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  • Articles  (48)
  • Polymerase Chain Reaction  (48)
  • American Association for the Advancement of Science (AAAS)  (48)
  • American Chemical Society (ACS)
  • American Meteorological Society
  • 1990-1994  (48)
  • 1992  (48)
Collection
  • Articles  (48)
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Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (48)
  • American Chemical Society (ACS)
  • American Meteorological Society
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  • 1990-1994  (48)
Year
Journal
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  • 1
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    Modulation of DNA binding specificity by alternative splicing of the Wilms tumor wt1 gene transcript (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-10
    Description: The technique of whole-genome polymerase chain reaction was used to study the DNA binding properties of the product of the wt1 gene. The zinc finger region of this gene is alternatively spliced such that the major transcript encodes a protein with three extra amino acids between the third and fourth fingers. The minor form of the protein binds specifically to DNA. It is now shown that the major form of wt1 messenger RNA encodes a protein that binds to DNA with a specificity that differs from that of the minor form. Therefore, alternative splicing within the DNA binding domain of a transcription factor can generate proteins with distinct DNA binding specificities and probably different physiological targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bickmore, W A -- Oghene, K -- Little, M H -- Seawright, A -- van Heyningen, V -- Hastie, N D -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):235-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Human Genetics Unit, Western General Hospital, Edinburgh, Scotland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1321494" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites/*genetics ; Binding, Competitive ; Chromosomes, Human, Pair 11 ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; *RNA Splicing ; RNA, Messenger/*metabolism ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; WT1 Proteins ; Wilms Tumor/*genetics ; Zinc Fingers/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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  • 2
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    Identification of ras oncogene mutations in the stool of patients with curable colorectal tumors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Colorectal (CR) tumors are usually curable if detected before metastasis. Because genetic alterations are associated with the development of these tumors, mutant genes may be found in the stool of individuals with CR neoplasms. The stools of nine patients whose tumors contained mutations of K-ras were analyzed. In eight of the nine cases, the ras mutations were detectable in DNA purified from the stool. These patients included those with benign and malignant neoplasms from proximal and distal colonic epithelium. Thus, colorectal tumors can be detected by a noninvasive method based on the molecular pathogenesis of the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Tokino, T -- Hamilton, S R -- Kinzler, K W -- Levin, B -- Frost, P -- Vogelstein, B -- CA06973/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566048" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Carcinoma/diagnosis/*genetics/pathology ; Colonic Neoplasms/diagnosis/*genetics/pathology ; DNA, Neoplasm/genetics/*isolation & purification ; Feces/chemistry ; Female ; *Genes, ras ; Humans ; Male ; Middle Aged ; Molecular Sequence Data ; *Mutation ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Prognosis ; Rectal Neoplasms/diagnosis/*genetics/pathology
    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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    Carnivorous plants: phylogeny and structural evolution (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-11
    Description: The carnivorous habit in flowering plants represents a grade of structural organization. Different morphological features associated with the attraction, trapping, and digestion of prey characterize a diversity of specialized forms, including the familiar pitcher and flypaper traps. Phylogenetic analysis of nucleotide sequence data from the plastic rbcL gene indicates that both carnivory and stereotyped trap forms have arisen independently in different lineages of angiosperms. Furthermore, these results demonstrate that flypaper traps share close common ancestry with all other trap forms. Recognition of these patterns of diversification may provide ideal, naturally occurring systems for studies of developmental processes underlying macromorphological evolution in angiosperms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albert, V A -- Williams, S E -- Chase, M W -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1491-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523408" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Biological Evolution ; Molecular Sequence Data ; *Phylogeny ; *Plant Physiological Phenomena ; Plants/*classification/genetics ; Polymerase Chain Reaction ; Restriction Mapping
    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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  • 4
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    Selective transmission of human immunodeficiency virus type-1 variants from mothers to infants (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-28
    Description: Multiple human immunodeficiency virus type-1 sequences from the V3 and V4-V5 regions of the envelope gene were analyzed from three mother-infant pairs. The infants' viral sequences were less diverse than those of their mothers. In two pairs, a proviral form infrequently found in the mother predominated in her infant. A conserved N-linked glycosylation site within the V3 region, present in each mother's sequence set, was absent in all of the infants' sequence sets. These findings demonstrate that a minor subset of maternal virus is transmitted to the infant.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolinsky, S M -- Wike, C M -- Korber, B T -- Hutto, C -- Parks, W P -- Rosenblum, L L -- Kunstman, K J -- Furtado, M R -- Munoz, J L -- AI-32535/AI/NIAID NIH HHS/ -- HD26619-01/HD/NICHD NIH HHS/ -- P01-25569/PHS HHS/ -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Northwestern University Medical School, Chicago, IL 60611.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546316" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/congenital/microbiology/*transmission ; Amino Acid Sequence ; Base Sequence ; Female ; Genotype ; Glycosylation ; HIV Antigens/genetics ; HIV Envelope Protein gp120/genetics/immunology ; HIV-1/*genetics/immunology ; Humans ; Infant ; Maternal-Fetal Exchange ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; Pregnancy ; Selection, Genetic ; Sequence Alignment
    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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  • 5
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    Body-wall muscle formation in Caenorhabditis elegans embryos that lack the MyoD homolog hlh-1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: The myoD family of DNA binding proteins has been implicated in the control of myogenesis in a variety of organisms. Searches for homologs in the nematode Caenorhabditis elegans yielded only one gene, designated hlh-1, expressed in body-wall muscle cells and their precursors. To assess the role of hlh-1 in C. elegans myogenesis, genetic deficiencies spanning the hlh-1 locus were isolated after gamma irradiation. Embryos homozygous for these deficiencies exhibited extensive body-wall muscle differentiation, including expression of several characteristic myofilament proteins and weak contracile behavior. Thus, zygotic hlh-1 expression was not required for body-wall muscle precursors to adopt muscle cell fates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, L -- Krause, M -- Draper, B -- Weintraub, H -- Fire, A -- R01 GM037706/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):240-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314423" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis/embryology/genetics/*physiology ; Cell Differentiation ; *Chromosome Deletion ; Chromosome Mapping ; Crosses, Genetic ; DNA/genetics/isolation & purification ; DNA-Binding Proteins/*genetics ; Embryo, Nonmammalian/cytology/physiology/radiation effects ; Gamma Rays ; Homozygote ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/*genetics ; Muscles/*embryology/physiology/radiation effects ; MyoD Protein ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
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  • 6
