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  • Amino Acid Sequence  (67)
  • Male  (56)
  • Transcription, Genetic  (37)
  • American Association for the Advancement of Science (AAAS)  (145)
  • American Association of Petroleum Geologists (AAPG)
  • 1985-1989  (145)
  • 1987  (145)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (145)
  • American Association of Petroleum Geologists (AAPG)
Years
  • 1985-1989  (145)
Year
  • 1
    Publication Date: 1987-06-05
    Description: The use of molecular biological approaches has defined new mechanisms that store information in the mammalian nervous system. Environmental stimuli alter steady-state levels of messenger RNA species encoding neurotransmitters, thereby altering synaptic, neuronal, and network function over time. External or internal stimuli alter impulse activity, which alters membrane depolarization and selectively changes the expression of specific transmitter genes. These processes occur in diverse peripheral and central neurons, suggesting that information storage is widespread in the neuraxis. The temporal profile of any particular molecular mnemonic process is determined by specific kinetics of turnover and by the geometry of the neuron resulting in axonal transport of molecules to different synaptic arrays at different times. Generally, transmitters, the agents of millisecond-to-millisecond communication, are subject to relatively long-lasting changes in expression, ensuring that ongoing physiological function is translated into information storage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Black, I B -- Adler, J E -- Dreyfus, C F -- Friedman, W F -- LaGamma, E F -- Roach, A H -- HD 12108/HD/NICHD NIH HHS/ -- NS 10259/NS/NINDS NIH HHS/ -- NS 20788/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1263-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2884727" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Medulla/metabolism ; Animals ; Brain/physiology ; Memory/*physiology ; Nervous System/anatomy & histology/metabolism ; *Nervous System Physiological Phenomena ; Neurons/physiology ; Neurotransmitter Agents/metabolism/*physiology ; Sympathetic Nervous System/metabolism/physiology ; Transcription, Genetic
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  • 2
    Publication Date: 1987-11-13
    Description: The long-term effects of excitotoxic lesions in the nucleus basalis magnocellularis of the rat were found to mimic several neuropathological and chemical changes associated with Alzheimer's disease. Neuritic plaque-like structures, neurofibrillary changes, and neuronal atrophy or loss were observed in the frontoparietal cortex, hippocampus, amygdala, and entorhinal cortex 14 months after the lesions were made. Cholinergic markers in neocortex were reduced, while catecholamine and indoleamine metabolism was largely unaffected at this time. Bilateral lesions of the nucleus basalis magnocellularis increased somatostatin and neuropeptide Y in the cortex of the rat by at least 138 and 284 percent, respectively, suggesting a functional interaction between cholinergic and peptidergic neurons that may differ from that in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arendash, G W -- Millard, W J -- Dunn, A J -- Meyer, E M -- HD 17933/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 13;238(4829):952-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of South Florida, Tampa 33620.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2890210" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholinesterase/metabolism ; Animals ; Biogenic Amines/metabolism ; Brain/metabolism/*pathology ; Cerebral Cortex/metabolism/*pathology ; Choline/metabolism ; Choline O-Acetyltransferase/metabolism ; Male ; Neuropeptide Y/analysis ; Olivary Nucleus/*physiology ; Organ Specificity ; Rats ; Rats, Inbred Strains ; Somatostatin/analysis
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Booth, W -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):355-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2885919" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*transmission ; Animals ; *Culicidae ; DNA Replication ; Female ; HIV/genetics ; Humans ; Insect Bites and Stings ; Insect Vectors ; Male ; Virus Replication
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-09
    Description: In sharp contrast with the experiences of all other industrialized nations, the size of the labor force of the United States is growing rapidly while, simultaneously, its age, gender, and ethnic composition are changing markedly. Consequently, human resource issues present an unprecedented challenge in the nation's quest to achieve a fully employed and equitable society. New public policies that focus on labor market adjustment policies will be required if these developments are to be a boon rather than a bane to the emerging postindustrial economy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Briggs, V M Jr -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):176-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉New York State School of Industrial and Labor Relations, Cornell University, Ithaca 14851.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659908" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Age Factors ; Australia ; Canada ; Emigration and Immigration ; *Employment ; Europe ; Female ; Humans ; Japan ; Male ; *Population ; Unemployment ; United States
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  • 5
    Publication Date: 1987-01-02
    Description: The alpha-chain of the nicotinic acetylcholine receptor carries the binding sites both for cholinergic ligands and for most experimentally induced or naturally occurring antibodies to the native receptor. By means of expression cloning in Escherichia coli, fusion proteins were derived from specific fragments of a complementary DNA encoding the mouse alpha-chain, allowing the mapping of the toxin-binding site to residues 160-216 and the main immunogenic region to residues 6-85. This approach permits the independent study of different functional domains of a complex receptor molecule and should be generally applicable to other proteins for which complementary DNA clones are available.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barkas, T -- Mauron, A -- Roth, B -- Alliod, C -- Tzartos, S J -- Ballivet, M -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):77-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432658" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Binding Sites ; Binding, Competitive ; Bungarotoxins/metabolism ; Cloning, Molecular ; Epitopes ; Humans ; Immunosorbent Techniques ; Ligands ; Mice ; Receptors, Nicotinic/genetics/*immunology ; Recombinant Fusion Proteins/immunology ; Species Specificity ; Structure-Activity Relationship
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-02
    Description: Overall, each of the program packages performed their tasks satisfactorily. For analyses where there was a well-defined answer, such as a search for a restriction site, there were few significant differences between the program sets. However, for tasks in which a degree of flexibility is desirable, such as homology or similarity determinations and database searches, DNASTAR consistently afforded the user more options in conducting the required analysis than did the other two packages. However, for laboratories where sequence analysis is not a major effort and the expense of a full sequence analysis workstation cannot be justified, MicroGenie and IBI-Pustell offer a satisfactory alternative. MicroGenie is a polished program system. Many may find that its user interface is more "user friendly" than the standard menu-driven interfaces. Its system of filing sequences under individual passwords facilitates use by more than one person. MicroGenie uses a hardware device for software protection that occupies a card slot in the computer on which it is used. Although I am sympathetic to the problem of software piracy, I feel that a less drastic solution is in order for a program likely to be sharing limited computer space with other software packages. The IBI-Pustell package performs the required analysis functions as accurately and quickly as MicroGenie but it lacks the clearness and ease of use. The menu system seems disjointed, and new or infrequent users often find themselves at apparent "dead-end menus" where the only clear alternative is to restart the entire program package. It is suggested from published accounts that the user interface is going to be upgraded and perhaps when that version is available, use of the system will be improved. The documentation accompanying each package was relatively clear as to how to run the programs, but all three packages assumed that the user was familiar with the computational techniques employed. MicroGenie and IBI-Pustell further complicated their documentation by mixing instructions for the version based on floppy disk operation with that for the hard disk version.(ABSTRACT TRUNCATED AT 400 WORDS)〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cannon, G C -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):97-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659902" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Sequence Homology, Nucleic Acid ; *Software
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barnes, D M -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):128-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037699" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy ; Amino Acid Sequence ; Antigens, Differentiation, T-Lymphocyte ; Antigens, Surface/metabolism ; Antiviral Agents/pharmacology/*therapeutic use ; Brain/metabolism ; Depression, Chemical ; Drug Evaluation ; HIV/drug effects/physiology ; HIV Envelope Protein gp120 ; Humans ; Male ; Oligopeptides/pharmacology/*therapeutic use ; Peptide T ; Protein Binding/drug effects ; Receptors, Virus/drug effects ; Retroviridae Proteins/metabolism ; Virus Replication/drug effects
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  • 8
    Publication Date: 1987-11-20
    Description: Cleavage of the peptide bonds of preprosomatostatin at basic residues near the carboxyl terminus yields somatostatin-14, somatostatin-28, and somatostatin-28 (1-12). However, little is known about the molecular forms derived from the amino terminal portion of the precursor, even though this part of the prohormone is highly conserved through evolution. By using an antibody against the amino terminus of prosomatostatin, a decapeptide with the structure Ala-Pro-Ser-Asp-Pro-Arg-Leu-Arg-Gln-Phe, corresponding to preprosomatostatin (25-34), was isolated from the endocrine portion of the rat stomach, the gastric antrum. The antral decapeptide may represent a bioactive product generated from prosomatostatin after a monobasic cleavage similar to that involved in the formation of somatostatin-28. In fact, a monobasic cleavage requires two basic residues and a domain containing nonpolar amino acids such as alanine or leucine, or both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoit, R -- Ling, N -- Esch, F -- AM I88II/AM/NIADDK NIH HHS/ -- HD 09690/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Montreal General Hospital Research Institute, Department of Medicine, McGill University, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2891188" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Hydrolysis ; Immunologic Techniques ; Peptide Fragments/physiology ; Protein Precursors/immunology/*physiology ; Protein Processing, Post-Translational ; Rats ; Somatostatin/immunology/*physiology ; Stomach/*physiology ; Structure-Activity Relationship
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  • 9
    Publication Date: 1987-10-23
    Description: Intraperitoneal administration of human recombinant interleukin-1 (IL-1) to rats can increase blood levels of corticosterone and adrenocorticotropic hormone (ACTH). The route by which IL-1 affects pituitary-adrenal activity is unknown. That the IL-1-induced pituitary-adrenal activation involves an increased secretion of corticotropin-releasing factor (CRF) is indicated by three lines of evidence. First, immunoneutralization of CRF markedly attenuated the IL-1-induced increase of ACTH blood levels. Second, after blockade of fast axonal transport in hypothalamic neurons by colchicine, IL-1 administration decreased the CRF immunostaining in the median eminence, indicating an enhanced release of CRF in response to IL-1. Third, IL-1 did not stimulate ACTH release from primary cultures of anterior pituitary cells. These data further support the notion of the existence of an immunoregulatory feedback circuit between the immune system and the brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkenbosch, F -- van Oers, J -- del Rey, A -- Tilders, F -- Besedovsky, H -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):524-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Medical Faculty, Free University, Amsterdam, the Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2443979" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/physiology ; Adrenocorticotropic Hormone/secretion ; Animals ; Axonal Transport/drug effects ; Colchicine/pharmacology ; Corticotropin-Releasing Hormone/immunology/*physiology ; Fluorescent Antibody Technique ; Hypothalamus/*metabolism ; Immune Sera/pharmacology ; Interleukin-1/*physiology ; Male ; Median Eminence/metabolism ; Neurons/*metabolism ; Pituitary Gland, Anterior/physiology ; Rats ; Rats, Inbred Strains
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  • 10
    Publication Date: 1987-03-20
    Description: Elevation of glucose transport is an alteration common to most virally induced tumors. Rat fibroblasts transformed with wild-type or a temperature-sensitive Fujinami sarcoma virus (FSV) were studied in order to determine the mechanisms underlying the increased transport. Five- to tenfold increases in total cellular glucose transporter protein in response to transformation were accompanied by similar increases in transporter messenger RNA levels. This, in turn, was preceded by an absolute increase in the rate of glucose transporter gene transcription within 30 minutes after shift of the temperature-sensitive FSV-transformed cells to the permissive temperature. The transporter messenger RNA levels in transformed fibroblasts were higher than those found in proliferating cells maintained at the nonpermissive temperature. The activation of transporter gene transcription by transformation represents one of the earliest known effects of oncogenesis on the expression of a gene encoding a protein of well-defined function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaum, M J -- Haspel, H C -- Rosen, O M -- AM35430-01/AM/NIADDK NIH HHS/ -- DK 35158/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1495-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3029870" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses ; Cell Division ; Cell Line ; *Cell Transformation, Viral ; Fibroblasts ; Gene Expression Regulation ; Kinetics ; Monosaccharide Transport Proteins/*genetics ; RNA, Messenger/genetics ; Rats ; Transcription, Genetic
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-06
    Description: The c-erbA gene belongs to a multigene family that encodes transcriptional regulatory proteins including the v-erbA oncogene product, steroid hormone receptors, and the vitamin D3 receptor. A v-erbA DNA probe encoding the DNA-binding region of the v-erbA protein was used to screen a human complementary DNA testis library. One of the clones isolated, erbA-T-1, was found to encode a 490-amino acid protein (erbA-T). The erbA-T polypeptide shows high homology with the proteins encoded by both the chicken c-erbA and the human c-erbA-beta genes but is most closely related to the chicken gene. The chicken c-erbA and the human c-erbA-beta genes encode high-affinity receptors for thyroid hormone, and here it is shown that the erbA-T protein binds specifically to 3,5,3'-triiodo-L-thyronine with a dissociation constant of 3.8 +/- 0.2 x 10(-10) M. These data imply that more than one thyroid hormone receptor exists in humans and that these receptors might have different tissue- and gene-activating specificities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benbrook, D -- Pfahl, M -- DK-35083/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, La Jolla Cancer Research Foundation, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672126" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; DNA/*metabolism ; *Genes ; Humans ; Kinetics ; Male ; Protein Biosynthesis ; *Proto-Oncogenes ; Receptors, Thyroid Hormone/*genetics/metabolism ; Testis/*metabolism ; Transcription, Genetic
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  • 12
    Publication Date: 1987-10-30
    Description: The major late transcription factor (MLTF) is a 46-kilodalton polypeptide that specifically binds to and activates transcription from the major late promoter of adenovirus. The presence of this promoter-specific transcription factor in uninfected HeLa cell extracts suggests that MLTF is also involved in the transcription of cellular genes. This report demonstrates that MLTF specifically stimulates transcription of the rat gamma-fibrinogen gene through a high-affinity binding site. Stimulation of transcription by MLTF was not dependent on the exact position of the MLTF binding site with respect either to the transcription initiation site or to adjacent promoter elements. These results suggest that one of the cellular functions of MLTF is to control gamma-fibrinogen gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chodosh, L A -- Carthew, R W -- Morgan, J G -- Crabtree, G R -- Sharp, P A -- P01-CA42063/CA/NCI NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):684-8.〈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/3672119" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*genetics ; Animals ; DNA-Binding Proteins/*genetics ; Fibrinogen/*genetics ; *Gene Expression Regulation ; *Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Rats ; Regulatory Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunn, A J -- Powell, M L -- Gaskin, J M -- MH25486/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, College of Medicine, University of Florida, Gainesville 32610.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685987" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Corticosterone/*blood ; Female ; Hypophysectomy ; Lymphocytes/physiology ; Male ; Mice ; Mice, Inbred Strains ; Models, Biological ; Newcastle Disease/*blood ; Pituitary-Adrenal System/*physiopathology ; Postoperative Complications/blood ; Stress, Physiological/blood
