpha 2 and beta 2 mRNAs was resistant to the alpha-neurotoxin Bgt3.1. In situ hybridization histochemistry showed that alpha 2 mRNA was expressed in a small number of regions, in contrast to the wide distribution of the other known agonist-binding subunits (alpha 3 and alpha 4) mRNAs. These results demonstrate that the alpha 2 subunit differs from other known agonist-binding alpha-subunits of nAChRs in its distribution in the brain and in its pharmacology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wada, K -- Ballivet, M -- Boulter, J -- Connolly, J -- Wada, E -- Deneris, E S -- Swanson, L W -- Heinemann, S -- Patrick, J -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):330-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832952" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*metabolism ; DNA Restriction Enzymes ; Female ; *Genes ; Molecular Sequence Data ; Neurons/metabolism ; Nucleotide Mapping ; Oocytes/metabolism ; Rats ; Receptors, Nicotinic/*genetics/metabolism ; Transcription, Genetic ; Xenopus laevis
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  • 12
    Publication Date: 1988-04-29
    Description: Zeins, the storage proteins of maize, are totally lacking in the essential amino acids lysine and tryptophan. Lysine codons and lysine- and tryptophan-encoding oligonucleotides were introduced at several positions into a 19-kilodalton zein complementary DNA by oligonucleotide-mediated mutagenesis. A 450-base pair open reading frame from a simian virus 40 (SV40) coat protein was also engineered into the zein coding region. Messenger RNAs for the modified zeins were synthesized in vitro with an SP6 RNA polymerase system and injected into Xenopus laevis oocytes. The modifications did not affect the translation, signal peptide cleavage, or stability of the zeins. The ability of the modified zeins to assemble into structures similar to maize protein bodies was assayed by two criteria: assembly into membrane-bound vesicles resistant to exogenously added protease, and ability to self-aggregate into dense structures. All of the modified zeins were membrane-bound; only the one containing a 17-kilodalton SV40 protein fragment was unable to aggregate. These findings suggest that it may be possible to create high-lysine corn by genetic engineering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, J C -- Galili, G -- Kawata, E E -- Cuellar, R E -- Shotwell, M A -- Larkins, B A -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):662-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/metabolism ; DNA/genetics ; DNA, Recombinant ; Female ; Genetic Engineering ; *Lysine/genetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Oocytes/*metabolism ; Peptide Hydrolases/metabolism ; RNA, Messenger/genetics ; Simian virus 40/genetics ; Xenopus laevis ; Zea mays ; Zein/genetics/*metabolism
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-08-05
    Description: Although the proteinase inhibitor alpha-2-antiplasmin (alpha 2AP) is known to control the activity of plasmin through rapid formation of stable complexes, it also efficiently inactivates chymotrypsin. These interactions are shown to occur at adjacent, overlapping sites so that plasmin attacks the inhibitor at an Arg364-Met365 peptide bond, while chymotrypsin interacts at a Met365-Ser366 sequence one residue downstream. Thus, a naturally occurring plasma serine proteinase inhibitor can have multiple specificities through interactions at adjacent sites. It also illustrates the potential flexibility of the reactive site loop in this class of inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potempa, J -- Shieh, B H -- Travis, J -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):699-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2456616" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Carboxypeptidase B ; Carboxypeptidases/metabolism ; Carboxypeptidases A ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chymotrypsin/antagonists & inhibitors/metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Molecular Sequence Data ; Peptide Fragments/metabolism ; Protease Inhibitors ; alpha-2-Antiplasmin/*metabolism
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  • 14
    Publication Date: 1988-07-22
    Description: The parasitic protozoon Trypanosoma brucei contains a highly organized membrane skeleton, consisting of a dense array of parallel, singlet microtubules that are laterally interconnected and that are also in tight contact with the overlying cell membrane. A high molecular weight, heat-stable protein from this membrane skeleton was isolated that is localized along the microtubules. Protease digestion experiments and sequencing of a cloned gene segment showed that most of the protein is built up by more than 50 nearly identical tandem repeats with a periodicity of 38 amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, A -- Hemphill, A -- Wyler, T -- Seebeck, T -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur allgemeine Mikrobiologie, Universitat Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3393912" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Compartmentation ; Cell Membrane/ultrastructure ; Cloning, Molecular ; Microscopy, Electron ; Microtubule-Associated Proteins/*analysis/genetics ; Microtubules/ultrastructure ; Molecular Sequence Data ; Molecular Weight ; Repetitive Sequences, Nucleic Acid ; Trypanosoma brucei brucei/*analysis/genetics/ultrastructure
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  • 15
    Publication Date: 1988-07-08
    Description: The amyloid beta protein peptide is a major constituent of amyloid plaque cores in Alzheimer's disease and is apparently derived from a higher molecular weight precursor. It is now shown that the core protein of a heparan sulfate proteoglycan secreted from a nerve cell line (PC12) has an amino acid sequence and a size very similar to those of the amyloid beta protein precursor and that these molecules are antigenically related. This amyloid beta protein precursor-related protein is not found in the conditioned medium of a variant cell line (F3 PC12) that does not secrete heparan sulfate proteoglycan. The synaptic localization and metabolism of this class of proteoglycans are consistent with its potential involvement in central nervous system dysfunction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schubert, D -- Schroeder, R -- LaCorbiere, M -- Saitoh, T -- Cole, G -- AG 05131/AG/NIA NIH HHS/ -- F2 AG 05424A/AG/NIA NIH HHS/ -- NS 09658/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2968652" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amino Acid Sequence ; Amyloid/*metabolism ; Amyloid beta-Peptides ; Animals ; Cell Line ; Chondroitin Sulfate Proteoglycans/*metabolism ; Chromatography, High Pressure Liquid ; Glycosaminoglycans/*metabolism ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate/*metabolism ; Immunologic Techniques ; Peptide Fragments ; Proteoglycans/*metabolism ; Rats ; Viral Core Proteins/*metabolism
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  • 16
    Publication Date: 1988-08-12
    Description: Interleukin-6 (IL-6/BSF-2/IFN beta 2) is a multifunctional cytokine that regulates the growth and differentiation of various tissues, and is known particularly for its role in the immune response and acute phase reactions. A complementary DNA encoding the human IL-6 receptor (IL-6-R) has now been isolated. The IL-6-R consists of 468 amino acids, including a signal peptide of approximately 19 amino acids and a domain of approximately 90 amino acids that is similar to a domain in the immunoglobulin (Ig) superfamily. The cytoplasmic domain of approximately 82 amino acids lacks a tyrosine/kinase domain, unlike other growth factor receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamasaki, K -- Taga, T -- Hirata, Y -- Yawata, H -- Kawanishi, Y -- Seed, B -- Taniguchi, T -- Hirano, T -- Kishimoto, T -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):825-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3136546" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Cloning, Molecular ; DNA/genetics/isolation & purification ; *Genes ; Humans ; Immunoglobulin kappa-Chains/genetics ; Molecular Sequence Data ; Receptors, Immunologic/genetics ; Receptors, Interleukin-6 ; Sequence Homology, Nucleic Acid ; *Transcription, Genetic
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  • 17
    Publication Date: 1988-05-06
    Description: A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser. Epstein-Barr virus-transformed lymphocytes from this patient synthesize an insulin receptor precursor that is normally glycosylated and inserted into the plasma membrane but is not cleaved to mature alpha and beta subunits. Insulin binding to these cells is severely reduced but can be increased about fivefold by gentle treatment with trypsin, accompanied by the appearance of normal alpha subunits. These results indicate that proteolysis of the proreceptor is necessary for its normal full insulin-binding sensitivity and signal-transducing activity and that a cellular protease that is more stringent in its specificity than trypsin is required to process the receptor precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshimasa, Y -- Seino, S -- Whittaker, J -- Kakehi, T -- Kosaki, A -- Kuzuya, H -- Imura, H -- Bell, G I -- Steiner, D F -- AM 13914/AM/NIADDK NIH HHS/ -- AM 20595/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1988 May 6;240(4853):784-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283938" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; DNA/genetics ; Diabetes Mellitus/*genetics/metabolism ; Female ; Glycosylation ; Humans ; Insulin/metabolism ; Insulin Resistance/*genetics ; Lymphocytes/metabolism ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Protein Precursors/*genetics/metabolism ; RNA, Messenger/metabolism ; Receptor, Insulin/*genetics/metabolism ; Trypsin/metabolism
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  • 18
    Publication Date: 1988-12-16
    Description: Protein extracts derived from bone can initiate the process that begins with cartilage formation and ends in de novo bone formation. The critical components of this extract, termed bone morphogenetic protein (BMP), that direct cartilage and bone formation as well as the constitutive elements supplied by the animal during this process have long remained unclear. Amino acid sequence has been derived from a highly purified preparation of BMP from bovine bone. Now, human complementary DNA clones corresponding to three polypeptides present in this BMP preparation have been isolated, and expression of the recombinant human proteins have been obtained. Each of the three (BMP-1, BMP-2A, and BMP-3) appears to be independently capable of inducing the formation of cartilage in vivo. Two of the encoded proteins (BMP-2A and BMP-3) are new members of the TGF-beta supergene family, while the third, BMP-1, appears to be a novel regulatory molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wozney, J M -- Rosen, V -- Celeste, A J -- Mitsock, L M -- Whitters, M J -- Kriz, R W -- Hewick, R M -- Wang, E A -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1528-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tissue Growth and Repair Program, Genetics Institute, Inc., Cambridge, MA 02140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201241" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone Morphogenetic Proteins ; Cartilage/cytology/drug effects ; Cell Line ; DNA/genetics ; Growth Substances/*genetics ; Humans ; Molecular Sequence Data ; *Osteogenesis ; Proteins/*genetics/pharmacology ; Recombinant Proteins/pharmacology ; Sequence Homology, Nucleic Acid ; Transforming Growth Factors/genetics
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  • 19
    Publication Date: 1988-10-14
    Description: The signal sequence of simian virus 40 (SV40) large T-antigen for translocation into the nucleus is composed of positively charged amino acids Lys-Lys-Lys-Arg-Lys. Rabbit antibodies to a synthetic peptide containing the negatively charged amino acid sequence Asp-Asp-Asp-Glu-Asp were obtained. Indirect immunofluorescence of the antigens recognized by the antibody was punctate at the nuclear rim or the nuclear surface, depending on the plane of focus. The antibody blocked transport of nuclear proteins into the nucleus. The antigens recognized by the antibody were predominantly localized to the nuclear pores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoneda, Y -- Imamoto-Sonobe, N -- Matsuoka, Y -- Iwamoto, R -- Kiho, Y -- Uchida, T -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):275-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3051382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/immunology ; Antigens, Polyomavirus Transforming ; Biological Transport ; Cell Line ; Cell Nucleus/*metabolism ; Fluorescent Antibody Technique ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Nucleoplasmins ; Oligopeptides/immunology/*physiology ; *Phosphoproteins ; Protein Sorting Signals/*physiology ; Rats
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):863-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/prevention & control ; Amino Acid Sequence ; Antigens/*immunology ; Epitopes/immunology ; Major Histocompatibility Complex ; Protein Conformation ; T-Lymphocytes/*immunology ; Viral Vaccines
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-09-02
    Description: Transcription of zygotic genes does not occur in early Xenopus embryos until the mid-blastula transition, 6 to 7 hours after fertilization. Before this time, development is directed by maternal proteins and messenger RNAs stored within the egg. Two different forms of the A chain of platelet-derived growth factor (PDGF) are shown here to be encoded by maternal messenger RNAs. The two forms closely resemble human PDGF; however, the long form contains a hydrophobic region near the carboxyl terminus. The presence of PDGF messenger RNA in the embryo supports the idea that endogenous growth factors act at the earliest stages of embryogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, M -- Melton, D A -- Stiles, C D -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1223-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413486" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blastocyst/metabolism ; DNA/genetics/isolation & purification ; Gastrula/analysis ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oocytes/analysis ; Platelet-Derived Growth Factor/*genetics ; RNA, Messenger/analysis/genetics ; Xenopus laevis/*embryology/genetics
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  • 22
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-11-11
    Description: A peptide 60 residues in length that corresponds to the homeo domain of Antennapedia (Antp), a protein governing development in Drosophila, was synthesized by segment condensation with protected peptide segments prepared on an oxime resin. A footprinting assay showed that the homeo domain binds specifically to a TAA repeat DNA sequence in the Antp gene. Thus the Antp homeo domain has a sequence-specific DNA binding property. The circular dichroism spectra of the homeo domain peptide showed the presence of a significant amount of alpha-helical structure in aqueous solution and in 50 percent trifluoroethanol. The alpha helicity measured in water appears to depend on the peptide concentration, which suggests that the peptide aggregates. These results support the hypothesis that the homeo domain binds to DNA through a helix-turn-helix motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mihara, H -- Kaiser, E T -- RR 862/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):925-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2903553" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromatography, High Pressure Liquid ; Circular Dichroism ; DNA/*metabolism ; Drosophila/*growth & development ; Electrophoresis, Polyacrylamide Gel ; *Genes, Homeobox ; Insect Hormones/*chemical synthesis/genetics/metabolism ; Molecular Sequence Data ; Peptide Fragments/*chemical synthesis/genetics ; Protein Conformation ; Repetitive Sequences, Nucleic Acid
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  • 23
    Publication Date: 1988-10-14
    Description: A survey of rat tissues by RNA analysis, aimed at uncovering the physiological function of the parathyroid hormone-like peptide (PTH-LP) associated with hypercalcemia of malignancy, revealed the presence of a 1.5-kilobase messenger RNA encoding this peptide in lactating mammary glands. PTH-LP messenger RNA is expressed in mammary tissue only during lactation; it appears and disappears rapidly (2 to 4 hours) as a function of the sucking stimulus. The identity of this messenger RNA was confirmed by cloning the rat PTH-LP complementary DNA, which predicts a peptide with strong similarity to the human homolog. Moreover, extracts from lactating mammary tissue stimulated parathyroid hormone-dependent adenylate cyclase. These findings suggest that PTH-LP plays a physiological role in lactation, possibly as a hormone for the mobilization or transfer (or both) of calcium to the milk.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiede, M A -- Rodan, G A -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bone Biology and Osteoporosis Research, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175653" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Cloning, Molecular ; DNA/genetics ; Female ; *Gene Expression Regulation ; Humans ; Lactation/*metabolism ; Mammary Glands, Animal/*metabolism ; Molecular Sequence Data ; Neoplasm Proteins/*genetics/physiology ; Parathyroid Hormone-Related Protein ; Pregnancy ; RNA, Messenger/genetics/*metabolism ; Rats ; Sequence Homology, Nucleic Acid ; Tissue Distribution