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    Selection of a ribozyme that functions as a superior template in a self-copying reaction (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: The sunY ribozyme is derived from a self-splicing RNA group I intron. This ribozyme was chosen as a starting point for the design of a self-replicating RNA because of its small size. As a means of facilitating the self-replication process, the size of this ribozyme was decreased by the deletion of nonconserved structural domains; however, when such deletions were made, there were severe losses of enzymatic activity. In vitro genetic selection was used to identify mutations that reactivate a virtually inactive sunY deletion mutant. A selected mutant with five substitution mutations scattered throughout the primary sequence showed greater catalytic activity than the original ribozyme under the selection conditions. The sunY ribozyme and its small selected variant can both catalyze template-directed oligonucleotide assembly. The small size and reduced secondary structure of the selected variant results in an enhancement, relative to that of the original ribozyme, of its rate of self-copying. This engineered ribozyme is able to function effectively both as a catalyst and as a template in self-copying reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, R -- Szostak, J W -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1910-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470913" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T4/*genetics ; Base Sequence ; Escherichia coli/*genetics ; Exons ; Introns ; Models, Structural ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligodeoxyribonucleotides ; Oligoribonucleotides ; Polymerase Chain Reaction ; RNA, Catalytic/*biosynthesis/chemistry/genetics ; Sequence Deletion ; Templates, Genetic
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  • 7
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    A human gene responsible for Zellweger syndrome that affects peroxisome assembly (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-28
    Description: The primary defect arising from Zellweger syndrome appears to be linked to impaired assembly of peroxisomes. A human complementary DNA has been cloned that complements the disease's symptoms (including defective peroxisome assembly) in fibroblasts from a patient with Zellweger syndrome. The cause of the syndrome in this patient was a point mutation that resulted in the premature termination of peroxisome assembly factor-1. The homozygous patient apparently inherited the mutation from her parents, each of whom was heterozygous for that mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimozawa, N -- Tsukamoto, T -- Suzuki, Y -- Orii, T -- Shirayoshi, Y -- Mori, T -- Fujiki, Y -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Gifu University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; DNA Mutational Analysis ; Genes ; Genetic Complementation Test ; Humans ; Membrane Proteins/*genetics ; Microbodies/*ultrastructure ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Pedigree ; Polymerase Chain Reaction ; Transfection ; Zellweger Syndrome/*genetics
    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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    Science innovation '92: the San Francisco sequel (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selvin, P -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):885-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502555" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*genetics/isolation & purification ; DNA Fingerprinting ; Genetic Techniques ; *Human Genome Project ; Humans ; Oligodeoxyribonucleotides/isolation & purification ; Polymerase Chain Reaction
    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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  • 9
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    MacroH2A, a core histone containing a large nonhistone region (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-04
    Description: A histone, macroH2A, nearly three times the size of conventional H2A histone, was found in rat liver nucleosomes. Its N-terminal third is 64 percent identical to a full-length mouse H2A. However, it also contains a large nonhistone region. This region has a segment that resembles a leucine zipper, a structure known to be involved in dimerization of some transcription factors. Nucleosomes containing macroH2A may have novel functions, possibly involving interactions with other nuclear proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pehrson, J R -- Fried, V A -- CA 06927/CA/NCI NIH HHS/ -- GM 24019/GM/NIGMS NIH HHS/ -- RR 05539/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1398-400.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fox Chase Cancer Center, Institute for Cancer Research, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529340" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/chemistry ; Histones/*chemistry/genetics ; Leucine Zippers ; Liver/*ultrastructure ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Nucleosomes/*chemistry ; Polymerase Chain Reaction ; Rats ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
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  • 10
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    GAP domains responsible for ras p21-dependent inhibition of muscarinic atrial K+ channel currents (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: The interaction between the low molecular weight G protein ras p21 and a guanosine triphosphatase activating protein (GAP) uncouples a heterotrimeric G protein (Gk) from muscarinic receptors. Through the use of isolated atrial cell membranes and genetically engineered GAP deletion mutants, the src homology regions (SH2-SH3) at the amino terminus of GAP have been identified as the domains responsible for this effect. Deletion of the domain required to stimulate the guanosine triphosphatase activity of ras p21 relieves the requirement for ras p21 in this system. A model is presented that suggests that ras p21 induces a conformational change in GAP, which allows the SH2-SH3 regions of GAP to function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, G A -- Yatani, A -- Clark, R -- Conroy, L -- Polakis, P -- Brown, A M -- McCormick, F -- CA51992-01/CA/NCI NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):192-4.〈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/1553544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Baculoviridae ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genetic Engineering ; Genetic Vectors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Guinea Pigs ; Heart/*physiology ; Heart Atria ; Models, Biological ; Polymerase Chain Reaction ; Potassium Channels/drug effects/*physiology ; Proteins/genetics/*physiology ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Muscarinic/drug effects/*physiology ; ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
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  • 11
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    Lymphoid development in mice congenitally lacking T cell receptor alpha beta-expressing cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: Vertebrate T cells express either an alpha beta or gamma delta T cell receptor (TCR). The developmental relatedness of the two cell types is unresolved. alpha beta + T cells respond to specific pathogens by collaborating with immunoglobulin-producing B cells in distinct lymphoid organs such as the spleen and Peyer's patches. The precise influence of alpha beta + T cells on B cell development is poorly understood. To investigate the developmental effects of alpha beta + T cells on B cells and gamma delta + T cells, mice homozygous for a disrupted TCR alpha gene were generated. The homozygotes showed elimination of alpha beta + T cells and the loss of thymic medullae. Despite this, gamma delta + T cells developed in normal numbers, and there was an increase in splenic B cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philpott, K L -- Viney, J L -- Kay, G -- Rastan, S -- Gardiner, E M -- Chae, S -- Hayday, A C -- Owen, M J -- GM37759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1448-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund, London, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604321" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/*immunology ; Blastocyst ; Blotting, Southern ; Chimera ; Clone Cells ; DNA/genetics/isolation & purification ; Female ; Lymphoid Tissue/growth & development/*immunology ; Macromolecular Substances ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Mutant Strains ; Peyer's Patches/immunology ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/*genetics ; Spleen/immunology ; T-Lymphocytes/*immunology ; Thymus Gland/immunology
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  • 12