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D R -- Schultz, P G -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1401-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Single-Stranded/metabolism ; Hydrolysis ; Micrococcal Nuclease/*genetics/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Staphylococcus aureus/enzymology/genetics ; Substrate Specificity
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  • 15
    Publication Date: 1987-02-20
    Description: Four clones were isolated from an adult human brain complementary DNA library with an oligonucleotide probe corresponding to the first 20 amino acids of the beta peptide of brain amyloid from Alzheimer's disease. The open reading frame of the sequenced clone coded for 97 amino acids, including the known amino acid sequence of this polypeptide. The 3.5-kilobase messenger RNA was detected in mammalian brains and human thymus. The gene is highly conserved in evolution and has been mapped to human chromosome 21.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldgaber, D -- Lerman, M I -- McBride, O W -- Saffiotti, U -- Gajdusek, D C -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):877-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3810169" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics ; Amino Acid Sequence ; Amyloid/*genetics ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; DNA/genetics ; Humans ; Protein Conformation ; RNA, Messenger/genetics ; Solubility ; Transcription, Genetic
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-27
    Description: The earliest known response of eggs to sperm in many species is a change in egg membrane potential. However, for no species is it known what components of the sperm cause the opening of the egg plasma membrane channels. Protein isolated from sperm acrosomal granules of the marine worm Urechis caused electrical responses in oocytes with the same form, amplitude, and ion dependence as the fertilization potentials induced by living sperm. Sperm initiated fertilization potentials in oocytes when sperm-oocyte fusion, but not binding, was inhibited by clamping oocyte membrane potentials to positive values. Acrosomal protein also initiated electrical responses in clamped oocytes. These results support the hypothesis that it is the sperm acrosomal protein that opens ion channels in the oocyte membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gould, M -- Stephano, J L -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1654-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823908" target="_blank"〉PubMed〈/a〉
    Keywords: Acrosome/*physiology ; Action Potentials ; Animals ; Annelida ; Calcium/metabolism ; Carrier Proteins/isolation & purification/*pharmacology ; Electric Stimulation ; Electrophysiology ; Female ; Fertilization ; Male ; Sodium/metabolism ; *Sperm-Ovum Interactions ; Spermatozoa/*physiology
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  • 17
    Publication Date: 1987-10-09
    Description: An abnormal alpha 2-antiplasmin that is associated with a serious bleeding tendency has been found in a Dutch family and is referred to as alpha 2-antiplasmin Enschede. This abnormal alpha 2-antiplasmin is converted from an inhibitor of plasmin to a substrate. The molecular defect of alpha 2-antiplasmin Enschede, as revealed by sequencing of cloned genomic DNA fragments, consists of an alanine insertion near the active site region of the molecule. Substitution of this fragment into complementary DNA for a wild-type alpha 2-antiplasmin yields a translation product with physical and functional properties typical of the abnormal alpha 2-antiplasmin Enschede. The naturally occurring mutant may serve as a model for investigating the structures that determine the properties of an inhibitor versus those of a substrate in serine protease inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lijnen, H R -- Nelles, L -- Kluft, C -- Nieuwenhuis, H K -- Rijken, D C -- Collen, D -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):209-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Thrombosis and Vascular Research, University of Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2958938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/metabolism ; Fibrinolysin/*antagonists & inhibitors ; *Genes ; Humans ; Molecular Sequence Data ; *Mutation ; Protein Biosynthesis ; alpha-2-Antiplasmin/*genetics/metabolism
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-18
    Description: The regulatory domain of protein kinase C contains an amino acid sequence between residues 19 and 36 that resembles a substrate phosphorylation site in its distribution of basic residue recognition determinants. The corresponding synthetic peptide (Arg19-Phe-Ala-Arg-Lys-Gly-Ala25-Leu-Arg-Gln-Lys-Asn-Val-His -Glu-Val-Lys-Asn36) acts as a potent substrate antagonist with an inhibitory constant of 147 +/- 9 nM. It is a specific inhibitor of protein kinase C and inhibits both autophosphorylation and protein substrate phosphorylation. Substitution of Ala25 with serine transforms the pseudosubstrate into a potent substrate. These results demonstrate that the conserved region of the regulatory domain (residues 19 to 36) of protein kinase C has the secondary structural features of a pseudosubstrate and may be responsible for maintaining the enzyme in the inactive form in the absence of allosteric activators such as phospholipids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉House, C -- Kemp, B E -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1726-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Melbourne, Repatriation General Hospital, West Heidelberg, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3686012" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Homeostasis ; Kinetics ; Myosin-Light-Chain Kinase/metabolism ; Protein Kinase C/*metabolism ; Substrate Specificity
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  • 19
    Publication Date: 1987-07-17
    Description: The calcium-calmodulin-dependent protein kinase II is a major component of brain synaptic junctions and has been proposed to play a variety of important roles in brain function. A complementary DNA representing a portion of the smaller 50-kilodalton subunit of the rat brain enzyme has been cloned and sequenced. The calmodulin-binding region has been identified and a synthetic analog prepared that binds calmodulin with high affinity in the presence of calcium. Like the 50-kilodalton kinase polypeptide, the concentration of the messenger RNA varies both neuroanatomically and during postnatal development of the brain. The broad tissue and species cross-reactivity of the complementary DNA suggests that the 50-kilodalton subunit found in rat brain is evolutionarily conserved and is the product of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanley, R M -- Means, A R -- Ono, T -- Kemp, B E -- Burgin, K E -- Waxham, N -- Kelly, P T -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):293-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037704" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; Biological Assay ; Brain/enzymology/growth & development ; Calcium-Calmodulin-Dependent Protein Kinases ; Cloning, Molecular ; DNA/genetics ; Protein Kinases/*genetics ; RNA, Messenger/genetics ; Rats ; Species Specificity
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, C -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):158-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659906" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Humans ; *Life Expectancy ; Male ; Sex Factors ; Sex Ratio
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedrick, P W -- New York, N.Y. -- Science. 1987 Aug 28;237(4818):963.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3616627" target="_blank"〉PubMed〈/a〉
    Keywords: Acinonyx/*genetics ; Animals ; Carnivora/*genetics ; Genetic Variation ; *Genetics, Population ; Houseflies/*genetics ; Male ; Mice/genetics ; Reproduction
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  • 22
    Publication Date: 1987-12-18
    Description: Growth factors and their receptors are involved in the regulation of cell proliferation and also play a key role in oncogenesis. In this study, a novel putative kinase receptor gene, termed eph, has been identified and characterized by molecular cloning. Its primary structure is similar to that of tyrosine kinase receptors thus far cloned and includes a cysteine-rich region in the extracellular domain. However, other features of the sequence distinguish the eph gene product from known receptors with tyrosine kinase activity. Thus the eph protein may define a new class of these molecules. The eph gene is overexpressed in several human carcinomas, suggesting that this gene may be involved in the neoplastic process of some tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirai, H -- Maru, Y -- Hagiwara, K -- Nishida, J -- Takaku, F -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1717-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825356" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Restriction Enzymes ; *Genes ; Humans ; Molecular Sequence Data ; Neoplasms/metabolism ; Oncogenes ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/*genetics ; Transcription, Genetic
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  • 23
    Publication Date: 1987-05-15
    Description: A new human T-lymphotropic virus (HTLV-4) was recently described in healthy people from Senegal. This virus has many properties in common with members of the human T-lymphotropic viruses, particularly the human immunodeficiency virus or HIV, the etiologic agent of acquired immune deficiency syndrome (AIDS), but does not appear to be associated with immunodeficiency-related disorders. In the present study, serum samples were obtained from 4248 individuals from six West African countries, including Senegal, Guinea, Guinea Bissau, Mauritania, Burkina Faso, and Ivory Coast. These samples, collected during 1985-1987, were from people categorized as healthy control, sexually active risk, and disease populations. All samples were analyzed for reactivity to HTLV-4 and HIV by radioimmunoprecipitation-sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. Evidence for HTLV-4 infection was found in five of the six countries. The seroprevalence varied markedly from country to country. Healthy sexually active individuals in the risk category had the highest levels of HTLV-4 infection compared to individuals in the healthy control category and the disease category, the latter including AIDS patients. The seroprevalence of HIV infection in most of these countries was quite low, although tightly associated with the rare cases of AIDS. The biology of HTLV-4 infection thus differs from that of HIV in Central Africa or the United States and Europe. The presence of these viruses and their different pathogenicities in several countries of West Africa indicate the necessity for serologic assays that will distinguish between them. Further studies of their origin and distribution as well as of their biology will be important in advancing our understanding of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanki, P J -- M'Boup, S -- Ricard, D -- Barin, F -- Denis, F -- Boye, C -- Sangare, L -- Travers, K -- Albaum, M -- Marlink, R -- CA 18216/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- FOD 630/OD/NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):827-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3033826" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology ; Adult ; Africa, Western ; Deltaretrovirus/*isolation & purification ; Demography ; Female ; HIV/*isolation & purification ; Humans ; Inpatients ; Male ; Pregnancy ; Prisoners ; Prostitution ; Reference Values ; Risk
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  • 24
    Publication Date: 1987-10-16
    Description: A portion of the Duchenne muscular dystrophy (DMD) gene transcript from human fetal skeletal muscle and mouse adult heart was sequenced, representing approximately 25 percent of the total, 14-kb DMD transcript. The nucleic acid and predicted amino acid sequences from the two species are nearly 90 percent homologous. The amino acid sequence that is predicted from this portion of the DMD gene indicates that the protein product might serve a structural role in muscle, but the abundance and tissue distribution of the messenger RNA suggests that the DMD protein is not nebulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E P -- Monaco, A P -- Feener, C C -- Kunkel, L M -- 2T 32 GM07753-07/GM/NIGMS NIH HHS/ -- HD18658/HD/NICHD NIH HHS/ -- R01 NS23740/NS/NINDS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):347-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Genetics, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*genetics ; DNA, Recombinant ; Exons ; Humans ; Male ; Mice ; Molecular Sequence Data ; Muscle Proteins/genetics ; Muscles/analysis/embryology ; Muscular Dystrophies/*genetics ; Muscular Dystrophy, Animal/*genetics ; Myocardium/analysis ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; X Chromosome
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1987 Jun 26;236(4809):1626-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603001" target="_blank"〉PubMed〈/a〉
    Keywords: Humans ; Male ; National Institutes of Health (U.S.) ; Prostatic Neoplasms/*therapy ; United States
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  • 26
    Publication Date: 1987-01-16
    Description: In the process of protein secretion, amino-terminal signal sequences are key recognition elements; however, the relation between the primary sequence of an amino-terminal peptide and its ability to function as an export signal remains obscure. The limits of variation permitted for functional signal sequences were determined by replacement of the normal signal sequence of Saccharomyces cerevisiae invertase with essentially random peptide sequences. Since about one-fifth of these sequences can function as an export signal the specificity with which signal sequences are recognized must be very low.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, C A -- Preuss, D -- Grisafi, P -- Botstein, D -- GM18973/GM/NIGMS NIH HHS/ -- GM21253/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 16;235(4786):312-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3541205" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cytoplasm/enzymology ; Extracellular Space/enzymology ; Glycoside Hydrolases/*secretion ; Glycosylation ; Protein Sorting Signals/*physiology ; Saccharomyces cerevisiae/enzymology/metabolism ; Structure-Activity Relationship ; beta-Fructofuranosidase
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  • 27
    Publication Date: 1987-09-11
    Description: The envelope of the human immunodeficiency virus type 1 (HIV-1) plays a central role in the process of virus entry into the host cell and in the cytopathicity of the virus for lymphocytes bearing the CD4 molecule. Mutations that affect the ability of the envelope glycoprotein to form syncytia in CD4+ cells can be divided into five groups: those that decrease the binding of the envelope protein to the CD4 molecule, those that prevent a post-binding fusion reaction, those that disrupt the anchorage of the envelope glycoprotein in the membrane, those that affect the association of the two subunits of the envelope glycoprotein, and those that affect post-translational proteolytic processing of the envelope precursor protein. These findings provide a functional model of the HIV envelope glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kowalski, M -- Potz, J -- Basiripour, L -- Dorfman, T -- Goh, W C -- Terwilliger, E -- Dayton, A -- Rosen, C -- Haseltine, W -- Sodroski, J -- AI24755/AI/NIAID NIH HHS/ -- CA40658/CA/NCI NIH HHS/ -- CA40659/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 11;237(4820):1351-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629244" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Genes ; Genes, Viral ; Glycoproteins/analysis/*genetics ; HIV/*genetics ; Mutation ; Phenotype ; Plasmids ; Viral Envelope Proteins/analysis/*genetics
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  • 28
    Publication Date: 1987-12-04
    Description: The inherited genetic defect in adenomatous polyposis has been localized to a small region on the long arm of chromosome 5. Sixteen DNA marker loci were used to construct a linkage map of the chromosome. When five kindreds segregating a gene for adenomatous polyposis coli were characterized with a number of the markers, significant linkage was found between one marker and the disease gene. Linkage analysis determined the location of the defective gene within a primary genetic map of chromosome 5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leppert, M -- Dobbs, M -- Scambler, P -- O'Connell, P -- Nakamura, Y -- Stauffer, D -- Woodward, S -- Burt, R -- Hughes, J -- Gardner, E -- CA40641/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1411-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Human Genetics, 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/3479843" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; *Chromosomes, Human, Pair 5 ; Colonic Polyps/*genetics ; Female ; Gardner Syndrome/genetics ; *Genes ; Genetic Markers ; Humans ; Lod Score ; Male ; Neoplasms, Multiple Primary/*genetics
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  • 29
    Publication Date: 1987-08-14