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  • 24
    Publication Date: 1988-03-04
    Description: The enzyme dihydrofolate reductase (DHFR) is found ubiquitously in both prokaryotes and eukaryotes. It is essential for de novo synthesis of purines and of deoxythymidine monophosphate for DNA synthesis. Among viruses, however, only the T-even and T5 bacteriophage have been found to encode their own DHFR. In this study a gene for DHFR was found in a specific subgroup of the gamma or lymphotropic class of herpesviruses. DNA sequences for DHFR were found in herpesvirus saimiri and herpesvirus ateles but not in Epstein-Barr virus, Marek's disease virus, herpes simplex virus, varicella-zoster virus, herpesvirus tamarinus, or human cytomegalovirus. The predicted sequence of herpesvirus saimiri DHFR is 186 amino acids in length, the same length as human, murine, and bovine DHFR. The human and herpesvirus saimiri DHFRs share 83 percent positional identity in amino acid sequence. The herpesvirus saimiri DHFR gene is devoid of intron sequences, suggesting that it was acquired by some process involving reverse transcription. This is to our knowledge the first example of a mammalian virus with a gene for DHFR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trimble, J J -- Murthy, S C -- Bakker, A -- Grassmann, R -- Desrosiers, R C -- 31363/PHS HHS/ -- RR00168/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1145-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉New England Regional Primate Research Center, Harvard Medical School, Southborough, MA 01772.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830673" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Chickens ; Cytomegalovirus/enzymology ; Herpesviridae/*enzymology ; Herpesvirus 2, Saimiriine/*enzymology ; Herpesvirus 4, Human/enzymology ; Humans ; Introns ; Mice ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; Tetrahydrofolate Dehydrogenase/*genetics
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  • 25
    Publication Date: 1988-07-29
    Description: Interleukin-1 alpha and -1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis. A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells. The product of the cloned complementary DNA binds both IL-1 alpha and IL-1 beta in a manner indistinguishable from that of the native T cell IL-1 receptor. The extracellular, IL-1 binding portion of the receptor is 319 amino acids in length and is composed of three immunoglobulin-like domains. The cytoplasmic portion of the receptor is 217 amino acids long.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J E -- March, C J -- Cosman, D -- Widmer, M B -- MacDonald, H R -- McMahan, C J -- Grubin, C E -- Wignall, J M -- Jackson, J L -- Call, S M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):585-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2969618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Genes, Immunoglobulin ; Interleukin-1/*physiology ; Mice ; Molecular Sequence Data ; *Multigene Family ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-1
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  • 26
    Publication Date: 1988-08-05
    Description: Qa-2, a cell-surface glycoprotein anchored by phosphatidylinositol (PI), is structurally related to the class I transplantation antigens H-2 K, D, and L, which are integral membrane glycoproteins. The predicted transmembrane segment of Qa-2 differs from those of H-2 K, D, and L by the presence of an aspartate in place of a valine at position 295. A single base change that replaced this aspartate with valine resulted in cell-surface Qa-2 molecules that were insensitive to hydrolysis by a PI-specific phospholipase C and more resistant to papain cleavage, properties shared by H-2D. Cells expressing Asp----Val mutant Qa-2 proteins were still able to attach a PI anchor to endogenous proteins such as Thy-1 and J11D. It therefore appears that this single amino acid change converts Qa-2 from a PI-linked form into an integral membrane protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waneck, G L -- Stein, M E -- Flavell, R A -- AI24562/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):697-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biogen Research Corporation, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399901" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigens, Surface/genetics ; *Aspartic Acid ; Cell Line ; DNA/genetics ; H-2 Antigens ; *Histocompatibility Antigens/genetics ; *Histocompatibility Antigens Class I ; Membrane Proteins/genetics/*metabolism ; Mutation ; Papain/metabolism ; Phosphatidylinositols/*metabolism ; Thymoma ; Thymus Neoplasms ; Transfection ; Tumor Cells, Cultured ; Type C Phospholipases/metabolism ; *Valine
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  • 27
    Publication Date: 1988-08-19
    Description: The myosin light chain kinase requires calmodulin for activation. Tryptic cleavage of the enzyme generates an inactive 64-kilodalton (kD) fragment that can be further cleaved to form a constitutively active, calmodulin-independent, 61-kD fragment. Microsequencing and amino acid analysis of purified peptides after proteolysis of the 61- and 64-kD fragments were used to determine the amino-terminal and carboxyl-terminal sequences of the 64-kD fragment. Cleavage within the calmodulin-binding region at Arg505 generates the catalytically inactive 64-kD fragment, which is incapable of binding calmodulin. Further digestion removes a carboxyl-terminal fragment, including the pseudosubstrate sequence Ser484-Lys-Asp-Arg-Met-Lys-Lys-Tyr-Met- Ala-Arg-Arg-Lys-Trp-Gln-Lys-Thr-Gly-His-Ala-Val-Arg505 and results in a calmodulin-independent 61-kD fragment. Both the 61- and 64-kD fragments have the same primary amino-terminal sequences. These results provide direct support for the concept that the pseudosubstrate structure binds the active site and that the role of calmodulin is to modulate this interaction. Pseudosubstrates may be utilized in analogous ways by other allosterically regulated enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, R B -- Wettenhall, R E -- Means, A R -- Hartshorne, D J -- Kemp, B E -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):970-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Melbourne, Repatriation General Hospital, Heidelberg, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3406746" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/*metabolism ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Molecular Sequence Data ; Muscle, Smooth/*enzymology ; Myosin-Light-Chain Kinase/analysis/*metabolism ; Peptide Mapping ; Substrate Specificity
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-03-18
    Description: The genome of the human immunodeficiency virus (HIV) is known to contain eight open reading frames (ORFs) on the minus strand of the double-stranded DNA replicative intermediate. Data presented here indicate that the DNA plus strand of HIV contains a previously unidentified ORF in a region complementary to the envelope gene sequence. This ORF could encode a protein of approximately 190 amino acid residues with a relative molecular mass of 20 kilodaltons if translation began from the first initiation codon. The predicted protein is highly hydrophobic and thus could be membrane associated. It is possible, therefore, that the HIV genome encodes a protein on antisense messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, R H -- U41-01685-05/PHS HHS/ -- New York, N.Y. -- Science. 1988 Mar 18;239(4846):1420-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hepatitis Viruses Section, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3347840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Codon ; DNA, Viral/*genetics ; *Genes, Viral ; HIV/*genetics ; Molecular Sequence Data ; Molecular Weight ; RNA, Messenger/genetics ; Viral Envelope Proteins/genetics ; Viral Proteins/genetics
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  • 29
    Publication Date: 1988-11-18
    Description: Genes for the principal sigma factor (rpoD genes) of various eubacteria were identified with a synthetic oligonucleotide probe corresponding to a conserved sequence in rpoD gene products of Escherichia coli and Bacillus subtilis. Multiple rpoD homologs were found in the strains of Micrococcus, Pseudomonas, and Streptomyces, whereas single genes were detected in E. coli, B. subtilis, and Staphylococcus aureus. The four rpoD homologs of Streptomyces coelicolor A3(2) were cloned and sequenced. A homologous portion with 13 amino acids was found in the rpoD genes of S. coelicolor A3(2), E. coli, and B. subtilis and was named the "rpoD box."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, K -- Shiina, T -- Takahashi, H -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1040-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Applied Microbiology, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/*genetics ; DNA Probes ; DNA, Bacterial/genetics ; DNA-Binding Proteins/*genetics ; *Genes, Bacterial ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Sequence Homology, Nucleic Acid ; Sigma Factor/*genetics ; Transcription Factors/*genetics
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  • 30
    Publication Date: 1988-02-19
    Description: A replication-defective variant of feline leukemia virus was molecularly cloned directly from infected tissue and found to induce a rapid and fatal immunodeficiency syndrome in cats. Studies with cloned viruses also showed that subtle mutational changes would convert a minimally pathogenic virus into one that would induce an acute form of immunodeficiency. The data suggest that acutely pathogenic viruses may be selected against by current methods for isolation of the human and simian immunodeficiency viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Overbaugh, J -- Donahue, P R -- Quackenbush, S L -- Hoover, E A -- Mullins, J I -- CA01058/CA/NCI NIH HHS/ -- CA07966/CA/NCI NIH HHS/ -- CA43216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):906-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2893454" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome ; Amino Acid Sequence ; Animals ; Base Sequence ; Bone Marrow/microbiology ; Cats ; *Cloning, Molecular ; DNA, Viral/genetics ; Humans ; Immunologic Deficiency Syndromes/*etiology/microbiology ; Leukemia Virus, Feline/*genetics/pathogenicity ; Molecular Sequence Data ; Mutation ; Polymorphism, Restriction Fragment Length ; Transfection ; Virus Replication
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  • 31
    Publication Date: 1988-12-16
    Description: A sequence of developmental events transforms neurons from their immature state to their mature, terminally differentiated state. The elav locus is one of the first examples of a gene that is expressed in neurons early during this developmental sequence. This gene has been shown to be required for the proper development of young neurons and for the maintenance of mature neurons. DNA sequence data presented in this report suggest that the elav gene product is an RNA binding protein, based on the presence of RNP (ribonucleoprotein) consensus sequences. This leads to the proposal that this protein is involved in the RNA metabolism of neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robinow, S -- Campos, A R -- Yao, K M -- White, K -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1570-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02254-9110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144044" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/*genetics/physiology ; Drosophila melanogaster/*genetics ; *Genes ; Molecular Sequence Data ; Neurons/*physiology ; RNA-Binding Proteins
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  • 32
    Publication Date: 1988-08-26
    Description: Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, J S -- Kretz, K A -- Dewji, N -- Wenger, D A -- Esch, F -- Fluharty, A L -- DK 38795/DK/NIDDK NIH HHS/ -- HD 18983/HD/NICHD NIH HHS/ -- NS 08682/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1098-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma, Hepatocellular/analysis ; Chromosome Mapping ; Chromosomes, Human, Pair 10 ; DNA/genetics/isolation & purification ; Glycoproteins/analysis/*genetics ; Humans ; Liver Neoplasms/analysis ; Male ; Mice ; Mice, Nude ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Precursors/analysis/genetics ; Protein Processing, Post-Translational ; Rats ; Saposins ; Sphingolipid Activator Proteins ; Tissue Distribution
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  • 33
    Publication Date: 1988-02-26
    Description: The T cell antigen receptor is a multi-subunit receptor complex present on the surface of all mature and many developing T cells. It consists of clonotypic heterodimers noncovalently linked to five invariant chains that are encoded by four genes and referred to as the CD3 complex. The CD3 gamma, delta, and epsilon chains have been molecularly characterized. In this report the molecular cloning of a complementary DNA encoding the zeta chain of the murine T cell antigen receptor is described. The predicted protein sequence of the zeta chain suggests a structure distinct from those of any of the previously described receptor subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, A M -- Baniyash, M -- Hou, D -- Samelson, L E -- Burgess, W H -- Klausner, R D -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3278377" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Membrane/metabolism ; Chromatography, High Pressure Liquid ; *Cloning, Molecular ; Cyanogen Bromide ; DNA/genetics ; Electrophoresis, Polyacrylamide Gel ; Immunosorbent Techniques ; Macromolecular Substances ; *Membrane Proteins ; Mice ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Peptide Fragments ; Protein Biosynthesis ; RNA, Messenger/genetics ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/analysis ; Transcription, Genetic ; Tumor Cells, Cultured
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  • 34
    Publication Date: 1988-04-22
    Description: A cytoplasmic protein that greatly enhances the guanosine triphosphatase (GTPase) activity of N-ras protein but does not affect the activity of oncogenic ras mutants has been recently described. This protein (GAP) is shown here to be ubiquitous in higher eukaryotes and to interact with H-ras as well as with N-ras proteins. To identify the region of ras p21 with which GAP interacts, 21 H-ras mutant proteins were purified and tested for their ability to undergo stimulation of GTPase activity by GAP. Mutations in nonessential regions of H-ras p21 as well as mutations in its carboxyl-terminal domain (residues 165-185) and purine binding region (residues 117 and 119) did not decrease the ability of the protein to respond to GAP. In addition, an antibody against the carboxyl-terminal domain did not block GAP activity, supporting the conclusion that GAP does not interact with this region. Transforming mutations at positions 12, 59, and 61 (the phosphoryl binding region) abolished GTPase stimulation by GAP. Point mutations in the putative effector region of ras p21 (amino acids 35, 36, and 38) were also insensitive to GAP. However, a point mutation at position 39, shown previously not to impair effector function, did not alter GAP-p21 interaction. These results indicate that GAP interaction may be essential for ras p21 biological activity and that it may be a ras effector protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adari, H -- Lowy, D R -- Willumsen, B M -- Der, C J -- McCormick, F -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2833817" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; DNA Mutational Analysis ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; *Genes, ras ; Immunologic Techniques ; In Vitro Techniques ; Phosphoric Monoester Hydrolases/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Structure-Activity Relationship ; ras GTPase-Activating Proteins
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  • 35
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-04-15
    Description: Complementary DNAs (cDNAs) encoding androgen receptors were obtained from human testis and rat ventral prostate cDNA libraries. The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors. The human cDNA was transcribed and the RNA product was translated in cell-free systems to yield a 76-kilodalton protein. The protein was immunoprecipitable by human autoimmune antibodies to the androgen receptor. The protein bound androgens specifically and with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, C S -- Kokontis, J -- Liao, S T -- DK-09461/DK/NIDDK NIH HHS/ -- DK-37694/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353726" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; *Cloning, Molecular ; DNA/genetics ; *Genes ; Humans ; Male ; Molecular Sequence Data ; Molecular Weight ; Rats ; Receptors, Androgen/*genetics/metabolism ; Sequence Homology, Nucleic Acid ; Species Specificity ; Testis/metabolism
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  • 36
    Publication Date: 1988-07-01