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    How technique is changing science (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, S S -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):344-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/analysis ; Drosophila/genetics ; Fiber Optic Technology ; Microscopy/methods ; Polymerase Chain Reaction ; Radioimmunoassay ; Research/instrumentation ; *Research Design
    Print ISSN: 0036-8075
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  • 13
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    Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
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  • 14
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    High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: The T cell receptor (TCR) zeta chain was attached to the TCR alpha and beta extracellular domains to induce efficient expression of alpha beta heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed alpha beta was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR zeta domains and protease cleavage sites to TCR alpha and beta induces expression of demonstrably functional heterodimers that can be solubilized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, I -- Ottenhoff, T H -- Klausner, R D -- New York, N.Y. -- Science. 1992 May 29;256(5061):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598575" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/immunology ; Disulfides ; Flow Cytometry ; Histocompatibility Antigens/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/genetics/isolation & purification/*metabolism ; Solubility ; Transfection
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  • 15
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    Mutation of the POU-specific domain of Pit-1 and hypopituitarism without pituitary hypoplasia (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: A point mutation in the POU-specific portion of the human gene that encodes the tissue-specific POU-domain transcription factor, Pit-1, results in hypopituitarism, with deficiencies of growth hormone, prolactin, and thyroid-stimulating hormone. In two unrelated Dutch families, a mutation in Pit-1 that altered an alanine in the first putative alpha helix of the POU-specific domain to proline was observed. This mutation generated a protein capable of binding to DNA response elements but unable to effectively activate its known target genes, growth hormone and prolactin. The phenotype of the affected individuals suggests that the mutant Pit-1 protein is competent to initiate other programs of gene activation required for normal proliferation of somatotrope, lactotrope, and thyrotrope cell types. Thus, a mutation in the POU-specific domain of Pit-1 has a selective effect on a subset of Pit-1 target genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfaffle, R W -- DiMattia, G E -- Parks, J S -- Brown, M R -- Wit, J M -- Jansen, M -- Van der Nat, H -- Van den Brande, J L -- Rosenfeld, M G -- Ingraham, H A -- HD24960/HD/NICHD NIH HHS/ -- HD2697/HD/NICHD NIH HHS/ -- NIDDK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, 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/1509263" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Northern ; DNA/chemistry/metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Growth Hormone/deficiency ; Humans ; Hypopituitarism/*genetics/pathology ; Mice ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Pituitary Gland, Anterior/*pathology ; Pituitary Hormones/*deficiency ; Polymerase Chain Reaction ; Prolactin/deficiency ; Rats ; Sequence Homology, Nucleic Acid ; Thyrotropin/deficiency ; Transcription Factor Pit-1 ; Transcription Factors/*genetics/metabolism ; Transfection
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  • 16
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    Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Activation of B lymphocytes by engagement of their immunoglobulin M antigen receptors results in phosphorylation of a number of proteins on tyrosine residues. One such protein is p95vav, the product of the vav proto-oncogene. Tyrosine phosphorylation of p95vav occurred within seconds of immunoglobulin M cross-linking and was independent of other events induced during stimulation of B cells, such as protein kinase C activation, guanosine triphosphate-binding protein signaling, and calcium mobilization. Moreover, engagement of antigen receptors induced the rapid (approximately 5 seconds) and transient (approximately 60 seconds) association of p95vav with a 70-kilodalton tyrosine-phosphorylated protein, Vap-1, an interaction mediated by the Src homology 2 domain of p95vav. These results suggest that the vav proto-oncogene participates in the signaling processes that mediate the antigen-induced activation of B lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bustelo, X R -- Barbacid, M -- New York, N.Y. -- Science. 1992 May 22;256(5060):1196-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375396" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; B-Lymphocytes/immunology/*physiology ; *Cell Cycle Proteins ; Cell Line ; Kinetics ; *Lymphocyte Activation ; Mice ; Phosphorylation ; Phosphotyrosine ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-vav ; *Proto-Oncogenes ; Tyrosine/analogs & derivatives/analysis
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  • 17
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    Lack of protective immunity against reinfection with hepatitis C virus (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: Some individuals infected with hepatitis C virus (HCV) experience multiple episodes of acute hepatitis. It is unclear whether these episodes are due to reinfection with HCV or to reactivation of the original virus infection. Markers of viral replication and host immunity were studied in five chimpanzees sequentially inoculated over a period of 3 years with different HCV strains of proven infectivity. Each rechallenge of a convalescent chimpanzee with the same or a different HCV strain resulted in the reappearance of viremia, which was due to infection with the subsequent challenge virus. The evidence indicates that HCV infection does not elicit protective immunity against reinfection with homologous or heterologous strains, which raises concerns for the development of effective vaccines against HCV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farci, P -- Alter, H J -- Govindarajan, S -- Wong, D C -- Engle, R -- Lesniewski, R R -- Mushahwar, I K -- Desai, S M -- Miller, R H -- Ogata, N -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):135-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hepatitis Viruses Section, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279801" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Aged ; Alanine Transaminase/biosynthesis ; Animals ; Base Sequence ; Hepacivirus/physiology ; Hepatitis Antibodies/biosynthesis ; Hepatitis C/*immunology ; Hepatitis C Antibodies ; Humans ; Immunity, Active ; Longitudinal Studies ; Molecular Sequence Data ; Pan troglodytes ; Polymerase Chain Reaction ; Sequence Homology ; Transcription, Genetic ; Viremia ; Virus Replication
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  • 18
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    Dendritic cells exposed to human immunodeficiency virus type-1 transmit a vigorous cytopathic infection to CD4+ T cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: The paucity of virus-laden CD4+ cells in individuals infected with human immunodeficiency virus type-1 (HIV-1) contrasts with the greatly reduced numbers and function of these lymphocytes. A pathway is described whereby dendritic cells carry HIV-1 to uninfected T cells, amplifying the cytopathic effects of small amounts of virus. After exposure to HIV-1, dendritic cells continue to present superantigens and antigens, forming clusters with T cells that are driven to replicate. Infection of the dendritic cells cannot be detected, but the clustered T cells form syncytia, release virions, and die. Carriage of HIV-1 by dendritic cells may facilitate the lysis and loss of antigen specific CD4+ T cells in acquired immunodeficiency syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cameron, P U -- Freudenthal, P S -- Barker, J M -- Gezelter, S -- Inaba, K -- Steinman, R M -- AI 24775/AI/NIAID NIH HHS/ -- MOI-RR00102/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):383-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cellular Physiology and Immunology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1352913" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/drug therapy/*transmission ; Animals ; Antigen-Presenting Cells/immunology ; CD4-Positive T-Lymphocytes/*immunology/*microbiology ; Cell Separation ; Dendritic Cells/*immunology/*microbiology ; Flow Cytometry ; HIV Core Protein p24/biosynthesis ; HIV Long Terminal Repeat/physiology ; HIV-1/*pathogenicity ; In Vitro Techniques ; Lymphocyte Culture Test, Mixed ; Mice ; Microscopy, Electron ; Polymerase Chain Reaction ; Zidovudine/pharmacology