    Description: Foreign DNA was successfully introduced into the germline of the African mosquito vector of malaria Anopheles gambiae. Stable integration of genes into the germlines of insects had been achieved previously only in Drosophila melanogaster and related species and required the use of the P element transposon. In these experiments with Anopheles gambiae, the plasmid pUChsneo was used, which contains the selectable marker neo gene flanked by P element inverted repeats. Mosquitoes injected with this plasmid were screened for resistance to the neomycin analog G-418. A single event of plasmid insertion was recovered. Integration appears to be stable and, thus far, resistance to G-418 has been expressed for eight generations. The transformation event appears to be independent of P.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, L H -- Sakai, R K -- Romans, P -- Gwadz, R W -- Kantoff, P -- Coon, H G -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):779-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3039658" target="_blank"〉PubMed〈/a〉
    Keywords: Anopheles/embryology/*genetics ; DNA Transposable Elements ; DNA, Bacterial/genetics ; Drosophila melanogaster/genetics ; Drug Resistance/genetics ; Female ; *Genes, Bacterial ; Gentamicins/pharmacology ; Male ; Microinjections ; Plasmids ; *Transformation, Genetic
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  • 30
    Publication Date: 1987-12-11
    Description: A new human retrovirus was isolated from a continuous cell line derived from a patient with CD4+ Tac- cutaneous T cell lymphoma/leukemia. This virus is related to but distinct from human T cell leukemia/lymphoma virus types I and II (HTLV-I and HTLV-II) and human immunodeficiency virus (HIV-1). With the use of a fragment of provirus cloned from one patient with T cell leukemia, closely related sequences were found in DNA of the cell line and of tumor cells from seven other patients with the same disease; these sequences were only distantly related to HTLV-I. The phenotype of the cells and the clinical course of the disease were clearly distinguishable from leukemia associated with HTLV-I. All patients and the wife of one patient showed a weak serological cross-reactivity with both HTLV-I and HIV-1 antigens. None of the patients proved to be at any apparent risk for HIV-1 infection. The name proposed for this virus is HTLV-V, and the date indicate that it may be a primary etiological factor in the major group of cutaneous T cell lymphomas/leukemias, including the sporadic lymphomas known as mycoses fungoides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Manzari, V -- Gismondi, A -- Barillari, G -- Morrone, S -- Modesti, A -- Albonici, L -- De Marchis, L -- Fazio, V -- Gradilone, A -- Zani, M -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1581-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dipartimento di Medicina Sperimentale e Scienze Biochimiche II, Universita di Roma, Tor Vergata, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825353" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/analysis ; Deltaretrovirus/classification/*isolation & purification/ultrastructure ; Female ; Humans ; Leukemia/*microbiology ; Lymphoma/*microbiology ; Male ; Microscopy, Electron ; T-Lymphocytes/cytology
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  • 31
    Publication Date: 1987-07-24
    Description: Neuronal cells express a pp60c-src variant that displays an altered electrophoretic mobility and a different V8 peptide pattern relative to pp60c-src expressed in tissues of non-neuronal origin. To determine whether the neuronal form of pp60c-src is encoded by a brain-specific messenger RNA, a mouse brain complementary DNA (cDNA) library was screened with a chicken c-src probe and a 3.8-kilobase c-src cDNA clone was isolated. This clone encodes a 60-kilodalton protein that differs from chicken or human pp60c-src primarily in having six extra amino acids (Arg-Lys-Val-Asp-Val-Arg) within the NH2-terminal 16 kilodaltons of the molecule. S1 nuclease protection analysis confirmed that brain c-src RNA contains an 18-nucleotide insertion at the position of the extra six amino acids. This insertion occurs at a position that corresponds to a splice junction in the chicken and human c-src genes. The isolated c-src cDNA clone encodes a protein that displays an identical V8 peptide pattern to that observed in pp60c-src isolated from tissues of neuronal origin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez, R -- Mathey-Prevot, B -- Bernards, A -- Baltimore, D -- P0I CA38497/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):411-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2440106" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/enzymology ; Chickens ; Cloning, Molecular ; DNA/metabolism ; DNA Restriction Enzymes ; DNA Transposable Elements ; Humans ; Isoenzymes/*genetics ; Mice ; Neurons/*enzymology ; Protein Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins pp60(c-src) ; Sequence Homology, Nucleic Acid ; Species Specificity
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  • 32
    Publication Date: 1987-07-24
    Description: Abnormal accumulation of connective tissue in blood vessels contributes to alterations in vascular physiology associated with disease states such as hypertension and atherosclerosis. Elastin synthesis was studied in blood vessels from newborn calves with severe pulmonary hypertension induced by alveolar hypoxia in order to investigate the cellular stimuli that elicit changes in pulmonary arterial connective tissue production. A two- to fourfold increase in elastin production was observed in pulmonary artery tissue and medial smooth muscle cells from hypertensive calves. This stimulation of elastin production was accompanied by a corresponding increase in elastin messenger RNA consistent with regulation at the transcriptional level. Conditioned serum harvested from cultures of pulmonary artery smooth muscle cells isolated from hypertensive animals contained one or more low molecular weight elastogenic factors that stimulated the production of elastin in both fibroblasts and smooth muscle cells and altered the chemotactic responsiveness of fibroblasts to elastin peptides. These results suggest that connective tissue changes in the pulmonary vasculature in response to pulmonary hypertension are orchestrated by the medial smooth muscle cell through the generation of specific differentiation factors that alter both the secretory phenotype and responsive properties of surrounding cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mecham, R P -- Whitehouse, L A -- Wrenn, D S -- Parks, W C -- Griffin, G L -- Senior, R M -- Crouch, E C -- Stenmark, K R -- Voelkel, N F -- CA31777/CA/NCI NIH HHS/ -- HD20521/HD/NICHD NIH HHS/ -- HL14985/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):423-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia ; Cattle ; Connective Tissue/pathology/*physiopathology ; Disease Models, Animal ; Elastin/genetics/physiology ; Humans ; Hypertension, Pulmonary/pathology/*physiopathology ; Muscle, Smooth, Vascular/pathology/*physiopathology ; RNA, Messenger/genetics ; Transcription, Genetic
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  • 33
    Publication Date: 1987-09-11
    Description: The role of polypeptide growth factors in the processes of inflammation and repair was investigated by analyzing the influence of transforming growth factor-beta (TGF-beta), applied directly to linear incisions made through rat dorsal skin. A dose-dependent, direct stimulatory effect of a single application of TGF-beta on the breaking strength of healing incisional wounds was demonstrated. An increase in maximum wound strength of 220 percent of control was observed at 5 days; the healing rate was accelerated by approximately 3 days for at least 14 days after production of the wound and application of TGF-beta. These increases in wound strength were accompanied by an increased influx of mononuclear cells and fibroblasts and by marked increases in collagen deposition at the site of application of TGF-beta. TGF-beta is thus a potent pharmacologic agent that can accelerate wound healing in rats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mustoe, T A -- Pierce, G F -- Thomason, A -- Gramates, P -- Sporn, M B -- Deuel, T F -- New York, N.Y. -- Science. 1987 Sep 11;237(4820):1333-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2442813" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Growth Substances/*pharmacology ; Male ; Peptides/*pharmacology ; Rats ; Rats, Inbred Strains ; Staining and Labeling ; Transforming Growth Factors ; Wound Healing/*drug effects ; Wounds, Penetrating/*pathology
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  • 34
    Publication Date: 1987-01-09
    Description: In Xuan Wei County, Yunnan Province, lung cancer mortality is among China's highest and, especially in females, is more closely associated with indoor burning of "smoky" coal, as opposed to wood or "smokeless" coal, than with tobacco smoking. Indoor air samples were collected during the burning of all three fuels. In contrast to wood and smokeless coal emissions, smoky coal emission has high concentrations of submicron particles containing mutagenic organics, especially in aromatic and polar fractions. These studies suggested an etiologic link between domestic smoky coal burning and lung cancer in Xuan Wei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mumford, J L -- He, X Z -- Chapman, R S -- Cao, S R -- Harris, D B -- Li, X M -- Xian, Y L -- Jiang, W Z -- Xu, C W -- Chuang, J C -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):217-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798109" target="_blank"〉PubMed〈/a〉
    Keywords: China ; *Coal ; Female ; Humans ; Male ; Neoplasms/etiology/*mortality ; Polycyclic Compounds/analysis ; Smoke/*adverse effects/analysis ; Wood
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  • 35
    Publication Date: 1987-05-15
    Description: Antibody-producing cells display a special form of regulation whereby each cell produces immunoglobulin from only one of its two sets of antibody genes. This phenomenon, called allelic exclusion, is thought to be mediated by the product of one heavy chain allele restricting the expression of the other. Heavy chains are synthesized in two molecular forms, secreted and membrane bound. In order to determine whether it is specifically the membrane-bound form of the immunoglobulin M (IgM) heavy chain (mu) that mediates this regulation, transgenic mice were created that carry a human mu chain gene altered so that it can only direct the synthesis of the membrane-bound protein. The membrane-bound form of the human mu chain was made by most of the B cells in these animals as measured by assays of messenger RNA and surface immunoglobulins. Further, the many B cells that express the human gene do not express endogenous mouse IgM, and the few B cells that express endogenous mouse mu do not express the transgene. Thus, the membrane-bound form of the mu chain is sufficient to mediate allelic exclusion. In addition, the molecular structures recognized for this purpose are conserved between human and mouse systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nussenzweig, M C -- Shaw, A C -- Sinn, E -- Danner, D B -- Holmes, K L -- Morse, H C 3rd -- Leder, P -- New York, N.Y. -- Science. 1987 May 15;236(4803):816-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107126" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; Antibody-Producing Cells/*immunology ; Gene Expression Regulation ; *Genes ; Humans ; Immunoglobulin M/genetics ; Immunoglobulin mu-Chains/*genetics ; Mice ; Mice, Inbred Strains ; RNA, Messenger/genetics ; Transcription, Genetic
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-09
    Description: The MerR protein mediates the induction of the mercury resistance phenotype in bacteria; it has been isolated in order to study the effects of metal-ion induced changes in the metabolism of prokaryotic cells at the molecular level. After DNA sequences responsible for negative autoregulation were removed, the 16-kilodalton protein was overproduced and purified to more than 90 percent homogeneity by a salt extraction procedure that yields about 5 milligrams of protein per gram of cells. Complementation data, amino terminal analysis, gel filtration, and deoxyribonuclease I protection studies demonstrate that the purified merR gene product is a dimer under nondenaturing conditions and that it binds specifically to DNA, in the presence and absence of mercury, at a palindromic site which is directly between the -10 and -35 regions of the structural genes and adjacent to its own promoter. These initial results indicate that MerR is a DNA-binding metalloregulatory protein that plays a central role in this heavy metal responsive system and they delineate an operator site in the mer operon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Halloran, T -- Walsh, C -- AI07256/AI/NIAID NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):211-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/genetics/*isolation & purification ; Base Sequence ; Chromatography, Gel ; DNA/metabolism ; DNA-Binding Proteins/genetics/*isolation & purification ; Macromolecular Substances ; *Mercury ; Operator Regions, Genetic ; R Factors/*genetics ; Transcription, Genetic
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  • 37
    Publication Date: 1987-06-12
    Description: A basic amphiphilic alpha-helix is a structural feature common to many calmodulin-binding peptides and proteins. A set of fluorescent analogues of a very tight binding inhibitor (dissociation constant of 200 picomolar) of calmodulin has been synthesized. The fluorescent amino acid tryptophan has been systematically moved throughout the sequence of this peptide. The fluorescence properties for the peptides repeat every three to four residues and are consistent with the periodicity observed for an alpha-helix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neil, K T -- Wolfe, H R Jr -- Erickson-Viitanen, S -- DeGrado, W F -- New York, N.Y. -- Science. 1987 Jun 12;236(4807):1454-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3589665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/metabolism ; Calmodulin-Binding Proteins/*metabolism ; Muscle, Smooth/enzymology ; Muscles/enzymology ; Myosin-Light-Chain Kinase/metabolism ; Protein Conformation ; Spectrometry, Fluorescence ; Tryptophan
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, A R -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1217.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685970" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA, Mitochondrial/*genetics ; Female ; Fertilization ; Male ; Spermatozoa/*physiology ; Zygote/physiology
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  • 39
    Publication Date: 1987-08-14
    Description: On the basis of electrophysiological analysis of Shaker mutants, the Shaker locus of Drosophila melanogaster has been proposed to encode a structural component of a voltage-dependent potassium channel, the A channel. Unlike sodium channels, acetylcholine receptors, and calcium channels, K+ channels have not been purified biochemically. To facilitate biochemical studies of a K+ channel, genomic DNA from the Shaker locus has been cloned. Rearrangements in five Shaker mutants have been mapped to a 60-kilobase segment of the genome. Four complementary DNA clones have been analyzed. These clones indicate that the Shaker gene contains multiple exons distributed over at least 65 kilobases of genomic DNA in the region where the mutations mapped. Furthermore, the gene may produce several classes of alternatively spliced transcripts. Two of the complementary DNA clones have been sequenced and their sequences support the hypothesis that Shaker encodes a component of a K+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papazian, D M -- Schwarz, T L -- Tempel, B L -- Jan, Y N -- Jan, L Y -- NS15963/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):749-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441470" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Drosophila melanogaster/*genetics ; Exons ; *Ion Channels ; Membrane Proteins/*genetics ; Mutation ; Nucleic Acid Hybridization ; Potassium/*metabolism ; RNA Splicing ; Transcription, Genetic ; Translocation, Genetic
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  • 40
    Publication Date: 1987-02-13
    Description: A highly T-lymphotropic virus was isolated from cats in a cattery in which all the animals were seronegative for feline leukemia virus. A number of cats in one pen had died and several had an immunodeficiency-like syndrome. Only 1 of 18 normal cats in the cattery showed serologic evidence of infection with this new virus, whereas 10 of 25 cats with signs of ill health were seropositive for the virus. Tentatively designated feline T-lymphotropic lentivirus, this new feline retrovirus appears to be antigenically distinct from human immunodeficiency virus. There is no evidence for cat-to-human transmission of the agent. Kittens experimentally infected by way of blood or plasma from naturally infected animals developed generalized lymphadenopathy several weeks later, became transiently febrile and leukopenic, and continued to show a generalized lymphadenopathy 5 months after infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedersen, N C -- Ho, E W -- Brown, M L -- Yamamoto, J K -- CA-39016-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):790-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3643650" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/analysis ; Cat Diseases/*microbiology ; Cats/*microbiology ; Female ; HIV/immunology ; Immunologic Deficiency Syndromes/microbiology/*veterinary ; Lymphocytes/ultrastructure ; Male ; Microscopy, Electron ; Retroviridae/immunology/*isolation & purification/ultrastructure ; Species Specificity
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-04-10