    Description: In recent years, members of the protein kinase family have been discovered at an accelerated pace. Most were first described, not through the traditional biochemical approach of protein purification and enzyme assay, but as putative protein kinase amino acid sequences deduced from the nucleotide sequences of molecularly cloned genes or complementary DNAs. Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional characterization of these newly identified family members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanks, S K -- Quinn, A M -- Hunter, T -- GM38793/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):42-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Laboratory, Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3291115" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Catalysis ; Humans ; Molecular Sequence Data ; *Phylogeny ; Protein Kinases/*genetics
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  • 37
    Publication Date: 1988-08-12
    Description: The interaction between receptors and guanine nucleotide binding (G) proteins leads to G protein activation and subsequent regulation of effector enzymes. The molecular basis of receptor-G protein interaction has been examined by using the ability of the G protein from rods (transducin) to cause a conformational change in rhodopsin as an assay. Synthetic peptides corresponding to two regions near the carboxyl terminus of the G protein alpha subunit, Glu311-Val328 and Ile340-Phe350, compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys321 is required for this effect. Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamm, H E -- Deretic, D -- Arendt, A -- Hargrave, P A -- Koenig, B -- Hofmann, K P -- EY06062/EY/NEI NIH HHS/ -- EY06225/EY/NEI NIH HHS/ -- RP05369/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):832-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3136547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antigen-Antibody Complex ; Binding Sites ; GTP-Binding Proteins/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Retinal Pigments/*metabolism ; Rhodopsin/analogs & derivatives/*metabolism ; Transducin
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  • 38
    Publication Date: 1988-12-09
    Description: Cyclic AMP (cAMP) is an intracellular second messenger that activates transcription of many cellular genes. A palindromic consensus DNA sequence, TGACGTCA, functions as a cAMP-responsive transcriptional enhancer (CRE). The CRE binds a cellular protein of 38 kD in placental JEG-3 cells. A placental lambda gt11 library was screened for expression of specific CRE-binding proteins with the CRE sequence as a radioactive probe. A cDNA encoding a protein of 326 amino acids with the binding properties of a specific CRE-binding protein (CREB) was isolated. The protein contains a COOH-terminal basic region adjacent to a sequence similar to the "leucine zipper" sequence believed to be involved in DNA binding and in protein-protein contacts in several other DNA-associated transcriptional proteins including the products of the c-myc, c-fos, and c-jun oncogenes and GCN4. The CREB protein also contains an NH2-terminal acidic region proposed to be a potential transcriptional activation domain. The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoeffler, J P -- Meyer, T E -- Yun, Y -- Jameson, J L -- Habener, J F -- DK 25532/DK/NIDDK NIH HHS/ -- DK 30457/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Endocrinology, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2974179" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; Cyclic AMP Response Element-Binding Protein ; DNA/*genetics ; DNA-Binding Proteins/*genetics/physiology ; Enhancer Elements, Genetic ; Female ; Humans ; Molecular Sequence Data ; Placenta/*metabolism ; Pregnancy ; Transcription, Genetic
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  • 39
    Publication Date: 1988-02-26
    Description: Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an antiserum directed against amino acids 254 to 274 of env was efficient in neutralizing three different isolates of HIV in vitro, without affecting the binding of the virus to CD4-positive cells. Therefore, this conserved region of gp120 appears to be critical in a postbinding event during virus penetration and may represent a target for antibody neutralization of HIV. These findings may be applicable in the design of a vaccine for the acquired immunodeficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, D D -- Kaplan, J C -- Rackauskas, I E -- Gurney, M E -- AI25541/AI/NIAID NIH HHS/ -- KO8-AI00685/AI/NIAID NIH HHS/ -- NS21442/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1021-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, Cedars-Sinai Medical Center, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830667" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Differentiation, T-Lymphocyte/immunology ; Glucose-6-Phosphate Isomerase ; Growth Substances ; HIV/*immunology/physiology ; HIV Antibodies ; HIV Envelope Protein gp120 ; HIV Seropositivity ; Hemocyanin/immunology ; Humans ; Immune Sera/immunology ; Immunization ; Immunosorbent Techniques ; Lymphokines ; Molecular Sequence Data ; Neutralization Tests ; Receptors, Antigen, T-Cell/immunology ; Retroviridae Proteins/*immunology/physiology ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/immunology/microbiology ; Viral Envelope Proteins/*immunology/physiology
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  • 40
    Publication Date: 1988-07-08
    Description: A protein designated p14 was purified from a simian immunodeficiency virus (SIVMne) and was shown by amino acid sequence analysis to be nearly identical to the predicted translational product of a unique open reading frame (X-ORF) in the nucleotide sequences of SIVmac and human immunodeficiency virus type 2 (HIV-2). Thus the X-ORF is proven to be a new retroviral gene. The p14 is present in SIVMne in molar amounts equivalent to those of the gag proteins. This is the first example of a retrovirus that contains a substantial quantity of a viral protein that is not a product of the gag, pro, pol, or env genes. SIV p14 and its homolog in HIV-2 may function as nucleic acid binding proteins since purified p14 binds to single-stranded nucleic acids in vitro. Antisera to the purified protein detected p14 in SIVMne, SIVmac, and a homologous protein (16 kilodaltons) in HIV-2 but did not react with HIV-1. Diagnostic procedures based on this novel protein will distinguish between HIV-1 and HIV-2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, L E -- Sowder, R C -- Copeland, T D -- Benveniste, R E -- Oroszlan, S -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bionetics Research, Inc., National Cancer Institute, Frederick, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388031" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments/analysis ; *Retroviridae ; Retroviridae Proteins/*isolation & purification
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  • 41
    Publication Date: 1988-09-16
    Description: Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin. The 757-amino acid sequence predicted from a cloned rat adipocyte complementary DNA showed no homology with any other known lipase or protein. The activity-controlling phosphorylation site was localized to Ser563 in a markedly hydrophilic domain, and a lipid-binding consensus site was tentatively identified. One or several messenger RNA species (3.3, 3.5, or 3.9 kilobases) were expressed in adipose and steroidogenic tissues and heart and skeletal muscle. The human hormone-sensitive lipase gene mapped to chromosome 19 cent-q13.3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holm, C -- Kirchgessner, T G -- Svenson, K L -- Fredrikson, G -- Nilsson, S -- Miller, C G -- Shively, J E -- Heinzmann, C -- Sparkes, R S -- Mohandas, T -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1503-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical and Physiological Chemistry, University of Lund, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420405" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Rats ; Sterol Esterase/*genetics
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  • 42
    Publication Date: 1988-02-26
    Description: A 50-nucleotide untranslated region is shown to be present within the coding sequence of Escherichia coli bacteriophage T4 gene 60, which encodes one of the subunits for its type II DNA topoisomerase. This interruption is part of the transcribed messenger RNA and appears not to be removed before translation. Thus, the usual colinearity between messenger RNA and the encoded protein sequence apparently does not exist in this case. The interruption is bracketed by a direct repeat of five base pairs. A mechanism is proposed in which folding of the untranslated region brings together codons separated by the interruption so that the elongating ribosome may skip the 50 nucleotides during translation. The alternative possibility, that the protein is efficiently translated from a very minor and undetectable form of processed messenger RNA, seems unlikely, but has not been completely ruled out.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, W M -- Ao, S Z -- Casjens, S -- Orlandi, R -- Zeikus, R -- Weiss, R -- Winge, D -- Fang, M -- GM 21960/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1005-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA/genetics ; DNA Topoisomerases, Type I/*genetics ; DNA, Recombinant ; *Genes, Viral ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; Protein Biosynthesis ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; T-Phages/enzymology/*genetics ; Transcription, Genetic
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  • 43
    Publication Date: 1988-07-29
    Description: Neurons that release serotonin as a neurotransmitter project to most regions of the central and peripheral nervous system and mediate diverse neural functions. The physiological effects of serotonin are initiated by the activation of multiple, distinct receptor subtypes. Cloning in RNA expression vectors was combined with a sensitive electrophysiological assay in Xenopus oocytes in order to isolate a functional cDNA clone encoding the 5HTlc serotonin receptor. Injection of RNA transcribed in vitro from this clone into Xenopus oocytes elicits serotonin sensitivity. Mouse fibroblasts transformed with this clone bind serotonin agonists and antagonists and exhibit an increase in intracellular Ca2+ concentrations in response to serotonin. The sequence of the 5HTlc receptor reveals that it belongs to the family of G protein-coupled receptors, which are thought to traverse the cytoplasmic membrane seven times. Moreover, in situ hybridization and RNA blot analysis indicate that the 5HTlc receptor is expressed in neurons in many regions of the central nervous system and suggest that this subclass of receptor may mediate many of the central actions of serotonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julius, D -- MacDermott, A B -- Axel, R -- Jessell, T M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):558-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399891" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Fibroblasts/physiology ; Gene Expression Regulation ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Oocytes/physiology ; Phosphoproteins/physiology ; Rats ; Receptors, Serotonin/*genetics ; Serotonin/*physiology ; Xenopus laevis
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  • 44
    Publication Date: 1988-09-16
    Description: During the early stages of its developmental program, Dictyostelium discoideum expresses cell surface cyclic adenosine monophosphate (cyclic AMP) receptors. It has been suggested that these receptors coordinate the aggregation of individual cells into a multicellular organism and regulate the expression of a large number of developmentally regulated genes. The complementary DNA (cDNA) for the cyclic AMP receptor has now been cloned from lambda gt-11 libraries by screening with specific antiserum. The 2-kilobase messenger RNA (mRNA) that encodes the receptor is undetectable in growing cells, rises to a maximum at 3 to 4 hours of development, and then declines. In vitro transcribed complementary RNA, when hybridized to cellular mRNA, specifically arrests in vitro translation of the receptor polypeptide. When the cDNA is expressed in Dictyostelium cells, the undifferentiated cells specifically bind cyclic AMP. Cell lines transformed with a vector that expresses complementary mRNA (antisense) do not express the cyclic AMP receptor protein. These cells fail to enter the aggregation stage of development during starvation, whereas control and wild-type cells aggregate and complete the developmental program within 24 hours. The phenotype of the antisense transformants suggests that the cyclic AMP receptor is essential for development. The deduced amino acid sequence of the receptor reveals a high percentage of hydrophobic residues grouped in seven domains, similar to the rhodopsins and other receptors believed to interact with G proteins. It shares amino acid sequence identity and is immunologically cross-reactive with bovine rhodopsin. A model is proposed in which the cyclic AMP receptor crosses the bilayer seven times with a serine-rich cytoplasmic carboxyl terminus, the proposed site of ligand-induced receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, P S -- Sun, T J -- Saxe, C L 3rd -- Kimmel, A R -- Johnson, R L -- Devreotes, P N -- GM 34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1467-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Dictyostelium/*growth & development/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; Solubility
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  • 45
    Publication Date: 1988-10-14
    Description: Sarafotoxins, a group of 21-residue cardiotoxic peptides from snake venom that induce coronary vasoconstriction, show high-affinity binding to rat atrial and brain membranes and activate the hydrolysis of phosphoinositides. Neither their binding nor their activity is affected by blockers or activators of known receptors and ion channels, suggesting that sarafotoxins act either directly on the phosphoinositide phosphodiesterase system or on a novel receptor. Their amino acid sequence shows a high degree of homology with that of endothelin, a recently described 21-residue vasoconstrictor peptide found in porcine aortic endothelium. This is remarkable, since endothelin is a natural compound of the mammalian vascular system while sarafotoxins are highly toxic components of snake venom.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kloog, Y -- Ambar, I -- Sokolovsky, M -- Kochva, E -- Wollberg, Z -- Bdolah, A -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):268-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Calcium/metabolism ; Cell Membrane/metabolism ; Endothelins ; Enzyme Activation ; Heart Atria/metabolism ; Hydrolysis ; Inositol/metabolism ; Molecular Sequence Data ; Myocardium/*metabolism ; Peptides ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphatidylinositols/*metabolism ; Phosphoric Diester Hydrolases/metabolism ; Rats ; Sequence Homology, Nucleic Acid ; Vasoconstriction ; Viper Venoms/*metabolism
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  • 46
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-08-26
    Description: An assay for the presence of given DNA sequences has been developed, based on the ability of two oligonucleotides to anneal immediately adjacent to each other on a complementary target DNA molecule. The two oligonucleotides are then joined covalently by the action of a DNA ligase, provided that the nucleotides at the junction are correctly base-paired. Thus single nucleotide substitutions can be distinguished. This strategy permits the rapid and standardized identification of single-copy gene sequences in genomic DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landegren, U -- Kaiser, R -- Sanders, J -- Hood, L -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1077-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; DNA/*analysis/genetics/metabolism ; DNA Ligases/*metabolism ; DNA, Recombinant/metabolism ; Fluorescent Dyes ; Globins/genetics ; Humans ; Molecular Sequence Data ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Polynucleotide Ligases/*metabolism
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  • 47
    Publication Date: 1988-03-11
    Description: Urate oxidase (E.C. 1.7.3.3) catalyzes the oxidation of uric acid to allantoin in most mammals except humans and certain primates. The amino-terminal amino acid sequence for porcine urate oxidase was determined and used in a novel procedure for generating complementary DNA (cDNA) probes to this amino acid sequence. The procedure is based on the polymerase chain reaction and utilizes mixed oligonucleotide primers complementary to the reverse translation products of an amino acid sequence. This rapid and simple cDNA cloning procedure is generally applicable and requires only a partial amino acid sequence. A cDNA probe developed by this procedure was used to isolate a full-length porcine urate oxidase cDNA and to demonstrate the presence of homologous genomic sequences in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, C C -- Wu, X W -- Gibbs, R A -- Cook, R G -- Muzny, D M -- Caskey, C T -- DK31428/DK/NIDDK NIH HHS/ -- GM34428/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344434" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Cloning, Molecular ; DNA/*genetics ; Gene Amplification ; Liver/enzymology ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Swine ; Urate Oxidase/*genetics