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  • 19
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    Myoglobin in a cyanobacterium (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-19
    Description: Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune. This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa Paramecium caudatum and Tetrahymena pyriformis. Cyanoglobin is encoded by the glbN gene, which is positioned between nifU and nifH-two genes essential for nitrogen fixation-in the genome of Nostoc. Cyanoglobin was detected in Nostoc cells only when they were starved for nitrogen and incubated microaerobically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potts, M -- Angeloni, S V -- Ebel, R E -- Bassam, D -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1690-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg Va 24061.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1609281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromosome Mapping ; Cloning, Molecular ; Cyanobacteria/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Myoglobin/*genetics ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
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  • 20
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    The B cell antigen receptor complex: association of Ig-alpha and Ig-beta with distinct cytoplasmic effectors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The B cell antigen receptor complex is a hetero-oligomeric structure composed of antigen binding, membrane immunoglobulin, and transducer-transporter substructures. The transducer-transporter substructure is composed of disulfide-linked dimers of immunoglobulin (Ig)-alpha and Ig-beta/gamma subunits that are products of the mb-1(alpha) and B29 (beta/gamma) genes. Although the receptor complex associates with Src family kinases that are activated after receptor ligation, the site of interaction of these and other cytoplasmic effector molecules with receptor subunits is unknown. The cytoplasmic tails of Ig-alpha and Ig-beta chains were found to associate with distinct sets of effector molecules. The Ig-alpha chain cytoplasmic domain bound to the Src family kinases Lyn and Fyn, phosphatidylinositol-3 kinase (PI-3 kinase), and an unidentified 38-kilodalton phosphoprotein; the cytoplasmic tail of Ig-beta bound PI-3 kinase and unidentified 40- and 42-kilodalton phosphoproteins. Binding activity was found to occur within a 26-amino acid sequence of Ig-alpha and Ig-beta that contains a motif [(Asp or Glu)-(any amino acid)7-(Asp or Glu)-Tyr-(any amino acid)3-Leu-(any amino acid)7-Tyr-(any amino acid)2-(Leu or Ile)] previously implicated in signal transduction via other receptors including the Fc epsilon receptor I and the T cell antigen receptor. These findings indicate that the subunits act independently to activate distinct second messenger pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, M R -- Campbell, K S -- Kazlauskas, A -- Johnson, S A -- Hertz, M -- Potter, T A -- Pleiman, C -- Cambier, J C -- AI20519/AI/NIAID NIH HHS/ -- AI21768/AI/NIAID NIH HHS/ -- AR01864/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):123-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439759" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*metabolism ; Antigens, CD79 ; Base Sequence ; Cytoplasm/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Genes, src ; Humans ; Immunoblotting ; Immunoglobulin M/*metabolism ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Kinases/metabolism ; Receptors, Antigen, B-Cell/*metabolism ; Recombinant Fusion Proteins ; Signal Transduction/physiology
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  • 21
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    Protective effects of a live attenuated SIV vaccine with a deletion in the nef gene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: Vaccine protection against the human immunodeficiency virus (HIV) and the related simian immunodeficiency virus (SIV) in animal models is proving to be a difficult task. The difficulty is due in large part to the persistent, unrelenting nature of HIV and SIV infection once infection is initiated. SIV with a constructed deletion in the auxiliary gene nef replicates poorly in rhesus monkeys and appears to be nonpathogenic in this normally susceptible host. Rhesus monkeys vaccinated with live SIV deleted in nef were completely protected against challenge by intravenous inoculation of live, pathogenic SIV. Deletion of nef or of multiple genetic elements from HIV may provide the means for creating a safe, effective, live attenuated vaccine to protect against acquired immunodeficiency syndrome (AIDS).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Daniel, M D -- Kirchhoff, F -- Czajak, S C -- Sehgal, P K -- Desrosiers, R C -- AI25328/AI/NIAID NIH HHS/ -- AI26463/AI/NIAID NIH HHS/ -- AI26507/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1938-41.〈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/1470917" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Viral/analysis/genetics/isolation & purification ; *Genes, nef ; Macaca mulatta ; Molecular Sequence Data ; Polymerase Chain Reaction ; *Sequence Deletion ; Simian Acquired Immunodeficiency Syndrome/*immunology/prevention & control ; Simian Immunodeficiency Virus/*genetics/*immunology/isolation & purification ; Vaccines, Attenuated/*immunology ; Viral Vaccines/*immunology
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  • 22
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    Myotonic dystrophy mutation: an unstable CTG repeat in the 3' untranslated region of the gene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-06
    Description: Myotonic dystrophy (DM) is the most common inherited neuromuscular disease in adults, with a global incidence of 1 in 8000 individuals. DM is an autosomal dominant, multisystemic disorder characterized primarily by myotonia and progressive muscle weakness. Genomic and complementary DNA probes that map to a 10-kilobase Eco RI genomic fragment from human chromosome 19q13.3 have been used to detect a variable length polymorphism in individuals with DM. Increases in the size of the allele in patients with DM are now shown to be due to an increased number of trinucleotide CTG repeats in the 3' untranslated region of a DM candidate gene. An increase in the severity of the disease in successive generations (genetic anticipation) is accompanied by an increase in the number of trinucleotide repeats. Nearly all cases of DM (98 percent or 253 of 258 individuals) displayed expansion of the CTG repeat region. These results suggest that DM is primarily caused by mutations that generate an amplification of a specific CTG repeat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahadevan, M -- Tsilfidis, C -- Sabourin, L -- Shutler, G -- Amemiya, C -- Jansen, G -- Neville, C -- Narang, M -- Barcelo, J -- O'Hoy, K -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1253-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of Ottawa, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546325" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosomes, Human, Pair 19 ; Codon ; DNA/*chemistry ; Deoxyribonuclease EcoRI ; Humans ; Molecular Sequence Data ; *Mutation ; Myotonic Dystrophy/*genetics ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Repetitive Sequences, Nucleic Acid ; Restriction Mapping
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  • 23
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    Widespread dispersion of neuronal clones across functional regions of the cerebral cortex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-24
    Description: The cerebral cortex of the mammalian brain has expanded rapidly during the course of evolution and acquired structurally distinguishable areas devoted to separate functions. In some brain regions, topographic restrictions to cell intermixing occur during embryonic development. As a means of examining experimentally whether such restrictions occur during formation of functional subdivisions in the rat neocortex, clonally related neocortical cells were marked by retroviral-mediated transfer of a histochemical marker gene. Clonal boundaries were determined by infection of the developing brain with a library of genetically distinct viruses and amplification of single viral genomes by the polymerase chain reaction. Many clonally related neurons in the cerebral cortex became widely dispersed across functional areas of the cortex. Specification of cortical areas therefore occurs after neurogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walsh, C -- Cepko, C L -- NS 23021/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):434-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1734520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Brain Mapping ; Cerebral Cortex/*cytology/embryology ; Clone Cells ; Genetic Vectors ; Molecular Sequence Data ; Neurons/*cytology ; Oligonucleotides/chemistry ; Polymerase Chain Reaction ; Rats ; Retroviridae/genetics