    Description: A cycloheximide-sensitive protein responsive to adenosine 3',5'-monophosphate has been postulated to participate in the regulation of cholesterol side-chain cleavage activity in steroidogenic tissues. Such a steroidogenesis activator polypeptide (SAP) had been isolated from rat adrenocortical tissue and partially characterized. Now a polypeptide with comparable chromatographic behavior and biological activity has been purified from the rat H-540 Leydig cell tumor in quantities sufficient for amino acid sequencing. The activator contains 30 amino acid residues and has a molecular weight of 3215. The synthetic construct based on this sequence is virtually equipotent with native H-540 tumor SAP in an adrenal mitochondrial cholesterol side-chain cleavage assay. Hormonal regulation of the intracellular concentration of this activator may control the rate of cholesterol metabolism in steroidogenic organs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pedersen, R C -- Brownie, A C -- AM18141/AM/NIADDK NIH HHS/ -- HD00613/HD/NICHD NIH HHS/ -- HD19309/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 10;236(4798):188-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3563495" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Cortex/analysis ; Amino Acid Sequence ; Animals ; Cholesterol/metabolism ; Cholesterol Side-Chain Cleavage Enzyme/*metabolism ; Chromatography, High Pressure Liquid ; *Heat-Shock Proteins ; Leydig Cell Tumor/*analysis ; Male ; Mitochondria/enzymology ; *Molecular Chaperones ; Oxidoreductases/*metabolism ; Peptide Fragments/analysis ; Proteins/*analysis ; Rats ; Steroids/*biosynthesis
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  • 42
    Publication Date: 1987-05-01
    Description: A partial amino acid sequence obtained for porcine atrial muscarinic acetylcholine receptor was used to isolate complementary DNA clones containing the complete receptor coding region. The deduced 466-amino acid polypeptide exhibits extensive structural and sequence homology with other receptors coupled to guanine nucleotide binding (G) proteins (for example, the beta-adrenergic receptor and rhodopsins); this similarity predicts a structure of seven membrane-spanning regions distinguished by the disposition of a large cytoplasmic domain. Stable transfection of the Chinese hamster ovary cell line with the atrial receptor complementary DNA leads to the binding of muscarinic antagonists in these cells with affinities characteristic of the M2 receptor subtype. The atrial muscarinic receptor is encoded by a unique gene consisting of a single coding exon and multiple, alternatively spliced 5' noncoding regions. The atrial receptor is distinct from the cerebral muscarinic receptor gene product, sharing only 38% overall amino acid homology and possessing a completely nonhomologous large cytoplasmic domain, suggesting a role for the latter region in differential effector coupling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peralta, E G -- Winslow, J W -- Peterson, G L -- Smith, D H -- Ashkenazi, A -- Ramachandran, J -- Schimerlik, M I -- Capon, D J -- CA16417/CA/NCI NIH HHS/ -- HL23632/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):600-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107123" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA/genetics ; Exons ; GTP-Binding Proteins/metabolism ; Heart Atria/analysis ; Immunosorbent Techniques ; Membrane Proteins ; Molecular Weight ; Nucleic Acid Hybridization ; Peptide Fragments/metabolism ; Quinuclidinyl Benzilate/metabolism ; Receptors, Muscarinic/*genetics/metabolism ; Sequence Homology, Nucleic Acid ; Swine ; Transfection
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  • 43
    Publication Date: 1987-07-10
    Description: Inhibin is a gonadal glycoprotein hormone that regulates the production of follicle-stimulating hormone (FSH) by the anterior pituitary gland and exhibits intragonadal actions as well. The present study shows that inhibin-like immunoreactivity (inhibin-LI) is present in cells of the cytotrophoblast layer of human placenta at term and in primary cultures of human trophoblasts. Human chorionic gonadotropin (hCG) stimulated secretion of inhibin-LI from these cultured placental cells. This effect was mimicked by 8-bromo-cyclic adenosine monophosphate (8-bromo-cAMP), forskolin, and cholera toxin, suggesting that the mechanism of hCG induction of placental inhibin-LI secretion is cAMP-dependent. Incubation with an antiserum that binds the alpha-subunit of human inhibin increased the secretion of hCG and gonadotropin-releasing hormone-like immunoreactivity (GnRH-LI) from trophoblast cells in culture, suggesting a local tonic inhibitory action of endogenous inhibin on hCG and GnRH-LI release. The action of inhibin on hCG secretion may partially require the presence of placental GnRH, as suggested by evidence that a synthetic GnRH antagonist partially reverses the hCG increase induced by inhibin immunoneutralization. Results suggest paracrine roles for both inhibin and GnRH in the regulation of placental hCG production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petraglia, F -- Sawchenko, P -- Lim, A T -- Rivier, J -- Vale, W -- AM26741/AM/NIADDK NIH HHS/ -- HD13527/HD/NICHD NIH HHS/ -- NS21182/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 10;237(4811):187-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299703" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Cells, Cultured ; Cholera Toxin/pharmacology ; Chorionic Gonadotropin/pharmacology/*secretion ; Chorionic Villi/analysis ; Colforsin/pharmacology ; Feedback ; Female ; Gonadotropin-Releasing Hormone/antagonists & inhibitors/pharmacology/secretion ; Humans ; Infant, Newborn ; Inhibins/analysis/*physiology ; Male ; Pregnancy ; Secretory Rate/drug effects ; Trophoblasts/analysis/drug effects/*secretion
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  • 44
    Publication Date: 1987-04-03
    Description: The primary structure of human uromodulin, a 616-amino acid, 85-kilodalton glycoprotein with in vitro immunosuppressive properties, was determined through isolation and characterization of complementary DNA and genomic clones. The amino acid sequence encoded by one of the exons of the uromodulin gene has homology to the low-density-lipoprotein receptor and the epidermal growth factor precursor. Northern hybridization analyses demonstrate that uromodulin is synthesized by the kidney. Evidence is provided that uromodulin is identical to the previously characterized Tamm-Horsfall glycoprotein, the most abundant protein in normal human urine.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennica, D -- Kohr, W J -- Kuang, W J -- Glaister, D -- Aggarwal, B B -- Chen, E Y -- Goeddel, D V -- New York, N.Y. -- Science. 1987 Apr 3;236(4797):83-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3453112" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Base Sequence ; Chemistry, Physical ; Cloning, Molecular ; Cysteine ; DNA/genetics ; Gene Expression Regulation ; Genes ; Glycoproteins/*genetics ; Humans ; Mucoproteins/*analysis/*genetics ; Peptide Fragments/analysis ; Physicochemical Phenomena ; RNA, Messenger/genetics ; Uromodulin
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  • 45
    Publication Date: 1987-02-13
    Description: Deregulation of c-myc expression in association with chromosomal translocations occurs in over 95% of murine plasmacytomas, rat immunocytomas, and human Burkitt lymphomas. Infection with a murine retrovirus (J-3) containing an avian v-myc rapidly induced plasmacytomas in pristane-primed BALB/cAn mice. Only 17% of the induced plasmacytomas that were karyotyped showed the characteristic chromosomal translocations involving the c-myc locus. Instead, all of the translocation-negative tumors demonstrated characteristic J-3 virus integration sites that were actively transcribed. Thus, the high levels of v-myc expression have replaced the requirement for chromosomal translocation in plasmacytomagenesis and accelerated the process of transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potter, M -- Mushinski, J F -- Mushinski, E B -- Brust, S -- Wax, J S -- Wiener, F -- Babonits, M -- Rapp, U R -- Morse, H C 3rd -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):787-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3810165" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds ; *Cell Transformation, Neoplastic ; *Genes, Viral ; Mice ; Mice, Inbred BALB C ; Mice, Inbred Strains ; Moloney murine leukemia virus/*genetics ; Nucleic Acid Hybridization ; *Oncogenes ; Plasmacytoma/genetics/*microbiology ; Retroviridae/*genetics ; Transcription, Genetic ; *Translocation, Genetic
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  • 46
    Publication Date: 1987-12-04
    Description: A specific inhibitor of the neuraminidase of the protozoan parasite Trypanosoma cruzi was isolated recently and named cruzin. It is now shown that cruzin is similar to high-density lipoprotein by amino acid homology, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, by immunoblot analysis, and by isoelectric focusing. Cruzin purified by ion exchange chromatography and high-density lipoprotein isolated by density gradient ultracentrifugation inhibited Trypanosoma cruzi neuraminidase to the same extent. Cruzin or high-density lipoprotein restores to normal the decreased multiplication rate of Trypanosoma cruzi epimastigotes grown in a medium depleted of lipoproteins, suggesting that it may be important for survival of the parasite in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prioli, R P -- Ordovas, J M -- Rosenberg, I -- Schaefer, E J -- Pereira, M E -- AI 07380/AI/NIAID NIH HHS/ -- AI 18102/AI/NIAID NIH HHS/ -- HL 35243/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1417-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Geographic Medicine and Infectious Diseases, New England Medical Center Hospitals, Inc., Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Anti-Infective Agents ; Apolipoprotein A-I ; Apolipoproteins A/genetics/immunology ; Blood Proteins/immunology/pharmacology/*physiology ; Isoelectric Focusing ; Lipoproteins, HDL/*physiology ; Neuraminidase/antagonists & inhibitors ; Trypanosoma cruzi/*enzymology/growth & development
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-02-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Racker, E -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):959-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434995" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/metabolism ; Cloning, Molecular ; Crystallization ; Humans ; Ion Channels/physiology ; Membrane Proteins/genetics/*physiology ; Mitochondria/metabolism ; Mutation ; Protein Conformation ; Receptors, Cell Surface/physiology
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  • 48
    Publication Date: 1987-08-07
    Description: The avian acute leukemia virus E26 induces a mixed erythroid-myeloid leukemia in chickens and carries two distinct oncogenes, v-myb and v-ets. Recently, a novel gene named erg, closely related to the v-ets oncogene, was identified in human COLO 320 cells and the nucleotide sequence of its approximately 5.0-kilobase transcript, erg 1 was determined. In the present study, the nucleotide sequence of the alternatively spliced transcript, erg 2, was found to differ from erg 1 by a splicing event that causes a coding frameshift near the amino terminus, resulting in an additional 99-amino acid insertion at the amino-terminus. Expression of complementary DNAs for the two transcripts in vitro resulted in synthesis of polypeptides of approximately 41 and 52 kilodaltons, suggesting the use of alternative translation initiation codons in the case of erg proteins. The erg gene was localized by somatic cell genetic analysis to human chromosome 21. It is proposed that alternative sites of splicing and polyadenylation, together with alternative sites of translation initiation, allow the synthesis of two related polypeptides from a single erg gene transcriptional unit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rao, V N -- Papas, T S -- Reddy, E S -- New York, N.Y. -- Science. 1987 Aug 7;237(4815):635-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299708" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Chromosomes, Human, Pair 21 ; Cloning, Molecular ; Humans ; Oncogenes ; Plasmids ; Poly A/metabolism ; *Protein Biosynthesis ; Proto-Oncogene Proteins/biosynthesis ; *Proto-Oncogenes ; *RNA Splicing ; RNA, Messenger ; Sequence Homology, Nucleic Acid
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-28
    Description: Chemical evidence is needed in both insect endocrinology and sensory physiology to understand hormone and pheromone action at the molecular level. Radiolabeled pheromones and hormones have been synthesized and used to identify binding and catabolic proteins from insect tissues. Chemically modified analogs, including photoaffinity labels and enzyme inhibitors, are among the tools used to covalently modify the specific acceptor or catalytic sites. Such targeted agents can also provide leads for the design of growth and mating disruptants by allowing manipulation of the physiologically important interactions of the chemical signals with macromolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prestwich, G D -- GM-30899/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 28;237(4818):999-1006.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3616631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bees/metabolism ; Chemical Phenomena ; Chemistry ; Cockroaches/metabolism ; Female ; Insect Hormones/*metabolism ; Insects/metabolism ; Juvenile Hormones/metabolism ; Male ; Methoprene/metabolism ; Moths/metabolism ; Pheromones/*metabolism
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-27
    Description: Many RNAs are complex, globular molecules formed from elements of secondary and tertiary structure analogous to those found in proteins. Little is known about recognition of RNAs by proteins. In the case of transfer RNAs (tRNAs), considerable evidence suggests that elements dispersed in both the one- and three-dimensional structure are important for recognition by aminoacyl tRNA synthetases. Fragments of alanine tRNA synthetase were created by in vitro manipulations of the cloned alaS gene and examined for their interaction with alanine-specific tRNA. Sequences essential for recognition were located near the middle of the polypeptide, juxtaposed to the carboxyl-terminal side of the domain for aminoacyl adenylate synthesis. The most essential part of the tRNA interaction strength and specificity was dependent on a sequence of fewer than 100 amino acids. Within this sequence, and in the context of the proper conformation, a segment of no more than 17 amino acids was responsible for 25% or more of the total synthetase-tRNA free energy of association. The results raise the possibility that an important part of specific RNA recognition by an aminoacyl tRNA synthetase involves a polypeptide segment that is short relative to the total size of the protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- Bowie, J -- Schimmel, P -- GM23562/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1651-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2435005" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alanine-tRNA Ligase/metabolism ; Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/*metabolism ; Base Sequence ; Cloning, Molecular ; Escherichia coli/enzymology ; RNA/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Structure-Activity Relationship ; Substrate Specificity ; Thermodynamics
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-09
    Description: A D-alanine-containing peptide termed dermorphin, with potent opiate-like activity, has been isolated from skin of the frog Phyllomedusa sauvagei. Complementary DNA (cDNA) libraries were constructed from frog skin messenger RNA and screened with a mixture of oligonucleotides that contained the codons complementary to five amino acids of dermorphin. Clones were detected with inserts coding for different dermorphin precursors. The predicted amino acid sequences of these precursors contained homologous repeats of 35 amino acids that included one copy of the heptapeptide dermorphin. In these cloned cDNAs, the alanine codon GCG occurred at the position where D-alanine is present in the end product. This suggests the existence of a novel post-translational reaction for the conversion of an L-amino acid to its D-isomer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richter, K -- Egger, R -- Kreil, G -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):200-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, Austrian Academy of Sciences, Salzburg.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659910" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/*metabolism ; Amino Acid Sequence ; Animals ; Anura ; Base Sequence ; Cloning, Molecular ; DNA/analysis ; Molecular Sequence Data ; Oligopeptides/*genetics ; Opioid Peptides ; RNA, Messenger/genetics ; Skin/*metabolism ; Stereoisomerism
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  • 52
    Publication Date: 1987-09-04
    Description: Although cocaine binds to several sites in the brain, the biochemical receptor mechanism or mechanisms associated with its dependence producing properties are unknown. It is shown here that the potencies of cocaine-like drugs in self-administration studies correlate with their potencies in inhibiting [3H]mazindol binding to the dopamine transporters in the rat striatum, but not with their potencies in binding to a large number of other presynaptic and postsynaptic binding sites. Thus, the cocaine receptor related to substance abuse is proposed to be the one associated with dopamine uptake inhibition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ritz, M C -- Lamb, R J -- Goldberg, S R -- Kuhar, M J -- New York, N.Y. -- Science. 1987 Sep 4;237(4819):1219-23.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2820058" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/drug effects/*metabolism ; Cattle ; Cocaine/administration & dosage/*pharmacology ; Corpus Striatum/metabolism ; Dopamine/metabolism ; Haplorhini ; Male ; Mazindol/metabolism ; Norepinephrine/metabolism ; Rats ; Rats, Inbred Strains ; Receptors, Adrenergic/drug effects/metabolism ; Receptors, Dopamine/drug effects/*metabolism ; Receptors, Serotonin/drug effects/metabolism ; Self Administration ; Serotonin/metabolism
