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  • Male  (150)
  • Amino Acid Sequence  (128)
  • American Association for the Advancement of Science (AAAS)  (272)
  • Cell Press
  • 1995-1999
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  • 1988  (128)
  • 1985  (144)
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  • American Association for the Advancement of Science (AAAS)  (272)
  • Cell Press
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  • 1995-1999
  • 1985-1989  (272)
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  • 1975-1979
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  • 1
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    DNA amplification for direct detection of HIV-1 in DNA of peripheral blood mononuclear cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-15
    Description: By means of a selective DNA amplification technique called polymerase chain reaction, proviral sequences of the human immunodeficiency virus (HIV-1) were identified directly in DNA isolated from peripheral blood mononuclear cells (PBMCs) of persons seropositive but not in DNA isolated from PBMCs of persons seronegative for the virus. Primer pairs from multiple regions of the HIV-1 genome were used to achieve maximum sensitivity of provirus detection. HIV-1 sequences were detected in 100% of DNA specimens from seropositive, homosexual men from whom the virus was isolated by coculture, but in none of the DNA specimens from a control group of seronegative, virus culture-negative persons. However, HIV-1 sequences were detected in 64% of DNA specimens from seropositive, virus culture-negative homosexual men. This method of DNA amplification made it possible to obtain results within 3 days, whereas virus isolation takes up to 3 to 4 weeks. The method may therefore be used to complement or replace virus isolation as a routine means of determining HIV-1 infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ou, C Y -- Kwok, S -- Mitchell, S W -- Mack, D H -- Sninsky, J J -- Krebs, J W -- Feorino, P -- Warfield, D -- Schochetman, G -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):295-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Infectious Diseases, Centers for Disease Control, Atlanta, GA 30333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3336784" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*microbiology ; Base Sequence ; DNA, Viral/*blood ; DNA-Directed DNA Polymerase ; *Gene Amplification ; HIV/*genetics/isolation & purification ; HIV Seropositivity ; Homosexuality ; Humans ; Leukocytes, Mononuclear/*analysis ; Male ; Nucleic Acid Amplification Techniques ; Nucleic Acid Hybridization ; Virus Cultivation
    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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  • 2
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    Molecular cloning of odorant-binding protein: member of a ligand carrier family (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-15
    Description: Odorant-binding protein (OBP) is found in nasal epithelium, and it selectively binds odorants. Three complementary DNAs encoding rat odorant-binding protein have now been cloned and sequenced. One clone contains an open reading frame predicted to encode an 18,091-dalton protein. RNA blot analysis confirms the localization of OBP messenger RNA in the nasal epithelium. This OBP has 33 percent amino acid identity to alpha 2-microglobulin, a secreted plasma protein. Other members of an alpha 2-microglobulin superfamily bind and transport hydrophobic ligands. Thus, OBP probably binds and carries odorants within the nasal epithelium to putative olfactory receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pevsner, J -- Reed, R R -- Feinstein, P G -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- GM-07626/GM/NIGMS NIH HHS/ -- P01 CA16519-13/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):336-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388043" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*genetics ; Cloning, Molecular ; Ligands ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nasal Mucosa/*physiology ; Rats ; *Receptors, Odorant ; Smell/*physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    AIDS: an international perspective (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-05
    Description: The acquired immunodeficiency syndrome (AIDS) and infection with the human immunodeficiency virus type 1 (HIV-1) constitute a worldwide public health problem. Whereas in Europe and in most of the Americas transmission of HIV-1 has occurred predominantly among homosexual men and intravenous drug abusers, in Africa a distinct epidemiologic pattern has emerged that indicates that HIV-1 infection is mainly heterosexually acquired. Heterosexual transmission appears to be increasing in some parts of Latin America and the Caribbean, and possibly in the United States. In addition to HIV-1, at least one other human retrovirus, namely HIV-2, has been implicated as a cause of AIDS in Africa and Europe. Factors that influence heterosexual transmission of HIV-1 include genital ulcerations, early or late stages of HIV-1 infection in the index case, and possibly oral contraception and immune activation. The rate of perinatal transmission is enhanced when the mother's illness is more advanced. AIDS and HIV-1 infection may have a significant impact not only on public health, but also on the demography and socioeconomic conditions of some developing countries. Programs for the prevention and control of AIDS should be an immediate priority in all countries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Piot, P -- Plummer, F A -- Mhalu, F S -- Lamboray, J L -- Chin, J -- Mann, J M -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):573-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Institute of Tropical Medicine, Antwerp, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3277271" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/prevention & ; control/*transmission ; Female ; HIV/classification/pathogenicity ; Humans ; Infant, Newborn ; Male ; Pregnancy ; Sexual Behavior
    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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  • 4
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    Helix signals in proteins (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: The alpha helix, first proposed by Pauling and co-workers, is a hallmark of protein structure, and much effort has been directed toward understanding which sequences can form helices. The helix hypothesis, introduced here, provides a tentative answer to this question. The hypothesis states that a necessary condition for helix formation is the presence of residues flanking the helix termini whose side chains can form hydrogen bonds with the initial four-helix greater than N-H groups and final four-helix greater than C-O groups; these eight groups would otherwise lack intrahelical partners. This simple hypothesis implies the existence of a stereochemical code in which certain sequences have the hydrogen-bonding capacity to function as helix boundaries and thereby enable the helix to form autonomously. The three-dimensional structure of a protein is a consequence of the genetic code, but the rules relating sequence to structure are still unknown. The ensuing analysis supports the idea that a stereochemical code for the alpha helix resides in its boundary residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Presta, L G -- Rose, G D -- AG 06084/AG/NIA NIH HHS/ -- GM 29458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1632-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Hershey Medical Center, Pennsylvania State University, Hershey 17033.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2837824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carboxypeptidases ; Carboxypeptidases A ; Cytochrome c Group ; Flavodoxin ; Humans ; Hydrogen Bonding ; Models, Chemical ; Molecular Sequence Data ; Muramidase ; Myoglobin ; Pancreatic Polypeptide ; Parvalbumins ; Plastocyanin ; *Protein Conformation ; Ribonucleases ; Scorpion Venoms ; Tetrahydrofolate Dehydrogenase ; Triose-Phosphate Isomerase ; Trypsin Inhibitors ; X-Ray Diffraction
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  • 5
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    Characterization of a helical protein designed from first principles (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- DeGrado, W F -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):976-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research & Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; Chromatography, Gel ; Escherichia coli/genetics ; Molecular Sequence Data ; Plasmids ; *Protein Conformation ; *Proteins/genetics
    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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  • 6
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    Amino acid preferences for specific locations at the ends of alpha helices (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: A definition based on alpha-carbon positions and a sample of 215 alpha helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Richardson, J S -- Richardson, D C -- GM-15000/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1648-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Duke University, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3381086" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acids ; Asparagine ; Hydrogen Bonding ; Proline ; *Protein Conformation
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    A larger spectrum of severe HIV-1--related disease in intravenous drug users in New York City (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: Increasing mortality in intravenous (IV) drug users not reported to surveillance as acquired immunodeficiency syndrome (AIDS) has occurred in New York City coincident with the AIDS epidemic. From 1981 to 1986, narcotics-related deaths increased on average 32% per year from 492 in 1981 to 1996 in 1986. This increase included deaths from AIDS increasing from 0 to 905 and deaths from other causes, many of which were infectious diseases, increasing from 492 to 1091. Investigations of these deaths suggest a causal association with human immunodeficiency virus (HIV) infection. These deaths may represent a spectrum of HIV-related disease that has not been identified through AIDS surveillance and has resulted in a large underestimation of the impact of AIDS on IV drug users and blacks and Hispanics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stoneburner, R L -- Des Jarlais, D C -- Benezra, D -- Gorelkin, L -- Sotheran, J L -- Friedman, S R -- Schultz, S -- Marmor, M -- Mildvan, D -- Maslansky, R -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):916-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉AIDS Research Unit, New York City Department of Health, NY 10013.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187532" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/complications/*epidemiology/microbiology ; Cause of Death ; Endocarditis/complications ; Hiv ; HIV Seropositivity ; Homosexuality ; Humans ; Male ; New York City ; Pneumonia/complications ; Substance-Related Disorders/*complications/epidemiology/mortality ; Tuberculosis/complications
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Steroid binding at sigma receptors suggests a link between endocrine, nervous, and immune systems (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-08
    Description: Specific sigma binding sites have been identified in the mammalian brain and lymphoid tissue. In this study, certain gonadal and adrenal steroids, particularly progesterone, were found to inhibit sigma receptor binding in homogenates of brain and spleen. The findings suggest that steroids are naturally occurring ligands for sigma receptors and raise the possibility that these sites mediate some aspects of steroid-induced mental disturbances and alterations in immune functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, T P -- London, E D -- Jaffe, J H -- New York, N.Y. -- Science. 1988 Apr 8;240(4849):219-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Addiction Research Center, National Institute on Drug Abuse, Baltimore, MD 21224.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832949" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Endocrine Glands/*physiology ; Guinea Pigs ; Haloperidol/metabolism ; *Immunity ; Male ; *Nervous System Physiological Phenomena ; Phenazocine/analogs & derivatives/metabolism ; Receptors, Opioid/*metabolism ; Receptors, sigma ; Spleen/metabolism ; Steroids/*metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Longevity and gender (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McLaren, D S -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):399-400.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3393905" target="_blank"〉PubMed〈/a〉
    Keywords: Energy Metabolism ; Female ; Humans ; *Longevity ; Male ; Sex Factors
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Cryopreservation, culture, and transplantation of human fetal mesencephalic tissue into monkeys (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-04
    Description: Studies in animals suggest that fetal neural grafts might restore lost neurological function in Parkinson's disease. In monkeys, such grafts survive for many months and reverse signs of parkinsonism, without attendant graft rejection. The successful and reliable application of a similar transplantation procedure to human patients, however, will require neural tissue obtained from human fetal cadavers, with demonstrated cellular identity, viability, and biological safety. In this report, human fetal neural tissue was successfully grafted into the brains of monkeys. Neural tissue was collected from human fetal cadavers after 9 to 12 weeks of gestation and cryopreserved in liquid nitrogen. Viability after up to 2 months of storage was demonstrated by cell culture and by transplantation into monkeys. Cryopreservation and storage of human fetal neural tissue would allow formation of a tissue bank. The stored cells could then be specifically tested to assure their cellular identity, viability, and bacteriological and virological safety before clinical use. The capacity to collect and maintain viable human fetal neural tissue would also facilitate research efforts to understand the development and function of the human brain and provide opportunities to study neurological diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Redmond, D E Jr -- Naftolin, F -- Collier, T J -- Leranth, C -- Robbins, R J -- Sladek, C D -- Roth, R H -- Sladek, J R Jr -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):768-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2903552" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Survival ; Cells, Cultured ; Cercopithecus ; Fetus ; Freezing ; Humans ; Male ; Mesencephalon/cytology/embryology/enzymology/*transplantation ; Preservation, Biological ; Transplantation, Heterologous ; Tyrosine 3-Monooxygenase/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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    Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-01
    Description: A method of combinatorial cassette mutagenesis was designed to readily determine the informational content of individual residues in protein sequences. The technique consists of simultaneously randomizing two or three positions by oligonucleotide cassette mutagenesis, selecting for functional protein, and then sequencing to determine the spectrum of allowable substitutions at each position. Repeated application of this method to the dimer interface of the DNA-binding domain of lambda repressor reveals that the number and type of substitutions allowed at each position are extremely variable. At some positions only one or two residues are functionally acceptable; at other positions a wide range of residues and residue types are tolerated. The number of substitutions allowed at each position roughly correlates with the solvent accessibility of the wild-type side chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reidhaar-Olson, J F -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):53-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388019" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Codon ; DNA/genetics/metabolism ; *DNA-Binding Proteins ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Plasmids ; Protein Conformation ; Repressor Proteins/*genetics ; Structure-Activity Relationship ; Transcription Factors/*genetics ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 12
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    Breast cancer-associated pS2 protein: synthesis and secretion by normal stomach mucosa (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: The human pS2 gene is specifically expressed under estrogen transcriptional control in a subclass of estrogen receptor-containing human breast cancer cells. The pS2 gene encodes an 84-amino acid protein that is secreted after signal peptide cleavage. The distribution of pS2 protein in normal human tissues was studied with antibodies to pS2; pS2 was specifically expressed and secreted by mucosa cells of the normal stomach antrum and body of both female and male individuals. Moreover, no estrogen receptor could be detected in these cells, indicating that pS2 gene expression is estrogen-independent in the stomach. The function of the pS2 protein in the gastrointestinal tract is unknown. However, the pS2 protein is similar in sequence to a porcine pancreatic protein that has been shown to inhibit gastrointestinal motility and gastric secretion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rio, M C -- Bellocq, J P -- Daniel, J Y -- Tomasetto, C -- Lathe, R -- Chenard, M P -- Batzenschlager, A -- Chambon, P -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):705-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CNRS et U. 184 de l'INSERM, Institut de Chimie Biologique, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041593" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Breast Neoplasms/*metabolism ; Estrogens/pharmacology ; Exons ; Female ; Gastric Mucosa/*metabolism ; *Gene Expression Regulation ; Histocytochemistry ; Humans ; Immunoenzyme Techniques ; Male ; Molecular Sequence Data ; Neoplasm Proteins/*biosynthesis/genetics/secretion ; *Proteins ; RNA, Messenger/metabolism ; Receptors, Estrogen/metabolism ; Sequence Homology, Nucleic Acid ; Tissue Distribution ; Tumor Cells, Cultured ; Tumor Suppressor Proteins