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  • 24
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    A single amino acid that determines the sensitivity of progesterone receptors to RU486 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: The progesterone analog RU486, an abortifacient, inhibits the action of progestins in humans but not in chickens or hamsters. Substitution of cysteine at position 575 by glycine in the hormone binding domain (HBD) of the chicken progesterone receptor (cPR) generated a cPR that binds RU486 and whose activity is antagonized by that compound. In fact, all receptors that bind RU486 have a glycine at the corresponding position. The hamster PR, like cPR, has a cysteine. Only glycine--not methionine or leucine--at position 575 allowed binding of RU486 to cPR. Substitution of this glycine by cysteine in the human PR (hPR) abrogated binding of RU486 but not that of an agonist. The corresponding mutation in the human glucocorticoid receptor resulted in a loss of binding of both dexamethasone and RU486. Examination of a series of 11 beta-substituted steroids showed that antagonism is not an intrinsic property of an antihormone, because one hPR antagonist acted as an agonist for a mutated hPR. The positioning of an aromatic 11 beta-substitution in the PR HBD appears to be critical for generating agonistic or antagonistic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benhamou, B -- Garcia, T -- Lerouge, T -- Vergezac, A -- Gofflo, D -- Bigogne, C -- Chambon, P -- Gronemeyer, H -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):206-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department Endocrinologie, Centre de Recherche Roussel-Uclaf, Romainville, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1372753" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; Female ; Humans ; Mifepristone/*pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Progesterone/analogs & derivatives/metabolism ; RNA/genetics/isolation & purification ; Receptors, Mineralocorticoid ; Receptors, Progesterone/*drug effects/genetics/metabolism ; Receptors, Steroid/drug effects/genetics/metabolism ; Recombinant Proteins/drug effects/metabolism ; Restriction Mapping ; Uterus/metabolism
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  • 25
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    The human Y chromosome: a 43-interval map based on naturally occurring deletions (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-10-02
    Description: A deletion map of the human Y chromosome was constructed by testing 96 individuals with partial Y chromosomes for the presence or absence of many DNA loci. The individuals studied included XX males, XY females, and persons in whom chromosome banding had revealed translocated, deleted, isodicentric, or ring Y chromosomes. Most of the 132 Y chromosomal loci mapped were sequence-tagged sites, detected by means of the polymerase chain reaction. These studies resolved the euchromatic region (short arm, centromere, and proximal long arm) of the Y chromosome into 43 ordered intervals, all defined by naturally occurring chromosomal breakpoints and averaging less than 800 kilobases in length. This deletion map should be useful in identifying Y chromosomal genes, in exploring the origin of chromosomal disorders, and in tracing the evolution of the Y chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vollrath, D -- Foote, S -- Hilton, A -- Brown, L G -- Beer-Romero, P -- Bogan, J S -- Page, D C -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):52-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Whitehead Institute, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439769" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosome Mapping ; Electrophoresis, Polyacrylamide Gel ; Female ; *Gene Deletion ; *Genome, Human ; Humans ; Male ; Molecular Sequence Data ; Polymerase Chain Reaction ; Sequence Tagged Sites ; *Y Chromosome
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  • 26
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    Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Max is a basic-helix-loop-helix-leucine zipper protein capable of forming sequence-specific DNA binding complexes with Myc proteins. An alternatively spliced messenger RNA has been identified that encodes a form of Max truncated at the COOH-terminus. This delta Max protein retained the ability to bind to the CACGTG motif in a complex with c-Myc but lacks the nuclear localization signal and the putative regulatory domain of Max. When tested in a myc-ras cotransformation assay in rat embryo fibroblasts, Max suppressed, whereas delta Max enhanced, transformation. Thus, the max gene may encode both a negative and a positive regulator of c-Myc function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makela, T P -- Koskinen, P J -- Vastrik, I -- Alitalo, K -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic/*drug effects/genetics ; DNA/chemistry/metabolism ; DNA-Binding Proteins/genetics/metabolism/*pharmacology ; Fibroblasts ; *Genes, myc ; *Genes, ras ; Humans ; Immunosorbent Techniques ; Molecular Sequence Data ; Polymerase Chain Reaction ; Proto-Oncogene Proteins c-myc/genetics/metabolism ; RNA Splicing ; RNA, Messenger/genetics ; Rats ; Structure-Activity Relationship ; *Transcription Factors ; Transfection
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    On somatic recombination in the central nervous system of transgenic mice (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abeliovich, A -- Gerber, D -- Tanaka, O -- Katsuki, M -- Graybiel, A M -- Tonegawa, S -- NS25529/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):404-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631561" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Southern ; Brain/physiology ; Chromosome Mapping ; DNA/analysis ; Gene Rearrangement, T-Lymphocyte ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Variable Region/genetics ; Mice ; Mice, Transgenic/*genetics ; Molecular Sequence Data ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/genetics ; *Recombination, Genetic ; beta-Galactosidase/biosynthesis
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    Speeding up a chemical game of chance (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amato, I -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):330-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631554" target="_blank"〉PubMed〈/a〉
    Keywords: *Drug Design ; Peptide Chain Elongation, Translational ; Polymerase Chain Reaction
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  • 29
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    A mutation in the POU-homeodomain of Pit-1 responsible for combined pituitary hormone deficiency (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Pit-1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals. Mutations in the gene encoding Pit-1 have been found in two dwarf mouse strains displaying hypoplasia of growth hormone, prolactin, and thyroid-stimulating, hormone-secreting cell types in the anterior pituitary. A point mutation in this gene was identified on one allele in a patient with combined pituitary hormone deficiency. Mutant Pit-1 binds DNA normally but acts as a dominant inhibitor of Pit-1 action in the pituitary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radovick, S -- Nations, M -- Du, Y -- Berg, L A -- Weintraub, B D -- Wondisford, F E -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Rainbow Babies and Childrens Hospital, Cleveland, OH.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509262" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics ; Growth Hormone/deficiency/genetics ; Humans ; Molecular Sequence Data ; *Mutation ; Pituitary Gland, Anterior/metabolism/pathology ; Pituitary Hormones/*deficiency ; Polymerase Chain Reaction ; Prolactin/deficiency/genetics ; Promoter Regions, Genetic ; Thyrotropin/deficiency/genetics ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/*genetics ; Transfection
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  • 30
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    An unstable triplet repeat in a gene related to myotonic muscular dystrophy (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-16