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1987 Jul 3;237(4810):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603009" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Arteriosclerosis/*therapy ; Cholesterol/*adverse effects ; Colestipol/therapeutic use ; Dietary Fats/adverse effects ; Humans ; Male ; Middle Aged ; Niacin/therapeutic use
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  • 54
    Publication Date: 1987-09-25
    Description: A complementary DNA clone derived from rat brain messenger RNA has been isolated on the basis of homology to the human thyroid hormone receptor gene. Expression of this complementary DNA produces a high-affinity binding protein for thyroid hormones. Sequence analysis and the mapping of this gene to a distinct human genetic locus indicate the existence of multiple human thyroid hormone receptors. Messenger RNA from this gene is expressed in a tissue-specific fashion with highest levels in the central nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, C C -- Weinberger, C -- Lebo, R -- Evans, R M -- GM-266444-09/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1610-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; DNA/genetics ; DNA-Binding Proteins/*genetics ; Gene Expression Regulation ; Genes ; Humans ; RNA, Messenger/genetics ; Rats ; Receptors, Thyroid Hormone/*genetics/metabolism ; Tissue Distribution ; Triiodothyronine/metabolism
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  • 55
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-24
    Description: The ornithine transcarbamylase-deficient sparse fur mouse is an excellent model to study the most common human urea cycle disorder. The mutation has been well characterized by both biochemical and enzymological methods, but its exact nature has not been revealed. A single base substitution in the complementary DNA for ornithine transcarbamylase from the sparse fur mouse has been identified by means of a combination of two recently described techniques for rapid mutational analysis. This strategy is simpler than conventional complementary DNA library construction, screening, and sequencing, which has often been used to find a new mutation. The ornithine transcarbamylase gene in the sparse fur mouse contains a C to A transversion that alters a histidine residue to an asparagine residue at amino acid 117.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Veres, G -- Gibbs, R A -- Scherer, S E -- Caskey, C T -- HD21452/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):415-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603027" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/analysis ; Disease Models, Animal ; *Genes ; Mice ; Mice, Mutant Strains ; *Mutation ; Ornithine Decarboxylase/deficiency/*genetics ; RNA, Messenger/genetics
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-13
    Description: Although homelessness has been recognized as a serious and growing urban social problem, scientifically acceptable methods for estimating the composition and size of the homeless population have been lacking. A new research approach to estimating the size and composition of undomiciled urban populations is presented, and its utility is illustrated through a description of the literal homeless of Chicago. The homeless in the Chicago sample are unaffiliated persons living in extreme poverty, with high levels of physical and mental disability. Homelessness is interpreted as a manifestation of extreme poverty among persons without families in housing markets with declining stocks of inexpensive dwelling units suitable for single persons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rossi, P H -- Wright, J D -- Fisher, G A -- Willis, G -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1336-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2950592" target="_blank"〉PubMed〈/a〉
    Keywords: Chicago ; Demography ; Disabled Persons ; Employment ; Female ; *Homeless Persons ; Humans ; Income ; Interviews as Topic ; Male ; Poverty ; Research Design ; Sampling Studies ; Social Isolation ; *Urban Population
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  • 57
    Publication Date: 1987-07-24
    Description: Fragile X syndrome is a common form of mental retardation associated with a fragile site on the human X chromosome. Although fragility at this site is usually evident as a nonstaining chromatid gap, it remains unclear whether or not actual chromosomal breakage occurs. By means of somatic cell hybrids containing either a normal human X or a fragile X chromosome and utilizing two genes that flank the fragile site as markers of chromosome integrity, segregation of these markers was shown to be more frequent if they encompass the fragile site under appropriate culture conditions. Hybrid cells that reveal marker segregation were found to contain rearranged X chromosomes involving the region at or near the fragile site, thus demonstrating true chromosomal breakage within this area. Two independent translocation chromosomes were identified involving a rodent chromosome joined to the human X at the location of the fragile site. DNA analysis of closely linked, flanking loci was consistent with the position of the breakpoint being at or very near the fragile X site. Fragility at the translocation junctions was observed in both hybrids, but at significantly lower frequencies than that seen in the intact X of the parental hybrid. This observation suggests that the human portion of the junctional DNA may contain part of a repeated fragility sequence. Since the translocation junctions join heterologous DNA, the molecular cloning of the fragile X sequence should now be possible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warren, S T -- Zhang, F -- Licameli, G R -- Peters, J F -- CA31777/CA/NCI NIH HHS/ -- HD20521/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):420-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603029" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromosome Banding ; *Cloning, Molecular ; Female ; Fragile X Syndrome/*genetics ; Glucosephosphate Dehydrogenase/genetics ; Humans ; Hybrid Cells/cytology ; Hypoxanthine Phosphoribosyltransferase/genetics ; Male ; Sex Chromosome Aberrations/*genetics ; Translocation, Genetic
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  • 58
    Publication Date: 1987-03-20
    Description: A 4-kilobase complementary DNA (cDNA) encoding human macrophage-specific colony-stimulating factor (CSF-1) was isolated. When introduced into mammalian cells, this cDNA directs the expression of CSF-1 that is structurally and functionally indistinguishable from the natural human urinary CSF-1. Direct structural analysis of both the recombinant CSF-1 and the purified human urinary protein revealed that these species contain a sequence of at least 40 amino acids at their carboxyl termini which are not found in the coding region of a 1.6-kilobase CSF-1 cDNA that was previously described. These results demonstrate that the human CSF-1 gene can be expressed to yield at least two different messenger RNA species that encode distinct but related forms of CSF-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G G -- Temple, P A -- Leary, A C -- Witek-Giannotti, J S -- Yang, Y C -- Ciarletta, A B -- Chung, M -- Murtha, P -- Kriz, R -- Kaufman, R J -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1504-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3493529" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Colony-Stimulating Factors/*genetics/urine ; DNA/genetics ; Gene Expression Regulation ; Humans ; Macrophages/physiology ; Molecular Weight ; Peptide Fragments ; Protein Processing, Post-Translational ; RNA, Messenger/genetics
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  • 59
    Publication Date: 1987-10-23
    Description: The fluorescence anisotropy of 1,6-diphenyl-1,3,5-hexatriene in labeled platelet membranes, an index of membrane fluidity, identifies a prominent subgroup of patients with Alzheimer's disease who manifest distinct clinical features. In a family study, the prevalence of this platelet membrane abnormality was 3.2 to 11.5 times higher in asymptomatic, first-degree relatives of probands with Alzheimer's disease than in neurologically healthy control subjects chosen without regard to family history of dementia. The pattern of the platelet membrane abnormality within families was consistent with that of a fully penetrant autosomal dominant trait. Thus, this abnormality of platelet membranes may be an inherited factor that is related to the development of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zubenko, G S -- Wusylko, M -- Cohen, B M -- Boller, F -- Teply, I -- AG03705/AG/NIA NIH HHS/ -- AG05133/AG/NIA NIH HHS/ -- MH30915/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):539-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of Pittsburgh, Western Psychiatric Institute and Clinic, PA 15213.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659926" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Alzheimer Disease/blood/*genetics ; Blood Platelets/*ultrastructure ; Cell Membrane/physiology ; Diphenylhexatriene ; Female ; Fluorescence Polarization ; Humans ; Male ; *Membrane Fluidity ; Middle Aged ; Risk Factors
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  • 60
    Publication Date: 1987-03-20
    Description: A human B-cell growth factor (BCGF) (12 kilodaltons) supports the clonal proliferation of B lymphocytes. A clone was isolated that contained the proper structural sequence to encode biologically active, 12-kilodalton BCGF in Escherichia coli and to hybridize to a specific messenger RNA, identified by in vitro translation in Xenopus laevis oocytes. A relatively hydrophobic region of 18 amino acids was found at the amino terminal of the 124-amino acid-long polypeptide. The carboxyl terminal is composed of at least 32 amino acids that are derived from nucleotide sequences bearing significant homology to the Alu repeat family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, S -- Mehta, S -- Morgan, J -- Maizel, A -- 16672/PHS HHS/ -- CA38499/CA/NCI NIH HHS/ -- CA39798/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1489-92.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3547651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; B-Lymphocytes/*physiology ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Escherichia coli ; Gene Expression Regulation ; Growth Substances/*genetics ; Interleukin-4 ; Lymphokines/*genetics ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid
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  • 61
    Publication Date: 1987-12-11
    Description: To investigate the mechanism by which immune activation augments replication of the human immunodeficiency virus type 1 (HIV-1) in infected T cells, four different classes of T cell mitogens were evaluated for their effects on the HIV-1 long terminal repeat (LTR). Phytohemagglutinin (PHA), a mitogenic lectin; phorbol 12-myristic 13-acetate, a tumor promoter; ionomycin, a calcium ionophore; and tat-1, the trans-activator protein from the human T cell leukemia/lymphoma virus type I (HTLV-I) each stimulated the HIV-1 LTR. Studies of deleted forms of the LTR supported a central role in these responses for the HIV-1 enhancer, which alone was sufficient for mitogen inducibility, but also suggested that other 5' positive and negative regulatory elements contribute to the overall magnitude of the response. Synergistic activation of the HIV-1 LTR (up to several thousandfold) was observed with combinations of these mitogens and the HIV-1--derived tat-III protein. Cyclosporin A, an immunosuppressive agent, inhibited PHA-mediated activation of the HIV-1 LTR but was without effect in the presence of other mitogens. Thus, HIV-1 gene expression and replication appear to be regulated, via the HIV-1 LTR, by the same mitogenic signals that induce T cell activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siekevitz, M -- Josephs, S F -- Dukovich, M -- Peffer, N -- Wong-Staal, F -- Greene, W C -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1575-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Duke University School of Medicine, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825351" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cyclosporins/pharmacology ; Deltaretrovirus/*physiology ; Genes, Viral ; HIV/drug effects/genetics/*growth & development ; Mitogens/*pharmacology ; Retroviridae Proteins/*physiology ; T-Lymphocytes/*immunology ; Trans-Activators ; Transcription Factors/*physiology ; Transcription, Genetic ; *Virus Activation/drug effects
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-02
    Description: The occurrence of seizure activity in human temporal lobe epilepsy or status epilepticus is often associated with a characteristic pattern of cell loss in the hippocampus. An experimental model that replicates this pattern of damage in normal animals by electrical stimulation of the afferent pathway to the hippocampus was developed to study changes in structure and function that occur as a result of repetitive seizures. Hippocampal granule cell seizure activity caused a persistent loss of recurrent inhibition and irreversibly damaged adjacent interneurons. Immunocytochemical staining revealed unexpectedly that gamma-aminobutyric acid (GABA)-containing neurons, thought to mediate inhibition in this region and predicted to be damaged by seizures, had survived. In contrast, there was a nearly complete loss of adjacent somatostatin-containing interneurons and mossy cells that may normally activate inhibitory neurons. These results suggest that the seizure-induced loss of a basket cell-activating system, rather than a loss of inhibitory basket cells themselves, may cause disinhibition and thereby play a role in the pathophysiology and pathology of the epileptic state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sloviter, R S -- NS 18201/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):73-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2879352" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cholecystokinin/physiology ; Disease Models, Animal ; Electric Stimulation ; Epilepsy/pathology/*physiopathology ; Hippocampus/*physiopathology ; Immunologic Techniques ; Interneurons/*pathology/physiopathology ; Male ; Neural Inhibition ; Rats ; Somatostatin/*physiology ; Time Factors ; Vasoactive Intestinal Peptide/metabolism ; gamma-Aminobutyric Acid/*physiology
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-30
    Description: The Drosophila gene, dorsal, is a maternal effect locus that is essential for the establishment of dorsal-ventral polarity in the developing embryo. The dorsal protein was predicted from the complementary DNA sequence; it is almost 50 percent identical, over an extensive region, to the protein encoded by the avian oncogene v-rel, its cellular homolog, c-rel, and a human c-rel fragment. The oncogene v-rel is highly oncogenic in avian lymphoid, spleen, and bone marrow cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steward, R -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):692-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3118464" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Drosophila melanogaster/embryology/*genetics ; Genes ; Molecular Sequence Data ; *Morphogenesis ; Oogenesis ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogenes ; Sequence Homology, Nucleic Acid
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  • 64
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-09-04
    Description: In John Walsh's article "Some refuseniks see no glasnost" (News & Comment, 24 July, p. 356), the Committee for Concerned Scientists was incorrecty identified as the "Union" of Concerned Scientists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1987 Sep 4;237(4819):1094.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629229" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/*rehabilitation ; Follow-Up Studies ; Humans ; Male
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  • 65
    Publication Date: 1987-03-20
    Description: This report describes the characterization of a genomic locus in the rat that encodes overlapping genes occupying both strands of the same piece of DNA. One gene (strand) encodes gonadotropin-releasing hormone (GnRH). A second gene, SH, is transcribed from the other DNA strand to produce RNA of undefined function. The RNAs transcribed from each DNA strand are spliced and polyadenylated, and share significant exon domains. GnRH is expressed in the central nervous system while SH transcripts are present in the heart. Thus, the genome of a mammalian organism encodes two distinct genes by using both strands of the same DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adelman, J P -- Bond, C T -- Douglass, J -- Herbert, E -- AM-16879/AM/NIADDK NIH HHS/ -- AM-30155/AM/NIADDK NIH HHS/ -- DA-02736/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 20;235(4795):1514-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3547652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/*genetics ; Exons ; *Genes ; Gonadotropin-Releasing Hormone/*genetics ; Heart/physiology ; Hypothalamus/physiology ; Introns ; RNA Splicing ; RNA, Messenger/*genetics ; Rats ; Templates, Genetic ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 66
    Publication Date: 1987-07-31