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  • 48
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-01-15
    Description: Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, G -- Cowan, N -- Kirschner, M -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; Codon ; DNA/genetics ; DNA, Recombinant ; Mice ; Microtubule-Associated Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/genetics ; Protein Conformation ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; tau Proteins
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  • 49
    Publication Date: 1988-04-01
    Description: A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contains a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levin, L R -- Kuret, J -- Johnson, K E -- Powers, S -- Cameron, S -- Michaeli, T -- Wigler, M -- Zoller, M J -- GM33986/GM/NIGMS NIH HHS/ -- R35 CA39829-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):68-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalysis ; Cyclic AMP/*pharmacology ; Genes, Fungal ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Structure-Activity Relationship ; Threonine
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  • 50
    Publication Date: 1988-04-08
    Description: The major histocompatibility complex is a chromosomal segment embodying several gene clusters among which those with immune functions are the best characterized. This region is suspected to host other as yet undetected genes whose characterization may shed light on the population genetics and evolution of the whole gene complex and thus on its unexplained character of marker locus for a number of diseases of nonimmune or unknown pathogenesis. A novel gene was identified that is transcribed in all tissues tested and is located in mouse and man between the CA and Bf genes of the H-2 and HLA complexes, respectively. From the nucleotide sequence, derived from liver complementary DNA clones, it is predicted that this novel single-copy gene encodes a 42-kilodalton polypeptide that bears no recognizable relation to the protein families known so far, but it displays striking hallmarks of natural selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levi-Strauss, M -- Carroll, M C -- Steinmetz, M -- Meo, T -- New York, N.Y. -- Science. 1988 Apr 8;240(4849):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U 276, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353717" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Genes ; Liver/physiology ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Periodicity ; Selection, Genetic
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  • 51
    Publication Date: 1988-11-11
    Description: The microtubule-associated protein MAP2 is a prominent large-sized component of purified brain microtubules that, like the 36- to 38-kilodalton tau proteins, bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease. The complete sequence of mouse brain MAP2 was determined from a series of overlapping cloned complementary DNAs. The sequence of the carboxyl-terminal 185 amino acids is very similar (67 percent) to a corresponding region of tau protein, and includes a series of three imperfect repeats, each 18 amino acids long and separated by 13 or 14 amino acids. A subcloned fragment spanning the first two of the 18-amino acid repeats was expressed as a polypeptide by translation in vitro. This polypeptide copurified with microtubules through two successive cycles of polymerization and depolymerization, whereas a control polypeptide derived from the amino-terminal region of MAP2 completely failed to copurify. These data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2. The occurrence of these repeats in tau protein suggests that these may be a general feature of microtubule binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewis, S A -- Wang, D H -- Cowan, N J -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3142041" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; DNA/genetics ; Mice ; Microtubule-Associated Proteins/genetics/*metabolism ; Microtubules/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins ; Protein Biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid ; Tubulin/metabolism ; tau Proteins
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  • 52
    Publication Date: 1988-08-05
    Description: Synthetic peptide segments of the CD4 molecule were tested for their ability to inhibit infection of CD4+ cells by the human immunodeficiency virus (HIV) and to inhibit HIV-induced cell fusion. A peptide mixture composed of CD4(76-94), and synthesis side products, blocked HIV-induced cell fusion at a nominal concentration of 125 micromolar. Upon high-performance liquid chromatography, the antisyncytial activity of the peptide mixture was found not in the fraction containing the peptide CD4(76-94) itself, but in a side fraction containing derivatized peptide products generated in the automated synthesis. Derivatized deletion and substitution peptides in the region CD4(76-94) were used to demonstrate sequence specificity, a requirement for benzyl derivatization, and a core seven-residue fragment required for antisyncytial activity. A partially purified S-benzyl-CD4(83-94) peptide mixture inhibited HIV-induced cell fusion at a nominal concentration of less than or equal to 32 micromolar. Derivatized CD4 peptides blocked cell fusion induced by several HIV isolates and by the simian immunodeficiency virus, SIV, and blocked infection in vitro by four HIV-1 isolates with widely variant envelope gene sequences. Purified CD4(83-94) dibenzylated at cysteine 86 and glutamate 87 possessed antisyncytial activity at 125 micromolar. Derivatization may specifically alter the conformation of CD4 holoreceptor peptide fragments, increasing their antiviral efficacy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lifson, J D -- Hwang, K M -- Nara, P L -- Fraser, B -- Padgett, M -- Dunlop, N M -- Eiden, L E -- AI 62559/AI/NIAID NIH HHS/ -- AI/CA-25922/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):712-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular Immunology, Genelabs Incorporated, Redwood City, CA 94063.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2969619" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigens, CD4 ; *Antigens, Differentiation, T-Lymphocyte/isolation & purification/pharmacology ; Antiviral Agents ; Cell Fusion ; Chromatography, High Pressure Liquid ; HIV/drug effects/*physiology ; Lymphocyte Culture Test, Mixed ; Mass Spectrometry ; Molecular Sequence Data ; Peptide Fragments/isolation & purification/*pharmacology ; T-Lymphocytes/immunology/*microbiology
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  • 53
    Publication Date: 1988-07-15
    Description: In a study of the immunologic significance of the genetic diversity present within single isolates of human immunodeficiency virus type 1 (HIV-1), the neutralization of viruses derived from molecular clones of the HIV-1 strain HTLV-IIIB by an extensive panel of sera was compared. Sera from HIV-1-infected patients and from goats immunized with polyacrylamide gel-purified HIV-1 envelope glycoprotein (gp120), native gp120, or gp120-derived recombinant peptides, showed marked heterogeneity in neutralizing activity against these closely related viruses. The change of a single amino acid residue in gp120 may account for such "clonal restriction" of neutralizing activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Looney, D J -- Fisher, A G -- Putney, S D -- Rusche, J R -- Redfield, R R -- Burke, D S -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Viral Diseases, Walter Reed Army Institute of Research, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388046" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Viral/*immunology ; Binding, Competitive ; Cloning, Molecular ; HIV/genetics/*immunology ; HIV Seropositivity/immunology ; Humans ; Molecular Sequence Data ; Neutralization Tests ; Oligopeptides/chemical synthesis/immunology
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  • 54
    Publication Date: 1988-04-15
    Description: The androgen receptor (AR) mediates the actions of male sex steroids. Human AR genomic DNA was cloned from a flow-sorted human X chromosome library by using a consensus nucleotide sequence from the DNA-binding domain of the family of nuclear receptors. The AR gene was localized on the human X chromosome between the centromere and q13. Cloned complementary DNA, selected with an AR-specific oligonucleotide probe, was expressed in monkey kidney (COS) cells and yielded a high-affinity androgen-binding protein with steroid-binding specificity corresponding to that of native AR. A predominant messenger RNA species of 9.6 kilobases was identified in human, rat, and mouse tissues known to contain AR and was undetectable in tissues lacking AR androgen-binding activity, including kidney and liver from androgen-insensitive mice. The deduced amino acid sequence of AR within the DNA-binding domain has highest sequence identity with the progesterone receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lubahn, D B -- Joseph, D R -- Sullivan, P M -- Willard, H F -- French, F S -- Wilson, E M -- HD04466/HD/NICHD NIH HHS/ -- HD16910/HD/NICHD NIH HHS/ -- HD21744/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of North Carolina, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353727" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; *Cloning, Molecular ; Codon ; *Genes ; Humans ; Molecular Sequence Data ; Receptors, Androgen/*genetics ; Sequence Homology, Nucleic Acid ; *X Chromosome
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  • 55
    Publication Date: 1988-03-04
    Description: Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II (IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptorCI), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for 125I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacDonald, R G -- Pfeffer, S R -- Coussens, L -- Tepper, M A -- Brocklebank, C M -- Mole, J E -- Anderson, J K -- Chen, E -- Czech, M P -- Ullrich, A -- CA 39240/CA/NCI NIH HHS/ -- DK 30648/DK/NIDDK NIH HHS/ -- DK 34063/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2964083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/genetics/*metabolism ; Cell Membrane/analysis/metabolism ; Chromatography, Affinity ; DNA/genetics ; Female ; Hexosephosphates/*metabolism ; Insulin-Like Growth Factor II/*metabolism ; Mannosephosphates/*metabolism ; Molecular Sequence Data ; Placenta/analysis ; Pregnancy ; Rats ; Receptor, IGF Type 2 ; Receptor, Insulin/genetics/*metabolism ; Receptors, Somatomedin ; Sequence Homology, Nucleic Acid ; Somatomedins/*metabolism
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-04-29
    Description: Apolipoprotein E is a plasma protein that serves as a ligand for low density lipoprotein receptors and, through its interaction with these receptors, participates in the transport of cholesterol and other lipids among various cells of the body. A mutant form of apolipoprotein E that is defective in binding to low density lipoprotein receptors is associated with familial type III hyperlipoproteinemia, a genetic disorder characterized by elevated plasma cholesterol levels and accelerated coronary artery disease. Apolipoprotein E is synthesized in various organs, including liver, brain, spleen, and kidney, and is present in high concentrations in interstitial fluid, where it appears to participate in cholesterol redistribution from cells with excess cholesterol to those requiring cholesterol. Apolipo-protein E also appears to be involved in the repair response to tissue injury; for example, markedly increased amounts of apolipoprotein E are found at sites of peripheral nerve injury and regeneration. Other functions of apolipoprotein E, unrelated to lipid transport, are becoming known, including immunoregulation and modulation of cell growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahley, R W -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):622-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoproteins E/genetics/*physiology ; Biological Transport ; Cholesterol/*metabolism ; Gene Expression Regulation ; Humans ; Hyperlipoproteinemia Type III/genetics/metabolism ; Immunity ; Lipid Metabolism ; Molecular Sequence Data ; Polymorphism, Genetic ; Protein Conformation ; Receptors, LDL/metabolism
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  • 57
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-10-14
    Description: Oligonucleotide-directed mutagenesis of the codons for glutamine-68 (Gln68), lysine-72 (Lys72), isoleucine-79 (Ile79), alanine-80 (Ala80), and threonine-81 (Thr81) of the Escherichia coli trpR (tryptophan aporepressor) gene was used to make mutant repressors with each of 36 different amino acid changes. Mutant repressors were tested for binding to each member of a set of 28 different operators closely related to the consensus trp operator. Of the 36 mutant repressors, 11 bind a subset of the 28 operators; 5 of these have new binding specificities. These new specificities indicate that the hydroxyl group of Thr81 makes a specific contact with one of the four critical base pairs in a trp operator half-site, and the methyl group of Thr81 determines specificity at a second, critical base pair. The Trp repressor does not use the first two amino acids of its "recognition alpha-helix," Ile79 and Ala80, to make sequence-specific DNA contacts, and interacts with its operator in vivo in a way fundamentally different from the way that phage lambda repressor, lambda Cro protein, and coliphage 434 repressor contact their respective binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bass, S -- Sorrells, V -- Youderian, P -- GM34150/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):240-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles 90089-1481.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140377" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/genetics ; Amino Acid Sequence ; Apoproteins/*genetics/metabolism ; Bacterial Proteins ; Base Sequence ; Binding Sites ; Codon ; DNA, Bacterial/*metabolism ; Escherichia coli/*genetics ; *Escherichia coli Proteins ; Glutamine/genetics ; Isoleucine/genetics ; Lysine/genetics ; Mutation ; Operator Regions, Genetic ; Protein Conformation ; Repressor Proteins/*genetics/metabolism ; Threonine/genetics ; Transcription Factors/*genetics
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  • 58
    Publication Date: 1988-10-28
    Description: Subattomole analysis of fluorescein isothiocyanate (FITC) derivatives of amino acids is accomplished by combining capillary zone electrophoresis for high-efficiency separation with laser-induced fluorescence for high-sensitivity detection. Concentration detection limits range from 5 x 10(-12) molar for alanine to 9 x 10(-11) molar for lysine, injected in the column; 9 x 10(-21) mole of alanine is contained within the approximately 1-nanoliter injection volume at the detection limit. The alanine detection limit corresponds to fewer than 6000 molecules injected onto the column and represents an improvement of four orders of magnitude in the state of the art for fluorescent detection of amino acids and an improvement of six orders of magnitude in the state of the art for the detection limit for isothiocyanate derivatives of amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, Y F -- Dovichi, N J -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):562-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140381" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*analysis ; Electrophoresis/*methods ; Fluorescein-5-isothiocyanate ; Fluoresceins ; Proteins/*analysis ; Spectrometry, Fluorescence/*instrumentation ; Thiocyanates
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  • 59
    Publication Date: 1988-10-07
    Description: Many adhesive interactions are mediated by Arg-Gly-Asp (RGD) sequences within adhesive proteins. Such RGD sequences are frequently recognized by structurally related heterodimers that are members of the integrin family of adhesion receptors. A region was found in the platelet RGD receptor, gpIIb/IIIa, to which an RGD peptide becomes chemically cross-linked. This region corresponds to residues 109 to 171 of gpIIIa. This segment is conserved among the beta subunits of the integrins (76 percent identity of sequence), indicating that it may play a role in the adhesive functions of this family of receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Souza, S E -- Ginsberg, M H -- Burke, T A -- Lam, S C -- Plow, E F -- HL16411/HL/NHLBI NIH HHS/ -- HL28235/HL/NHLBI NIH HHS/ -- HL38292/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):91-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3262922" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Blood Platelets/immunology ; Humans ; Integrins ; Membrane Glycoproteins/genetics/*metabolism ; Molecular Sequence Data ; Platelet Membrane Glycoproteins/genetics/metabolism ; Protein Binding ; Receptors, Immunologic/*metabolism ; *Receptors, Peptide
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  • 60
    Publication Date: 1988-08-12