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  • 13
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    Cloning of a membrane protein that induces a slow voltage-gated potassium current (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: A rat kidney messenger RNA that induces a slowly activating, voltage-dependent potassium current on its expression in Xenopus oocytes was identified by combining molecular cloning with an electrophysiological assay. The cloned complementary DNA encodes a novel membrane protein that consists of 130 amino acids with a single putative transmembrane domain. This protein differs from the known ion channel proteins but is involved in the induction of selective permeation of potassium ions by membrane depolarization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takumi, T -- Ohkubo, H -- Nakanishi, S -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Immunology, Kyoto University Faculty of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194754" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Electric Conductivity ; Membrane Potentials ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Potassium Channels/*physiology ; Rats ; Xenopus laevis
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  • 14
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    Imaging of phosphorescence: a novel method for measuring oxygen distribution in perfused tissue (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-23
    Description: The imaging of phosphorescence provides a method for monitoring oxygen distribution within the vascular system of intact tissues. Isolated rat lives were perfused through the portal vein with media containing palladium coproporphyrin, which phosphoresced and was used to image the liver at various perfusion rates. Because oxygen is a powerful quenching agent for phosphors, the transition from well-perfused liver to anoxia (no flow of oxygen) resulted in large increases of phosphorescence. During stepwise restoration of oxygen flow, the phosphorescence images showed marked heterogeneous patterns of tissue reoxygenation, which indicated that there were regional inequalities in oxygen delivery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rumsey, W L -- Vanderkooi, J M -- Wilson, D F -- GM 21524/GM/NIGMS NIH HHS/ -- GM 36393/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1649-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Coproporphyrins ; Liver Circulation ; *Luminescence ; Male ; Oxygen/*analysis ; Palladium ; Perfusion ; Rats ; Rats, Inbred Strains
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  • 15
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    A molecular basis for MHC class II--associated autoimmunity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-20
    Description: Class II major histocompatibility (MHC) molecules have an immunoregulatory role. These cell-surface glycoproteins present fragments of protein antigens (or peptides) to thymus-derived lymphocytes (T cells). Nucleotide sequence polymorphism in the genes that encode the class II MHC products determines the specificity of the immune response and is correlated with the development of autoimmune diseases. This study identifies certain class II polymorphic amino acid residues that are strongly associated with susceptibility to insulin-dependent diabetes mellitus, rheumatoid arthritis, and pemphigus vulgaris. These findings implicate particular class II MHC isotypes in susceptibility to each disease and suggest new prophylactic and therapeutic strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todd, J A -- Acha-Orbea, H -- Bell, J I -- Chao, N -- Fronek, Z -- Jacob, C O -- McDermott, M -- Sinha, A A -- Timmerman, L -- Steinman, L -- New York, N.Y. -- Science. 1988 May 20;240(4855):1003-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3368786" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arthritis, Rheumatoid/immunology ; Autoantibodies/*genetics ; Autoimmune Diseases/*genetics ; Diabetes Mellitus, Type 1/immunology ; HLA-D Antigens/*genetics ; Humans ; Major Histocompatibility Complex ; Molecular Sequence Data ; Pemphigus/immunology
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  • 16
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    Identification of an intracellular peptide segment involved in sodium channel inactivation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-23
    Description: Antibodies directed against a conserved intracellular segment of the sodium channel alpha subunit slow the inactivation of sodium channels in rat muscle cells. Of four site-directed antibodies tested, only antibodies against the short intracellular segment between homologous transmembrane domains III and IV slowed inactivation, and their effects were blocked by the corresponding peptide antigen. No effects on the voltage dependence of sodium channel activation or of steady-state inactivation were observed, but the rate of onset of the antibody effect and the extent of slowing of inactivation were voltage-dependent. Antibody binding was more rapid at negative potentials, at which sodium channels are not inactivated; antibody-induced slowing of inactivation was greater during depolarizations to more positive membrane potentials. The peptide segment recognized by this antibody appears to participate directly in rapid sodium channel inactivation during large depolarizations and to undergo a conformational change that reduces its accessibility to antibodies as the channel inactivates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vassilev, P M -- Scheuer, T -- Catterall, W A -- NS 15751/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, School of Medicine, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2458625" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies ; Cytoplasm/analysis ; In Vitro Techniques ; Ion Channels/*metabolism ; Membrane Potentials ; Molecular Sequence Data ; Peptides/*metabolism ; Rats ; Sodium/*metabolism
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  • 17
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    Molecular cloning of two types of GAP complementary DNA from human placenta (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-23
    Description: The ras p21 GTPase-activating protein (GAP) was purified from human placental tissue. Internal amino acid sequence was obtained from this 120,000-dalton protein and, by means of this sequence, two types of complementary DNA clones were isolated and characterized. One type encoded GAP with a predicted molecular mass of 116,000 daltons and 96% identity with bovine GAP. The messenger RNA of this GAP was detected in human lung, brain, liver, leukocytes, and placenta. The second type appeared to be generated by a differential splicing mechanism and encoded a novel form of GAP with a predicted molecular mass of 100,400 daltons. This protein lacks the hydrophobic amino terminus characteristic of the larger species, but retains GAP activity. The messenger RNA of this type was abundantly expressed in placenta and in several human cell lines, but not in adult tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trahey, M -- Wong, G -- Halenbeck, R -- Rubinfeld, B -- Martin, G A -- Ladner, M -- Long, C M -- Crosier, W J -- Watt, K -- Koths, K -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1697-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corp., Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201259" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Brain Chemistry ; *Cloning, Molecular ; DNA/*genetics/isolation & purification ; Female ; GTPase-Activating Proteins ; Gene Expression Regulation ; Humans ; Leukocytes/analysis ; Liver/analysis ; Lung/analysis ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Placenta/*analysis ; Pregnancy ; Proteins/*genetics/isolation & purification ; RNA, Messenger/analysis/genetics ; Sequence Homology, Nucleic Acid ; ras GTPase-Activating Proteins
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  • 18
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    Tandem array of human visual pigment genes at Xq28 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Unequal crossing-over within a head-to-tail tandem array of the homologous red and green visual pigment genes has been proposed to explain the observed variation in green-pigment gene number among individuals and the prevalence of red-green fusion genes among color-blind subjects. This model was tested by probing the structure of the red and green pigment loci with long-range physical mapping techniques. The loci were found to constitute a gene array with an approximately 39-kilobase repeat length. The position of the red pigment gene at the 5' edge of the array explains its lack of variation in copy number. Restriction maps of the array in four individuals who differ in gene number are consistent with a head-to-tail configuration of the genes. These results provide physical evidence in support of the model and help to explain the high incidence of color blindness in the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vollrath, D -- Nathans, J -- Davis, R W -- GM21891/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1669-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2837827" target="_blank"〉PubMed〈/a〉
    Keywords: Color Vision Defects/*genetics ; Crossing Over, Genetic ; DNA/genetics ; DNA Restriction Enzymes ; Electrophoresis, Agar Gel ; Exons ; Female ; Genetic Variation ; Humans ; Male ; Nucleic Acid Hybridization ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Retinal Pigments/*genetics ; *X Chromosome
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  • 19
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    Functional expression of a new pharmacological subtype of brain nicotinic acetylcholine receptor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-15
    Description: A new type of agonist-binding subunit of rat neuronal nicotinic acetylcholine receptors (nAChRs) was identified. Rat genomic DNA and complementary DNA encoding this subunit (alpha 2) were cloned and analyzed. Complementary DNA expression studies in Xenopus oocytes revealed that the injection of messenger RNAs (mRNAs) for alpha 2 and beta 2 (a neuronal nAChR subunit) led to the generation of a functional nAChR. In contrast to the other known neuronal nAChRs, the receptor produced by the injection of alpha 2 and beta 2 mRNAs was resistant to the alpha-neurotoxin Bgt3.1. In situ hybridization histochemistry showed that alpha 2 mRNA was expressed in a small number of regions, in contrast to the wide distribution of the other known agonist-binding subunits (alpha 3 and alpha 4) mRNAs. These results demonstrate that the alpha 2 subunit differs from other known agonist-binding alpha-subunits of nAChRs in its distribution in the brain and in its pharmacology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wada, K -- Ballivet, M -- Boulter, J -- Connolly, J -- Wada, E -- Deneris, E S -- Swanson, L W -- Heinemann, S -- Patrick, J -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):330-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832952" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*metabolism ; DNA Restriction Enzymes ; Female ; *Genes ; Molecular Sequence Data ; Neurons/metabolism ; Nucleotide Mapping ; Oocytes/metabolism ; Rats ; Receptors, Nicotinic/*genetics/metabolism ; Transcription, Genetic ; Xenopus laevis
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  • 20
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    Aggregation of lysine-containing zeins into protein bodies in Xenopus oocytes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: Zeins, the storage proteins of maize, are totally lacking in the essential amino acids lysine and tryptophan. Lysine codons and lysine- and tryptophan-encoding oligonucleotides were introduced at several positions into a 19-kilodalton zein complementary DNA by oligonucleotide-mediated mutagenesis. A 450-base pair open reading frame from a simian virus 40 (SV40) coat protein was also engineered into the zein coding region. Messenger RNAs for the modified zeins were synthesized in vitro with an SP6 RNA polymerase system and injected into Xenopus laevis oocytes. The modifications did not affect the translation, signal peptide cleavage, or stability of the zeins. The ability of the modified zeins to assemble into structures similar to maize protein bodies was assayed by two criteria: assembly into membrane-bound vesicles resistant to exogenously added protease, and ability to self-aggregate into dense structures. All of the modified zeins were membrane-bound; only the one containing a 17-kilodalton SV40 protein fragment was unable to aggregate. These findings suggest that it may be possible to create high-lysine corn by genetic engineering.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, J C -- Galili, G -- Kawata, E E -- Cuellar, R E -- Shotwell, M A -- Larkins, B A -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):662-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2834822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Membrane/metabolism ; DNA/genetics ; DNA, Recombinant ; Female ; Genetic Engineering ; *Lysine/genetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Oocytes/*metabolism ; Peptide Hydrolases/metabolism ; RNA, Messenger/genetics ; Simian virus 40/genetics ; Xenopus laevis ; Zea mays ; Zein/genetics/*metabolism
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  • 21
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    Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-09
    Description: Leber's hereditary optic neuropathy is a maternally inherited disease resulting in optic nerve degeneration and cardiac dysrhythmia. A mitochondrial DNA replacement mutation was identified that correlated with this disease in multiple families. This mutation converted a highly conserved arginine to a histidine at codon 340 in the NADH dehydrogenase subunit 4 gene and eliminated an Sfa NI site, thus providing a simple diagnostic test. This finding demonstrated that a nucleotide change in a mitochondrial DNA energy production gene can result in a neurological disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, D C -- Singh, G -- Lott, M T -- Hodge, J A -- Schurr, T G -- Lezza, A M -- Elsas, L J 2nd -- Nikoskelainen, E K -- NS21328/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1427-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201231" target="_blank"〉PubMed〈/a〉
    Keywords: African Continental Ancestry Group ; Animals ; Arginine ; Cytochrome Reductases/*genetics ; DNA, Mitochondrial/*genetics ; European Continental Ancestry Group ; Female ; *Genes ; Georgia ; Hereditary Sensory and Motor Neuropathy/*genetics ; Histidine ; Humans ; Macromolecular Substances ; Male ; *Mutation ; NADH Dehydrogenase/*genetics ; Optic Atrophies, Hereditary/*genetics ; Pedigree ; Reference Values
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  • 22
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    Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-24
    Description: The rate of lateral diffusion of integral membrane proteins is constrained in cells, but the constraining factors for most membrane proteins have not been defined. PH-20, a sperm surface protein involved in sperm-egg adhesion, was shown to be anchored in the plasma membrane by attachment to the lipid phosphatidylinositol and to have a diffusion rate that is highly restricted on testicular sperm, being more than a thousand times slower than lipid diffusion. These results support the hypothesis that lateral mobility of a membrane protein can be regulated exclusively by interactions of its ectodomain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phelps, B M -- Primakoff, P -- Koppel, D E -- Low, M G -- Myles, D G -- GM-23585/GM/NIGMS NIH HHS/ -- HD-16580/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 24;240(4860):1780-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut Health Center, Farmington 06032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3381102" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Surface ; Cell Adhesion Molecules ; Cell Compartmentation ; Cell Membrane/physiology ; Diffusion ; Guinea Pigs ; Male ; *Membrane Fluidity ; Membrane Proteins/*physiology ; Phosphatidylinositols/*physiology ; Sperm Maturation ; Spermatozoa/*physiology ; Testis/physiology
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  • 23
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    Alpha-2-antiplasmin: a serpin with two separate but overlapping reactive sites (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: Although the proteinase inhibitor alpha-2-antiplasmin (alpha 2AP) is known to control the activity of plasmin through rapid formation of stable complexes, it also efficiently inactivates chymotrypsin. These interactions are shown to occur at adjacent, overlapping sites so that plasmin attacks the inhibitor at an Arg364-Met365 peptide bond, while chymotrypsin interacts at a Met365-Ser366 sequence one residue downstream. Thus, a naturally occurring plasma serine proteinase inhibitor can have multiple specificities through interactions at adjacent sites. It also illustrates the potential flexibility of the reactive site loop in this class of inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potempa, J -- Shieh, B H -- Travis, J -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):699-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Jagiellonian University, Cracow, Poland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2456616" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Carboxypeptidase B ; Carboxypeptidases/metabolism ; Carboxypeptidases A ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chymotrypsin/antagonists & inhibitors/metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Molecular Sequence Data ; Peptide Fragments/metabolism ; Protease Inhibitors ; alpha-2-Antiplasmin/*metabolism
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  • 24
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    Seroprevalence and epidemiological correlates of HTLV-I infection in U.S. blood donors (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-29