    Description: Synthetic oligonucleotides containing GC-rich triplet sequences were used in a scanning strategy to identify unstable genetic sequences at the myotonic dystrophy (DM) locus. A highly polymorphic GCT repeat was identified and found to be unstable, with an increased number of repeats occurring in DM patients. In the case of severe congenital DM, the paternal triplet allele was inherited unaltered while the maternal, DM-associated allele was unstable. These studies suggest that the mutational mechanism leading to DM is triplet amplification, similar to that occurring in the fragile X syndrome. The triplet repeat sequence is within a gene (to be referred to as myotonin-protein kinase), which has a sequence similar to protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y H -- Pizzuti, A -- Fenwick, R G Jr -- King, J -- Rajnarayan, S -- Dunne, P W -- Dubel, J -- Nasser, G A -- Ashizawa, T -- de Jong, P -- 5-M01-RR00350/RR/NCRR NIH HHS/ -- P30-HG00210/HG/NHGRI NIH HHS/ -- P50HL42267-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1256-8.〈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/1546326" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/chemistry ; Humans ; Molecular Sequence Data ; Mutation ; Myotonic Dystrophy/*genetics ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Polymorphism, Genetic ; *Repetitive Sequences, Nucleic Acid
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    Rejection of the "flying primate" hypothesis by phylogenetic evidence from the epsilon-globin gene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bailey, W J -- Slightom, J L -- Goodman, M -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):86-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1301735" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chiroptera/*genetics ; *Genes ; Genetic Variation ; Globins/*genetics ; Humans ; *Models, Genetic ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; *Phylogeny ; Polymerase Chain Reaction ; Primates/*genetics
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  • 32
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    Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Epidermolytic hyperkeratosis is a hereditary skin disorder characterized by blistering and a marked thickening of the stratum corneum. In one family, affected individuals exhibited a mutation in the highly conserved carboxyl terminal of the rod domain of keratin 1. In two other families, affected individuals had mutations in the highly conserved amino terminal of the rod domain of keratin 10. Structural analysis of these mutations predicts that heterodimer formation would be unaffected, although filament assembly and elongation would be severely compromised. These data imply that an intact keratin intermediate filament network is required for the maintenance of both cellular and tissue integrity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothnagel, J A -- Dominey, A M -- Dempsey, L D -- Longley, M A -- Greenhalgh, D A -- Gagne, T A -- Huber, M -- Frenk, E -- Hohl, D -- Roop, D R -- HD25479/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1128-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380725" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/chemistry ; Humans ; Ichthyosiform Erythroderma, Congenital/*genetics ; Keratins/chemistry/*genetics ; Macromolecular Substances ; Molecular Sequence Data ; *Mutation ; Pedigree ; Polymerase Chain Reaction ; Protein Conformation
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    SV2, a brain synaptic vesicle protein homologous to bacterial transporters (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: Synaptic vesicle protein 2 (SV2) is a membrane glycoprotein specifically localized to secretory vesicles in neurons and endocrine cells. As a first step toward understanding the function of SV2 in neural secretion, a rat brain complementary DNA (cDNA) that encodes SV2 was isolated and characterized. Analyses of this cDNA predict that SV2 contains 12 transmembrane domains. The NH2-terminal half of the protein shows significant amino acid sequence identity to a family of bacterial proteins that transport sugars, citrate, and drugs. Expression of the SV2 cDNA in COS cells yielded a high level of SV2-like immunoreactivity distributed in a reticular and punctate pattern, which suggests localization to intracellular membranes. Its localization to vesicles, predicted membrane topology, and sequence identity to known transporters suggest that SV2 is a synaptic vesicle-specific transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bajjalieh, S M -- Peterson, K -- Shinghal, R -- Scheller, R H -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1271-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519064" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics ; Brain/*metabolism ; Carrier Proteins/genetics ; DNA/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/genetics ; Membrane Glycoproteins/*genetics ; Molecular Sequence Data ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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    Reciprocal regulation of adipogenesis by Myc and C/EBP alpha (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: 3T3-L1 adipoblasts that express large amounts of c-Myc cannot terminally differentiate, raising the possibility that Myc inhibits the expression of genes that promote adipogenesis. The CCAAT/enhancer binding protein (C/EBP alpha) is induced during 3T3-L1 adipogenesis when cells commit to the differentiation pathway. Transfection of 3T3-L1 adipoblasts with the gene that encodes C/EBP alpha caused overt expression of the adipocyte morphology. Expression of Myc prohibited the normal induction of C/EBP alpha and prevented adipogenesis. Enforced expression of C/EBP alpha overcame the Myc-induced block to differentiation. These results provide a molecular basis for the regulation of adipogenesis and implicate Myc and C/EBP alpha as pivotal controlling elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freytag, S O -- Geddes, T J -- CA51748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):379-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Research Program, Henry Ford Hospital, Detroit, MI 48202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566086" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*cytology/metabolism ; Animals ; Base Sequence ; CCAAT-Enhancer-Binding Proteins ; Cell Differentiation ; Cell Division ; Cell Line ; DNA-Binding Proteins/genetics/*physiology ; *Gene Expression Regulation ; Molecular Sequence Data ; Nuclear Proteins/genetics/*physiology ; Plasmids ; Polymerase Chain Reaction ; Proto-Oncogene Proteins c-myc/genetics/*physiology ; RNA, Messenger/analysis ; Rats ; Transfection
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    30-million-year-old DNA boosts an emerging field (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1860-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Fossils ; Insects/*genetics ; Polymerase Chain Reaction
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    The cloning of a family of genes that encode the melanocortin receptors (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-28
    Description: Melanocyte-stimulating hormone (MSH) and adrenocorticotropic hormone (ACTH) regulate pigmentation and adrenal cortical function, respectively. These peptides also have a variety of biological activities in other areas, including the brain, the pituitary, and the immune system. A complete understanding of the biological activities of these hormones requires the isolation and characterization of their corresponding receptors. The murine and human MSH receptors (MSH-Rs) and a human ACTH receptor (ACTH-R) were cloned. These receptors define a subfamily of receptors coupled to guanine nucleotide-binding proteins that may include the cannabinoid receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mountjoy, K G -- Robbins, L S -- Mortrud, M T -- Cone, R D -- R01 DK43859-02/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1325670" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Cortex/metabolism ; Amino Acid Sequence ; Animals ; Blotting, Northern ; Cloning, Molecular ; Dose-Response Relationship, Drug ; GTP-Binding Proteins/metabolism ; Humans ; Melanocyte-Stimulating Hormones/physiology ; Melanocytes/metabolism ; Mice ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA, Messenger/biosynthesis ; Receptors, Corticotropin ; Receptors, Pituitary Hormone/biosynthesis/*genetics ; Sequence Homology, Nucleic Acid
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    A comprehensive genetic linkage map of the human genome. NIH/CEPH Collaborative Mapping Group (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: A genetic linkage map of the human genome was constructed that consists of 1416 loci, including 279 genes and expressed sequences. The loci are represented by 1676 polymorphic systems genotyped with the CEPH reference pedigree resource. A total of 339 microsatellite repeat markers assayed by PCR are contained within the map, and of the 351 markers with heterozygosities of at least 70%, 205 are microsatellites. Seven telomere loci define physical and genetic endpoints for 2q, 4p, 7q, 8p, 14q, 16p, and 16q, and in other cases distal markers on the maps have been localized to terminal cytogenetic bands. Therefore, at least 92% of the autosomal length of the genome and 95% of the X chromosome is estimated to be spanned by the map. Since the maps have relatively high marker density and numerous highly informative loci, they can be used to map disease phenotypes, even for those with limited pedigree resources. The baseline map provides a foundation for achieving continuity of clone-based physical maps and for the development of a truly integrated physical, genetic, and cytogenetic map of the human.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉HD24605/HD/NICHD NIH HHS/ -- HG00373/HG/NHGRI NIH HHS/ -- HG00461/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):67-86.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439770" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Mapping ; *Chromosomes, Human ; DNA, Satellite ; Female ; *Genetic Linkage ; Genetic Markers ; *Genome, Human ; Humans ; Male ; Polymerase Chain Reaction