    Description: A novel x-ray diffraction technique, multiple-wavelength anomalous dispersion (MAD) phasing, has been applied to the de novo determination of an unknown protein structure, that of the "blue" copper protein isolated from cucumber seedlings. This method makes use of crystallographic phases determined from measurements made at several wavelengths and has recently been made technically feasible through the use of intense, polychromatic synchrotron radiation together with accurate data collection from multiwire electronic area detectors. In contrast with all of the conventional methods of solving protein structures, which require either multiple isomorphous derivatives or coordinates of a similar structure for molecular replacement, this technique allows direct solution of the classical "phase problem" in x-ray crystallography. MAD phase assignment should be particularly useful for determining structures of small to medium-sized metalloproteins for which isomorphous derivatives are difficult or impossible to make. The structure of this particular protein provides new insights into the spectroscopic and redox properties of blue copper proteins, an important class of metalloproteins widely distributed in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guss, J M -- Merritt, E A -- Phizackerley, R P -- Hedman, B -- Murata, M -- Hodgson, K O -- Freeman, H C -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):806-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Inorganic Chemistry, University of Sydney, New South Wales, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3406739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; *Metalloproteins/metabolism ; Models, Molecular ; Plants/*metabolism ; Protein Conformation ; X-Ray Diffraction/methods
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  • 61
    Publication Date: 1988-09-09
    Description: Mutants in the gene CDC34 of the yeast Saccharomyces cerevisiae are defective in the transition from G1 to the S phase of the cell cycle. This gene was cloned and shown to encode a 295-residue protein that has substantial sequence similarity to the product of the yeast RAD6 gene. The RAD6 gene is required for a variety of cellular functions including DNA repair and was recently shown to encode a ubiquitin-conjugating enzyme. When produced in Escherichia coli, the CDC34 gene product catalyzed the covalent attachment of ubiquitin to histones H2A and H2B in vitro, demonstrating that the CDC34 protein is another distinct member of the family of ubiquitin-conjugating enzymes. The cell cycle function of CDC34 is thus likely to be mediated by the ubiquitin-conjugating activity of its product.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goebl, M G -- Yochem, J -- Jentsch, S -- McGrath, J P -- Varshavsky, A -- Byers, B -- GM18541/GM/NIGMS NIH HHS/ -- GM31530/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 9;241(4871):1331-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842867" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cell Cycle ; Chromosome Mapping ; Cloning, Molecular ; *Genes, Fungal ; Molecular Sequence Data ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/*genetics ; Ubiquitins/*metabolism
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  • 62
    Publication Date: 1988-10-21
    Description: Single-chain antigen-binding proteins are novel recombinant polypeptides, composed of an antibody variable light-chain amino acid sequence (VL) tethered to a variable heavy-chain sequence (VH) by a designed peptide that links the carboxyl terminus of the VL sequence to the amino terminus of the VH sequence. These proteins have the same specificities and affinities for their antigens as the monoclonal antibodies whose VL and VH sequences were used to construct the recombinant genes that were expressed in Escherichia coli. Three of these proteins, one derived from the sequence for a monoclonal antibody to growth hormone and two derived from the sequences of two different monoclonal antibodies to fluorescein, were designed, constructed, synthesized, purified, and assayed. These proteins are expected to have significant advantages over monoclonal antibodies in a number of applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bird, R E -- Hardman, K D -- Jacobson, J W -- Johnson, S -- Kaufman, B M -- Lee, S M -- Lee, T -- Pope, S H -- Riordan, G S -- Whitlow, M -- 1-R43-GM39646-01/GM/NIGMS NIH HHS/ -- 1-R43-GM39662-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 21;242(4877):423-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genex Corporation, Gaithersburg, MD 20877.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140379" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Escherichia coli/genetics ; Genes ; Genetic Vectors ; Humans ; *Immunoglobulin Heavy Chains/genetics ; *Immunoglobulin Light Chains/genetics ; *Immunoglobulin Variable Region/genetics ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Recombinant Proteins ; X-Ray Diffraction
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  • 63
    Publication Date: 1988-02-19
    Description: The crystal structure at 2.7 A resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein consists of a six-stranded beta sheet, four alpha helices, and nine connecting loops. Four loops are involved in interactions with bound guanosine diphosphate: one with the phosphates, another with the ribose, and two with the guanine base. Most of the transforming proteins (in vivo and in vitro) have single amino acid substitutions at one of a few key positions in three of these four loops plus one additional loop. The biological functions of the remaining five loops and other exposed regions are at present unknown. However, one loop corresponds to the binding site for a neutralizing monoclonal antibody and another to a putative "effector region"; mutations in the latter region do not alter guanine nucleotide binding or guanosine triphosphatase activity but they do reduce the transforming activity of activated proteins. The data provide a structural basis for understanding the known biochemical properties of normal as well as activated ras oncogene proteins and indicate additional regions in the molecule that may possibly participate in other cellular functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vos, A M -- Tong, L -- Milburn, M V -- Matias, P M -- Jancarik, J -- Noguchi, S -- Nishimura, S -- Miura, K -- Ohtsuka, E -- Kim, S H -- CA 45593/CA/NCI NIH HHS/ -- GM 29287/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):888-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkely 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448879" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Binding Sites ; Catalysis ; Crystallization ; Epitopes/immunology ; Escherichia coli/genetics ; GTP Phosphohydrolases ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Neoplasms/genetics ; Phosphates/metabolism ; Protein Conformation ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogene Proteins p21(ras) ; Recombinant Proteins/metabolism ; X-Ray Diffraction
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  • 64
    Publication Date: 1988-02-12
    Description: The Philadelphia chromosome (Ph1) is a translocation between chromosomes 9 and 22 that is found in chronic myelogenous leukemia (CML) and a subset of acute lymphocytic leukemia patients (ALL). In CML, this results in the expression of a chimeric 8.5-kilobase BCR-ABL transcript that encodes the P210BCR-ABL tyrosine kinase. The Ph1 chromosome in ALL expresses a distinct ABL-derived 7-kilobase messenger RNA that encodes the P185ALL-ABL protein. Since the expression of different oncogene products may play a role in the distinctive presentation of Ph1-positive ALL versus CML, it is necessary to understand the molecular basis for the expression of P185ALL-ABL. Both P210BCR-ABL and P185ALL-ABL are recognized by an antiserum directed to BCR determinants in the amino-terminal region of both proteins. Antisera to BCR determinants proximal to the BCR-ABL junction in CML immunoprecipitated P210BCR-ABL but not P185ALL-ABL. Nucleotide sequence analysis of complementary DNA clones made from RNA from the Ph1-positive ALL SUP-B15 cell line, and S1 nuclease protection analysis confirmed the presence of BCR-ABL chimeric transcripts in Ph1-positive ALL cells. In Ph1-positive ALL, ABL sequences were joined to BCR sequences approximately 1.5 kilobases 5' of the CML junction. P185ALL-ABL represents the product of a BCR-ABL fusion gene in Ph1-positive ALL that is distinct from the BCR-ABL fusion gene of CML.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, S S -- McLaughlin, J -- Timmons, M -- Pendergast, A M -- Ben-Neriah, Y -- Dow, L W -- Crist, W -- Rovera, G -- Smith, S D -- Witte, O N -- CA-20180/CA/NCI NIH HHS/ -- CA-21765/CA/NCI NIH HHS/ -- CA-34233/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 12;239(4841 Pt 1):775-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, UCLA 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3422516" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Humans ; Leukemia, Lymphoid/*genetics ; Molecular Sequence Data ; *Oncogenes ; *Philadelphia Chromosome ; RNA, Messenger/genetics ; *Transcription, Genetic
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  • 65
    Publication Date: 1988-06-03
    Description: In a study aimed at developing a vaccine against the asexual blood stages of Plasmodium falciparum, two T cell epitopes were identified within a nonpolymorphic region of gp190 of Plasmodium falciparum merozoites. The two epitopes, which were revealed by deletion analysis, stimulated human T cell clones. Peptides containing sequences of the epitopes stimulated the cloned T cells and peripheral blood mononuclear cells (PBMC) from malaria-infected individuals. Moreover, the T cell clones responded to 11 different Plasmodium falciparum isolates in culture, showing that the epitopes are recognized in native parasites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crisanti, A -- Muller, H M -- Hilbich, C -- Sinigaglia, F -- Matile, H -- McKay, M -- Scaife, J -- Beyreuther, K -- Bujard, H -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2453924" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/*immunology ; Epitopes/analysis/*immunology ; Humans ; Molecular Sequence Data ; Peptide Fragments/immunology ; Plasmodium falciparum/*immunology ; T-Lymphocytes/*immunology ; T-Lymphocytes, Helper-Inducer/immunology
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  • 66
    Publication Date: 1988-11-04
    Description: The cellular cues that guide neuronal growth cones toward their targets are highly conserved in such diverse organisms as insects and vertebrates. Evidence presented here suggests that the molecular mechanisms underlying these events may be equally conserved. This article describes the structure and function of fasciclin II, a glycoprotein expressed on a subset of fasciculating axons in the grasshopper embryo. Antibody perturbation experiments suggest that fasciclin II functions in mediating one form of neuronal recognition: selective fasciculation. Fasciclin II is a member of the immunoglobulin gene superfamily and is homologous in structure and function to the neural cell adhesion molecule N-CAM and to several other vertebrate cell adhesion molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrelson, A L -- Goodman, C S -- HD21294/HD/NICHD NIH HHS/ -- NS18366/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):700-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*physiology ; Axons/*physiology ; Cell Adhesion Molecules ; *Cell Adhesion Molecules, Neuronal ; Grasshoppers ; Membrane Glycoproteins/*physiology ; Molecular Sequence Data ; Multigene Family ; Nerve Tissue Proteins/*physiology ; Nervous System/*growth & development
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  • 67
    Publication Date: 1988-03-25
    Description: The induction of an immune response in mammals is initiated by specifically reactive T lymphocytes. The specificity of the reaction is mediated by a complex receptor, part of which is highly variable in sequence and analogous to immunoglobulin heavy- and light-chain variable domains. The functional specificity of the T cell antigen receptor is, however, markedly different from immunoglobulins in that it mediates cell-cell interactions via the simultaneous recognition of foreign antigens and major histocompatibility complex-encoded molecules expressed on the surface of various lymphoid and nonlymphoid cells. The relation between the structure of the receptor and its functional specificity was investigated by analyzing the primary sequences of the receptors expressed by a series of T lymphocyte clones specific for a model antigen, pigeon cytochrome c. Within this set of T lymphocyte clones there was a striking selection for amino acid sequences in the receptor beta-chain in the region analogous to the third complementarity-determining region of immunoglobulins. Thus, despite the functional differences between T cell antigen receptors and immunoglobulin molecules, analogous regions appear to be important in determining ligand specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedrick, S M -- Engel, I -- McElligott, D L -- Fink, P J -- Hsu, M L -- Hansburg, D -- Matis, L A -- AI00662/AI/NIAID NIH HHS/ -- AI21372/AI/NIAID NIH HHS/ -- GM35880/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 25;239(4847):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832942" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Specificity ; Antigens/immunology ; Base Sequence ; Clone Cells/immunology ; Columbidae ; Cytochrome c Group/immunology ; Immunoglobulin Variable Region/immunology ; Major Histocompatibility Complex ; Molecular Sequence Data ; *Receptors, Antigen, T-Cell/genetics/immunology ; Sequence Homology, Nucleic Acid
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  • 68
    Publication Date: 1988-12-23
    Description: Hypocalcemic vitamin D-resistant rickets is a human genetic disease resulting from target organ resistance to the action of 1,25-dihydroxyvitamin D3. Two families with affected children homozygous for this autosomal recessive disorder were studied for abnormalities in the intracellular vitamin D receptor (VDR) and its gene. Although the receptor displays normal binding of 1,25-dihydroxyvitamin D3 hormone, VDR from affected family members has a decreased affinity for DNA. Genomic DNA isolated from these families was subjected to oligonucleotide-primed DNA amplification, and each of the nine exons encoding the receptor protein was sequenced for a genetic mutation. In each family, a different single nucleotide mutation was found in the DNA binding domain of the protein; one family near the tip of the first zinc finger (Gly----Asp) and one at the tip of the second zinc finger (Arg----Gly). The mutant residues were created in vitro by oligonucleotide directed point mutagenesis of wild-type VDR complementary DNA and this cDNA was transfected into COS-1 cells. The produced protein is biochemically indistinguishable from the receptor isolated from patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, M R -- Malloy, P J -- Kieback, D G -- Kesterson, R A -- Pike, J W -- Feldman, D -- O'Malley, B W -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2849209" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Calcitriol/metabolism ; Cell Line ; Cell Line, Transformed ; Codon ; DNA/genetics/metabolism ; Exons ; Female ; Gene Amplification ; Homozygote ; Humans ; Hypocalcemia/*genetics ; Immunoblotting ; Male ; Molecular Sequence Data ; *Mutation ; Receptors, Calcitriol ; Receptors, Steroid/*genetics/metabolism ; Rickets/*genetics ; Transfection
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  • 69
    Publication Date: 1988-05-20
    Description: The self-binding properties of a dominant idiotypic antibody (T15) and a minor idiotypic antibody (M603), both specific for phosphorylcholine, were examined as models of self-binding antibodies (autobodies). Observed differences in the self-binding affinity of T15 and M603 relate to variable sequence differences in their respective heavy and light chains. A molecular recognition theory based on the translation of coding and noncoding DNA strands was used to identify complementary amino acid sequences responsible for self-binding. The second hypervariable region of the heavy chain domain, extending into the third framework region, was predicted as the primary self-binding locus. Among peptides synthesized with different variable heavy and light chain regions, a 24-residue peptide spanning the second hypervariable and third framework regions of the heavy chain of T15 was nearly as effective as phosphorycholine in inhibiting the self-binding complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, C Y -- Brunck, T K -- Kieber-Emmons, T -- Blalock, J E -- Kohler, H -- AG04180/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1988 May 20;240(4855):1034-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IDEC Pharmaceuticals Corporation, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3368787" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Autoantibodies/*immunology ; Choline/pharmacology ; Immunoglobulin Idiotypes/*immunology ; Immunoglobulin Variable Region/*immunology ; Peptides/pharmacology ; Phosphorylcholine/pharmacology ; Protein Binding ; Structure-Activity Relationship
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  • 70
    Publication Date: 1988-12-09
