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  • Humans  (201)
  • INSTRUMENTATION AND PHOTOGRAPHY  (144)
  • SOLAR PHYSICS
  • 2010-2014
  • 1990-1994  (456)
  • 1980-1984
  • 1992  (261)
  • 1990  (195)
Collection
Keywords
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  • 2010-2014
  • 1990-1994  (456)
  • 1980-1984
Year
  • 1
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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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Comparative genomic hybridization for molecular cytogenetic analysis of solid tumors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-30
    Description: Comparative genomic hybridization produces a map of DNA sequence copy number as a function of chromosomal location throughout the entire genome. Differentially labeled test DNA and normal reference DNA are hybridized simultaneously to normal chromosome spreads. The hybridization is detected with two different fluorochromes. Regions of gain or loss of DNA sequences, such as deletions, duplications, or amplifications, are seen as changes in the ratio of the intensities of the two fluorochromes along the target chromosomes. Analysis of tumor cell lines and primary bladder tumors identified 16 different regions of amplification, many in loci not previously known to be amplified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kallioniemi, A -- Kallioniemi, O P -- Sudar, D -- Rutovitz, D -- Gray, J W -- Waldman, F -- Pinkel, D -- CA 44768/CA/NCI NIH HHS/ -- CA 45919/CA/NCI NIH HHS/ -- CA 47537/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359641" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; DNA Probes ; DNA, Neoplasm/*genetics ; Female ; Fluorescein-5-isothiocyanate ; Fluorescent Dyes ; Gene Amplification ; Gene Deletion ; Humans ; In Situ Hybridization, Fluorescence ; Male ; Mutation ; Neoplasms/*genetics ; *Nucleic Acid Hybridization ; Oncogenes ; Polymorphism, Restriction Fragment Length ; Rhodamines ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-07
    Description: The 39- to 43-amino acid amyloid beta protein (beta AP), which is deposited as amyloid in Alzheimer's disease, is encoded as an internal peptide that begins 99 residues from the carboxyl terminus of a 695- to 770-amino acid glycoprotein referred to as the amyloid beta protein precursor (beta APP). To clarify the processing that produces amyloid, carboxyl-terminal derivatives of the beta APP were analyzed. This analysis showed that the beta APP is normally processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives. The two largest derivatives in human brain have the entire beta AP at or near their amino terminus and are likely to be intermediates in the pathway leading to amyloid deposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Estus, S -- Golde, T E -- Kunishita, T -- Blades, D -- Lowery, D -- Eisen, M -- Usiak, M -- Qu, X M -- Tabira, T -- Greenberg, B D -- AG06656/AG/NIA NIH HHS/ -- AG08012/AG/NIA NIH HHS/ -- AG08992/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):726-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738846" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*biosynthesis ; Amyloid beta-Protein Precursor/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/chemistry ; Cerebral Cortex/chemistry ; Glycosylation ; Humans ; Immunoblotting ; Immunosorbent Techniques ; Molecular Weight ; Peptide Fragments/chemistry/isolation & purification/*metabolism ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Novel approaches to the construction of miniaturized analytical instrumentation (1992)
    In:  CASI
    Details
    Publication Date: 2019-06-28
    Description: This paper focuses on the design, construction, preliminary testing, and potential applications of three forms of miniaturized analytical instrumentation. The first is an optical fiber instrument for monitoring pH and other cations in aqueous solutions. The instrument couples chemically selective indicators that were immobilized at porous polymeric films with a hardware package that provides the excitation light source, required optical components, and detection and data processing hardware. The second is a new form of a piezoelectric mass sensor. The sensor was fabricated by the deposition of a thin (5.5 micron) film of piezoelectric aluminum nitride (AIN). The completed deposition process yields a thin film resonator (TFR) that is shaped as a 400 micron square and supports a standing bulk acoustic wave in a longitudinal mode at frequencies of approx. 1 GHz. Various deposition and vapor sorption studies indicate that the mass sensitivity of the TFR's rival those of the most sensitive mass sensors currently available, though offering such performance in a markedly smaller device. The third couples a novel form of liquid chromatography with microlithographic miniaturization techniques. The status of the miniaturization effort, the goal of which is to achieve chip-scale separations, is briefly discussed.
    Keywords: INSTRUMENTATION AND PHOTOGRAPHY
    Type: NASA-CR-191988 , NAS 1.26:191988
    Format: application/pdf
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  • 5
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    Novel approaches to the construction of miniaturized analytical instrumentation (1992)
    In:  Other Sources
    Details
    Publication Date: 2019-08-28
    Description: This paper focuses on the design, construction, preliminary testing, and potential applications of three forms of miniaturized analytical instrumentation. The first is an optical fiber instrument for monitoring pH and other cations in aqueous solutions. The instrument couples chemically selective indicators that were immobilized at porous polymeric films with a hardware package that provides the excitation light source, required optical components, and detection and data processing hardware. The second is a new form of a piezoelectric mass sensor. The sensor was fabricated by the deposition of a thin (5.5 micron) film of piezoelectric aluminum nitride (AIN). The completed deposition process yields a thin film resonator (TFR) that is shaped as a 400 micron square and supports a standing bulk acoustic wave in a longitudinal mode at frequencies of approx. 1 GHz. Various deposition and vapor sorption studies indicate that the mass sensitivity of the TFR's rival those of the most sensitive mass sensors currently available, though offering such performance in a markedly smaller device. The third couples a novel form of liquid chromatography with microlithographic miniaturization techniques. The status of the miniaturization effort, the goal of which is to achieve chip-scale separations, is briefly discussed.