    Description: Complementary DNAs for three different muscarinic acetylcholine receptors were isolated from a rat cerebral cortex library, and the cloned receptors were expressed in mammalian cells. Analysis of human and rat genomic clones indicates that there are at least four functional muscarinic receptor genes and that these genes lack introns in the coding sequence. This gene family provides a new basis for evaluating the diversity of muscarinic mechanisms in the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T I -- Buckley, N J -- Young, A C -- Brann, M R -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):527-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/metabolism ; Cloning, Molecular ; Codon ; Dna ; DNA Restriction Enzymes ; *Genes ; Genetic Code ; Humans ; Models, Molecular ; Nucleic Acid Hybridization ; Rats ; Receptors, Muscarinic/classification/*genetics ; Swine ; Transfection
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  • 67
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-30
    Description: The messenger RNA (mRNA) that encodes alpha subunit of the guanosine triphosphate-binding protein transducin (T alpha) and T alpha immunoreactivity were localized and measured in the rat retina during the light-dark cycle with in situ hybridization and immunohistochemistry. Both T alpha mRNA and T alpha immunoreactivity were observed only in photoreceptors. Within the photoreceptor T alpha mRNA was present primarily in the inner segments and to a lesser extent in the outer nuclear layer at all times during the day and night. However, the distribution of T alpha immunoreactivity varied profoundly with the light-dark cycle; during the day, T alpha immunoreactivity was highest in the inner segments, and at night the outer segments were more immunoreactive. The amounts of T alpha mRNA and T alpha immunoreactivity also depended on the light-dark cycle. Levels of T alpha mRNA were high immediately before and after lights on; levels were low for the rest of the light-dark cycle. During the day, T alpha immunoreactivity increased in the inner segments following the increase in T alpha mRNA. After the lights were turned off, T alpha immunoreactivity decreased in the inner segments and increased in the outer segments. Thus, it appears that T alpha is synthesized in the inner segments after a morning increase in T alpha mRNA. Newly synthesized T alpha remains in the inner segments until it is transported to the outer segments at night, where it may be involved in the increase in the sensitivity of photoreceptor rods at night.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brann, M R -- Cohen, L V -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):585-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3101175" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Circadian Rhythm ; GTP-Binding Proteins/*genetics/immunology/metabolism ; Gene Expression Regulation ; Immunoenzyme Techniques ; Male ; Membrane Proteins/*genetics/immunology/metabolism ; Photoreceptor Cells/*physiology/ultrastructure ; RNA, Messenger/genetics ; Rats ; Transducin
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  • 68
    Publication Date: 1987-10-16
    Description: The primary structure of human apolipoprotein (apo) B-48 has been deduced and shown by a combination of DNA excess hybridization, sequencing of tryptic peptides, cloned complementary DNAs, and intestinal messenger RNAs (mRNAs) to be the product of an intestinal mRNA with an in-frame UAA stop codon resulting from a C to U change in the codon CAA encoding Gln2153 in apoB-100 mRNA. The carboxyl-terminal Ile2152 of apoB-48 purified from chylous ascites fluid has apparently been cleaved from the initial translation product, leaving Met2151 as the new carboxyl-terminus. These data indicate that approximately 85% of the intestinal mRNAs terminate within approximately 0.1 to 1.0 kilobase downstream from the stop codon. The other approximately 15% have lengths similar to hepatic apoB-100 mRNA even though they have the same in-frame stop codon. The organ-specific introduction of a stop codon to a mRNA appears unprecedented and might have implications for cryptic polyadenylation signal recognition and RNA processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, S H -- Habib, G -- Yang, C Y -- Gu, Z W -- Lee, B R -- Weng, S A -- Silberman, S R -- Cai, S J -- Deslypere, J P -- Rosseneu, M -- GM-30998/GM/NIGMS NIH HHS/ -- HL-27341/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):363-6.〈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/3659919" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein B-48 ; Apolipoproteins B/*genetics/metabolism ; Base Sequence ; Chylous Ascites/metabolism ; *Codon ; DNA/genetics ; Humans ; Intestine, Small/analysis ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Peptide Fragments ; *RNA, Messenger/analysis/*genetics ; Trypsin/metabolism
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  • 69
    Publication Date: 1987-05-22
    Description: The DNA in human sperm chromatin is packaged into nucleoprotamine (approximately 85%) and nucleohistone (approximately 15%). Whether these two chromatin fractions are sequence-specific subsets of the spermatozoon genome is the question addressed in this report. Sequence-specific packaging would suggest distinct structural and functional roles for the nucleohistone and nucleoprotamine in late spermatogenesis or early development or both. After removal of histones with 0.65M NaCl, exposed DNA was cleaved with Bam HI restriction endonuclease and separated by centrifugation from insoluble nucleoprotamine. The DNA sequence distribution of nucleohistone DNA in the supernatant and nucleoprotamine DNA in the pellet was compared by cloning size-selected single-copy sequences and by using the derived clones as probes of nucleohistone DNA and nucleoprotamine DNA. Two clones derived from nucleohistone DNA preferentially hybridized to nucleohistone DNA, and two clones derived from nucleoprotamine DNA preferentially hybridized to nucleoprotamine DNA, which demonstrated the existence of sequence-specific nucleohistone and nucleoprotamine components within the human spermatozoon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatewood, J M -- Cook, G R -- Balhorn, R -- Bradbury, E M -- Schmid, C W -- GM-07377/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 22;236(4804):962-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576213" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/*physiology ; Cloning, Molecular ; DNA/*genetics/isolation & purification/metabolism ; Histones/isolation & purification ; Humans ; Male ; Nucleic Acid Hybridization ; Nucleoproteins/isolation & purification ; Spermatozoa/*physiology
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  • 70
    Publication Date: 1987-02-27
    Description: The circumsporozoite (CS) protein of Plasmodium falciparum is the focus of intense efforts to develop an antisporozoite malaria vaccine. Localization of sites for T-cell recognition on this molecule is critical for vaccine design. By using an algorithm designed to predict T-cell sites and a large panel of H-2 congenic mice, a major nonrepetitive T-cell site was located. When a synthetic peptide corresponding to this site was covalently linked to the major B-cell site on the molecule, an immunogen capable of eliciting a high-titer antibody response was formed. This peptide sequence could prime helper T cells for a secondary response to the intact CS protein. The new helper T-cell site is located outside the repetitive region of the CS protein and appears to be the immunodominant T site on the molecule. This approach should be useful in the rational design and construction of vaccines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Good, M F -- Maloy, W L -- Lunde, M N -- Margalit, H -- Cornette, J L -- Smith, G L -- Moss, B -- Miller, L H -- Berzofsky, J A -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):1059-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434994" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Antigens, Protozoan/immunology ; Antigens, Surface/*immunology ; B-Lymphocytes/immunology ; Epitopes/*immunology ; Mice ; Peptide Fragments/chemical synthesis/*immunology ; Plasmodium falciparum/*immunology ; *Protozoan Proteins ; Receptors, Antigen, B-Cell/immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/immunology ; T-Lymphocytes, Helper-Inducer/*immunology ; Vaccines/immunology
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  • 71
    Publication Date: 1987-06-05
    Description: An oocyte expression system was used to test the relation between a complementary DNA (cDNA) clone encoding the liver gap junction protein and cell-cell channels. Total liver polyadenylated messenger RNA injected into oocytes induced cell-cell channels between paired oocytes. This induction was blocked by simultaneous injection of antisense RNA transcribed from the gap junction cDNA. Messenger RNA selected by hybridization to the cDNA clone and translated in oocyte pairs yielded a higher junctional conductance than unselected liver messenger RNA. Cell-cell channels between oocytes were also formed when the cloned cDNA was expressed under the control of a heat-shock promoter. A concentration-dependent induction of channels was observed in response to injection with in vitro transcribed gap junction messenger RNA. Thus, the liver gap junction cDNA encodes a protein that is essential for the formation of functional cell-cell channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dahl, G -- Miller, T -- Paul, D -- Voellmy, R -- Werner, R -- GM 31125/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1290-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3035715" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Connexins ; DNA/metabolism ; Heat-Shock Proteins/genetics ; Intercellular Junctions/*metabolism ; Liver/*metabolism ; Membrane Proteins/biosynthesis/*genetics ; Nucleic Acid Hybridization ; Oocytes/metabolism ; Promoter Regions, Genetic ; RNA, Messenger/biosynthesis ; Rats ; Transcription, Genetic ; Xenopus
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  • 72
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-05-15
    Description: Allowing mice access to food immediately after an aversive training session enhances memory retention. Cholecystokinin-octapeptide (CCK-8), which is a gastrointestinal hormone released during feeding, also enhances memory retention when administered intraperitoneally. This memory-enhancing effect of CCK-8 is blocked when the vagus nerve is cut, indicating that CCK-8 may produce its effect on memory retention by activating ascending fibers in the vagus nerve. Thus, CCK-8, a peripherally acting peptide, may mediate the memory-enhancing effects of feeding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flood, J F -- Smith, G E -- Morley, J E -- New York, N.Y. -- Science. 1987 May 15;236(4803):832-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576201" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/drug effects ; Electroshock ; Male ; Memory/*drug effects ; Mice ; Mice, Inbred Strains ; Sincalide/*pharmacology ; Vagotomy ; Vagus Nerve/drug effects/*physiology
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  • 73
    Publication Date: 1987-05-29
    Description: The ribonucleocapsids of many plant viruses are extremely stable. The protein coat protects the RNA genome against degradation during the accumulation and spread of progeny virions. Chimeric single-stranded RNA molecules were transcribed in vitro from recombinant plasmids and later encapsidated, in vitro, into ribonucleoprotein particles (pseudoviruses) 60 nanometers long that resembled tobacco mosaic virus. Transcripts encoding an assayable enzyme, chloramphenicol acetyltransferase (CAT), were packaged into pseudovirus particles to assess the utility of this single-stranded RNA delivery system in a wide range of cell types. In all cases, packaged CAT messenger RNA was uncoated and transiently expressed. Significantly higher levels of CAT activity were detected with packaged than with naked CAT messenger RNA after inoculation of plant protoplasts in the presence of polyethylene glycol or abrasive inoculation of intact leaf surfaces. Structural events that lead to the uncoating and expression of CAT messenger RNA showed no cell specificity. This observation may support the view that the comparatively restricted host range of a true plant virus results from events that occur later during the infection cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallie, D R -- Sleat, D E -- Watts, J W -- Turner, P C -- Wilson, T M -- New York, N.Y. -- Science. 1987 May 29;236(4805):1122-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3472350" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Chloramphenicol O-Acetyltransferase ; Fabaceae/microbiology ; Genetic Engineering/*methods ; Plants, Medicinal ; Plants, Toxic ; Protoplasts/microbiology ; RNA, Messenger/*genetics ; Tobacco/microbiology ; *Tobacco Mosaic Virus ; Transcription, Genetic ; Virus Diseases/microbiology
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  • 74
    Publication Date: 1987-06-26
    Description: The retinoblastoma (Rb) gene is the prototype for a class of recessive human cancer genes in which loss of activity of both normal alleles is thought to be associated with tumorigenesis. Sixteen of 40 retinoblastomas examined with a complementary DNA probe shown to be the Rb gene had identifiable structural changes of the Rb gene including in some cases homozygous internal deletions with corresponding truncated transcripts. An osteosarcoma also had a homozygous internal deletion with a truncated transcript. In addition, possible hot spots for deletion were identified within the Rb genomic locus. Among those tumors with no identifiable structural changes there was either absence of an Rb transcript or abnormal expression of the Rb transcript. Comparison of the structural changes in the tumor cells and fibroblasts of certain patients provided support for Knudson's two-hit hypothesis for the development of retinoblastoma at the molecular level. The ability to detect germline structural deletions in fibroblasts from some patients with bilateral retinoblastoma also indicates that the isolated gene is useful for diagnostic purposes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fung, Y K -- Murphree, A L -- T'Ang, A -- Qian, J -- Hinrichs, S H -- Benedict, W F -- EY02715/EY/NEI NIH HHS/ -- EY0619502/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1987 Jun 26;236(4809):1657-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2885916" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Chromosome Deletion ; *Chromosome Mapping ; Cloning, Molecular ; Cricetinae ; Dna ; DNA Restriction Enzymes ; DNA, Neoplasm/analysis ; Eye Neoplasms/*genetics ; Fibroblasts/ultrastructure ; Genotype ; Humans ; Nucleic Acid Hybridization ; Osteosarcoma/genetics ; Polymorphism, Restriction Fragment Length ; Retinoblastoma/*genetics ; Transcription, Genetic
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  • 75
    Publication Date: 1987-01-30
    Description: In seven right-handed adults, the brain electrical patterns before accurate performance differed from the patterns before inaccurate performance. Activity overlying the left frontal cortex and the motor and parietal cortices contralateral to the performing hand preceded accurate left- or right-hand performance. Additional strong activity overlying midline motor and premotor cortices preceded left-hand performance. These measurements suggest that brief, spatially distributed neural activity patterns, or "preparatory sets," in distinct cognitive, somesthetic-motor, and integrative motor areas of the human brain may be essential precursors of accurate visuomotor performance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gevins, A S -- Morgan, N H -- Bressler, S L -- Cutillo, B A -- White, R M -- Illes, J -- Greer, D S -- Doyle, J C -- Zeitlin, G M -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):580-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3810158" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cerebral Cortex/*physiology ; Cognition/physiology ; Electroencephalography ; Electrophysiology ; Functional Laterality ; Humans ; Male ; Motor Activity/physiology ; Time Factors ; Visual Perception/physiology
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  • 76
    Publication Date: 1987-01-02
    Description: The 5' flanking region of the mouse alpha-fetoprotein (AFP) gene contains a tissue-specific promoter and three upstream regulatory elements that behave as classical enhancers. At least one of these enhancers is now shown to be required for the tissue-specific expression of the AFP gene when it is introduced into the mouse genome by microinjection of cloned DNA fragments into fertilized eggs. Each enhancer can direct expression in the appropriate tissues, the visceral endoderm of the yolk sac, the fetal liver, and the gastrointestinal tract, but each exerts different influence in these three tissues. These differences may explain the tissue-specific diversity in the levels of expression characteristic of the AFP gene. The postnatal repression of transcription of the AFP gene in both liver and gut, as well as the reinitiation of its transcription during liver regeneration, is mimicked by the introduced gene when it is linked to the enhancer domains together or singly. Thus, the DNA sequence elements responsible for directing the activation of AFP transcription, its repression, and reinduction are contained in a limited segment of DNA within or 5' to the gene (or both) and are operative in the absence of the closely linked albumin gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammer, R E -- Krumlauf, R -- Camper, S A -- Brinster, R L -- Tilghman, S M -- CA06927/CA/NCI NIH HHS/ -- CA28050/CA/NCI NIH HHS/ -- HD17321/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):53-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432657" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Enhancer Elements, Genetic ; Gene Expression Regulation ; Genes ; *Genes, Regulator ; Intestines/physiology ; Liver/physiology ; Mice ; Promoter Regions, Genetic ; RNA, Messenger/genetics ; Tissue Distribution ; Transcription, Genetic ; Transfection ; Yolk Sac/physiology ; alpha-Fetoproteins/*genetics
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  • 77
    Publication Date: 1987-05-01