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    Oxytocin gene expression in rat uterus (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-12
    Description: The neurohypophyseal hormone oxytocin (OT) is the most potent uterotonic agent known and is used to induce labor. Yet, endogenous circulating OT appears not to participate in the induction of labor. As shown here, the finding of OT messenger RNA and peptide in the uterus suggests a solution for this paradox. During gestation, rat uterus OT messenger RNA increased more than 150-fold and, at term, exceeded hypothalamic OT messenger RNA by 70-fold. Thus, during parturition, OT may act primarily as a local mediator and not as a circulating hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lefebvre, D L -- Giaid, A -- Bennett, H -- Lariviere, R -- Zingg, H H -- New York, N.Y. -- Science. 1992 Jun 12;256(5063):1553-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Endocrinology, Royal Victoria Hospital, McGill University, Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression ; Hypothalamus/physiology ; Nucleic Acid Hybridization ; Oxytocin/*genetics ; Polymerase Chain Reaction ; RNA, Messenger/genetics ; Rats ; Uterus/*physiology
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    No trial to come in Florida dentist case (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1992 Feb 14;255(5046):787.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1536000" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*etiology ; HIV/genetics ; Humans ; Insurance, Dental ; *Liability, Legal ; Male ; Polymerase Chain Reaction
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  • 40
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    A truncated erythropoietin receptor that fails to prevent programmed cell death of erythroid cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: A form of the human erythropoietin receptor (EPOR) was identified in which the cytoplasmic region is truncated by alternative splicing. The truncated form of the receptor (EPOR-T) is the most prevalent form of EPOR in early-stage erythroid progenitor cells, but the full-length EPOR (EPOR-F) becomes the most prevalent form in late-stage progenitors. EPOR-T can transduce a mitogenic signal. However, cells transfected with EPOR-T are more prone to programmed cell death than those expressing EPOR-F. EPOR-F may transduce a signal to prevent programmed cell death that is independent of the mitogenic signal, and alternative splicing of the EPOR gene may have an important role in erythropoiesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Y -- Komatsu, N -- Nakauchi, H -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Growth and Differentiation, Tsukuba Life Science Center, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1324524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/chemistry/genetics ; Erythrocyte Aging/*physiology ; Erythroid Precursor Cells/metabolism ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/genetics ; Receptors, Cell Surface/chemistry/genetics/*physiology ; Receptors, Erythropoietin ; Transfection
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    Activation of T cells by a tyrosine kinase activation domain in the cytoplasmic tail of CD3 epsilon (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: The multichain T cell antigen receptor functions by interacting with and activating one or more nonreceptor tyrosine kinases. The cytoplasmic tail of the zeta chain can activate T cells independently of the rest of the receptor complex. The function of the remaining invariant CD3 chains remains unknown. A 22-amino acid region of the cytoplasmic tail of CD3 epsilon was also able to independently activate T cells. Stimulation of T cells by means of the cytoplasmic tails of either zeta or CD3 epsilon resulted in quantitatively distinct patterns of tyrosine phosphorylation, suggesting activation of different biochemical pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letourneur, F -- Klausner, R D -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1532456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/genetics/*metabolism ; Cell Line ; Cell Membrane/immunology/metabolism ; Chimera ; Clone Cells ; Humans ; Interleukin-2/biosynthesis ; Kinetics ; *Lymphocyte Activation ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Antigen, T-Cell/genetics/*metabolism ; Receptors, Interleukin-2/genetics/metabolism ; T-Lymphocytes/enzymology/*immunology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 42
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    Identification of a naturally occurring transforming variant of the p65 subunit of NF-kappa B (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Transcription factor NF-kappa B comprises two proteins, p50 and p65, that have sequence similarity to the v-rel oncogene. In primary hematopoietic cell populations an alternatively spliced form of NF-kappa B p65 mRNA was observed that encoded a protein designated p65 delta. Expression of the p65 delta cDNA in Rat-1 fibroblasts resulted in focus formation, anchorage-independent growth in soft agar, and tumor formation in athymic nude mice, effects not obtained with expression of p65 or a p65 delta mutant that contains a disruption within the transcriptional activation domain. Thus, p65 delta, which associated weakly and interfered with DNA binding by p65, may sequester an essential limiting regulatory factor or factors required for NF-kappa B function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Narayanan, R -- Klement, J F -- Ruben, S M -- Higgins, K A -- Rosen, C A -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, Hoffmann-LaRoche, Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Transformation, Neoplastic/*genetics ; DNA/genetics/metabolism ; Fibroblasts/metabolism ; *Genetic Variation ; Hematopoietic Stem Cells/chemistry ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; NF-kappa B/*genetics ; Neoplasm Transplantation ; Oncogene Proteins v-rel ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/analysis/genetics ; Rats ; Retroviridae Proteins, Oncogenic/genetics ; Transfection
    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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  • 43
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    Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: The functional heterogeneity of potassium channels in eukaryotic cells arises not only from the multiple potassium channel genes and splice variants but also from the combinatorial mixing of different potassium channel polypeptides to form heteromultimeric channels with distinct properties. One structural element that determines the compatibility of different potassium channel polypeptides in subunit assembly has now been localized to the hydrophilic amino-terminal domain. A Drosophila Shaker B (ShB) potassium channel truncated polypeptide that contains only the hydrophilic amino-terminal domain can form a homomultimer; the minimal requirement for the homophilic interaction has been localized to a fragment of 114 amino acids. Substitution of the amino-terminal domain of a distantly related mammalian potassium channel polypeptide (DRK1) with that of ShB permits the chimeric DRK1 polypeptide to coassemble with ShB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, M -- Jan, Y N -- Jan, L Y -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1225-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Francisco 94143-0724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519059" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia ; Baculoviridae ; Biological Transport/drug effects ; Drosophila ; Electrophoresis, Polyacrylamide Gel ; Genes/*genetics ; Models, Biological ; Molecular Sequence Data ; Peptides/*genetics/physiology ; Polymerase Chain Reaction ; Potassium/pharmacokinetics ; Potassium Channels/*chemistry/drug effects/physiology ; Recombinant Fusion Proteins ; Sequence Homology, Nucleic Acid ; Shaker Superfamily of Potassium Channels
    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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  • 44
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    Multiple zinc finger forms resulting from developmentally regulated alternative splicing of a transcription factor gene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-25