    Description: A proteinase with high affinity for insulin has been proposed to play a role in the cellular processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been isolated and sequenced. The deduced amino acid sequence of the enzyme contained the sequences of 13 peptides derived from the isolated protein. The cDNA could be transcribed in vitro to yield a synthetic RNA that in cell-free translations produced a protein that coelectrophoresed with the native proteinase and could be immunoprecipitated with monoclonal antibodies to this enzyme. The deduced sequence of this proteinase did not contain the consensus sequences for any of the known classes of proteinases (that is, metallo, cysteine, aspartic, or serine), but it did show homology to an Escherichia coli proteinase (called protease III), which also cleaves insulin and is present in the periplasmic space. Thus, these two proteins may be members of a family of proteases that are involved in intercellular peptide signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Affholter, J A -- Fried, V A -- Roth, R A -- CA21765/CA/NCI NIH HHS/ -- DK01393/DK/NIDDK NIH HHS/ -- DK34926/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1415-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3059494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Endopeptidases/*genetics ; Escherichia coli/enzymology/*genetics ; Genes ; Humans ; Insulysin/*genetics ; *Metalloendopeptidases ; Molecular Sequence Data ; Peptide Hydrolases/*genetics ; Sequence Homology, Nucleic Acid
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  • 71
    Publication Date: 1988-10-14
    Description: Mycobacterium leprae induces T cell reactivity and protective immunity in the majority of exposed individuals, but the minority that develop leprosy exhibit various types of immunopathology. Thus, the definition of epitopes on M. leprae antigens that are recognized by T cells from different individuals might result in the development of an effective vaccine against leprosy. A sequence from the 65-kD protein of this organism was recognized by two HLA-DR2-restricted, M. leprae-specific helper T cell clones that were derived from a tuberculoid leprosy patient. Synthetic peptides were used to define this epitope as Leu-Gln-Ala-Ala-Pro-Ala-Leu-Asp-Lys-Leu. A similar peptide that was derived from the third hypervariable region of the HLA-DR2 chain, Glu-Gln-Ala-Arg-Ala-Ala-Val-Asp-Thr-Tyr, also activated the same clones. The unexpected cross-reactivity of this M. leprae-specific DR2-restricted T cell epitope with a DR2 peptide may have to be considered in the design of subunit vaccines against leprosy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, D C -- van Schooten, W C -- Barry, M E -- Janson, A A -- Buchanan, T M -- de Vries, R R -- AI-23982/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):259-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2459778" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antigens, Bacterial/*immunology ; Epitopes/*immunology ; HLA-DR Antigens/*immunology ; HLA-DR2 Antigen ; Leprosy/immunology ; Molecular Sequence Data ; Mycobacterium leprae/*immunology ; Peptides/immunology ; T-Lymphocytes/*immunology ; T-Lymphocytes, Helper-Inducer/immunology
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  • 72
    Publication Date: 1988-05-20
    Description: A chimeric mouse-human Fab protein that binds specifically to the human carcinoma cell line C3347 has been expressed and secreted from Escherichia coli. This molecule, which contains functionally assembled kappa and Fd proteins, binds as effectively to sites on the surface of C3347 cells as Fab fragments prepared proteolytically from whole chimeric or mouse antibody. The production in Escherichia coli of foreign heterodimeric protein reagents, such as Fab, should prove useful in the management of human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Better, M -- Chang, C P -- Robinson, R R -- Horwitz, A H -- New York, N.Y. -- Science. 1988 May 20;240(4855):1041-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉International Genetic Engineering Inc. (INGENE), Santa Monica, CA 90404.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3285471" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen-Antibody Complex/immunology ; Antigens, Surface/immunology ; Base Sequence ; Cell Line ; *Chimera ; Escherichia coli/*genetics ; Genes, Immunoglobulin ; Humans ; Immunoglobulin Fab Fragments/*genetics/immunology ; Mice ; Molecular Sequence Data ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 73
    Publication Date: 1988-07-01
    Description: The three-dimensional structure of ribulose-1,5-biphosphate carboxylase-oxygenase (RuBisCO), has been determined at 2.6 A resolution. This enzyme initiates photosynthesis by combining carbon dioxide with ribulose bisphosphate to form two molecules of 3-phosphoglycerate. In plants, RuBisCO is built from eight large (L) and eight small (S) polypeptide chains, or subunits. Both S chains and the NH2-terminal domain (N) of L are antiparallel beta, "open-face-sandwich" domains with four-stranded beta sheets and flanking alpha helices. The main domain (B) of L is an alpha/beta barrel containing most of the catalytic residues. The active site is in a pocket at the opening of the barrel that is partly covered by the N domain of a neighboring L chain. The domain contacts of the molecule and its conserved residues are discussed in terms of this structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, M S -- Suh, S W -- Curmi, P M -- Cascio, D -- Smith, W W -- Eisenberg, D S -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):71-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3133767" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Macromolecular Substances ; Molecular Sequence Data ; Plants/*enzymology ; Protein Conformation ; Rhodospirillum rubrum/enzymology ; *Ribulose-Bisphosphate Carboxylase ; X-Ray Diffraction
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  • 74
    Publication Date: 1988-09-23
    Description: Complementary DNAs were isolated and used to deduce the primary structures of the alpha 1 and alpha 2 subunits of the dihydropyridine-sensitive, voltage-dependent calcium channel from rabbit skeletal muscle. The alpha 1 subunit, which contains putative binding sites for calcium antagonists, is a hydrophobic protein with a sequence that is consistent with multiple transmembrane domains and shows structural and sequence homology with other voltage-dependent ion channels. In contrast, the alpha 2 subunit is a hydrophilic protein without homology to other known protein sequences. Nucleic acid hybridization studies suggest that the alpha 1 and alpha 2 subunit mRNAs are expressed differentially in a tissue-specific manner and that there is a family of genes encoding additional calcium channel subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellis, S B -- Williams, M E -- Ways, N R -- Brenner, R -- Sharp, A H -- Leung, A T -- Campbell, K P -- McKenna, E -- Koch, W J -- Hui, A -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1661-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458626" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Calcium Channel Blockers/pharmacology ; Cloning, Molecular ; *Dna ; DNA Restriction Enzymes ; Dihydropyridines/pharmacology ; *Ion Channels/drug effects ; Molecular Sequence Data ; Organ Specificity ; *Peptide Mapping ; RNA, Messenger/biosynthesis ; Rabbits ; Sequence Homology, Nucleic Acid
    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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  • 75
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-05-13
    Description: Analyses of steroid receptors are important for understanding molecular details of transcriptional control, as well as providing insight as to how an individual transacting factor contributes to cell identity and function. These studies have led to the identification of a superfamily of regulatory proteins that include receptors for thyroid hormone and the vertebrate morphogen retinoic acid. Although animals employ complex and often distinct ways to control their physiology and development, the discovery of receptor-related molecules in a wide range of species suggests that mechanisms underlying morphogenesis and homeostasis may be more ubiquitous than previously expected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, R M -- New York, N.Y. -- Science. 1988 May 13;240(4854):889-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92138-9216.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283939" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; DNA/metabolism ; Gene Expression Regulation ; Humans ; Receptors, Steroid/genetics/*physiology ; Receptors, Thyroid Hormone/genetics/*physiology
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  • 76
    Publication Date: 1988-06-10
    Description: The human T cell receptor delta (TCR delta) gene encodes one component of the TCR gamma delta-CD3 complex found on subsets of peripheral blood and thymic T cells. Human TCR delta diversity was estimated by characterizing rearrangements in TCR gamma delta cell lines and determining the structures of complementary DNA clones representing functional and nonfunctional transcripts in these cell lines. One V delta segment and one J delta segment were identified in all functional transcripts, although a distinct J delta segment was identified in a truncated transcript. Further, one D delta element was identified, and evidence for the use of an additional D delta element was obtained. Thus human TCR delta genes appear to use a limited number of germline elements. However, the apparent use of two D delta elements in tandem coupled with imprecise joining and extensive incorporation of N nucleotides generates unprecedented variability in the junctional region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hata, S -- Satyanarayana, K -- Devlin, P -- Band, H -- McLean, J -- Strominger, J L -- Brenner, M B -- Krangel, M S -- K01-AM01598/AM/NIADDK NIH HHS/ -- R01-AM30241/AM/NIADDK NIH HHS/ -- S07RR05526-24/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3259726" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Genes ; Genetic Variation ; Humans ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*immunology
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  • 77
    Publication Date: 1988-11-18
    Description: A complementary DNA clone corresponding to a 4.2-kilobase transcript that is present in the Xenopus oocyte and newly transcribed in the neurula stages of development has been isolated. This messenger RNA encodes a 155-amino acid protein that is 84% identical to the human basic fibroblast growth factor (bFGF). When expressed in Escherichia coli and purified, the Xenopus FGF induced mesoderm in animal cell blastomeres as measured by muscle actin expression. Immunoblots with an antibody to a Xenopus FGF peptide show that the oocyte and early embryo contain a store of the FGF polypeptide at high enough concentrations to induce mesoderm. The presence of FGF in the oocyte, together with the apparent lack of a secretory signal sequence in the protein, suggest that the regulation of mesoderm induction may involve novel mechanisms that occur after the translation of FGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimelman, D -- Abraham, J A -- Haaparanta, T -- Palisi, T M -- Kirschner, M W -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194757" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Blotting, Western ; Cloning, Molecular ; DNA/genetics ; DNA Probes ; Fibroblast Growth Factors/*physiology ; Gene Expression Regulation ; Mesoderm/*cytology ; Molecular Sequence Data ; Oocytes/physiology ; Xenopus laevis/*embryology
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  • 78
    Publication Date: 1988-06-03
    Description: The alpha 2 and beta 2 adrenergic receptors, both of which are activated by epinephrine, but which can be differentiated by selective drugs, have opposite effects (inhibitory and stimulatory) on the adenylyl cyclase system. The two receptors are homologous with each other, rhodopsin, and other receptors coupled to guanine nucleotide regulatory proteins and they contain seven hydrophobic domains, which may represent transmembrane spanning segments. The function of specific structural domains of these receptors was determined after construction and expression of a series of chimeric alpha 2-,beta 2-adrenergic receptor genes. The specificity for coupling to the stimulatory guanine nucleotide regulatory protein lies within a region extending from the amino terminus of the fifth hydrophobic domain to the carboxyl terminus of the sixth. Major determinants of alpha 2- and beta 2-adrenergic receptor agonist and antagonist ligand binding specificity are contained within the seventh membrane spanning domain. Chimeric receptors should prove useful for elucidating the structural basis of receptor function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Kobilka, T S -- Daniel, K -- Regan, J W -- Caron, M G -- Lefkowitz, R J -- HL 16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1310-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Chimera ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Humans ; Molecular Sequence Data ; Pindolol/analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Adrenergic, alpha/*genetics ; Receptors, Adrenergic, beta/*genetics ; Yohimbine/metabolism
    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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  • 79
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The effects of the nature of the polyols used in polyurethane (PUR) synthesis on the structural transformations after ageing by UV irradiation has been studied. The investigations were performed on PUR prepared from polyester and polyether diol oligomers.The characterization of the samples before and after ageing in view of the structural changes, which influence the course of the photooxidative degradation and photocrosslinking as well as in view of changes of mechanical properties has been done. Comparative investigations were performed by spectroscopic and viscometric measurements.The results show pronounced heterogeneity of the degradative reactions, including the existence of crosslinking processes and producing thus very inhomogeneous polymeric material. The course and the intensity of photooxidative degradation of PUR differ together with changes of mechanical properties depending whether polyester or polyether polyol have been used. The processes of photooxidative degradation is less expressed in polyesterurethane then in polyurethane based on polyether, under the same conditions of experiments. Different structures of polyester diols caused the various ageing behaviour of PUR too.
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  • 80
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: QUALIFICATION OF HALS COMPOUNDSA complex method of examination has been developed suitable for the qualification of light stabilizers; by this method, according to experience, the efficacy of HALS compounds can be extensively and expediently characterized.Several light stabilizers of the HALS-type were examined and qualified, used alone or together with a UV-absorber.It has been found that, when selecting the appropriate structure for a given polymer, the weatherability of polyolefine foils is effectively increase to six-eightfold; the increase is even tenfold when the stabilizer is combined with a benzophenone-type compound.As a utilization of these experiences, a contract with the industry, led to the production of an LDPE based agricultural foil with a life-time of several years.
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  • 81
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Natural hail impact tests are scarcely available because hailstorms are limited to a small area and cannot be predicted regarding time, place and intensity. Therefore we relied on laboratory tests simulating natural hailstones by polyamide balls (5-50 mm dia.) whose final velocity could be varied according to meteorological data. So the influence of diameter (weight) and velocity of the artificial hailstones could be taken into consideration independently.The energy of damage or equivalent natural hailstone diameter were determined for 16 mm double skin sheet from PMMA as 0.2 J (14 mm dia.) for star shaped cracks and 2 J (26 mm dia.) for holes. These values do not significantly decrease after 10 years weathering. 10 mm double skin sheets from PC show an extremly high energy of damage of abt. 10 J (38 mm dia.) which decreases to a medium level of 2 J (26 mm dia.) after several years weathering. This decrease is remarkably reduced by weather resistant protective coating.As hailstorms consist to more than 80% of hailstones below 10 mm dia. (0.04 J) the mentioned sheet materials are quite hail resistant also after long weathering periods, but they cannot withstand an extreme hail catastrophe as in Munich July 12, 1984.
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  • 82
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The influence of the specimen temperature on many ageing processes is well known. Two aspects is dealt with: -Measurements of the specimen temperature on several positions of a specimen in commercial weathering devices at different exposure conditions. Technical measures to achieve to uniform ageing at all positions of a planar and homogeneous specimen. Examples from practical use.-Changing specimen temperatures (+60°C to -20°C) during the course of accelerated weathering, i.e. a combination of conventional accelerated weathering with a temperature cycle test.