    Description: Screening for human T-lymphotropic virus type I (HTLV-I) antibodies was performed on sera from 39,898 blood donors at eight blood centers in geographically distinct areas of the United States. Ten donors (0.025 percent) showed evidence of HTLV-I seropositivity by enzyme immunoassays; this was confirmed by protein immunoblot and radioimmunoprecipitation. Seroprevalence rates ranged from 0 to 0.10 percent at the locations sampled, with HTLV-I antibodies found predominantly in donors from the southeastern and southwestern United States. Matched case-control interviews and laboratory studies were performed on five seropositive women and two seropositive men who participated in an identity-linked collection of sera from a subset of 33,893 donors at six of the eight blood centers. Four of the women and both men are black; one woman is Caucasian. Four of the seven seropositive individuals admitted to prior intravenous drug abuse or sexual contact with an intravenous drug user. Sexual contact with native inhabitants of an HTLV-I endemic area was the only identified risk factor for one male. The distribution of HTLV-I antibodies in this U.S. blood donor sample corroborates the previously reported epidemiology of this agent and suggests that additional donor screening measures, including the testing of donated blood for HTLV-I markers, may be necessary to prevent the spread of HTLV-I to transfusion recipients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, A E -- Fang, C T -- Slamon, D J -- Poiesz, B J -- Sandler, S G -- Darr, W F 2nd -- Shulman, G -- McGowan, E I -- Douglas, D K -- Bowman, R J -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):643-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉American Red Cross Jerome H. Holland Laboratory, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2896386" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antibodies, Viral/*analysis ; *Blood Donors ; Deltaretrovirus/*immunology/isolation & purification ; Deltaretrovirus Infections/diagnosis/*epidemiology/transmission ; Female ; Humans ; Immunoenzyme Techniques ; Immunosorbent Techniques ; Japan ; Male ; Middle Aged ; Risk Factors ; Sexual Partners ; Substance-Related Disorders ; United States
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  • 25
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    Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-22
    Description: The parasitic protozoon Trypanosoma brucei contains a highly organized membrane skeleton, consisting of a dense array of parallel, singlet microtubules that are laterally interconnected and that are also in tight contact with the overlying cell membrane. A high molecular weight, heat-stable protein from this membrane skeleton was isolated that is localized along the microtubules. Protease digestion experiments and sequencing of a cloned gene segment showed that most of the protein is built up by more than 50 nearly identical tandem repeats with a periodicity of 38 amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, A -- Hemphill, A -- Wyler, T -- Seebeck, T -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur allgemeine Mikrobiologie, Universitat Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3393912" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Compartmentation ; Cell Membrane/ultrastructure ; Cloning, Molecular ; Microscopy, Electron ; Microtubule-Associated Proteins/*analysis/genetics ; Microtubules/ultrastructure ; Molecular Sequence Data ; Molecular Weight ; Repetitive Sequences, Nucleic Acid ; Trypanosoma brucei brucei/*analysis/genetics/ultrastructure
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  • 26
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    Amyloid beta protein precursor is possibly a heparan sulfate proteoglycan core protein (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-08
    Description: The amyloid beta protein peptide is a major constituent of amyloid plaque cores in Alzheimer's disease and is apparently derived from a higher molecular weight precursor. It is now shown that the core protein of a heparan sulfate proteoglycan secreted from a nerve cell line (PC12) has an amino acid sequence and a size very similar to those of the amyloid beta protein precursor and that these molecules are antigenically related. This amyloid beta protein precursor-related protein is not found in the conditioned medium of a variant cell line (F3 PC12) that does not secrete heparan sulfate proteoglycan. The synaptic localization and metabolism of this class of proteoglycans are consistent with its potential involvement in central nervous system dysfunction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schubert, D -- Schroeder, R -- LaCorbiere, M -- Saitoh, T -- Cole, G -- AG 05131/AG/NIA NIH HHS/ -- F2 AG 05424A/AG/NIA NIH HHS/ -- NS 09658/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2968652" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*metabolism ; Amino Acid Sequence ; Amyloid/*metabolism ; Amyloid beta-Peptides ; Animals ; Cell Line ; Chondroitin Sulfate Proteoglycans/*metabolism ; Chromatography, High Pressure Liquid ; Glycosaminoglycans/*metabolism ; Heparan Sulfate Proteoglycans ; Heparitin Sulfate/*metabolism ; Immunologic Techniques ; Peptide Fragments ; Proteoglycans/*metabolism ; Rats ; Viral Core Proteins/*metabolism
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  • 27
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    Juvenile hormone action mediated in male accessory glands of Drosophila by calcium and kinase C (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-19
    Description: In an in vitro system for the Drosophila melanogaster male accessory gland, it was found that 10(-9)M juvenile hormone III could accurately mimic the copulation-induced response of increased protein synthesis in glands from virgin flies. Stimulation by this hormone required calcium in the medium. Experiments with tumor-promoting phorbol esters indicated that activation of protein kinase C can also cause the glands to increase protein synthesis. Stimulation of protein synthesis by juvenile hormone did not occur in mutants deficient in kinase C activity. These results suggest a membrane-protein-mediated effect of juvenile hormone that involves calcium and kinase C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, K -- Chadarevian, A -- Pellegrini, M -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):916-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Section, University of Southern California, Los Angeles 90089.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3124270" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology ; Drosophila melanogaster/*metabolism ; Enzyme Activation/drug effects ; Genitalia, Male/drug effects/metabolism ; Juvenile Hormones/genetics ; Male ; Membrane Proteins/metabolism ; Mutation ; Phorbol 12,13-Dibutyrate ; Phorbol Esters/pharmacology ; Protein Biosynthesis ; Protein Kinase C/*metabolism ; Sesquiterpenes/*pharmacology ; Tetradecanoylphorbol Acetate/pharmacology
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    Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: Interleukin-6 (IL-6/BSF-2/IFN beta 2) is a multifunctional cytokine that regulates the growth and differentiation of various tissues, and is known particularly for its role in the immune response and acute phase reactions. A complementary DNA encoding the human IL-6 receptor (IL-6-R) has now been isolated. The IL-6-R consists of 468 amino acids, including a signal peptide of approximately 19 amino acids and a domain of approximately 90 amino acids that is similar to a domain in the immunoglobulin (Ig) superfamily. The cytoplasmic domain of approximately 82 amino acids lacks a tyrosine/kinase domain, unlike other growth factor receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamasaki, K -- Taga, T -- Hirata, Y -- Yawata, H -- Kawanishi, Y -- Seed, B -- Taniguchi, T -- Hirano, T -- Kishimoto, T -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):825-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3136546" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Cloning, Molecular ; DNA/genetics/isolation & purification ; *Genes ; Humans ; Immunoglobulin kappa-Chains/genetics ; Molecular Sequence Data ; Receptors, Immunologic/genetics ; Receptors, Interleukin-6 ; Sequence Homology, Nucleic Acid ; *Transcription, Genetic
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    Familial imprinting determines H-2 selective mating preferences (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-03
    Description: Inbred male mice typically prefer to mate with females of a different, non-self H-2 haplotype. To determine whether this natural preference is irrevocable or results from familial imprinting, a test system was used which relied on previous observations that B6 males (H-2b) mate preferentially with congenic B6-H-2k rather than B6 females, and B6-H-2k males with B6 females. This preference was reversed in B6 males fostered by B6-H-2k parents and in B6-H-2k males fostered by B6 parents, preference in these cases favoring the same H-2 type. Thus, H-2 selective mating preference is acquired by imprinting on familial H-2 types.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamazaki, K -- Beauchamp, G K -- Kupniewski, D -- Bard, J -- Thomas, L -- Boyse, E A -- CA-39827/CA/NCI NIH HHS/ -- GMCA-32096/GM/NIGMS NIH HHS/ -- NS-22623/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1331-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monell Chemical Senses Center, Philadelphia, PA 19104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3375818" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; H-2 Antigens/*genetics ; *Imprinting (Psychology) ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Odors ; *Sexual Behavior, Animal ; Smell/physiology
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    Insulin-resistant diabetes due to a point mutation that prevents insulin proreceptor processing (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-06
    Description: A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser. Epstein-Barr virus-transformed lymphocytes from this patient synthesize an insulin receptor precursor that is normally glycosylated and inserted into the plasma membrane but is not cleaved to mature alpha and beta subunits. Insulin binding to these cells is severely reduced but can be increased about fivefold by gentle treatment with trypsin, accompanied by the appearance of normal alpha subunits. These results indicate that proteolysis of the proreceptor is necessary for its normal full insulin-binding sensitivity and signal-transducing activity and that a cellular protease that is more stringent in its specificity than trypsin is required to process the receptor precursor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshimasa, Y -- Seino, S -- Whittaker, J -- Kakehi, T -- Kosaki, A -- Kuzuya, H -- Imura, H -- Bell, G I -- Steiner, D F -- AM 13914/AM/NIADDK NIH HHS/ -- AM 20595/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1988 May 6;240(4853):784-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283938" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; DNA/genetics ; Diabetes Mellitus/*genetics/metabolism ; Female ; Glycosylation ; Humans ; Insulin/metabolism ; Insulin Resistance/*genetics ; Lymphocytes/metabolism ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; Protein Precursors/*genetics/metabolism ; RNA, Messenger/metabolism ; Receptor, Insulin/*genetics/metabolism ; Trypsin/metabolism
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    Novel regulators of bone formation: molecular clones and activities (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-16
    Description: Protein extracts derived from bone can initiate the process that begins with cartilage formation and ends in de novo bone formation. The critical components of this extract, termed bone morphogenetic protein (BMP), that direct cartilage and bone formation as well as the constitutive elements supplied by the animal during this process have long remained unclear. Amino acid sequence has been derived from a highly purified preparation of BMP from bovine bone. Now, human complementary DNA clones corresponding to three polypeptides present in this BMP preparation have been isolated, and expression of the recombinant human proteins have been obtained. Each of the three (BMP-1, BMP-2A, and BMP-3) appears to be independently capable of inducing the formation of cartilage in vivo. Two of the encoded proteins (BMP-2A and BMP-3) are new members of the TGF-beta supergene family, while the third, BMP-1, appears to be a novel regulatory molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wozney, J M -- Rosen, V -- Celeste, A J -- Mitsock, L M -- Whitters, M J -- Kriz, R W -- Hewick, R M -- Wang, E A -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1528-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tissue Growth and Repair Program, Genetics Institute, Inc., Cambridge, MA 02140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201241" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone Morphogenetic Proteins ; Cartilage/cytology/drug effects ; Cell Line ; DNA/genetics ; Growth Substances/*genetics ; Humans ; Molecular Sequence Data ; *Osteogenesis ; Proteins/*genetics/pharmacology ; Recombinant Proteins/pharmacology ; Sequence Homology, Nucleic Acid ; Transforming Growth Factors/genetics
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    Antibodies to Asp-Asp-Glu-Asp can inhibit transport of nuclear proteins into the nucleus (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-14
    Description: The signal sequence of simian virus 40 (SV40) large T-antigen for translocation into the nucleus is composed of positively charged amino acids Lys-Lys-Lys-Arg-Lys. Rabbit antibodies to a synthetic peptide containing the negatively charged amino acid sequence Asp-Asp-Asp-Glu-Asp were obtained. Indirect immunofluorescence of the antigens recognized by the antibody was punctate at the nuclear rim or the nuclear surface, depending on the plane of focus. The antibody blocked transport of nuclear proteins into the nucleus. The antigens recognized by the antibody were predominantly localized to the nuclear pores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoneda, Y -- Imamoto-Sonobe, N -- Matsuoka, Y -- Iwamoto, R -- Kiho, Y -- Uchida, T -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):275-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular and Cellular Biology, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3051382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/immunology ; Antigens, Polyomavirus Transforming ; Biological Transport ; Cell Line ; Cell Nucleus/*metabolism ; Fluorescent Antibody Technique ; Humans ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Nucleoplasmins ; Oligopeptides/immunology/*physiology ; *Phosphoproteins ; Protein Sorting Signals/*physiology ; Rats
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    The drug of champions (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):183-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175643" target="_blank"〉PubMed〈/a〉
    Keywords: *Anabolic Agents/adverse effects ; *Doping in Sports/legislation & jurisprudence ; Female ; Humans ; Male ; Risk Factors ; Stanozolol ; Substance-Related Disorders/*economics
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    What T cells see and how they see it (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):863-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/prevention & control ; Amino Acid Sequence ; Antigens/*immunology ; Epitopes/immunology ; Major Histocompatibility Complex ; Protein Conformation ; T-Lymphocytes/*immunology ; Viral Vaccines
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    DNA fingerprinting takes the witness stand (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1616-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2898170" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*analysis/blood ; Forensic Medicine/*methods ; Gene Amplification ; Hair/analysis ; Homicide ; Humans ; Male ; Polymorphism, Restriction Fragment Length ; Rape/legislation & jurisprudence ; Repetitive Sequences, Nucleic Acid ; Spermatozoa/analysis
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    A parent's sex may affect gene expression (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Jan 22;239(4838):352-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3336789" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/metabolism ; Female ; *Gene Expression Regulation ; Genes ; Humans ; Male ; Methylation ; Mice ; Mice, Transgenic ; *Sex Characteristics ; Tissue Distribution
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    Sexual responses are--almost--all in the brain (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):903-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043664" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Female ; Humans ; Male ; Menopause/*physiology ; Mice ; Pituitary Hormone-Releasing Hormones/*biosynthesis ; Puberty/*physiology ; Rats ; Sexual Maturation
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    Microinjected DNA from the X chromosome affects sex determination in Caenorhabditis elegans (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-25
    Description: The signal for sex determination in the nematode Caenorhabditis elegans is the ratio of the number of X chromosomes to the number of sets of autosomes (X/A ratio). By previous genetic tests, elements that feminized chromosomal males appeared to be widespread on the X chromosome, but the nature of these elements was not determined. In experiments to define a feminizing element molecularly, cloned sequences were added to chromosomally male embryos by microinjection into the mother. Three different X-chromosome clones, including part of an actin gene, part of a myosin heavy chain gene, and all of two myosin light chain genes, feminize chromosomal males. Both somatic and germline aspects of sex determination are affected. In contrast, about 40 kilobases of nematode autosomal DNA, phage lambda DNA, and plasmid pBR322 DNA do not affect sex determination. A feminizing region was localized to a maximum of 131 base pairs within an intron of the X-linked actin gene; a part of the gene that does not have this region is not feminizing. The results suggest that short, discrete elements found associated with many X-linked genes may act as signals for sex determination in C. elegans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCoubrey, W K -- Nordstrom, K D -- Meneely, P M -- 5T32CA09437-06/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1146-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2973125" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Animals ; Bacteriophage lambda/genetics ; Base Sequence ; Caenorhabditis/*genetics ; DNA, Recombinant ; DNA, Viral/genetics ; Disorders of Sex Development ; Exons ; Introns ; Male ; Microinjections ; Molecular Sequence Data ; Myosins/genetics ; Phenotype ; Plasmids ; *Sex Determination Analysis ; Transformation, Genetic ; *X Chromosome