    Description: Transcripts encoding the Drosophila putative transcription factor CF2 are subject to developmentally regulated alternative splicing, and they encode protein isoforms that differ in the number of zinc fingers. One testis-specific RNA encodes an isoform that includes three zinc fingers and a frame-shifted segment. Two other transcripts encode isoforms with six and seven zinc fingers which bind to distinct promoters and DNA target sequences. Thus, because of alternative splicing, a single gene appears to encode distinct DNA-binding proteins, each capable of regulating different gene sets in different tissues and developmental periods.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, T -- Gogos, J A -- Kirsh, S A -- Kafatos, F C -- New York, N.Y. -- Science. 1992 Sep 25;257(5078):1946-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411512" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chorion ; DNA-Binding Proteins/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; *Gene Expression Regulation ; Genes ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/genetics ; Sequence Alignment ; Transcription Factors/*genetics ; *Zinc Fingers
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 45
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    Protection of macaques against SIV infection by subunit vaccines of SIV envelope glycoprotein gp160 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-24
    Description: Simian immunodeficiency virus (SIV) is a primate lentivirus related to human immunodeficiency viruses and is an etiologic agent for acquired immunodeficiency syndrome (AIDS)-like diseases in macaques. To date, only inactivated whole virus vaccines have been shown to protect macaques against SIV infection. Protective immunity was elicited by recombinant subunit vaccines. Four Macaca fascicularis were immunized with recombinant vaccinia virus expressing SIVmne gp160 and were boosted with gp160 produced in baculovirus-infected cells. All four animals were protected against an intravenous challenge of the homologous virus at one to nine animal-infectious doses. These results indicate that immunization with viral envelope antigens alone is sufficient to elicit protective immunity against a primate immunodeficiency virus. The combination immunization regimen, similar to one now being evaluated in humans as candidate human immunodeficiency virus (HIV)-1 vaccines, appears to be an effective way to elicit such immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, S L -- Abrams, K -- Barber, G N -- Moran, P -- Zarling, J M -- Langlois, A J -- Kuller, L -- Morton, W R -- Benveniste, R E -- AI26503/AI/NIAID NIH HHS/ -- R01 AI28065/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):456-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, WA 98121.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1531159" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA, Viral/genetics ; Gene Products, env ; Genetic Vectors ; Lymphocyte Activation ; Macaca fascicularis ; Molecular Sequence Data ; Neutralization Tests ; Oligonucleotides/chemistry ; Polymerase Chain Reaction ; Simian Acquired Immunodeficiency Syndrome/immunology/*prevention & control ; Simian Immunodeficiency Virus/*immunology ; T-Lymphocytes, Helper-Inducer/immunology ; Time Factors ; Vaccination ; Vaccines, Synthetic/*immunology ; Viral Vaccines/*immunology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 46
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    A mutant of TTX-resistant cardiac sodium channels with TTX-sensitive properties (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The cardiac sodium channel alpha subunit (RHI) is less sensitive to tetrodotoxin (TTX) and saxitoxin (STX) and more sensitive to cadmium than brain and skeletal muscle (microliter) isoforms. An RHI mutant, with Tyr substituted for Cys at position 374 (as in microliter) confers three properties of TTX-sensitive channels: (i) greater sensitivity to TTX (730-fold); (ii) lower sensitivity to cadmium (28-fold); and (iii) altered additional block by toxin upon repetitive stimulation. Thus, the primary determinant of high-affinity TTX-STX binding is a critical aromatic residue at position 374, and the interaction may take place possibly through an ionized hydrogen bond. This finding requires revision of the sodium channel pore structure that has been previously suggested by homology with the potassium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Satin, J -- Kyle, J W -- Chen, M -- Bell, P -- Cribbs, L L -- Fozzard, H A -- Rogart, R B -- HL-20592/HL/NHLBI NIH HHS/ -- HL-37217/HL/NHLBI NIH HHS/ -- NS 23360/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 22;256(5060):1202-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375397" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/physiology ; Cadmium/pharmacology ; Cell Membrane/physiology ; Cloning, Molecular ; Drug Resistance/genetics ; Genetic Vectors ; Heart/*physiology ; Kinetics ; Molecular Sequence Data ; Muscles/physiology ; *Mutagenesis, Site-Directed ; Oocytes/drug effects/*physiology ; Polymerase Chain Reaction ; Protein Conformation ; RNA/genetics ; Rats ; Restriction Mapping ; Saxitoxin/pharmacology ; Sodium Channels/drug effects/genetics/*physiology ; Tetrodotoxin/*pharmacology ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 47
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    Directed evolution of an RNA enzyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: An in vitro evolution procedure was used to obtain RNA enzymes with a particular catalytic function. A population of 10(13) variants of the Tetrahymena ribozyme, a group I ribozyme that catalyzes sequence-specific cleavage of RNA via a phosphoester transfer mechanism, was generated. This enzyme has a limited ability to cleave DNA under conditions of high temperature or high MgCl2 concentration, or both. A selection constraint was imposed on the population of ribozyme variants such that only those individuals that carried out DNA cleavage under physiologic conditions were amplified to produce "progeny" ribozymes. Mutations were introduced during amplification to maintain heterogeneity in the population. This process was repeated for ten successive generations, resulting in enhanced (100 times) DNA cleavage activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beaudry, A A -- Joyce, G F -- AI30882/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):635-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Catalysis ; DNA, Single-Stranded/metabolism ; Genotype ; Hot Temperature ; Magnesium Chloride/pharmacology ; Molecular Sequence Data ; Mutagenesis ; Mutagenesis, Site-Directed ; Phenotype ; Polymerase Chain Reaction ; RNA, Catalytic/genetics/*metabolism ; Substrate Specificity ; Tetrahymena thermophila/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin receptor and laminin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: A family of highly polymorphic neuronal cell surface proteins, the neurexins, has been identified. At least two genes for neurexins exist. Each gene uses alternative promoters and multiple variably spliced exons to potentially generate more than a 100 different neurexin transcripts. The neurexins were discovered by the identification of one member of the family as the receptor for alpha-latrotoxin. This toxin is a component of the venom from black widow spiders; it binds to presynaptic nerve terminals and triggers massive neurotransmitter release. Neurexins contain single transmembrane regions and extracellular domains with repeated sequences similar to sequences in laminin A, slit, and agrin, proteins that have been implicated in axon guidance and synaptogenesis. An antibody to neurexin I showed highly concentrated immunoreactivity at the synapse. The polymorphic structure of the neurexins, their neural localization, and their sequence similarity to proteins associated with neurogenesis suggest a function as cell recognition molecules in the nerve terminal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ushkaryov, Y A -- Petrenko, A G -- Geppert, M -- Sudhof, T C -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):50-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621094" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/genetics ; Amino Acid Sequence ; Animals ; Antibodies ; Carrier Proteins/genetics ; Cloning, Molecular ; Cyclosporins/metabolism ; DNA/genetics ; Exons ; Laminin/*genetics ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics ; Organ Specificity ; PC12 Cells ; Peptidylprolyl Isomerase ; Polymerase Chain Reaction ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, Cholinergic/*genetics ; *Receptors, Peptide ; Sequence Homology, Nucleic Acid ; Spider Venoms/metabolism ; Synapses/*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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