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  • 83
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: An Folien (Dicke 100 pm) aus isotaktischem Polypropylen mit verschiedenen Antioxidansgehalten (0,0% bis 0,1%) wird die thermooxidative Alterunq mit der isothermen Langzeit-Differential-Thermo-Analyse (ILDTA) bis zu Temperaturen weit unter dem Kristallitschmelzbereich verfolqt und die Messwerte mit Ergebnissen aus dem Zeitstand-Zugversuch korreliert. Dabei zeigt sich, daß aus Messunqen mit der ILDTA bereits vor Einsetzen der autokatalytischen Zersetzunq sreaktion Ruckschlüsse auf die thermische Vorqeschichte der Proben und Aussagen auf das rnit einem Abfall der mechanischen Eigenschaften verbundene Ende der thermo-oxidativen Stabilität des Polymeren getroffen werden können.Weiters bietet die ILDTA die Moglichkeit, durch den direkten Zusamenhang zwischen Oxidationszeit und Antioxidansögehalt die örtliche Stabilisatorverteilung in Platten und in Folien zu bestimmen und damit Diffusionsvorqange zu verfolgen.
    Notes: Thermo-oxidative ageing processes were investigated in films (100 μm thick) made from isotactic polypropylene with different antioxidant concentrations between 0% and 0.1% using isothermal long-term differential thermal analysis (ILDTA). The end of the oven life of polypropylene coincided with the loss of mechanical properties which was confirmed by tensile tests at temperatures far below the crystallite melting range. Already prior to the beginning of autocatalytic decomposition, ILDTA experiments permits conclusions to be drawn on the thermal history of the specimens and statements made regarding the end of thermo-oxidative stability of the polymer, which is accompanied by a deterioration in the mechanical properties.In consequence of the correlation between oxidation time and antioxidant concentration the local antioxidant concentration in sheets or films can be measured by ILDTA. Thus, investigating the diffusion of an antioxidant in polypropylene using ILDTA is possible.
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  • 84
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Die Größenverteilungsfunktion von Dispersionen mit extrem breiter Verteilung (Durchmesserbereich 20 〈 D 〈 2000 nm) kann in der analytischen Ultrazentrifuge (AUC) nicht durch eine Standardmethode, z. B. durch Messung der Trübung τ bei einer einzigen Konzentration, bestimmt werden, weil sich die spezifische Trübung τ/c von sehr kleinen und sehr großen Teilchen zu stark unterscheidet. Um dieses Problem zu lösen, haben wir eine neue AUC-Technik, die sogenannte Coupling-PSD-Technik entwickelt. Dabei werden zwei unterschiedliche Konzentrationen derselben Dispersion gleichzeitig in einem einzigen AUC-Lauf vermessen und zwei korrespondierende Lichtintensitiit-Zeit-Kurven aufgezeichnet. Bei einer niedrigen Standardkonzentration cs werden hauptsachlich die größeren Teilchen erfaßt während bei einer 5 bis 30 mal heheren Konzentration ch vor allem die kleineren Teilchen registriert werden. Die beiden I(t)-Kurven werden mathematisch verkniipft und unter Verwendung des Stokeschen Gesetzes und der Streutheorie von Mie für homogene isotrope Kugeln in die gesuchte breite Verteilungsfunktion umgerechnet. Wir benutzen eine mit einem 8-Zellen-Rotor und einem Multiplexer ausgestattete AUC. Da sehr groBe und sehr kleine Teilchen gleichzeitig in einem einzigen Zentrifugenlauf bestimmt werden, kennen wir nicht mehr wie zuvor eine konstante Rotorgeschwindigkeit N anwenden, sondern miissen diese mit Hilfe eines Geschwindigkeitsprogramms N(t) innerhalb einer Stunde von 0 auf 40000 U/min erhehen.
    Notes: The particle size distribution (PSD) of extremely broad distributed dispersions (diameter range 20 〈 D 〈 2000 nm) is not possible to be measured by analytical ultracentrifuge (AUC) using the standard technique, i.e. measuring turbidity τ at a single concentration c, because the specific turbidity τ/c varies too much between very small and very large particles. To solve this problem we have developed a new AUC technique, the so-called Coupling-PSD-Technique. Here two different concentrations of the same dispersion are measured simultaneously by one single AUC run with two corresponding curves of light intensity I vs. time t being registered. At a low standard concentration cs, mainly the larger particles are detected, while at a concentration ch 5 to 30 times higher mainly the smaller particles are registered. Both I(t)-curves are coupled mathematically and transformed into the requested broad distribution curve employing Stokes' law and Mie's light scattering theory for homogeneous isotropic spheres.We use an AUC together with an 8-cells-rotor and a multiplexer. Because very large and very small particles are to be measured simultaneously in one single run, we can no more apply a constant rotor speed N as before, but by means of a time program N(t) we always have to increase the rotor speed from 0 to 40000 rpm within one hour.
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  • 85
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Makromolekulare Chemie 162 (1988), S. 135-148 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Die chemische Modifizierung von Polyvinylchlorid (PVC) durch ein Amin verleiht dem Polymeren höhere Reaktivität gegenüber der Pfropfcopolymerisation mit einem Vinylmonomeren. Die Pfropfcopolymerisation von Methylmethacrylat auf mit n-Butylamin modifiziertes PVC wurde thermisch mit Benzoylperoxid (Bz2O2) als Initiator oder photoaktiviert mit Benzophenon (BP) als Photosensibilisator gestartet. Das aus bestimmten Experimenten erhaltene rohe Polymerprodukt wurde durch fraktionierte Fällung in die verschiedenen Bestandteile wie Polymethylmethacrylat (PMMA, Homopolymeres), PVC-g-PMMA (Pfropfcopolymeres) und unverändertes (aminiertes) PVC aufgespalten. Die getrennten Fraktionen wurden mit Hilfe der IR-Spektroskopie und der Thermogravimetrie charakterisiert. Der Mechanismus der Pfropfcopolymerisation von den beiden verschiedenen Systemen wurde erörtert. In beiden Fällen wurden Pfropfausbeuten um 30 - 70%* und Pfropfcopolymerzusammensetzungen, PMMA/PVC (w/w) zwischen 2 und 3 erhalten.
    Notes: Chemical modification of poly(vinyl chloride), PVC, by an amine renders the polymer more reactive towards graft copolymerization with a vinyl monomer. The graft copolymerization of methyl methacrylate (MMA) on PVC modified by treatment with n-butylamine (n-BA) was started thermally at 30° using benzoyl peroxide (Bz2O2) as initiator and under photoactivation at 40° using benzophenone (BP) as photo sensitizer. The gross polymer products from selected experiments were fractionally separated into the constituent polymeric entities viz., poly(methyl methacrylate), PMMA (homopolymer), PVC-g-PMMA (graft copolymer), and unreacted (aminated) PVC following a method of fractional precipitation. The separated fractions were characterized by IR spectroscopy and thermogravimetry. The mechanisms of graft copolymerization for the two different systems have been discussed. In each case, grafting efficiencies of the order of 30-70% and graft copolymers having compositions given as PMMA/PVC (w/w) equal to 2-3 were readily obtained.
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  • 86
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Makromolekulare Chemie 162 (1988), S. 193-201 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Eine Reihe oberflächensulfonierter, makroporöser Styrol-Divinylbenzol-Copolymerer mit unterschiedlichen Gehalten an SO3H-Gruppen wurden hergestellt. Sowohl von diesen Copolymeren als auch vom nichtsulfonierten Copolymeren wurden Porenstruktur, Oberflächenhydrophilie und -polarität sowie das Sorptionsverhalten gegenüber einigen in Blut vorkommenden Substanzen bestimmt. Der Sorptionsgrad wird umso kleiner, je größer die Oberflächenpolarität ist. Die teilsulfonierten Polymeren könnten eine Anwendung in der Hämoperfusion finden.
    Notes: A series of surface sulphonated macroporous styrene-divinylbenzene (S-DVB) copolymers containing various amounts of  - SO3H groups was obtained. Porous structure, surface hydrophilicity and polarity, and sorption properties of these copolymers as well as those of starting S-DVB resin towards some substances which are present in blood were determined. The sorption degree becomes the smaller the higher is the surface polarity. The partially sulphonated copolymers may find an application in hemoperfusion.
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  • 87
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Der Einfluß einer chemischen Behandlung von dünnen Filmen einer Composit-Membran aus sulfoniertem Polyphenylenoxid wurde untersucht. Über den Einfluß der Konzentration von wáßrigen Lösungen von Formaldehyd, Schwefelsäure, Salzsäure, Phosporsäure, Natriumhydroxid sowie der Behandlungsdauer auf die Trenncharakteristik der inversen Osmose der Composit-Membranen mit einer Ionenaus-tauschkapazität von 2,14 und 2,50 meq/g in verschiedenen Kombinationen wird ausführlich berichtet. Die Ergebnisse zeigen, daß unter den besten chemischen Behandlungsbedingungen eine Erhöhung der Trenncharakteristik der inversen Osmose der sulfonierten Polyphenylenoxid/Polysulfon-Composit-Membran erreicht wird.
    Notes: The effect of chemical treatment on the reverse osmosis (RO) separation characteristics of sulfonated poly(phenylene oxide) (SPPO) thin film composite membranes was investigated. The effects of the concentrations of aqueous solutions of formaldehyde, sulfuric acid, hydrochloric acid, phosphoric acid, sodium hydroxide, and treatment time on the RO separation characteristics of the composite membranes with ion exchange capacity (IEC) of 2.14 and 2.50 meq/g in various combinations are reported in detail. The results indicate some enhancement in RO separation characteristics of the SPPO/polysulfone (PS) composite membrane under the best conditions of the chemical treatment.
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  • 88
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Bei der Herstellung dünner Filme von sulfonierten Polyphenylenoxid/Polysulfon (SPPO/PS)-Composit-Membranen wurde untersucht, daß ein Zusatz von Nitromethan zu einer Lösung von sulfoniertem Polyphenylenoxidnatrium erhöhte Wirkung auf die Trenncharakteristik der inversen Osmose besitzt. Der Einfluß von gamma-Strahlung auf dünne Filme der Composit-Membran unter nassen und trockenen Bedingungen wurde ebenfalls untersucht. Um die maximal mögliche Verbesserung zu erreichen, wurden die Composit-Membranen einer kombinierten chemischen und Gammastrahlen-Behandlung unter nassen und trockenen Bedingungen unterworfen.Die experimentellen Ergebnisse dieser kombinierten Behandlung zeigen, dalß die SPPO/PS Composit-Membran dabei abgebaut wird.
    Notes: The enhancement effect of the addition of nitromethane into the coating solution of sulfonated sodium poly(phenylene oxide) (SPPONa) polymer for the synthesis of sulfonated poly(phenylene oxide)/polysulfone (SPPO/PS) thin film composite membranes on reverse osmosis (RO) separation characteristic was studied. The effect of gamma-ray irradiation on the SPPO/PS thin film composite membranes was also evaluated when the membrane samples were in the wet and dry conditions. The composite membranes were also subjected to a chemical treatment combined with gamma-ray irradiation in both wet and dry conditions in the hope of obtaining the maximum possible enhancement under each treatment. However, the experimental data of this combined treatment indicated the possibility of some degradation of the SPPO/PS composite membranes.
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  • 89
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    Angewandte Makromolekulare Chemie 163 (1988), S. 37-45 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Mischungen aus Poly(styrol-co-butadien)/Polybutadien, Naturkautschuk/Poly-(ethylen-co-propylen-co-dien und Naturkautschuk/Poly(butadien-co-acrylnitril)) wurden nach drei unterschiedlichen Verfahren compoundiert und Härtungsverhalten sowie Zugfestigkeit und Bruchdehnung der Vulkanisate wurden verglichen.
    Notes: Compounding of styrene-butadiene copolymer/polybutadiene, natural rubber/ethylene-propylene-diene terpolymer and natural rubber/butadiene-acrylonitrile copolymer blends was done in three different ways and their curing behaviour and the tensile properties of the vulcanizates are compared.
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  • 90
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Methylmethacrylat (MMA) wurde mit Hilfe von Cerammoniumnitrat als Initiator auf Stärke gepfropft. Die Pfropfcopolymeren wurden durch selektive Lösungsextraktion in einem Soxhlet-Extraktor isoliert. Der Einfluß von Reaktionszeit, Initiatorkonzentration, Temperatur sowie der Monomer- und Särekonzentration auf die Pfropfausbeute wurde untersucht. Eine erste Studie der Kinetik dieser Pfropfcopolymerisationsreaktion zeigt, daß sie dem üblichen kinetischen Verhalten einer Radikalpolymerisation folgt.
    Notes: Methyl methacrylate (MMA) was grafted onto starch using ceric ammonium nitrate as initiator. The graft copolymers were isolated by selective solvent extraction in a Soxhlet apparatus. The effects of reaction time, initiator concentration, temperature, monomer, and acid concentrations on the graft yields were investigated. A preliminary kinetic study of the graft copolymerisation reactions shows that they follow the conventional kinetic behaviour of free radical polymerisation.
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  • 91
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    Angewandte Makromolekulare Chemie 163 (1988), S. 47-61 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Durch Verwendung von Phenol-Formaldehyd-Harz mit gepreßten Olivenkenen im Gewichtsverháltnis 20/80 wurden kleine zylindrische Formkörper durch Härtung hergestellt. Diese wurden pyrolysiert und einige Proben mit Wasserdampf aktiviert. Für diese Formkörper und für zwei kommerzielle Aktivkohlen für Laboratoriumsbzw. Industrie-Anwendungen wurden folgende Eigenschaften bestimmt: die spezifische Oberfláche, die Struktur, die Adsorptionseigenschaften sowie die Adsorptionskapazität. Die Ergebnisse zeigen, daß die hergestellten kohlenstoffhaltigen Materialien durch Aktivierung höhere Werte für die untersuchten Eigenschaften ergeben als die nur pyrolysierten Proben und die zwei kommerziellen Aktivkohlen. Es wurde festgestellt, daß die Adsorption des 4-Nitrophenols für alle untersuchten kohlenstoffhaltigen Materialien gemäß der Freundlich-Gleichung stattfindet. Die Raster-Elektronenmikroskopie zeigt, daß die hergestellten kohlenstoffhaltigen Materialien andere Porenarten aufweisen als die kommerziellen Aktivkohlen. Die experimentellen Ergebnisse werden durch die molekularen Dimensionen der zur Adsorption verwendeten Substanzen und den Polarisationseffekt der Substituenten am Benzolring erklärt.