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    Platelet-derived growth factor A chain is maternally encoded in Xenopus embryos (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Transcription of zygotic genes does not occur in early Xenopus embryos until the mid-blastula transition, 6 to 7 hours after fertilization. Before this time, development is directed by maternal proteins and messenger RNAs stored within the egg. Two different forms of the A chain of platelet-derived growth factor (PDGF) are shown here to be encoded by maternal messenger RNAs. The two forms closely resemble human PDGF; however, the long form contains a hydrophobic region near the carboxyl terminus. The presence of PDGF messenger RNA in the embryo supports the idea that endogenous growth factors act at the earliest stages of embryogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, M -- Melton, D A -- Stiles, C D -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1223-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413486" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blastocyst/metabolism ; DNA/genetics/isolation & purification ; Gastrula/analysis ; Humans ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oocytes/analysis ; Platelet-Derived Growth Factor/*genetics ; RNA, Messenger/analysis/genetics ; Xenopus laevis/*embryology/genetics
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    A chemically synthesized Antennapedia homeo domain binds to a specific DNA sequence (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-11
    Description: A peptide 60 residues in length that corresponds to the homeo domain of Antennapedia (Antp), a protein governing development in Drosophila, was synthesized by segment condensation with protected peptide segments prepared on an oxime resin. A footprinting assay showed that the homeo domain binds specifically to a TAA repeat DNA sequence in the Antp gene. Thus the Antp homeo domain has a sequence-specific DNA binding property. The circular dichroism spectra of the homeo domain peptide showed the presence of a significant amount of alpha-helical structure in aqueous solution and in 50 percent trifluoroethanol. The alpha helicity measured in water appears to depend on the peptide concentration, which suggests that the peptide aggregates. These results support the hypothesis that the homeo domain binds to DNA through a helix-turn-helix motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mihara, H -- Kaiser, E T -- RR 862/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):925-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2903553" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromatography, High Pressure Liquid ; Circular Dichroism ; DNA/*metabolism ; Drosophila/*growth & development ; Electrophoresis, Polyacrylamide Gel ; *Genes, Homeobox ; Insect Hormones/*chemical synthesis/genetics/metabolism ; Molecular Sequence Data ; Peptide Fragments/*chemical synthesis/genetics ; Protein Conformation ; Repetitive Sequences, Nucleic Acid
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    Diet and health in China (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberts, L -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):27.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353707" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; China ; *Diet ; Diet Surveys ; Female ; *Health ; Humans ; Male ; Middle Aged ; Neoplasms/epidemiology
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    Expression of a calcium-mobilizing parathyroid hormone-like peptide in lactating mammary tissue (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: A survey of rat tissues by RNA analysis, aimed at uncovering the physiological function of the parathyroid hormone-like peptide (PTH-LP) associated with hypercalcemia of malignancy, revealed the presence of a 1.5-kilobase messenger RNA encoding this peptide in lactating mammary glands. PTH-LP messenger RNA is expressed in mammary tissue only during lactation; it appears and disappears rapidly (2 to 4 hours) as a function of the sucking stimulus. The identity of this messenger RNA was confirmed by cloning the rat PTH-LP complementary DNA, which predicts a peptide with strong similarity to the human homolog. Moreover, extracts from lactating mammary tissue stimulated parathyroid hormone-dependent adenylate cyclase. These findings suggest that PTH-LP plays a physiological role in lactation, possibly as a hormone for the mobilization or transfer (or both) of calcium to the milk.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thiede, M A -- Rodan, G A -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):278-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bone Biology and Osteoporosis Research, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175653" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/*metabolism ; Cloning, Molecular ; DNA/genetics ; Female ; *Gene Expression Regulation ; Humans ; Lactation/*metabolism ; Mammary Glands, Animal/*metabolism ; Molecular Sequence Data ; Neoplasm Proteins/*genetics/physiology ; Parathyroid Hormone-Related Protein ; Pregnancy ; RNA, Messenger/genetics/*metabolism ; Rats ; Sequence Homology, Nucleic Acid ; Tissue Distribution
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    A gene for dihydrofolate reductase in a herpesvirus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-04
    Description: The enzyme dihydrofolate reductase (DHFR) is found ubiquitously in both prokaryotes and eukaryotes. It is essential for de novo synthesis of purines and of deoxythymidine monophosphate for DNA synthesis. Among viruses, however, only the T-even and T5 bacteriophage have been found to encode their own DHFR. In this study a gene for DHFR was found in a specific subgroup of the gamma or lymphotropic class of herpesviruses. DNA sequences for DHFR were found in herpesvirus saimiri and herpesvirus ateles but not in Epstein-Barr virus, Marek's disease virus, herpes simplex virus, varicella-zoster virus, herpesvirus tamarinus, or human cytomegalovirus. The predicted sequence of herpesvirus saimiri DHFR is 186 amino acids in length, the same length as human, murine, and bovine DHFR. The human and herpesvirus saimiri DHFRs share 83 percent positional identity in amino acid sequence. The herpesvirus saimiri DHFR gene is devoid of intron sequences, suggesting that it was acquired by some process involving reverse transcription. This is to our knowledge the first example of a mammalian virus with a gene for DHFR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trimble, J J -- Murthy, S C -- Bakker, A -- Grassmann, R -- Desrosiers, R C -- 31363/PHS HHS/ -- RR00168/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1145-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉New England Regional Primate Research Center, Harvard Medical School, Southborough, MA 01772.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830673" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Chickens ; Cytomegalovirus/enzymology ; Herpesviridae/*enzymology ; Herpesvirus 2, Saimiriine/*enzymology ; Herpesvirus 4, Human/enzymology ; Humans ; Introns ; Mice ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; Tetrahydrofolate Dehydrogenase/*genetics
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    cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-29
    Description: Interleukin-1 alpha and -1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis. A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells. The product of the cloned complementary DNA binds both IL-1 alpha and IL-1 beta in a manner indistinguishable from that of the native T cell IL-1 receptor. The extracellular, IL-1 binding portion of the receptor is 319 amino acids in length and is composed of three immunoglobulin-like domains. The cytoplasmic portion of the receptor is 217 amino acids long.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, J E -- March, C J -- Cosman, D -- Widmer, M B -- MacDonald, H R -- McMahan, C J -- Grubin, C E -- Wignall, J M -- Jackson, J L -- Call, S M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):585-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2969618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Genes, Immunoglobulin ; Interleukin-1/*physiology ; Mice ; Molecular Sequence Data ; *Multigene Family ; Receptors, Immunologic/*genetics ; Receptors, Interleukin-1
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  • 45
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    Conversion of a PI-anchored protein to an integral membrane protein by a single amino acid mutation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-05
    Description: Qa-2, a cell-surface glycoprotein anchored by phosphatidylinositol (PI), is structurally related to the class I transplantation antigens H-2 K, D, and L, which are integral membrane glycoproteins. The predicted transmembrane segment of Qa-2 differs from those of H-2 K, D, and L by the presence of an aspartate in place of a valine at position 295. A single base change that replaced this aspartate with valine resulted in cell-surface Qa-2 molecules that were insensitive to hydrolysis by a PI-specific phospholipase C and more resistant to papain cleavage, properties shared by H-2D. Cells expressing Asp----Val mutant Qa-2 proteins were still able to attach a PI anchor to endogenous proteins such as Thy-1 and J11D. It therefore appears that this single amino acid change converts Qa-2 from a PI-linked form into an integral membrane protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waneck, G L -- Stein, M E -- Flavell, R A -- AI24562/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):697-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biogen Research Corporation, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399901" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigens, Surface/genetics ; *Aspartic Acid ; Cell Line ; DNA/genetics ; H-2 Antigens ; *Histocompatibility Antigens/genetics ; *Histocompatibility Antigens Class I ; Membrane Proteins/genetics/*metabolism ; Mutation ; Papain/metabolism ; Phosphatidylinositols/*metabolism ; Thymoma ; Thymus Neoplasms ; Transfection ; Tumor Cells, Cultured ; Type C Phospholipases/metabolism ; *Valine
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  • 46
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    Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: The myosin light chain kinase requires calmodulin for activation. Tryptic cleavage of the enzyme generates an inactive 64-kilodalton (kD) fragment that can be further cleaved to form a constitutively active, calmodulin-independent, 61-kD fragment. Microsequencing and amino acid analysis of purified peptides after proteolysis of the 61- and 64-kD fragments were used to determine the amino-terminal and carboxyl-terminal sequences of the 64-kD fragment. Cleavage within the calmodulin-binding region at Arg505 generates the catalytically inactive 64-kD fragment, which is incapable of binding calmodulin. Further digestion removes a carboxyl-terminal fragment, including the pseudosubstrate sequence Ser484-Lys-Asp-Arg-Met-Lys-Lys-Tyr-Met- Ala-Arg-Arg-Lys-Trp-Gln-Lys-Thr-Gly-His-Ala-Val-Arg505 and results in a calmodulin-independent 61-kD fragment. Both the 61- and 64-kD fragments have the same primary amino-terminal sequences. These results provide direct support for the concept that the pseudosubstrate structure binds the active site and that the role of calmodulin is to modulate this interaction. Pseudosubstrates may be utilized in analogous ways by other allosterically regulated enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, R B -- Wettenhall, R E -- Means, A R -- Hartshorne, D J -- Kemp, B E -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):970-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Melbourne, Repatriation General Hospital, Heidelberg, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3406746" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/*metabolism ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Molecular Sequence Data ; Muscle, Smooth/*enzymology ; Myosin-Light-Chain Kinase/analysis/*metabolism ; Peptide Mapping ; Substrate Specificity
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  • 47
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    Kin selection and the evolution of monogamy (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-17
    Description: A two-locus genetic model is studied in which one locus controls the tendency of individuals to act altruistically toward siblings and the other locus controls the mating habits of females. It is demonstrated that genetic variation at the altruism locus is often sufficient to induce an increase in the frequency of genes that cause females to produce all of their offspring with a single mate. This occurs because of nonrandom associations that develop between genes that cause altruism and those that affect female mating behavior. The results provide a new explanation for the evolution of monogamy, and they suggest a previously unexplored mechanism for the evolution of a variety of other behavioral traits as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peck, J R -- Feldman, M W -- GM 10452/GM/NIGMS NIH HHS/ -- GM 28016/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1672-4.〈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/3381088" target="_blank"〉PubMed〈/a〉
    Keywords: *Altruism ; Animals ; *Biological Evolution ; Female ; Genotype ; Humans ; Male ; Mathematics ; Polymorphism, Genetic ; Recombination, Genetic ; *Sexual Behavior, Animal ; *Sibling Relations
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    Human immunodeficiency virus may encode a novel protein on the genomic DNA plus strand (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-18
    Description: The genome of the human immunodeficiency virus (HIV) is known to contain eight open reading frames (ORFs) on the minus strand of the double-stranded DNA replicative intermediate. Data presented here indicate that the DNA plus strand of HIV contains a previously unidentified ORF in a region complementary to the envelope gene sequence. This ORF could encode a protein of approximately 190 amino acid residues with a relative molecular mass of 20 kilodaltons if translation began from the first initiation codon. The predicted protein is highly hydrophobic and thus could be membrane associated. It is possible, therefore, that the HIV genome encodes a protein on antisense messenger RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, R H -- U41-01685-05/PHS HHS/ -- New York, N.Y. -- Science. 1988 Mar 18;239(4846):1420-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hepatitis Viruses Section, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3347840" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Codon ; DNA, Viral/*genetics ; *Genes, Viral ; HIV/*genetics ; Molecular Sequence Data ; Molecular Weight ; RNA, Messenger/genetics ; Viral Envelope Proteins/genetics ; Viral Proteins/genetics
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    Contributions of quisqualate and NMDA receptors to the induction and expression of LTP (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-23
    Description: The contributions of two subclasses of excitatory amino acid transmitter receptors to the induction and expression of long-term potentiation (LTP) were analyzed in hippocampal slices. The quisqualate/kainate receptor antagonist DNQX (6,7-dinitro-quinoxaline-2,3-dione) blocked 85% of the evoked field potential, leaving a small response that was sensitive to D-AP5 (D-2-amino-5-phosphonopentanoate), an N-methyl-D-aspartate (NMDA) receptor blocker. This residual D-AP5-sensitive response was of comparable size in control and previously potentiated inputs. High-frequency stimulation in the presence of DNQX did not result in the development of robust LTP. Washout of the drug, however, revealed the potentiation effect. Thus NMDA-mediated responses can induce, but are not greatly affected by, LTP; non-NMDA receptors, conversely, mediate responses that are not needed to elicit LTP but that are required for its expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, D -- Joly, M -- Lynch, G -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1694-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for the Neurobiology of Learning and Memory, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2904701" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Amino-5-phosphonovalerate ; Animals ; Electric Conductivity ; Electric Stimulation ; Evoked Potentials/drug effects ; Hippocampus/*physiology ; Magnesium/pharmacology ; Male ; Membrane Potentials/drug effects ; Quinoxalines/pharmacology ; Rats ; Rats, Inbred Strains ; Receptors, AMPA ; Receptors, N-Methyl-D-Aspartate ; Receptors, Neurotransmitter/drug effects/*physiology ; Synapses/*physiology ; Valine/analogs & derivatives/pharmacology
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  • 50
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    Multiple principal sigma factor homologs in eubacteria: identification of the "rpoD box" (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-18
    Description: Genes for the principal sigma factor (rpoD genes) of various eubacteria were identified with a synthetic oligonucleotide probe corresponding to a conserved sequence in rpoD gene products of Escherichia coli and Bacillus subtilis. Multiple rpoD homologs were found in the strains of Micrococcus, Pseudomonas, and Streptomyces, whereas single genes were detected in E. coli, B. subtilis, and Staphylococcus aureus. The four rpoD homologs of Streptomyces coelicolor A3(2) were cloned and sequenced. A homologous portion with 13 amino acids was found in the rpoD genes of S. coelicolor A3(2), E. coli, and B. subtilis and was named the "rpoD box."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, K -- Shiina, T -- Takahashi, H -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1040-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Applied Microbiology, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/*genetics ; DNA Probes ; DNA, Bacterial/genetics ; DNA-Binding Proteins/*genetics ; *Genes, Bacterial ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Sequence Homology, Nucleic Acid ; Sigma Factor/*genetics ; Transcription Factors/*genetics