    Description: GAP-43 is one of a small subset of cellular proteins selectively transported by a neuron to its terminals. Its enrichment in growth cones and its increased levels in developing or regenerating neurons suggest that it has an important role in neurite growth. A complementary DNA (cDNA) that encodes rat GAP-43 has been isolated to study its structural characteristics and regulation. The predicted molecular size is 24 kilodaltons, although its migration in SDS-polyacrylamide gels is anomalously retarded. Expression of GAP-43 is limited to the nervous system, where its levels are highest during periods of neurite outgrowth. Nerve growth factor or adenosine 3',5'-monophosphate induction of neurites from PC12 cells is accompanied by increased GAP-43 expression. GAP-43 RNA is easily detectable, although at diminished levels, in the adult rat nervous system. This regulation of GAP-43 is concordant with a role in growth-related processes of the neuron, processes that may continue in the mature animal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karns, L R -- Ng, S C -- Freeman, J A -- Fishman, M C -- New York, N.Y. -- Science. 1987 May 1;236(4801):597-600.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2437653" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/physiology ; Bacteriophage lambda/genetics ; Base Sequence ; *Cloning, Molecular ; DNA/*genetics ; Electrophoresis, Polyacrylamide Gel ; GAP-43 Protein ; Ganglia, Spinal/analysis/embryology ; Gene Expression Regulation ; Growth Substances/genetics ; Immunosorbent Techniques ; Membrane Proteins/*genetics ; Nerve Tissue Proteins/*genetics ; Protein Biosynthesis ; RNA/genetics ; RNA, Messenger/genetics ; Rats
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  • 78
    Publication Date: 1987-02-20
    Description: Human T-cell leukemia virus (HTLV) types I and II are unusual among replication-competent retroviruses in that they contain a fourth gene (chi) necessary for replication. The chi gene product, p chi, transcriptionally transactivates the viral long repeat (LTR), and is thus a positive regulator. To investigate p chi transactivation, sequences from the U3 regions of the LTRs of HTLV-I and -II were inserted into the Moloney murine leukemia virus (M-MuLV) LTR by recombinant DNA techniques. Transient expression assays of the chimeric LTRs indicated that the HTLV sequences conferred to the M-MuLV LTR responsiveness to HTLV p chi protein. M-MuLV enhancers were not required for function of the chimeric LTRs. Infectious recombinant M-MuLVs containing chimeric LTRs were also generated. These viruses showed higher infectivity when assayed in mouse cells expressing HTLV-II p chi protein compared to normal mouse cells. Thus the HTLV sequences were able to confer p chi responsiveness to infectious M-MuLV. The generation of a virus dependent on a transactivating protein for its replication has implications for the evolution of the human T-cell leukemia viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kitado, H -- Chen, I S -- Shah, N P -- Cann, A J -- Shimotohno, K -- Fan, H -- CA32454/CA/NCI NIH HHS/ -- CA32455/CA/NCI NIH HHS/ -- CA38597/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 20;235(4791):901-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027896" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Viral/*genetics ; Deltaretrovirus/*genetics ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Moloney murine leukemia virus/*genetics ; Promoter Regions, Genetic ; Repetitive Sequences, Nucleic Acid ; Retroviridae Proteins/*genetics ; Trans-Activators ; Transcription Factors/*genetics ; Transcription, Genetic ; *Virus Replication
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  • 79
    Publication Date: 1987-12-11
    Description: One mechanism considered responsible for the hypercalcemia that frequently accompanies malignancy is secretion by the tumor of a circulating factor that alters calcium metabolism. The structure of a tumor-secreted peptide was recently determined and found to be partially homologous to parathyroid hormone (PTH). The amino-terminal 1-34 region of the factor was synthesized and evaluated biologically. In vivo it produced hypercalcemia, acted on bone and kidney, and stimulated 1,25-dihydroxy-vitamin D3 formation. In vitro it interacted with PTH receptors and, in some systems, was more potent than PTH. These studies support a long-standing hypothesis regarding pathogenesis of malignancy-associated hypercalcemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horiuchi, N -- Caulfield, M P -- Fisher, J E -- Goldman, M E -- McKee, R L -- Reagan, J E -- Levy, J J -- Nutt, R F -- Rodan, S B -- Schofield, T L -- AR 36446/AR/NIAMS NIH HHS/ -- AR 39191/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1566-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regional Bone Center, Helen Hayes Hospital (New York State Department of Health), West Haverstraw 10993.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685994" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/blood ; Humans ; Hypercalcemia/etiology ; Neoplasms/*physiopathology ; Parathyroid Glands/physiology ; Parathyroid Hormone/pharmacology/*physiology ; Peptides/*physiology ; Rats ; Rats, Inbred Strains ; Thyroidectomy
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  • 80
    Publication Date: 1987-07-03
    Description: The human T cell receptor (TCR) gamma polypeptide occurs in structurally distinct forms on certain peripheral blood T lymphocytes. Complementary DNA clones representing the transcripts of functionally rearranged TCR gamma genes in these cells have been analyzed. The expression of a disulfide-linked and a nondisulfide-linked form of TCR gamma correlates with the use of the C gamma 1 and C gamma 2 constant-region gene segments, respectively. Variability in TCR gamma polypeptide size and disulfide linkage is determined by the number of copies and the sequence of a repeated segment of the constant region. Thus C gamma 1 and C gamma 2 are used to generate structurally distinct, yet functional, T3-associated receptor complexes on peripheral blood lymphocytes. Tryptic peptide mapping suggests that the T3-associated TCR gamma and delta peptides in the nondisulfide-linked form are distinct.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krangel, M S -- Band, H -- Hata, S -- McLean, J -- Brenner, M B -- 1-KO1-AM01598/AM/NIADDK NIH HHS/ -- 1-RO1-GM38308/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 3;237(4810):64-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2955517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Exons ; Genes ; Humans ; Peptide Fragments/*genetics ; Receptors, Antigen, T-Cell/*genetics ; Receptors, Antigen, T-Cell, gamma-delta ; Repetitive Sequences, Nucleic Acid ; T-Lymphocytes/*physiology
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  • 81
    facet.materialart.
    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: The major coat protein of bacteriophage M13 is synthesized as a precursor, the procoat, with a typical leader (signal) sequence of 23 residues at its NH2-terminus. A fusion protein that contains the NH2-terminal 141 residues of cytoplasmic ribulokinase and all but the first ten residues of M13 procoat was made. The fusion protein inserts into the plasma membrane of Escherichia coli and is processed by leader peptidase to give rise to a leader peptide of 155 residues and the mature coat protein of 50 residues. The NH2-terminus of the leader peptide remains in the cytoplasm and is protected from protease added to the medium outside of the cell. This indicates that M13 procoat inserts into the membrane as a loop structure and that the NH2-terminus of a leader peptide remains within the cytoplasm during membrane insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, A -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1413-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology Department, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317833" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Capsid/*metabolism ; Coliphages/*metabolism ; Escherichia coli/metabolism ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Protein Conformation ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Protein Sorting Signals/metabolism ; Recombinant Fusion Proteins/metabolism
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  • 82
    Publication Date: 1987-02-27
    Description: Molecular cloning techniques were used to isolate and characterize a protein possibly involved in the signal transducing system in olfactory tissue of the frog Rana pipiens. A complementary DNA library was constructed with messenger RNA obtained from frog olfactory neuroepithelium. A 700-base pair complementary DNA clone encoding a protein with a molecular weight of 20,300 was identified by differential hybridization analysis with polyadenylated RNA from olfactory epithelium and nonsensory respiratory epithelium. The messenger RNA corresponding to this clone was abundant in the cells of Bowman's glands in olfactory tissue but not in respiratory epithelium nor in several other tissues. The predicted sequence of this protein is homologous to members of a family of proteins that bind and transport small molecules in serum, suggesting that this protein may also bind and transport odorants in the mucus secreted by Bowman's glands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K H -- Wells, R G -- Reed, R R -- 5 PO1 CA16519/CA/NCI NIH HHS/ -- 5 T32 GM07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):1053-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3493528" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/*genetics/isolation & purification ; Epithelium/analysis ; Molecular Weight ; Mucus/metabolism ; Nucleic Acid Hybridization ; Odors ; Olfactory Mucosa/*analysis/physiology ; RNA, Messenger/genetics/metabolism ; Rana pipiens ; Respiratory System/analysis ; Retinol-Binding Proteins/genetics/*physiology
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  • 83
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1350-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685985" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Deception ; Female ; Male ; Primates
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  • 84
    Publication Date: 1987-04-24
    Description: Transcriptional enhancement is a general mechanism for regulation of gene expression in which particular proteins bound to specific DNA sequences stimulate the efficiency of initiation from linked promoters. One such protein, the glucocorticoid receptor, mediates enhancement in a glucocorticoid hormone-dependent manner. In this study, a region of the 795-amino acid rat glucocorticoid receptor that is active in transcriptional enhancement was identified. The active region was defined by expressing various receptor deletion mutants in stably and transiently transfected cells and examining the regulated transcription of hormone-responsive genes. Mutant receptors lacking as many as 439 amino-terminal amino acids retained activity, as did those with as many as 270 carboxyl-terminal amino acids deleted. This suggests that the 86-amino acid segment between the most extensive terminal deletions, which also includes sequences required for specific DNA binding in vitro, is sufficient for enhancer activation. In fact, a 150-amino acid receptor fragment that encompasses this segment mediates constitutive enhancement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miesfeld, R -- Godowski, P J -- Maler, B A -- Yamamoto, K R -- New York, N.Y. -- Science. 1987 Apr 24;236(4800):423-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3563519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA-Binding Proteins/*genetics ; *Enhancer Elements, Genetic ; *Genes, Regulator ; Mutation ; Rats ; Receptors, Glucocorticoid/*genetics ; Structure-Activity Relationship ; Transfection
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  • 85
    Publication Date: 1987-02-06
    Description: The human T-cell leukemia viruses, HTLV-I and HTLV-II, contain a gene, termed x, with transcriptional regulatory function. The properties of the x proteins were analyzed by constructing mutant genes containing site-directed deletions and point mutations. The results demonstrate that the amino terminal 17 amino acids of the x protein constitute part of a functional domain that is critical for the transcriptional activating properties of the protein. Within this region, substitution of a leucine residue for a proline residue results in major changes in the trans-activation phenotype of the protein. The mutant HTLV-II x protein, though incapable of activating the HTLV-II long terminal repeat, will block trans-activation of the HTLV-II long terminal repeat by the wild-type protein. The altered phenotype of this mutant suggests a potential negative regulatory function of the x protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wachsman, W -- Cann, A J -- Williams, J L -- Slamon, D J -- Souza, L -- Shah, N P -- Chen, I S -- CA 30388/CA/NCI NIH HHS/ -- CA 32727/CA/NCI NIH HHS/ -- CA 38597/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Feb 6;235(4789):674-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027894" target="_blank"〉PubMed〈/a〉
    Keywords: Deltaretrovirus/*genetics ; Gene Expression Regulation ; *Genes, Viral ; Mutation ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 86
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-30
    Description: Fertilization of eggs by sperm, the means by which sexual reproduction takes place in nearly all multicellular organisms, is fundamental to the maintenance of life. In both mammals and nonmammals, the pathway that leads to fusion of an egg with a single sperm consists of many steps that occur in a compulsory order. These steps include species-specific cellular recognition, intracellular and intercellular membrane fusions, and enzyme-catalyzed modifications of cellular investments. In several instances, the molecular mechanisms that underlie these events during mammalian fertilization are beginning to be revealed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wassarman, P M -- New York, N.Y. -- Science. 1987 Jan 30;235(4788):553-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027891" target="_blank"〉PubMed〈/a〉
    Keywords: Acrosome/physiology ; Animals ; *Fertilization ; Glycoproteins/physiology ; Humans ; Male ; Membrane Fusion ; Mice ; Ovum/*physiology ; Receptors, Cell Surface/physiology ; Sea Urchins ; Spermatozoa/*physiology
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  • 87
    Publication Date: 1987-10-23
    Description: There is now evidence that the immune system, during times of infectious challenge, can stimulate the secretion of glucocorticoids, the adrenal steroids that mediate important aspects of the response to stress. Specifically, secretion of interleukin-1 (IL-1), a monocyte lymphokine secreted after infection, appears at least in part responsible for this effect. Glucocorticoids are secreted in response to a neuroendocrine cascade involving, first, the brain, then the pituitary, and finally the adrenal gland. In this report, human IL-1 is shown to activate the adrenocortical axis at the level of the brain, stimulating the release of the controlling hormone corticotropin-releasing factor (CRF) from the hypothalamus. Infusion of IL-1 induced a significant secretion of CRF into the circulation exiting the hypothalamus, whereas immunoneutralization of CRF blocked the stimulatory effect of IL-1 on glucocorticoid secretion. IL-1 appeared to have no acute direct stimulatory effects on the pituitary or adrenal components of this system. Furthermore, IL-1 did not cause a nonspecific release of other hypothalamic hormones. Thus, the lymphokine acts in a specific manner to activate the adrenocortical axis at the level of the brain; this effect appears to be unrelated to the known pyrogenic effects of IL-1 within the hypothalamus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sapolsky, R -- Rivier, C -- Yamamoto, G -- Plotsky, P -- Vale, W -- AA06420/AA/NIAAA NIH HHS/ -- AM26741/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):522-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2821621" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Cortex/physiology ; Adrenocorticotropic Hormone/secretion ; Animals ; Cell Line ; Corticosterone/secretion ; Corticotropin-Releasing Hormone/*secretion ; Hypothalamus/*secretion ; Immunologic Techniques ; Interleukin-1/*physiology ; Male ; Pituitary Gland, Anterior/secretion ; Pituitary Neoplasms/secretion ; Rats ; Rats, Inbred Strains
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  • 88
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-06
    Description: Diversification of the antibody repertoire in mammals results from a series of apparently random somatically propagated gene rearrangement and mutational events. Nevertheless, it is well known that the adult repertoire of antibody specificities is acquired in a developmentally programmed fashion. As previously shown, rearrangement of the gene segments encoding the heavy-chain variable regions (VH) of mouse antibodies is also developmentally ordered: the number of VH gene segments rearranged in B lymphocytes of fetal mice is small but increased progressively after birth. In this report, human fetal B-lineage cells were also shown to rearrange a highly restricted set of VH gene segments. In a sample of heavy-chain transcripts from a 130-day human fetus the most frequently expressed human VH element proved to be closely related to the VH element most frequently expressed in murine fetal B-lineage cells. These observations are important in understanding the development of immunocompetence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroeder, H W Jr -- Hillson, J L -- Perlmutter, R M -- AI07470/AI/NIAID NIH HHS/ -- GM07454/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):791-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3118465" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Base Sequence ; Fetus ; *Genes, Immunoglobulin ; Humans ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Variable Region/genetics ; Mice ; Molecular Sequence Data ; Mutation ; Sequence Homology, Nucleic Acid