    Notes: Mixtures of phenol-formaldehyde-resin and pressed olive stones in a weight ratio of 20/80 were cured as small cylinders and then pyrolyzed. Some samples were also activated by steam. For these specimens and for two commercial activated carbons of laboratory or industrial uses the specific surface area, the structure, the adsorption properties, and the adsorption capacity were determined. The results indicate that the carbonaceous material produced by activation has greater values for the examined properties in comparison to the only pyrolyzed and the two commercial activated carbons, respectively. It was found that the Freundlich-equation is valid for the adsorption of 4-nitrophenol on all carbonaceous materials examined. The produced carbonaceous materials have different kinds of pores than the commercial activated carbons. The experimental results are explained with regard to the molecular dimensions of the adsorptive substances and the polarization effect of the substituents of the benzene ring.
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  • 92
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    Angewandte Makromolekulare Chemie 163 (1988), S. 101-114 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Durch Anwendung der nichtlinearen Programmiermethode basierend auf der mittleren harmonischen Näherung wurden aus den Kontaktwinkeldaten die freie Dispersions- und polare, freie Oberflächenenergie, γSVd und γSVp, sowie die kritische, freie Oberflächenenergie, γc, von Polymeren bestimmt. Die Komponenten der freien Oberflächenergie der zu untersuchenden Flüssigkeiten, γLVd und γLVp, die die Bedingungen für den maximalen Wechselwirkungsparameter, Φ, wiedergeben, wurden ebenfalls mit Hilfe dieser Methode bestimmt.
    Notes: The dispersion and polar surface free energy components, γSVd and γSVp, and the critical surface free energy, γc, of polymers were determined from contact angle data by the application of a nonlinear programming method using harmonic mean approximation.The surface free energy components of the probe liquids, γLVd and γLVp, which reflect the conditions of the maximized interaction parameter, Φ, were also simultaneously determined by this method.
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  • 93
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    Angewandte Makromolekulare Chemie 163 (1988), S. 169-193 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: The condensation reaction of bisphenol A, melamine, and formaldehyde was investigated by gel permeation chromatography, 13C-NMR-spectroscopy, IR-spectroscopy and elemental analysis. Because of the high reaction rates the condensation could be investigated only in the range of pH 6-10. At pH 6 and 7 the reaction of melamine with formaldehyde is dominating.With increasing pH-value the condensation of bisphenol A with formaldehyde is observed preferably. At pH 10 the condensation results in high molecular products. Cocondensation of melamine and bisphenol A through methylene bridges does not take place. But as a separation of the bisphenol A-formaldehyde condensates from the other condensation products was not possible, the three components may be connected through methylene-ether groups and/or intermolecular hydrogen bridges.
    Notes: Die gemeinsame Kondensation von Bisphenol A, Melamin und Formaldehyd wurde mit Hilfe der Gelpermeationschromatographie, der 13C-NMR-Spektroskopie, IR-Spektroskopie und Elementaranalyse untersucht. Wegen der hohen Kondensationsgeschwindigkeit verläuft die Reaktion in Gegenwart der drei Komponenten nur im Bereich von pH 6-10 kontrollierbar. Bei pH 6 und 7 überwigt die Kondensation zwischen Melamin und Formaldehyd. Mit steigendem pH-Wert tritt die Reaktion von Bisphenol A mit Formaldehyd in den Vordergrund und führt bei pH 10 zu hochmolekularen Kondensationsprodukten.Auf direkte Cokondensation hinweisende Methylenverknüpfungen zwischen der phenolischen Komponente und Melamin konnten nicht nachgewiesen werden. Die Kondensationsprodukte des Melamins bzw. des Bisphenol A mit Formaldehyd lassen sich aber nicht mehr vollständig aus den Reaktionsgemischen der Vorkondensation abtrennen, was dafür spricht, daß die Komponenten über Methylenetherbrücken und/oder intermolekularen Wasserstoffbrücken miteinander verknüpft sind.
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  • 94
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    Angewandte Makromolekulare Chemie 163 (1988), S. 205-207 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Cyclodextrin membrane-modified electrodes as sensor materials have been prepared by dipping platinum electrodes in the water suspensions of an oriented cyclodextrin polymer, followed by drying the polymer layers on the electrodes. The polymer is obtained by the solid-liquid reaction between the crystal of cyclodextrin inclusion complex and hexamethylene diisocyanate in anisole. The thickness (2 - 80 μm) of the cyclodextrin membrane is satisfactorily controlled by changing the concentration of the water suspension of the polymer. The cyclodextrin membranemodified electrodes show a significant response to p-nitrophenolate in water which is highly in contrast with no measurable response to o- and m-nitrophenolates.
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  • 95
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Im Zusammenhang mit dem Studium des Wirkungsmechanismus von industriell hergestellten Antidegradantien vom Typus der N-Phenyl-N′-sek-alkyl-1,Cphenylendiamine wurde die Reaktion von N-Phenyl-1,4-benzochinonimin (I) und 4-Hydroxydiphenylamin (II) mit dem Kohlenstoff-Radikal 1-Cyano-l-methylethyl (R·) studiert. Das Gemisch von I und II reagiert mit R· sehr leicht unter Bildung der Verbindungen III, VI und VIII. I allein reagiert wesentlich langsamer, und das Reaktionsgemisch enthält mehrere Produkte. Neben der Verbindung III wurden auch die Verbindungen IV und VII identifiziert. II allein reagiert bei denselben Bedingungen nicht. Die Verbindung IV bildet die zwei isomeren Strukturen syn und anti. Die Verbindung VIII ist ziemlich unbeständig; aus ihren Umwandlungsprodukten wurde XI isoliert. Bei der Reduktion von IV entsteht die Verbindung V, die ähnlich wie VIII unbeständig ist.
    Notes: The reaction of N-phenyl-1,4-benzoquinoneimine (I)Decoding of abbreviations see p. 103/104. and 4-hydroxydiphenylamine (II) with the carbon centred 1-cyano-1-methylethyl radical (R·) was studied in connection with an investigation of the action mechanism of industrial antidegradants, such as N-phenyl-N′-sec-alkyl-1,4-phenylenediamines. The mixture of I and II reacts very readily with R·, giving rise to III, VI, and VIII. I alone reacts much slowlier, and the reaction mixture contains more products. IV and VII were identified along with III. Under the conditions used, II alone does not react at all. IV exists in two isomeric forms, syn and anti. VIII is very labile; XI was isolated from its transformation products. Reduction of IV gives V, which is labile, similarly to VIII.
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  • 96
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    Angewandte Makromolekulare Chemie 156 (1988), S. 123-137 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Samples of polyoxymethylene (unstabilized and stabilized with the antiozonants N-isopropyl-N′-phenyl-p-phenylenediamin (IPPD) and bis-(1,2,3,6-tetrahydrobenzaldehyd)pentaerithritylacetal (Vulkazon AFS)) were ozonized under mechanical load in a special climate chamber. Surface damages were determined by IR-spectroscopy and scanning electron microscopy. During the ozonolysis a damaged layer is formed, the thickness of which increases with increasing time of ozonization. During this damaging reaction acetal groups are attacked and oligomers are formed.
    Notes: Proben von unstabilisiertem und mit den Antiozonantien N-Isopropyl-N′-phenyl-p-phenylendiamin (IPPD) und Bis-(1,2,3,6-tetrahydrobenzaldehyd)-pentaerithrityl-acetal (Vulkazon AFS) stabilisiertem Polyoxymethylen wurden unter mechanischer Belastung in einer Klimakammer ozonisiert. Die Schädigungen auf der Oberfläche wurden IR-spektroskopisch und rasterelektronenmikroskopisch untersucht. Während der Ozonisierung von POM bildet sich eine geschädigte Schicht, deren Dicke mit zunehmender Ozonisierungszeit wächst. Hierbei wird das Polymere an den Acetalbindungen angegriffen, wodurch Ketten gespalten werden und Oligomere entstehen.
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  • 97
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    Angewandte Makromolekulare Chemie 156 (1988), S. 105-121 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Mit Hilfe verschiedener Methoden wurde der Einfluß der Entfernung unterschiedlicher porenbildender Verdünner aus porösen Styrol-Ethylstyrol-Acrylnitril-Divinylbenzol-Copolymeren auf die Netzwerkstruktur untersucht. Der günstigste Weg, den ursprünglichen strukturellen Bau des porösen Netzwerkes zu bewahren, welches in Gegenwart von solvatisierenden Verdünnern erhalten wurde, ist das Entfernen des inerten Mediums mit Methanol. Wenn die Wasserdampfmethode angewendet wird, fin det der sog. Kollapseffekt statt, und die aus solchen Harzen hergestellten Anionenaustauscher adsorbieren weniger Farbstoff im Vergleich zu jenen, die aus Perlen hergestellt worden sind, die mit Methanol behandelt wurden; Grund hierfür ist die durch den Kollaps veränderte Porengröße. Es wurde ebenfalls festgestellt, daß die in Anwesenheit von solvatisierenden Verdünnern (Mischungen aus Quellungs- und Fällmitteln) hergestellten Copolymeren in Methanol sehr gut quellen, obwohl dieses ein Fällungsmittel für Polystyrol ist.
    Notes: The influence of the removal of various diluents, pore forming agents from the porous styrene-ethylstyrene-acrylonitrile-divinylbenzene copolymers on the structure of the matrix was investigated by several methods. The most advantageous pathway to preserve the initial structural edifice of the porous networks performed in the presence of solvating diluents consisted in the removal of the inert media with methanol as it was noticed from the experimental data. If the steam treatment is applied, the collapse effect takes place and the anion exchangers prepared from such matrices exchange/adsorb less dye stuff by comparison with ones formed from beads treated with methanol, because the pore size was changed. It was also noticed that the porous copolymers performed in the presence of the solvating diluents (mixtures of solvatings and precipitants) swell very well in methanol though it is a precipitating medium for the polystyrenic macromolecular chains.
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  • 98
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    Angewandte Makromolekulare Chemie 156 (1988), S. 139-149 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: An Styrol-Zinkacrylat-Copolymeren wurde die Abhängigkeit der Glasübergangstemperatur von der Aufheizgeschwindigkeit und der Zusammensetzung mit Hilfe der Differential-Scanning-Calorimetrie untersucht. Die Thermogravimetrie wurde benutzt, um die Pyrolyse dieser Copolymeren an Luft bei drei verschiedenen Aufheizge-schwindigkeiten zu untersuchen. Die thermische Zersetzung von Ionomeren ist ein 3-Stufen-Prozeß. Die Reaktionsordnung und Aktivierungsenergie wurde für jede Stufe der Zersetzung bestimmt unter Verwendung eines Computerprogramms, das auf den Methoden von Kissinger, Freeman-Carrol und Ozawa basiert. Es zeigte sich, daß die thermische Stabilität durch die ionischen Gruppen abnimmt.
    Notes: The dependence of glass temperature on the heating rate and the composition for styrene-zinc acrylate copolymers has been investigated by differential scanning calorimetry. Thermogravimetry was used in order to examine these copolymers undergoing pyrolysis in an atmosphere of air at three different heating rates. Thermal decomposition of ionomers is a three-stage process. The orders and activation energies have been determined for each stage of decomposition using the computer programs based on the methods of Kissinger, Freeman-Carrol, and Ozawa. It was found that the heat stability is lowered by the ionic groups.
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  • 99
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    Angewandte Makromolekulare Chemie 156 (1988), S. 151-162 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Die Pfropfung der hydrophilen Monomeren N-Vinylpyrrolidon, 2-Hydroxyethyl-methacrylat und Acrylamid auf ungesättigte segmentierte Polyurethane in N,N-Dimethylformamid mit 2,2′-Azobisisobutyronitril als Initiator wurde untersucht. Die Pfropfcopolymeren wurden von den Homopolymeren durch selektive Extraktion in Soxhlet-Apparaturen abgetrennt. Die kinetische Untersuchung der Pfropfcopolymerisation zeigte, daß die Reaktionen dem gewöhnlichen kinetischen Verhalten radikalischer Polymerisationen folgen. Die Abhängigkeiten der Pfropfungsgeschwindigkeit von der Initiator- und N-Vinylpyrrolidonkonzentration waren von 0,5 bzw. 1,0 Ordnung. Für 2-Hydroxyethylmethacrylat wurden sie zu jeweils 0,5 und 2,0 gefunden. Die Gesamtaktivierungsenergie der Pfropfcopolymerisation des 2-Hydroxyethylmethacrylats und des N-Vinylpyrrolidons betragen jeweilig 21,81 und 16,28 kJ/mol.
    Notes: Grafting of unsaturated segmented polyurethanes with some hydrophilic monomers such as N-vinyl pyrrolidone, 2-hydroxyethylmethacrylate and acrylamide in N,N-dimethylformamide have been studied using 2,2′-azobisisobutyronitrile (AIBN) as initiator. Graft copolymers were isolated from homopolymers by selected solvent extraction using a Soxhlet apparatus. A kinetic study of graft copolymerization reactions showed that the reactions follow the conventional kinetic behaviour of free radical polymerization. The dependencies of the grafting rate on initiator and N-vinyl pyrrolidone concentrations were of 0.5 and 1.00 order, respectively. However, for the 2-hydroxyethylmethacrylate, the dependencies of the grafting rate on initiator and monomer concentrations were found to be of 0.5 and 2.00 order, respectively. The overall activation energy for the graft copolymerization of the 2-hydroxyethylmethacrylate and N-vinyl pyrrolidone were 21.81 kJ/mol and 16.28 kJ/mol, respectively.
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  • 100
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    Angewandte Makromolekulare Chemie 156 (1988), S. 179-185 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Ultra fine particles were impregnated by using a finely porous cellulose gel membrane. The impregnated gel membrane is a green transparent one and looks like a solid solution. Highly dispersed Ni catalysts on carbon were obtained from thermal decomposition of these gel membranes. The particle size is in the range of several nm to a few ten nm. They show interesting catalytic properties for hydrogenation of olefins such as cyclooctadiene.
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