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    Molecular cloning of a feline leukemia virus that induces fatal immunodeficiency disease in cats (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-19
    Description: A replication-defective variant of feline leukemia virus was molecularly cloned directly from infected tissue and found to induce a rapid and fatal immunodeficiency syndrome in cats. Studies with cloned viruses also showed that subtle mutational changes would convert a minimally pathogenic virus into one that would induce an acute form of immunodeficiency. The data suggest that acutely pathogenic viruses may be selected against by current methods for isolation of the human and simian immunodeficiency viruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Overbaugh, J -- Donahue, P R -- Quackenbush, S L -- Hoover, E A -- Mullins, J I -- CA01058/CA/NCI NIH HHS/ -- CA07966/CA/NCI NIH HHS/ -- CA43216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):906-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Harvard School of Public Health, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2893454" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome ; Amino Acid Sequence ; Animals ; Base Sequence ; Bone Marrow/microbiology ; Cats ; *Cloning, Molecular ; DNA, Viral/genetics ; Humans ; Immunologic Deficiency Syndromes/*etiology/microbiology ; Leukemia Virus, Feline/*genetics/pathogenicity ; Molecular Sequence Data ; Mutation ; Polymorphism, Restriction Fragment Length ; Transfection ; Virus Replication
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    Wound macrophages express TGF-alpha and other growth factors in vivo: analysis by mRNA phenotyping (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-05
    Description: The presence of macrophages is required for the regeneration of many cell types during wound healing. Macrophages have been reported to express a wide range of mitogenic factors and cytokines, but none of these factors has been shown in vivo to sustain all the wound-healing processes. It has been suggested that transforming growth factor-alpha (TGF-alpha) may mediate angiogenesis, epidermal regrowth, and formation of granulation tissue in vivo. Macrophages isolated from a wound site, and not exposed to cell culture conditions, expressed messenger RNA transcripts for TGF-alpha, TGF-beta, platelet-derived growth factor A-chain, and insulin-like growth factor-1. The expression of these transcripts was determined by a novel method for RNA analysis in which low numbers of mouse macrophages were isolated from wound cylinders, their RNA was purified and reverse-transcribed, and the complementary DNA was amplified in a polymerase chain reaction primed with growth factor sequence-specific primers. This single-cell RNA phenotyping procedure is rapid and has the potential for quantification, and mRNA transcripts from a single cell or a few cells can be unambiguously demonstrated, with the simultaneous analysis of several mRNA species. Macrophages from wounds expressed TGF-alpha antigen, and wound fluids contained TGF-alpha. Elicited macrophages in culture also expressed TGF-alpha transcripts and polypeptide in a time-dependent manner after stimulation with modified low-density lipoproteins and lipopolysaccharide endotoxin, which are characteristic of the activators found in injured tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rappolee, D A -- Mark, D -- Banda, M J -- Werb, Z -- AR 32746/AR/NIAMS NIH HHS/ -- GM 27345/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Radiobiology and Environmental Health, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041594" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; DNA/genetics ; Enzyme-Linked Immunosorbent Assay ; Epidermal Growth Factor/biosynthesis/genetics ; Fibroblast Growth Factors/biosynthesis/genetics ; Fibroblasts/metabolism ; Fluorescent Antibody Technique ; Growth Substances/*biosynthesis/genetics ; Insulin-Like Growth Factor I/biosynthesis/genetics ; Macrophages/*metabolism ; Male ; Mice ; Nucleic Acid Hybridization ; *Peptide Biosynthesis ; Peptides/genetics ; Platelet-Derived Growth Factor/biosynthesis/genetics ; Protein Biosynthesis ; RNA, Messenger/*biosynthesis ; Rabbits ; Transcription, Genetic ; Transforming Growth Factors ; *Wound Healing ; Wounds and Injuries/*pathology
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    The elav gene product of Drosophila, required in neurons, has three RNP consensus motifs (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-16
    Description: A sequence of developmental events transforms neurons from their immature state to their mature, terminally differentiated state. The elav locus is one of the first examples of a gene that is expressed in neurons early during this developmental sequence. This gene has been shown to be required for the proper development of young neurons and for the maintenance of mature neurons. DNA sequence data presented in this report suggest that the elav gene product is an RNA binding protein, based on the presence of RNP (ribonucleoprotein) consensus sequences. This leads to the proposal that this protein is involved in the RNA metabolism of neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Robinow, S -- Campos, A R -- Yao, K M -- White, K -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1570-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02254-9110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144044" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/*genetics/physiology ; Drosophila melanogaster/*genetics ; *Genes ; Molecular Sequence Data ; Neurons/*physiology ; RNA-Binding Proteins
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    Ethical issues in the prevention and treatment of HIV infection and AIDS (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-05
    Description: The epidemic of infection with the human immunodeficiency virus (HIV) and the acquired immunodeficiency syndrome (AIDS) poses a major ethical question: How can we control the epidemic and the harm that it causes without unjustly discriminating against particular social groups and without unnecessarily infringing on the freedom of individuals? This question pertains to three spheres of public policy in the United States: public health, the delivery of health care, and research. In the public health sphere, vigorous educational efforts will be required, as will modified approaches to intravenous drug use, prostitution, and homosexual and bisexual sexual activity. Carefully targeted, voluntary testing and screening programs should be coupled with counseling and with guarantees of confidentiality and nondiscrimination where these are appropriate. Both health care workers and the health care system have a moral obligation to provide care to people with HIV infection, but heroic self-sacrifice should not be required provided that infection control precautions are observed. Patients with neurological involvement and terminally ill patients will benefit from statutes allowing recognition of advance directives about preferred modes of care or nontreatment. There is a moral imperative to perform intensive research directed toward the understanding, treatment, and prevention of HIV infection and AIDS. The research process will raise challenging ethical questions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walters, L -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):597-603.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Bioethics, Kennedy Institute of Ethics, Washington, DC 20057.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3340846" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*prevention & control/therapy ; Adult ; Beneficence ; Biomedical Research ; Bisexuality ; Brain Diseases ; Delivery of Health Care ; *Ethics, Medical ; Female ; Government Regulation ; Health Education ; Health Policy ; Homosexuality ; Humans ; Male ; Mandatory Programs ; *Moral Obligations ; Personal Autonomy ; Resource Allocation ; Risk Assessment ; Social Justice ; Substance-Related Disorders ; United States ; *Voluntary Programs
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  • 55
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    Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-26
    Description: Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, J S -- Kretz, K A -- Dewji, N -- Wenger, D A -- Esch, F -- Fluharty, A L -- DK 38795/DK/NIDDK NIH HHS/ -- HD 18983/HD/NICHD NIH HHS/ -- NS 08682/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1098-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma, Hepatocellular/analysis ; Chromosome Mapping ; Chromosomes, Human, Pair 10 ; DNA/genetics/isolation & purification ; Glycoproteins/analysis/*genetics ; Humans ; Liver Neoplasms/analysis ; Male ; Mice ; Mice, Nude ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Precursors/analysis/genetics ; Protein Processing, Post-Translational ; Rats ; Saposins ; Sphingolipid Activator Proteins ; Tissue Distribution
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    Sex survey (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinrich, J D -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):16.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175628" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology ; Bisexuality ; Homosexuality/*statistics & numerical data ; Humans ; Male ; United States
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    Molecular cloning of the zeta chain of the T cell antigen receptor (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: The T cell antigen receptor is a multi-subunit receptor complex present on the surface of all mature and many developing T cells. It consists of clonotypic heterodimers noncovalently linked to five invariant chains that are encoded by four genes and referred to as the CD3 complex. The CD3 gamma, delta, and epsilon chains have been molecularly characterized. In this report the molecular cloning of a complementary DNA encoding the zeta chain of the murine T cell antigen receptor is described. The predicted protein sequence of the zeta chain suggests a structure distinct from those of any of the previously described receptor subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weissman, A M -- Baniyash, M -- Hou, D -- Samelson, L E -- Burgess, W H -- Klausner, R D -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3278377" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Membrane/metabolism ; Chromatography, High Pressure Liquid ; *Cloning, Molecular ; Cyanogen Bromide ; DNA/genetics ; Electrophoresis, Polyacrylamide Gel ; Immunosorbent Techniques ; Macromolecular Substances ; *Membrane Proteins ; Mice ; Molecular Sequence Data ; Molecular Weight ; Nucleic Acid Hybridization ; Peptide Fragments ; Protein Biosynthesis ; RNA, Messenger/genetics ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/analysis ; Transcription, Genetic ; Tumor Cells, Cultured
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    A mutation of the circadian system in golden hamsters (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-02
    Description: A mutation has been found that dramatically shortens the period of the circadian locomotor rhythm of golden hamsters. The pattern of inheritance of this mutation suggests that it occurred at a single, autosomal locus (tau). Wild-type animals have rhythms with free-running periods averaging about 24 hours; animals heterozygous for the mutation have periods of about 22 hours, whereas homozygous animals have rhythms with periods close to 20 hours. Animals that carry the mutant alleles exhibit abnormal entrainment to 24-hour light:dark cycles or are unable to entrain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ralph, M R -- Menaker, M -- HD 13162/HD/NICHD NIH HHS/ -- MH 09483/MH/NIMH NIH HHS/ -- MH 17148/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1225-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Neuroscience, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413487" target="_blank"〉PubMed〈/a〉
    Keywords: *Activity Cycles ; Animals ; *Circadian Rhythm ; Cricetinae/*genetics ; Heterozygote ; Homozygote ; Light ; Male ; Mesocricetus/*genetics/physiology ; Motor Activity/physiology ; Mutation ; Periodicity ; Phenotype
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    Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-22
    Description: A cytoplasmic protein that greatly enhances the guanosine triphosphatase (GTPase) activity of N-ras protein but does not affect the activity of oncogenic ras mutants has been recently described. This protein (GAP) is shown here to be ubiquitous in higher eukaryotes and to interact with H-ras as well as with N-ras proteins. To identify the region of ras p21 with which GAP interacts, 21 H-ras mutant proteins were purified and tested for their ability to undergo stimulation of GTPase activity by GAP. Mutations in nonessential regions of H-ras p21 as well as mutations in its carboxyl-terminal domain (residues 165-185) and purine binding region (residues 117 and 119) did not decrease the ability of the protein to respond to GAP. In addition, an antibody against the carboxyl-terminal domain did not block GAP activity, supporting the conclusion that GAP does not interact with this region. Transforming mutations at positions 12, 59, and 61 (the phosphoryl binding region) abolished GTPase stimulation by GAP. Point mutations in the putative effector region of ras p21 (amino acids 35, 36, and 38) were also insensitive to GAP. However, a point mutation at position 39, shown previously not to impair effector function, did not alter GAP-p21 interaction. These results indicate that GAP interaction may be essential for ras p21 biological activity and that it may be a ras effector protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adari, H -- Lowy, D R -- Willumsen, B M -- Der, C J -- McCormick, F -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):518-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2833817" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; DNA Mutational Analysis ; Enzyme Activation ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; *Genes, ras ; Immunologic Techniques ; In Vitro Techniques ; Phosphoric Monoester Hydrolases/*metabolism ; Proteins/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Structure-Activity Relationship ; ras GTPase-Activating Proteins
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    Suppression of macrophage activation and T-lymphocyte function in hypoprolactinemic mice (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-22
    Description: The effects of prolactin on lactation and reproductive organs are well known. However, the other possible target organs and physiological consequences of altered levels of circulating prolactin remain poorly understood. In this study, mice were treated with bromocryptine, a dopamine receptor agonist that inhibits pituitary prolactin secretion. Bromocryptine treatment prevented T-cell-dependent induction of macrophage tumoricidal activity after the intraperitoneal injection of Listeria monocytogenes or Mycobacterium bovis. Coincident treatment with ovine prolactin reversed this effect. Of the multiple events leading to macrophage activation in vivo, the production by T-lymphocytes of gamma-interferon was the most impaired in bromocryptine-treated mice. Lymphocyte proliferation after stimulation with mitogens in vitro was also depressed in spleens of bromocryptine-treated mice, and coadministration of prolactin also reversed this effect. Bromocryptine treatment also reduced the number of deaths resulting from inoculation of mice with Listeria; exogenous prolactin significantly reversed this effect. The critical influence of pituitary prolactin release on maintenance of lymphocyte function and on lymphokine-dependent macrophage activation suggests that, in mice, lymphocytes are an important target tissue for circulating prolactin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernton, E W -- Meltzer, M S -- Holaday, J W -- New York, N.Y. -- Science. 1988 Jan 22;239(4838):401-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Neurosciences, Walter Reed Army Institute of Research, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122324" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Bromocriptine/pharmacology ; Concanavalin A/pharmacology ; Hypopituitarism/blood/*immunology ; Interferon-gamma/biosynthesis ; Lipopolysaccharides/pharmacology ; Listeriosis/immunology ; Lymphocyte Activation/drug effects ; Lymphokines/physiology ; Macrophage Activation/drug effects ; Macrophage-Activating Factors ; Macrophages/*immunology ; Male ; Mice ; Mice, Inbred C3H ; Mycobacterium bovis ; Prolactin/*blood/pharmacology ; Salmonella ; Spleen/cytology ; T-Lymphocytes/*immunology ; Tuberculosis/immunology
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    Chernobyl claims another victim (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickson, D -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3375827" target="_blank"〉PubMed〈/a〉
    Keywords: *Accidents ; Humans ; Male ; *Nuclear Reactors ; Suicide ; Ukraine
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    Molecular cloning of human and rat complementary DNA encoding androgen receptors (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: Complementary DNAs (cDNAs) encoding androgen receptors were obtained from human testis and rat ventral prostate cDNA libraries. The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors. The human cDNA was transcribed and the RNA product was translated in cell-free systems to yield a 76-kilodalton protein. The protein was immunoprecipitable by human autoimmune antibodies to the androgen receptor. The protein bound androgens specifically and with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, C S -- Kokontis, J -- Liao, S T -- DK-09461/DK/NIDDK NIH HHS/ -- DK-37694/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):324-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353726" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; *Cloning, Molecular ; DNA/genetics ; *Genes ; Humans ; Male ; Molecular Sequence Data ; Molecular Weight ; Rats ; Receptors, Androgen/*genetics/metabolism ; Sequence Homology, Nucleic Acid ; Species Specificity ; Testis/metabolism
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    The protein kinase family: conserved features and deduced phylogeny of the catalytic domains (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-01