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  • 89
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segal, S L -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):350.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603021" target="_blank"〉PubMed〈/a〉
    Keywords: *Anxiety ; Female ; Gender Identity ; Humans ; Male ; *Mathematics ; Students ; Universities ; *Women
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  • 90
    Publication Date: 1987-07-31
    Description: The decline in the high incidence of amyotrophic lateral sclerosis, parkinsonism, and Alzheimer-type dementia among the Chamorro population of the western Pacific islands of Guam and Rota, coupled with the absence of demonstrable viral and hereditable factors in this disease, suggests the gradual disappearance of an environmental factor selectively associated with this culture. One candidate is seed of the neurotoxic plant Cycas circinalis L., a traditional source of food and medicine which has been used less with the Americanization of the Chamorro people after World War II. Macaques were fed the Cycas amino acid beta-N-methylamino-L-alanine, a low-potency convulsant that has excitotoxic activity in mouse brain, which is attenuated by N-methyl-D-aspartate receptor antagonists. These animals developed corticomoto-neuronal dysfunction, parkinsonian features, and behavioral anomalies, with chromatolytic and degenerative changes of motor neurons in cerebral cortex and spinal cord. In concert with existing epidemiological and animal data, these findings support the hypothesis that cycad exposure plays an important role in the etiology of the Guam disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spencer, P S -- Nunn, P B -- Hugon, J -- Ludolph, A C -- Ross, S M -- Roy, D N -- Robertson, R C -- NS-19611/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):517-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603037" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids, Diamino/*toxicity ; Amyotrophic Lateral Sclerosis/*chemically induced ; Animals ; Basal Ganglia Diseases/*chemically induced ; Environmental Exposure ; Guam ; Macaca fascicularis ; Male ; Motor Cortex/drug effects ; Motor Neurons/drug effects ; Neural Conduction/drug effects ; Neuromuscular Diseases/chemically induced ; Neurotoxins/*toxicity ; *Plants, Toxic ; Spinal Cord/drug effects ; Substantia Nigra/drug effects
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  • 91
    Publication Date: 1987-11-20
    Description: Complementary DNA and genomic clones were isolated and sequenced corresponding to rat and human synaptophysin (p38), a major integral membrane protein of synaptic vesicles. The deduced amino acid sequences indicate an evolutionarily highly conserved protein that spans the membrane four times. Both amino and carboxyl termini face the cytoplasm, with the latter containing ten copies of a tyrosine-rich pentapeptide repeat. The structure of synaptophysin suggests that the protein may function as a channel in the synaptic vesicle membrane, with the carboxyl terminus serving as a binding site for cellular factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudhof, T C -- Lottspeich, F -- Greengard, P -- Mehl, E -- Jahn, R -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1142-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Genetics, University of Texas Health Science Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; *Membrane Proteins/genetics ; Molecular Sequence Data ; Protein Conformation ; Rats ; Solubility ; Synaptic Vesicles/ultrastructure ; Synaptophysin
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  • 92
    Publication Date: 1987-07-17
    Description: Low-stringency hybridization with human glucocorticoid receptor (hGR) complementary DNA was used to isolate a new gene encoding a predicted 107-kilodalton polypeptide. Expression studies demonstrate its ability to bind aldosterone with high affinity and to activate gene transcription in response to aldosterone, thus establishing its identity as the human mineralocorticoid receptor (hMR). This molecule also shows high affinity for glucocorticoids and stimulates a glucocorticoid-responsive promoter. Together the hMR and hGR provide unexpected functional diversity in which hormone-binding properties, target gene interactions, and patterns of tissue-specific expression may be used in a combinatorial fashion to achieve complex physiologic control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arriza, J L -- Weinberger, C -- Cerelli, G -- Glaser, T M -- Handelin, B L -- Housman, D E -- Evans, R M -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):268-75.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosomes, Human, Pair 4 ; Cloning, Molecular ; DNA/genetics ; DNA-Binding Proteins/genetics ; Humans ; Rats ; Receptors, Glucocorticoid/*genetics ; Receptors, Mineralocorticoid ; Receptors, Steroid/*genetics ; Sequence Homology, Nucleic Acid ; Tissue Distribution ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 93
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-08-21
    Description: Gene expression is dependent on the interaction of DNA binding factors with distinct promoter control elements to activate RNA synthesis. The expression of the HIS4 gene in yeast is under two different control systems. One of these, general amino acid control, involves a DNA binding protein, GCN4, that stimulates transcription in response to amino acid starvation by binding to 5'-TGACTC-3' sequences in the HIS4 promoter region. A second system, the basal level control, stimulates HIS4 transcription in the absence of amino acid starvation. The basal level transcription of the HIS4 gene is under the control of two genes, BAS1 and BAS2, which are also required for the control of purine biosynthesis. In addition, BAS2 is required for the utilization of organic phosphates in the growth medium. Genetic mapping and DNA sequence analysis show that BAS2 is PHO2, a gene previously identified as a regulator of phosphate metabolism. Direct biochemical analysis shows that the BAS2 gene encodes a protein that binds to both the HIS4 and PHO5 promoters. The involvement of a single DNA binding protein in the regulation of histidine, adenine, and phosphate metabolism suggests that yeast may use a few key DNA binding proteins to coordinate the regulation of diverse metabolic pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arndt, K T -- Styles, C -- Fink, G R -- GM 35010-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 21;237(4817):874-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3303332" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Phosphatase/*genetics ; Chromosome Mapping ; Gene Expression Regulation ; Genes, Fungal ; Histidine/*genetics ; Mutation ; Phosphates/physiology ; Promoter Regions, Genetic ; Saccharomyces cerevisiae/*genetics ; Transcription Factors/physiology ; Transcription, Genetic
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  • 94
    Publication Date: 1987-02-13
    Description: A monoclonal antibody bound to a protein antigen slows the rate of chemical modification of amino acid residues located at the epitope. By comparing the degree of acetylation of 18 lysine and 7 threonine residues in free and antibody-bound horse cytochrome c, a discontiguous, conformational epitope was characterized on this protein antigen. The new approach is particularly suitable to probe discontiguous and conformational epitopes, which are difficult to analyze by other procedures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnens, A -- Demotz, S -- Corradin, G -- Binz, H -- Bosshard, H R -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):780-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2433768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; *Antigen-Antibody Complex ; Cytochrome c Group/*immunology ; Epitopes/*immunology ; Horses ; Humans ; Models, Molecular ; Protein Conformation ; Species Specificity
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  • 95
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-02-13
    Description: The Hin recombinase binds to specific sites on DNA and mediates a recombination event that results in DNA inversion. In order to define the DNA-binding domain of the Hin protein two peptides 31 and 52 amino acids long were synthesized. Even though the 31mer encompassed the sequence encoding the putative helix-coil-helix-binding domain, it was not sufficient for binding to the 26-base pair DNA crossover site. However, the 52mer specifically interacted with the site and also effectively inhibited the Hin-mediated recombination reaction. The 52mer bound effectively to both the 26-base pair complete site and to a 14-base pair "half site." Nuclease and chemical protection studies with the 52mer helped to define the DNA base pairs that contributed to the specificity of binding. The synthetic peptide provides opportunities for new approaches to the study of the nature of protein-DNA interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bruist, M F -- Horvath, S J -- Hood, L E -- Steitz, T A -- Simon, M I -- GM-09534-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):777-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3027895" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemical synthesis/metabolism ; Base Composition ; DNA/*metabolism ; DNA Nucleotidyltransferases/*metabolism ; Peptides/chemical synthesis ; Protein Binding ; Protein Conformation
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  • 96
    Publication Date: 1987-05-29
    Description: Linkage analysis of 15 Utah kindreds demonstrated that a gene responsible for von Recklinghausen neurofibromatosis (NF) is located near the centromere on chromosome 17. The families also gave no evidence for heterogeneity, indicating that a significant proportion of NF cases are due to mutations at a single locus. Further genetic analysis can now refine this localization and may lead to the eventual identification and cloning of the defective gene responsible for this disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barker, D -- Wright, E -- Nguyen, K -- Cannon, L -- Fain, P -- Goldgar, D -- Bishop, D T -- Carey, J -- Baty, B -- Kivlin, J -- CA 28854/CA/NCI NIH HHS/ -- CA 36362/CA/NCI NIH HHS/ -- GM 29090/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 29;236(4805):1100-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107130" target="_blank"〉PubMed〈/a〉
    Keywords: Centromere ; Chromosome Mapping ; *Chromosomes, Human, Pair 17/ultrastructure ; DNA, Recombinant ; Female ; *Genes ; Genetic Linkage ; Humans ; Male ; Neurofibromatosis 1/*genetics ; Nucleic Acid Hybridization
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  • 97
    Publication Date: 1987-05-15
    Description: The neural cell adhesion molecule, N-CAM, appears on early embryonic cells and is important in the formation of cell collectives and their boundaries at sites of morphogenesis. Later in development it is found on various differentiated tissues and is a major CAM mediating adhesion among neurons and between neurons and muscle. To provide a molecular basis for understanding N-CAM function, the complete amino acid sequences of the three major polypeptides of N-CAM and most of the noncoding sequences of their messenger RNA's were determined from the analysis of complementary DNA clones and were verified by amino acid sequences of selected CNBr fragments and proteolytic fragments. The extracellular region of each N-CAM polypeptide includes five contiguous segments that are homologous in sequence to each other and to members of the immunoglobulin superfamily, suggesting that interactions among immunoglobulin-like domains form the basis for N-CAM homophilic binding. Although different in their membrane-associated and cytoplasmic domains, the amino acid sequences of the three polypeptides appear to be identical throughout this extracellular region (682 amino acids) where the binding site is located. Variations in N-CAM activity thus do not occur by changes in the amino acid sequence that alter the specificity of binding. Instead, regulation is achieved by cell surface modulation events that alter N-CAM affinity, prevalence, mobility, and distribution on the surface. A major mechanism for modulation is alternative RNA splicing resulting in N-CAM's with different cytoplasmic domains that differentially interact with the cell membrane. Such regulatory mechanisms may link N-CAM binding function with other primary cellular processes during the embryonic development of pattern.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B A -- Hemperly, J J -- Murray, B A -- Prediger, E A -- Brackenbury, R -- Edelman, G M -- AM-04256/AM/NIADDK NIH HHS/ -- HD-09635/HD/NICHD NIH HHS/ -- HD-16550/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):799-806.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576199" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Surface/*genetics/immunology ; Base Sequence ; Cell Adhesion ; Cell Adhesion Molecules ; Cloning, Molecular ; DNA/metabolism ; Immunoglobulins ; Oligosaccharides/analysis ; Peptide Fragments/analysis ; *RNA Splicing ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-04-24
    Description: Clinical, genetic, and neuropsychopharmacological studies of developmental factors in alcoholism are providing a better understanding of the neurobiological bases of personality and learning. Studies of the adopted-away children of alcoholics show that the predisposition to initiate alcohol-seeking behavior is genetically different from susceptibility to loss of control after drinking begins. Alcohol-seeking behavior is a special case of exploratory appetitive behavior and involves different neurogenetic processes than do susceptibility to behavioral tolerance and dependence on the antianxiety or sedative effects of alcohol. Three dimensions of personality have been described that may reflect individual differences in brain systems modulating the activation, maintenance, and inhibition of behavioral responses to the effects of alcohol and other environmental stimuli. These personality traits distinguish alcoholics with different patterns of behavioral, neurophysiological, and neuropharmacological responses to alcohol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cloninger, C R -- AA-003539/AA/NIAAA NIH HHS/ -- MH-00048/MH/NIMH NIH HHS/ -- MH-31302/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1987 Apr 24;236(4800):410-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2882604" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/etiology/genetics/*physiopathology/psychology ; Appetite/physiology ; Avoidance Learning/physiology ; Behavior/physiology ; Extinction, Psychological ; Female ; Male ; Neurotransmitter Agents/physiology ; Reinforcement (Psychology)
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
    Publication Date: 1987-05-01
    Description: Mammalian X-chromosome inactivation involves a coordinate shutting down of physically linked genes. Several proposed models require the presence of specific sequences near genes to permit the spread of inactivation into these regions. If such models are correct, one might predict that heterologous genes transferred onto the X chromosome might lack the appropriate signal sequences and therefore escape inactivation. To determine whether a foreign gene inserted into the X chromosome is subject to inactivation, transgenic mice harboring 11 copies of the complete, 17-kilobase chicken transferrin gene on the X chromosome were used. Male mice hemizygous for this insert were bred with females bearing Searle's translocation, an X-chromosome rearrangement that is always active in heterozygous females (the unrearranged X chromosome is inactive). Female offspring bearing the Searle's translocation and the chicken transferrin gene had the same amount of chicken transferrin messenger RNA in liver as did transgenic male mice or transgenic female mice lacking the Searle's chromosome. This result shows that the inserted gene is not subject to X-chromosome inactivation and suggests that the inactivation process cannot spread over 187 kilobases of DNA in the absence of specific signal sequences required for inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, M A -- Stokes, K R -- Idzerda, R L -- McKnight, G S -- Hammer, R E -- Brinster, R L -- Gartler, S M -- HD14412/HD/NICHD NIH HHS/ -- HD16659/HD/NICHD NIH HHS/ -- HD17321/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1987 May 1;236(4801):593-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2437652" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chickens ; DNA/metabolism ; *Dosage Compensation, Genetic ; Female ; Male ; Methylation ; Mice ; Transferrin/*genetics ; *Transformation, Genetic ; Translocation, Genetic ; X Chromosome ; Y Chromosome ; alpha-Fetoproteins/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
    Publication Date: 1987-11-13
    Description: Two structurally distinct nuclear genes code for cytoplasmic small subunit ribosomal RNA's in the parasite Plasmodium berghei. Stable transcripts from one of the ribosomal RNA genes are found almost exclusively in those stages of the life cycle that develop in the mosquito. When the parasite infects the mammalian host, transcripts from the second gene become the predominant small subunit ribosomal RNA species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gunderson, J H -- Sogin, M L -- Wollett, G -- Hollingdale, M -- de la Cruz, V F -- Waters, A P -- McCutchan, T F -- GM 32964/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 13;238(4829):933-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672135" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Genes ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmodium/*genetics/growth & development ; RNA, Ribosomal/*genetics ; Ribosomes/*physiology ; 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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