    Description: In recent years, members of the protein kinase family have been discovered at an accelerated pace. Most were first described, not through the traditional biochemical approach of protein purification and enzyme assay, but as putative protein kinase amino acid sequences deduced from the nucleotide sequences of molecularly cloned genes or complementary DNAs. Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional characterization of these newly identified family members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanks, S K -- Quinn, A M -- Hunter, T -- GM38793/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):42-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Laboratory, Salk Institute for Biological Studies, San Diego, CA 92138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3291115" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Catalysis ; Humans ; Molecular Sequence Data ; *Phylogeny ; Protein Kinases/*genetics
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    Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: The interaction between receptors and guanine nucleotide binding (G) proteins leads to G protein activation and subsequent regulation of effector enzymes. The molecular basis of receptor-G protein interaction has been examined by using the ability of the G protein from rods (transducin) to cause a conformational change in rhodopsin as an assay. Synthetic peptides corresponding to two regions near the carboxyl terminus of the G protein alpha subunit, Glu311-Val328 and Ile340-Phe350, compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys321 is required for this effect. Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamm, H E -- Deretic, D -- Arendt, A -- Hargrave, P A -- Koenig, B -- Hofmann, K P -- EY06062/EY/NEI NIH HHS/ -- EY06225/EY/NEI NIH HHS/ -- RP05369/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):832-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3136547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antigen-Antibody Complex ; Binding Sites ; GTP-Binding Proteins/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Retinal Pigments/*metabolism ; Rhodopsin/analogs & derivatives/*metabolism ; Transducin
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    Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-09
    Description: Cyclic AMP (cAMP) is an intracellular second messenger that activates transcription of many cellular genes. A palindromic consensus DNA sequence, TGACGTCA, functions as a cAMP-responsive transcriptional enhancer (CRE). The CRE binds a cellular protein of 38 kD in placental JEG-3 cells. A placental lambda gt11 library was screened for expression of specific CRE-binding proteins with the CRE sequence as a radioactive probe. A cDNA encoding a protein of 326 amino acids with the binding properties of a specific CRE-binding protein (CREB) was isolated. The protein contains a COOH-terminal basic region adjacent to a sequence similar to the "leucine zipper" sequence believed to be involved in DNA binding and in protein-protein contacts in several other DNA-associated transcriptional proteins including the products of the c-myc, c-fos, and c-jun oncogenes and GCN4. The CREB protein also contains an NH2-terminal acidic region proposed to be a potential transcriptional activation domain. The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoeffler, J P -- Meyer, T E -- Yun, Y -- Jameson, J L -- Habener, J F -- DK 25532/DK/NIDDK NIH HHS/ -- DK 30457/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Endocrinology, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2974179" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; *Cloning, Molecular ; Cyclic AMP Response Element-Binding Protein ; DNA/*genetics ; DNA-Binding Proteins/*genetics/physiology ; Enhancer Elements, Genetic ; Female ; Humans ; Molecular Sequence Data ; Placenta/*metabolism ; Pregnancy ; Transcription, Genetic
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    Second conserved domain of gp120 is important for HIV infectivity and antibody neutralization (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-26
    Description: Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an antiserum directed against amino acids 254 to 274 of env was efficient in neutralizing three different isolates of HIV in vitro, without affecting the binding of the virus to CD4-positive cells. Therefore, this conserved region of gp120 appears to be critical in a postbinding event during virus penetration and may represent a target for antibody neutralization of HIV. These findings may be applicable in the design of a vaccine for the acquired immunodeficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, D D -- Kaplan, J C -- Rackauskas, I E -- Gurney, M E -- AI25541/AI/NIAID NIH HHS/ -- KO8-AI00685/AI/NIAID NIH HHS/ -- NS21442/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1021-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Infectious Diseases, Cedars-Sinai Medical Center, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830667" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Differentiation, T-Lymphocyte/immunology ; Glucose-6-Phosphate Isomerase ; Growth Substances ; HIV/*immunology/physiology ; HIV Antibodies ; HIV Envelope Protein gp120 ; HIV Seropositivity ; Hemocyanin/immunology ; Humans ; Immune Sera/immunology ; Immunization ; Immunosorbent Techniques ; Lymphokines ; Molecular Sequence Data ; Neutralization Tests ; Receptors, Antigen, T-Cell/immunology ; Retroviridae Proteins/*immunology/physiology ; Sequence Homology, Nucleic Acid ; T-Lymphocytes/immunology/microbiology ; Viral Envelope Proteins/*immunology/physiology
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    Isolation and characterization of a novel protein (X-ORF product) from SIV and HIV-2 (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-08
    Description: A protein designated p14 was purified from a simian immunodeficiency virus (SIVMne) and was shown by amino acid sequence analysis to be nearly identical to the predicted translational product of a unique open reading frame (X-ORF) in the nucleotide sequences of SIVmac and human immunodeficiency virus type 2 (HIV-2). Thus the X-ORF is proven to be a new retroviral gene. The p14 is present in SIVMne in molar amounts equivalent to those of the gag proteins. This is the first example of a retrovirus that contains a substantial quantity of a viral protein that is not a product of the gag, pro, pol, or env genes. SIV p14 and its homolog in HIV-2 may function as nucleic acid binding proteins since purified p14 binds to single-stranded nucleic acids in vitro. Antisera to the purified protein detected p14 in SIVMne, SIVmac, and a homologous protein (16 kilodaltons) in HIV-2 but did not react with HIV-1. Diagnostic procedures based on this novel protein will distinguish between HIV-1 and HIV-2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, L E -- Sowder, R C -- Copeland, T D -- Benveniste, R E -- Oroszlan, S -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bionetics Research, Inc., National Cancer Institute, Frederick, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388031" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments/analysis ; *Retroviridae ; Retroviridae Proteins/*isolation & purification
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    Hormone-sensitive lipase: sequence, expression, and chromosomal localization to 19 cent-q13.3 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin. The 757-amino acid sequence predicted from a cloned rat adipocyte complementary DNA showed no homology with any other known lipase or protein. The activity-controlling phosphorylation site was localized to Ser563 in a markedly hydrophilic domain, and a lipid-binding consensus site was tentatively identified. One or several messenger RNA species (3.3, 3.5, or 3.9 kilobases) were expressed in adipose and steroidogenic tissues and heart and skeletal muscle. The human hormone-sensitive lipase gene mapped to chromosome 19 cent-q13.3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holm, C -- Kirchgessner, T G -- Svenson, K L -- Fredrikson, G -- Nilsson, S -- Miller, C G -- Shively, J E -- Heinzmann, C -- Sparkes, R S -- Mohandas, T -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1503-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical and Physiological Chemistry, University of Lund, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420405" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/genetics ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Rats ; Sterol Esterase/*genetics
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    A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60 (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-26
    Description: A 50-nucleotide untranslated region is shown to be present within the coding sequence of Escherichia coli bacteriophage T4 gene 60, which encodes one of the subunits for its type II DNA topoisomerase. This interruption is part of the transcribed messenger RNA and appears not to be removed before translation. Thus, the usual colinearity between messenger RNA and the encoded protein sequence apparently does not exist in this case. The interruption is bracketed by a direct repeat of five base pairs. A mechanism is proposed in which folding of the untranslated region brings together codons separated by the interruption so that the elongating ribosome may skip the 50 nucleotides during translation. The alternative possibility, that the protein is efficiently translated from a very minor and undetectable form of processed messenger RNA, seems unlikely, but has not been completely ruled out.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, W M -- Ao, S Z -- Casjens, S -- Orlandi, R -- Zeikus, R -- Weiss, R -- Winge, D -- Fang, M -- GM 21960/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1005-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular, Viral and Molecular Biology, University of Utah Medical Center, Salt Lake City 84132.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2830666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon ; DNA/genetics ; DNA Topoisomerases, Type I/*genetics ; DNA, Recombinant ; *Genes, Viral ; Molecular Sequence Data ; Nucleic Acid Conformation ; Plasmids ; Protein Biosynthesis ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; T-Phages/enzymology/*genetics ; Transcription, Genetic
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    Molecular characterization of a functional cDNA encoding the serotonin 1c receptor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-29
    Description: Neurons that release serotonin as a neurotransmitter project to most regions of the central and peripheral nervous system and mediate diverse neural functions. The physiological effects of serotonin are initiated by the activation of multiple, distinct receptor subtypes. Cloning in RNA expression vectors was combined with a sensitive electrophysiological assay in Xenopus oocytes in order to isolate a functional cDNA clone encoding the 5HTlc serotonin receptor. Injection of RNA transcribed in vitro from this clone into Xenopus oocytes elicits serotonin sensitivity. Mouse fibroblasts transformed with this clone bind serotonin agonists and antagonists and exhibit an increase in intracellular Ca2+ concentrations in response to serotonin. The sequence of the 5HTlc receptor reveals that it belongs to the family of G protein-coupled receptors, which are thought to traverse the cytoplasmic membrane seven times. Moreover, in situ hybridization and RNA blot analysis indicate that the 5HTlc receptor is expressed in neurons in many regions of the central nervous system and suggest that this subclass of receptor may mediate many of the central actions of serotonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julius, D -- MacDermott, A B -- Axel, R -- Jessell, T M -- New York, N.Y. -- Science. 1988 Jul 29;241(4865):558-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3399891" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; DNA/genetics ; Fibroblasts/physiology ; Gene Expression Regulation ; Membrane Glycoproteins/genetics ; Molecular Sequence Data ; Oocytes/physiology ; Phosphoproteins/physiology ; Rats ; Receptors, Serotonin/*genetics ; Serotonin/*physiology ; Xenopus laevis
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  • 71
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    A chemoattractant receptor controls development in Dictyostelium discoideum (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-16
    Description: During the early stages of its developmental program, Dictyostelium discoideum expresses cell surface cyclic adenosine monophosphate (cyclic AMP) receptors. It has been suggested that these receptors coordinate the aggregation of individual cells into a multicellular organism and regulate the expression of a large number of developmentally regulated genes. The complementary DNA (cDNA) for the cyclic AMP receptor has now been cloned from lambda gt-11 libraries by screening with specific antiserum. The 2-kilobase messenger RNA (mRNA) that encodes the receptor is undetectable in growing cells, rises to a maximum at 3 to 4 hours of development, and then declines. In vitro transcribed complementary RNA, when hybridized to cellular mRNA, specifically arrests in vitro translation of the receptor polypeptide. When the cDNA is expressed in Dictyostelium cells, the undifferentiated cells specifically bind cyclic AMP. Cell lines transformed with a vector that expresses complementary mRNA (antisense) do not express the cyclic AMP receptor protein. These cells fail to enter the aggregation stage of development during starvation, whereas control and wild-type cells aggregate and complete the developmental program within 24 hours. The phenotype of the antisense transformants suggests that the cyclic AMP receptor is essential for development. The deduced amino acid sequence of the receptor reveals a high percentage of hydrophobic residues grouped in seven domains, similar to the rhodopsins and other receptors believed to interact with G proteins. It shares amino acid sequence identity and is immunologically cross-reactive with bovine rhodopsin. A model is proposed in which the cyclic AMP receptor crosses the bilayer seven times with a serine-rich cytoplasmic carboxyl terminus, the proposed site of ligand-induced receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, P S -- Sun, T J -- Saxe, C L 3rd -- Kimmel, A R -- Johnson, R L -- Devreotes, P N -- GM 34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1467-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Dictyostelium/*growth & development/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; Solubility
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    Sarafotoxin, a novel vasoconstrictor peptide: phosphoinositide hydrolysis in rat heart and brain (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-14
    Description: Sarafotoxins, a group of 21-residue cardiotoxic peptides from snake venom that induce coronary vasoconstriction, show high-affinity binding to rat atrial and brain membranes and activate the hydrolysis of phosphoinositides. Neither their binding nor their activity is affected by blockers or activators of known receptors and ion channels, suggesting that sarafotoxins act either directly on the phosphoinositide phosphodiesterase system or on a novel receptor. Their amino acid sequence shows a high degree of homology with that of endothelin, a recently described 21-residue vasoconstrictor peptide found in porcine aortic endothelium. This is remarkable, since endothelin is a natural compound of the mammalian vascular system while sarafotoxins are highly toxic components of snake venom.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kloog, Y -- Ambar, I -- Sokolovsky, M -- Kochva, E -- Wollberg, Z -- Bdolah, A -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):268-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*metabolism ; Calcium/metabolism ; Cell Membrane/metabolism ; Endothelins ; Enzyme Activation ; Heart Atria/metabolism ; Hydrolysis ; Inositol/metabolism ; Molecular Sequence Data ; Myocardium/*metabolism ; Peptides ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphatidylinositols/*metabolism ; Phosphoric Diester Hydrolases/metabolism ; Rats ; Sequence Homology, Nucleic Acid ; Vasoconstriction ; Viper Venoms/*metabolism
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  • 73
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    Fertilization events induced by neurotransmitters after injection of mRNA in Xenopus eggs (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-22
    Description: Fertilization initiates in the egg a dramatic increase in intracellular calcium that opens ion channels and causes exocytosis. To explore the possibility that these events might involve a receptor-mediated pathway, receptors for serotonin or acetylcholine (M1 muscarinic) were expressed in the Xenopus egg; serotonin or acetylcholine then could initiate a series of responses similar to those normally initiated by sperm. Thus, there may be an endogenous receptor in the egg membrane that is activated by sperm, and the serotonin or M1 muscarinic receptor may replace the sperm receptor in this pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kline, D -- Simoncini, L -- Mandel, G -- Maue, R A -- Kado, R T -- Jaffe, L A -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut Health Center, Farmington 06032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3134693" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cytoplasmic Granules/physiology ; Endocytosis ; Exocytosis ; Female ; *Fertilization ; GTP-Binding Proteins/physiology ; Genetic Engineering ; Inositol Phosphates/physiology ; Male ; Membrane Potentials ; Receptors, Muscarinic/*physiology ; Receptors, Serotonin/*physiology ; Sperm-Ovum Interactions ; Xenopus laevis
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    A ligase-mediated gene detection technique (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-26
    Description: An assay for the presence of given DNA sequences has been developed, based on the ability of two oligonucleotides to anneal immediately adjacent to each other on a complementary target DNA molecule. The two oligonucleotides are then joined covalently by the action of a DNA ligase, provided that the nucleotides at the junction are correctly base-paired. Thus single nucleotide substitutions can be distinguished. This strategy permits the rapid and standardized identification of single-copy gene sequences in genomic DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landegren, U -- Kaiser, R -- Sanders, J -- Hood, L -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1077-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413476" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; DNA/*analysis/genetics/metabolism ; DNA Ligases/*metabolism ; DNA, Recombinant/metabolism ; Fluorescent Dyes ; Globins/genetics ; Humans ; Molecular Sequence Data ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Polymorphism, Genetic ; Polynucleotide Ligases/*metabolism
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    Generation of cDNA probes directed by amino acid sequence: cloning of urate oxidase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-03-11
    Description: Urate oxidase (E.C. 1.7.3.3) catalyzes the oxidation of uric acid to allantoin in most mammals except humans and certain primates. The amino-terminal amino acid sequence for porcine urate oxidase was determined and used in a novel procedure for generating complementary DNA (cDNA) probes to this amino acid sequence. The procedure is based on the polymerase chain reaction and utilizes mixed oligonucleotide primers complementary to the reverse translation products of an amino acid sequence. This rapid and simple cDNA cloning procedure is generally applicable and requires only a partial amino acid sequence. A cDNA probe developed by this procedure was used to isolate a full-length porcine urate oxidase cDNA and to demonstrate the presence of homologous genomic sequences in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, C C -- Wu, X W -- Gibbs, R A -- Cook, R G -- Muzny, D M -- Caskey, C T -- DK31428/DK/NIDDK NIH HHS/ -- GM34428/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344434" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Cloning, Molecular ; DNA/*genetics ; Gene Amplification ; Liver/enzymology ; Mice ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Swine ; Urate Oxidase/*genetics
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    The primary structure and heterogeneity of tau protein from mouse brain (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-15
    Description: Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, G -- Cowan, N -- Kirschner, M -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; Codon ; DNA/genetics ; DNA, Recombinant ; Mice ; Microtubule-Associated Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/genetics ; Protein Conformation ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; tau Proteins
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    A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-01
    Description: A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contains a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levin, L R -- Kuret, J -- Johnson, K E -- Powers, S -- Cameron, S -- Michaeli, T -- Wigler, M -- Zoller, M J -- GM33986/GM/NIGMS NIH HHS/ -- R35 CA39829-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):68-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalysis ; Cyclic AMP/*pharmacology ; Genes, Fungal ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Structure-Activity Relationship ; Threonine
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    A previously undetected MHC gene with an unusual periodic structure (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-08
    Description: The major histocompatibility complex is a chromosomal segment embodying several gene clusters among which those with immune functions are the best characterized. This region is suspected to host other as yet undetected genes whose characterization may shed light on the population genetics and evolution of the whole gene complex and thus on its unexplained character of marker locus for a number of diseases of nonimmune or unknown pathogenesis. A novel gene was identified that is transcribed in all tissues tested and is located in mouse and man between the CA and Bf genes of the H-2 and HLA complexes, respectively. From the nucleotide sequence, derived from liver complementary DNA clones, it is predicted that this novel single-copy gene encodes a 42-kilodalton polypeptide that bears no recognizable relation to the protein families known so far, but it displays striking hallmarks of natural selection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levi-Strauss, M -- Carroll, M C -- Steinmetz, M -- Meo, T -- New York, N.Y. -- Science. 1988 Apr 8;240(4849):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INSERM U 276, Institut Pasteur, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353717" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cloning, Molecular ; Genes ; Liver/physiology ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Periodicity ; Selection, Genetic
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    Subtleties of mating competition (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):668.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187517" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Female ; Male ; Primates/*physiology ; Sexual Behavior, Animal/*physiology ; Spermatozoa/physiology ; Testis/anatomy & histology
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    Hotshots, hotspots, and female preference (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1277-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3375815" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds/physiology ; Female ; Male ; *Sex Characteristics ; *Sexual Behavior, Animal
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    Why is the world full of large females? (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-05-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1988 May 13;240(4854):884.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3363371" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Constitution ; Body Height ; Body Weight ; Female ; *Fertility ; Male ; Models, Biological ; *Sex Characteristics
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    Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: The microtubule-associated protein MAP2 is a prominent large-sized component of purified brain microtubules that, like the 36- to 38-kilodalton tau proteins, bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease. The complete sequence of mouse brain MAP2 was determined from a series of overlapping cloned complementary DNAs. The sequence of the carboxyl-terminal 185 amino acids is very similar (67 percent) to a corresponding region of tau protein, and includes a series of three imperfect repeats, each 18 amino acids long and separated by 13 or 14 amino acids. A subcloned fragment spanning the first two of the 18-amino acid repeats was expressed as a polypeptide by translation in vitro. This polypeptide copurified with microtubules through two successive cycles of polymerization and depolymerization, whereas a control polypeptide derived from the amino-terminal region of MAP2 completely failed to copurify. These data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2. The occurrence of these repeats in tau protein suggests that these may be a general feature of microtubule binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewis, S A -- Wang, D H -- Cowan, N J -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):936-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3142041" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; DNA/genetics ; Mice ; Microtubule-Associated Proteins/genetics/*metabolism ; Microtubules/*metabolism ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins ; Protein Biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sequence Homology, Nucleic Acid ; Tubulin/metabolism ; tau Proteins
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  • 83
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    Synthetic CD4 peptide derivatives that inhibit HIV infection and cytopathicity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-05
    Description: Synthetic peptide segments of the CD4 molecule were tested for their ability to inhibit infection of CD4+ cells by the human immunodeficiency virus (HIV) and to inhibit HIV-induced cell fusion. A peptide mixture composed of CD4(76-94), and synthesis side products, blocked HIV-induced cell fusion at a nominal concentration of 125 micromolar. Upon high-performance liquid chromatography, the antisyncytial activity of the peptide mixture was found not in the fraction containing the peptide CD4(76-94) itself, but in a side fraction containing derivatized peptide products generated in the automated synthesis. Derivatized deletion and substitution peptides in the region CD4(76-94) were used to demonstrate sequence specificity, a requirement for benzyl derivatization, and a core seven-residue fragment required for antisyncytial activity. A partially purified S-benzyl-CD4(83-94) peptide mixture inhibited HIV-induced cell fusion at a nominal concentration of less than or equal to 32 micromolar. Derivatized CD4 peptides blocked cell fusion induced by several HIV isolates and by the simian immunodeficiency virus, SIV, and blocked infection in vitro by four HIV-1 isolates with widely variant envelope gene sequences. Purified CD4(83-94) dibenzylated at cysteine 86 and glutamate 87 possessed antisyncytial activity at 125 micromolar. Derivatization may specifically alter the conformation of CD4 holoreceptor peptide fragments, increasing their antiviral efficacy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lifson, J D -- Hwang, K M -- Nara, P L -- Fraser, B -- Padgett, M -- Dunlop, N M -- Eiden, L E -- AI 62559/AI/NIAID NIH HHS/ -- AI/CA-25922/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):712-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular Immunology, Genelabs Incorporated, Redwood City, CA 94063.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2969619" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antigens, CD4 ; *Antigens, Differentiation, T-Lymphocyte/isolation & purification/pharmacology ; Antiviral Agents ; Cell Fusion ; Chromatography, High Pressure Liquid ; HIV/drug effects/*physiology ; Lymphocyte Culture Test, Mixed ; Mass Spectrometry ; Molecular Sequence Data ; Peptide Fragments/isolation & purification/*pharmacology ; T-Lymphocytes/immunology/*microbiology
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  • 84
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    Type-restricted neutralization of molecular clones of human immunodeficiency virus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-15
    Description: In a study of the immunologic significance of the genetic diversity present within single isolates of human immunodeficiency virus type 1 (HIV-1), the neutralization of viruses derived from molecular clones of the HIV-1 strain HTLV-IIIB by an extensive panel of sera was compared. Sera from HIV-1-infected patients and from goats immunized with polyacrylamide gel-purified HIV-1 envelope glycoprotein (gp120), native gp120, or gp120-derived recombinant peptides, showed marked heterogeneity in neutralizing activity against these closely related viruses. The change of a single amino acid residue in gp120 may account for such "clonal restriction" of neutralizing activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Looney, D J -- Fisher, A G -- Putney, S D -- Rusche, J R -- Redfield, R R -- Burke, D S -- Gallo, R C -- Wong-Staal, F -- New York, N.Y. -- Science. 1988 Jul 15;241(4863):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Viral Diseases, Walter Reed Army Institute of Research, Washington, DC 20307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388046" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Viral/*immunology ; Binding, Competitive ; Cloning, Molecular ; HIV/genetics/*immunology ; HIV Seropositivity/immunology ; Humans ; Molecular Sequence Data ; Neutralization Tests ; Oligopeptides/chemical synthesis/immunology
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  • 85
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    A model-based estimate of the mean incubation period for AIDS in homosexual men (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-03
    Description: Because of the difficulty in identifying the date of exposure to type 1 of the human immunodeficiency virus (HIV-1) infection in persons other than transfusion recipients, studies of the incubation periods for acquired immunodeficiency syndrome (AIDS) have been limited. When data from a cohort of 84 homosexual and bisexual men that provided the information to determine the years of conversion of sera infected with HIV-1 were analyzed, a model for the proportion likely to develop AIDS and the incubation period for AIDS in homosexual men could be derived. The maximum likelihood estimate for the proportion of infected homosexual men developing AIDS is 0.99 (90% confidence interval ranging from 0.38 to 1). Furthermore, the maximum likelihood estimate for the mean incubation period for AIDS in homosexual men is 7.8 years (90% confidence interval ranging from 4.2 years to 15.0 years), which is close to the estimate of 8.2 years for adults developing transfusion-associated AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lui, K J -- Darrow, W W -- Rutherford, G W 3rd -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1333-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Injury Epidemiology and Control, Centers for Disease Control, Atlanta, GA 30333.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3163848" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/etiology/immunology/*physiopathology ; Antibodies, Viral/analysis ; Blood Transfusion ; Enzyme-Linked Immunosorbent Assay ; HIV/physiology ; HIV Antibodies ; HIV Seropositivity ; *Homosexuality ; Humans ; Immunoassay ; Male ; Mathematics ; *Models, Biological ; Time Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 86
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    Cloning of human androgen receptor complementary DNA and localization to the X chromosome (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: The androgen receptor (AR) mediates the actions of male sex steroids. Human AR genomic DNA was cloned from a flow-sorted human X chromosome library by using a consensus nucleotide sequence from the DNA-binding domain of the family of nuclear receptors. The AR gene was localized on the human X chromosome between the centromere and q13. Cloned complementary DNA, selected with an AR-specific oligonucleotide probe, was expressed in monkey kidney (COS) cells and yielded a high-affinity androgen-binding protein with steroid-binding specificity corresponding to that of native AR. A predominant messenger RNA species of 9.6 kilobases was identified in human, rat, and mouse tissues known to contain AR and was undetectable in tissues lacking AR androgen-binding activity, including kidney and liver from androgen-insensitive mice. The deduced amino acid sequence of AR within the DNA-binding domain has highest sequence identity with the progesterone receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lubahn, D B -- Joseph, D R -- Sullivan, P M -- Willard, H F -- French, F S -- Wilson, E M -- HD04466/HD/NICHD NIH HHS/ -- HD16910/HD/NICHD NIH HHS/ -- HD21744/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):327-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of North Carolina, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3353727" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; *Cloning, Molecular ; Codon ; *Genes ; Humans ; Molecular Sequence Data ; Receptors, Androgen/*genetics ; Sequence Homology, Nucleic Acid ; *X Chromosome
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  • 87
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    A single receptor binds both insulin-like growth factor II and mannose-6-phosphate (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-04
    Description: Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II (IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptorCI), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for 125I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacDonald, R G -- Pfeffer, S R -- Coussens, L -- Tepper, M A -- Brocklebank, C M -- Mole, J E -- Anderson, J K -- Chen, E -- Czech, M P -- Ullrich, A -- CA 39240/CA/NCI NIH HHS/ -- DK 30648/DK/NIDDK NIH HHS/ -- DK 34063/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Massachusetts Medical Center, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2964083" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/genetics/*metabolism ; Cell Membrane/analysis/metabolism ; Chromatography, Affinity ; DNA/genetics ; Female ; Hexosephosphates/*metabolism ; Insulin-Like Growth Factor II/*metabolism ; Mannosephosphates/*metabolism ; Molecular Sequence Data ; Placenta/analysis ; Pregnancy ; Rats ; Receptor, IGF Type 2 ; Receptor, Insulin/genetics/*metabolism ; Receptors, Somatomedin ; Sequence Homology, Nucleic Acid ; Somatomedins/*metabolism
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  • 88
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    Apolipoprotein E: cholesterol transport protein with expanding role in cell biology (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-29
    Description: Apolipoprotein E is a plasma protein that serves as a ligand for low density lipoprotein receptors and, through its interaction with these receptors, participates in the transport of cholesterol and other lipids among various cells of the body. A mutant form of apolipoprotein E that is defective in binding to low density lipoprotein receptors is associated with familial type III hyperlipoproteinemia, a genetic disorder characterized by elevated plasma cholesterol levels and accelerated coronary artery disease. Apolipoprotein E is synthesized in various organs, including liver, brain, spleen, and kidney, and is present in high concentrations in interstitial fluid, where it appears to participate in cholesterol redistribution from cells with excess cholesterol to those requiring cholesterol. Apolipo-protein E also appears to be involved in the repair response to tissue injury; for example, markedly increased amounts of apolipoprotein E are found at sites of peripheral nerve injury and regeneration. Other functions of apolipoprotein E, unrelated to lipid transport, are becoming known, including immunoregulation and modulation of cell growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahley, R W -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):622-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoproteins E/genetics/*physiology ; Biological Transport ; Cholesterol/*metabolism ; Gene Expression Regulation ; Humans ; Hyperlipoproteinemia Type III/genetics/metabolism ; Immunity ; Lipid Metabolism ; Molecular Sequence Data ; Polymorphism, Genetic ; Protein Conformation ; Receptors, LDL/metabolism
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  • 89
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    Rapid mutations in mice? (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1985 Dec 20;230(4732):1406-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4071059" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Male ; Mice/*genetics ; Mice, Inbred Strains/genetics ; Mice, Mutant Strains/genetics ; *Mutation ; Species Specificity
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  • 90
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    A new HTLV-III/LAV encoded antigen detected by antibodies from AIDS patients (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-11-15
    Description: A newly identified protein from HTLV-III/LAV, the virus implicated as the etiologic agent of the acquired immune deficiency syndrome, was studied. This protein, which has a molecular weight of 27,000 (p27), was shown by amino acid sequencing to have a coding origin 3' to the env gene on the HTLV-III genome. The presence of antibodies to p27 in virus-exposed individuals indicated that this gene is functional in the natural host.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Lee, T H -- McLane, M F -- Kanki, P J -- Groopman, J E -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA23885/CA/NCI NIH HHS/ -- CA37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):810-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology/microbiology ; Amino Acid Sequence ; Animals ; Antibodies, Viral/*immunology ; Antibody Formation ; Antigens, Viral/*immunology ; Deltaretrovirus/genetics/*immunology ; Electrophoresis, Polyacrylamide Gel ; Haplorhini/microbiology ; Humans ; Male ; Molecular Weight ; Repetitive Sequences, Nucleic Acid
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  • 91
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    Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-31
    Description: Antibodies from the serum of patients with the acquired immune deficiency syndrome (AIDS) or with the AIDS-related complex and from the serum of seropositive healthy homosexuals, recognize two major glycoproteins in cells infected with human T-cell lymphotropic virus type III (HTLV III). These glycoproteins, gp160 and gp120, are encoded by the 2.5-kilobase open reading frame located in the 3' end of the HTLV-III genome, as determined by amino terminus sequence analysis of the radiolabeled forms of these proteins. It is hypothesized that gp160 and gp120 represent the major species of virus-encoded envelope gene products for HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allan, J S -- Coligan, J E -- Barin, F -- McLane, M F -- Sodroski, J G -- Rosen, C A -- Haseltine, W A -- Lee, T H -- Essex, M -- 2T32-CA09031/CA/NCI NIH HHS/ -- CA 13885/CA/NCI NIH HHS/ -- CA 37466/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 May 31;228(4703):1091-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2986290" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*immunology ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antigens, Viral/genetics/*immunology ; Base Sequence ; Deltaretrovirus/*immunology ; Genes, Viral ; Glycoproteins/genetics/immunology ; Humans ; Molecular Weight ; Tunicamycin/pharmacology ; Viral Envelope Proteins/genetics/*immunology
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  • 92
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    Ethanol withdrawal in mice precipitated and exacerbated by hyperbaric exposure (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-08-23
    Description: Mice were fed an ethanol-containing liquid diet for 9 days. On removal of the diet, exposure to 12 atmospheres absolute of a mixture of helium and oxygen precipitated earlier withdrawal, increased withdrawal scores for the first 6 hours, and increased the peak withdrawal intensity compared to dependent animals exposed to control conditions. The enhanced withdrawal did not appear to reflect alterations in ethanol elimination, oxygen or helium partial pressures, body temperature, or general excitability. These results extend to chronically treated animals the evidence that hyperbaric exposure antagonizes the membrane actions of ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alkana, R L -- Finn, D A -- Galleisky, G G -- Syapin, P J -- Malcolm, R D -- R01AA03972/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):772-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4040651" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atmospheric Pressure ; Cell Membrane/drug effects/physiology ; Ethanol/*adverse effects/pharmacology ; Humans ; Male ; Mice ; Substance Withdrawal Syndrome/*physiopathology
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  • 93
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    Neurovisceral and skeletal GM1-gangliosidosis in dogs with beta-galactosidase deficiency (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-08-02
    Description: Beta-galactosidase-deficient siblings in two litters of English springer spaniel puppies showed a progressive neurological impairment, dwarfism, orbital hypertelorism, and dysostosis multiplex. An excess of GM1-ganglioside was found in the brain. Three abnormal oligosaccharides were present in samples of urine, brain, liver, and cartilage. Light microscopy of selected tissue specimens revealed cytoplasmic vacuoles in neurons, circulating blood cells, macrophages, and chondrocytes. Ultrastructural studies demonstrated that these membrane-bound vacuoles were of two types--one containing lamellated membranes and the other, finely granular material. These clinical and pathological findings are similar to those observed in human patients affected by the infantile form of GM1-gangliosidosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alroy, J -- Orgad, U -- Ucci, A A -- Schelling, S H -- Schunk, K L -- Warren, C D -- Raghavan, S S -- Kolodny, E H -- HD 05515/HD/NICHD NIH HHS/ -- HD04147/HD/NICHD NIH HHS/ -- NS 21765/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Aug 2;229(4712):470-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3925555" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Diseases, Metabolic/enzymology/genetics/*veterinary ; Dog Diseases/*enzymology/genetics/pathology ; Dogs ; Female ; G(M1) Ganglioside ; Gangliosidoses/enzymology/genetics/pathology/*veterinary ; Humans ; Lactose Intolerance/genetics/metabolism/*veterinary ; Male ; Neurons/pathology ; Oligosaccharides/metabolism ; Pedigree ; Vacuoles/pathology
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  • 94
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    Induced expression of the glucocorticoid receptor in the rat intermediate pituitary lobe (1985)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1985-07-19
    Description: Synthesis and release of pro-opiomelanocortin-derived peptides are under differential regulation in the anterior and intermediate lobes of the pituitary. Glucocorticoids inhibit synthesis of pro-opiomelanocortin-related peptides in the anterior lobe but not in the intermediate lobe. These two lobes are also characterized by differences in neural innervation and blood flow, both of which may represent routes of access for regulatory factors (the intermediate lobe is avascular). Immunoreactive glucocorticoid receptor, which can be demonstrated in many tissues, is absent from the intermediate lobe. Immunocytochemistry was used to demonstrate the presence of immunoreactive glucocorticoid receptor in the intermediate lobe after pituitary stalk transection, neurointermediate lobe grafts to kidney capsule, or monolayer culture of neurointermediate pituitary cells. This appearance of the glucocorticoid receptor is presumably a consequence of removal of intermediate pituitary cells from neural influences that may be responsible for inhibiting their expression under normal conditions in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Antakly, T -- Sasaki, A -- Liotta, A S -- Palkovits, M -- Krieger, D T -- NSO2893/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):277-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3892690" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Immunoenzyme Techniques ; Immunoglobulin G/immunology ; Male ; Melanocyte-Stimulating Hormones/physiology ; Pituitary Gland/analysis/*metabolism/surgery ; Pituitary Gland, Anterior/analysis/metabolism ; Rabbits/immunology ; Rats ; Rats, Inbred F344 ; Receptors, Glucocorticoid/*biosynthesis/genetics ; Receptors, Steroid/*biosynthesis ; Serotonin/analysis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Circumsporozoite protein of Plasmodium vivax: gene cloning and characterization of the immunodominant epitope (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-15
    Description: The gene encoding the circumsporozoite (CS) protein of the human malaria parasite Plasmodium vivax has been cloned. The deduced sequence of the protein consists of 373 amino acids with a central region of 19 tandem repeats of the nonapeptide Asp-Arg-Ala-Asp/Ala-Gly-Gln-Pro-Ala-Gly. A synthetic 18-amino acid peptide containing two tandem repeats binds to a monoclonal antibody directed to the CS protein of Plasmodium vivax and inhibits the interaction of this antibody with the native protein in sporozoite extracts. The portions of the CS gene that do not contain repeats are closely related to the corresponding regions of the CS genes of two simian malarias, Plasmodium cynomolgi and Plasmodium knowlesi. In contrast, the homology between the CS genes of Plasmodium vivax and Plasmodium falciparum, another malaria parasite of humans, is very limited.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arnot, D E -- Barnwell, J W -- Tam, J P -- Nussenzweig, V -- Nussenzweig, R S -- Enea, V -- New York, N.Y. -- Science. 1985 Nov 15;230(4727):815-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2414847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antigens, Surface/*genetics/immunology ; Cloning, Molecular ; Epitopes/*genetics/immunology ; Haplorhini/parasitology ; Humans ; Malaria/parasitology ; Nucleic Acid Hybridization ; Plasmodium/immunology ; Plasmodium vivax/*genetics/immunology ; *Protozoan Proteins ; Repetitive Sequences, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 96
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    Specific expression of hepatitis B surface antigen (HBsAg) in transgenic mice (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-12-06
    Description: Two transgenic mice were obtained that contain in their chromosomes the complete hepatitis B virus (HBV) genome except for the core gene. These mice secrete particles of HBV surface antigen (HBsAg) in the serum. In one mouse, HBV DNA sequences that had integrated at two different sites were shown to segregate independently in the first filial generation (F1) and only one of the sequences allowed expression of the surface antigen. Among these animals the males produced five to ten times more HBsAg than the females. A 2.1-kilobase messenger RNA species comigrating with the major surface gene messenger RNA is expressed specifically in the liver in the two original mice. The results suggest that the HBV sequences introduced into the mice are able to confer a tissue-specific expression to the S gene. In addition, the HBV transgenic mice represent a new model for the chronic carrier state of hepatitis B virus infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babinet, C -- Farza, H -- Morello, D -- Hadchouel, M -- Pourcel, C -- CA37300-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Dec 6;230(4730):1160-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3865370" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier State ; DNA, Recombinant ; Female ; *Genetic Engineering ; Hepatitis B/genetics ; Hepatitis B Surface Antigens/*genetics ; Humans ; Male ; Mice ; Mice, Inbred C57BL/genetics ; Nucleic Acid Hybridization ; RNA, Messenger/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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  • 97
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    Trans-activator gene of human T-lymphotropic virus type III (HTLV-III) (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-05
    Description: Human T-lymphotropic virus type III (HTLV-III) encodes a trans-acting factor that activates the expression of genes linked to the HTLV-III long terminal repeat. By functional mapping of complementary DNA transcripts of viral messenger RNA's the major functional domain of the gene encoding this factor was localized to a region immediately before the env gene of the virus, a region previously thought to be noncoding. This newly identified gene consists of three exons, and its transcription into messenger RNA involves two splicing events bringing together sequences from the 5' part (287 base pairs), middle (268 base pairs), and 3'part (1258 base pairs) of the HTLV-III genome. A similar messenger RNA with a truncated second exon (70 base pairs) does not encode a trans-acting function. It is proposed that this second messenger RNA is the transcript of a gene (3'-orf) located after the env gene. Messenger RNA's were also identified for the env and gag-pol genes of HTLV-III.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arya, S K -- Guo, C -- Josephs, S F -- Wong-Staal, F -- New York, N.Y. -- Science. 1985 Jul 5;229(4708):69-73.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2990040" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Deltaretrovirus/*genetics ; Gene Expression Regulation ; Genes, Regulator ; *Genes, Viral ; Humans ; RNA Splicing ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Repetitive Sequences, Nucleic Acid ; Transcription Factors/*genetics ; Viral Proteins/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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  • 98
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    Immunogenicity of synthetic peptides from circumsporozoite protein of Plasmodium falciparum (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-24
    Description: In a study of recombinant proteins that might be useful in developing a vaccine against malaria, synthetic peptides from the circumsporozoite (CS) protein of Plasmodium falciparum were found to be immunogenic for mice and rabbits. Antibody to peptides from the repeating region of the CS protein recognized native CS protein and blocked sporozoite invasion of human hepatoma cells in vitro. Antibodies to peptides from regions I and II had no biologic activity, although antibody to region I recognized processed CS protein by Western blot analysis. These data support the feasibility of developing a vaccine against the sporozoite stage of the malaria parasite by using synthetic peptides of the repeating region of the CS protein conjugated to a carrier protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ballou, W R -- Rothbard, J -- Wirtz, R A -- Gordon, D M -- Williams, J S -- Gore, R W -- Schneider, I -- Hollingdale, M R -- Beaudoin, R L -- Maloy, W L -- New York, N.Y. -- Science. 1985 May 24;228(4702):996-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988126" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/immunology ; Antibody Formation ; Antigens, Surface/*immunology ; Carcinoma, Hepatocellular ; Cell Line ; Cross Reactions ; Fluorescent Antibody Technique ; Humans ; Immune Sera/immunology ; Liver Neoplasms ; Malaria/prevention & control ; Mice ; Peptides/chemical synthesis/*immunology ; Plasmodium/immunology ; Plasmodium falciparum/*immunology/physiology ; Precipitin Tests ; *Protozoan Proteins ; Rabbits ; Vaccines/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Neuroendocrine response to estrogen and sexual orientation (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baum, M J -- Carroll, R S -- Erskine, M S -- Tobet, S A -- New York, N.Y. -- Science. 1985 Nov 22;230(4728):960-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2997925" target="_blank"〉PubMed〈/a〉
    Keywords: Estrogens, Conjugated (USP)/*pharmacology ; Female ; *Homosexuality ; Humans ; Luteinizing Hormone/*secretion ; Male
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Reduced numbers of somatostatin receptors in the cerebral cortex in Alzheimer's disease (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-07-19
    Description: Somatostatin receptor concentrations were measured in patients with Alzheimer's disease and controls. In the frontal cortex (Brodmann areas 6, 9, and 10) and temporal cortex (Brodmann area 21), the concentrations of somatostatin in receptors in the patients were reduced to approximately 50 percent of control values. A 40 percent reduction was seen in the hippocampus, while no significant changes were found in the cingulate cortex, postcentral gyrus, temporal pole, and superior temporal gyrus. Scatchard analysis showed a reduction in receptor number rather than a change in affinity. Somatostatin-like immunoreactivity was significantly reduced in both the frontal and temporal cortex. Somatostatin-like immunoreactivity was linearly related to somatostatin-receptor binding in the cortices of Alzheimer's patients. These findings may reflect degeneration of postsynaptic neurons or cortical afferents in the patients' cerebral cortices. Alternatively, decreased somatostatin-like immunoreactivity in Alzheimer's disease might indicate increased release of somatostatin and down regulation of postsynaptic receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beal, M F -- Mazurek, M F -- Tran, V T -- Chattha, G -- Bird, E D -- Martin, J B -- 1P50AG05134/AG/NIA NIH HHS/ -- IR23NS19867-1/NS/NINDS NIH HHS/ -- MN/NS31862/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1985 Jul 19;229(4710):289-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2861661" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/*metabolism ; Cerebral Cortex/*analysis ; Chromatography, High Pressure Liquid ; Female ; Frontal Lobe/analysis ; Humans ; Male ; Middle Aged ; Neurons/metabolism/physiology ; Radioimmunoassay ; Receptors, Cell Surface/*analysis ; Receptors, Somatostatin ; Somatostatin/metabolism/physiology ; Temporal Lobe/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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