    Keywords: INSTRUMENTATION AND PHOTOGRAPHY
    Type: SAE PAPER 921179 , ; 11 p.|SAE, International Conference on Environmental Systems; Jul 13, 1992 - Jul 16, 1992; Seattle, WA; United States
    Format: text
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  • 6
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    Fiber-coupled high resolution infrared array spectrometer for the Kuiper Airborne Observatory (1990)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: A novel cryogenic grating spectrometer (FCAS) is being designed for observations of volatiles in cometary and planetary atmospheres, and in newly forming planetary systems. The instrument features two-dimensional detector arrays coupled to a high-dispersion echelle by infrared fibers, and will achieve a spectral resolving power of about 40,000. The primary observational platform for this instrument will be the Kuiper Airborne Observatory, but it will also be configured for use at ground-based observatories. Initially, the spectrometer will use a 58 x 62, 1- to 5-micron InSb array. Larger-format IR arrays and arrays of different composition, will later be incorporated as they become available. The instrument will be used in two modes. The first uses a large format IR array in the spectral image plane for the customary one-dimensional spectral-one-dimensional spatial coverage. In the second mode, a massive, coherent bundle of infrared transmitting ZrF4 fibers will be installed after the dispersive element, to reformat the two-dimensional array into an elongated one-dimensional array for wide spectral coverage, allowing multiple lines to be measured in a single integration with high sensitivity. The overall instrument design is discussed, and the system sensitivity is estimated.
    Keywords: INSTRUMENTATION AND PHOTOGRAPHY
    Type: Instrumentation in Astronomy VII; Feb 13, 1990 - Feb 17, 1990; Tucson, AZ; United States
    Format: text
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  • 7
    Electronic Resource
    Electronic Resource
    The evolution of two west African populations (1992)
    Springer
    Journal of molecular evolution 34 (1992), S. 336-344 
    Details
    ISSN: 1432-1432
    Keywords: Humans ; Mitochondrial DNA ; Nuclear polymorphisms ; Heteroplasmy ; Genetic differentiation ; Sickle cell ; Rain forest refuges
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The identification of genetically coherent populations is essential for understanding human evolution. Among the culturally uniform ethnic groups of west Africa, there are two geographically distinct populations with high frequencies of sickle-cell hemoglobin (HbS). Although the HbS mutation in each group is found on distinguishable chromosomes 11, these populations have been assumed to be parts of a single population. Analysis of mitochondrial DNA (mtDNA) in these populations demonstrated that the two populations identified by alternative chromosomes 11 bearing HbS have distinct distributions of mitochondrial genotypes, i.e., they are maternally separate. These studies also showed that, contrary to expectation, the mtDNA of some individuals is heteroplasmic. For nuclear loci, a comparison of the frequency of alternative alleles established that these populations are genetically distinct. Both the mitochondrial and nuclear data indicate that these populations have been separate for approximately 50,000 years. Although HbS in the two populations is usually attributed to recent, independent mutations, the duration of the separation and the observed geographic distribution of the population allow for the possibility of an ancient origin of HbS. Assuming an ancient mutation and considering the known biogeography, we suggest that HbS protected selected populations from malaria in rain forest refuges during the most recent ice age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00160241
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    Paper (German National Licenses)
    Fulltext
  • 8
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    Isotope-edited NMR of cyclosporin A bound to cyclophilin: evidence for a trans 9,10 amide bond (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-07
    Description: The binding of a 13C-labeled cyclosporin A (CsA) analog to cyclophilin (peptidyl prolyl isomerase) was examined by means of isotope-edited nuclear magnetic resonance (NMR) techniques. A trans 9,10 peptide bond was adopted when CsA was bound to cyclophilin, in contrast to the cis 9,10 peptide bond found in the crystalline and solution conformations of CsA. Furthermore, nuclear Overhauser effects (NOEs) were observed between the zeta 3 and epsilon 3 protons of the methylleucine (MeLeu) residue at position 9 of CsA and tryptophan121 (Trp121) and phenylalanine (Phe) protons of cyclophilin, suggesting that the MeLeu9 residue of CsA interacts with cyclophilin. These results illustrate the power of isotope-edited NMR techniques for rapidly providing useful information about the conformations and active site environment of inhibitors bound to their target enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fesik, S W -- Gampe, R T Jr -- Holzman, T F -- Egan, D A -- Edalji, R -- Luly, J R -- Simmer, R -- Helfrich, R -- Kishore, V -- Rich, D H -- New York, N.Y. -- Science. 1990 Dec 7;250(4986):1406-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2255910" target="_blank"〉PubMed〈/a〉
    Keywords: Amides ; Amino Acid Isomerases/chemistry/*metabolism ; Carbon Isotopes ; Carrier Proteins/chemistry/*metabolism ; Cyclosporins/chemistry/*metabolism ; Escherichia coli/genetics ; Humans ; Leucine/analogs & derivatives/chemistry ; Magnetic Resonance Spectroscopy/methods ; Peptidylprolyl Isomerase ; Phenylalanine/chemistry ; Protein Binding ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism ; Tryptophan/chemistry
    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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    RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-22
    Description: The vast repertoire of immunoglobulins and T cell receptors is generated, in part, by V(D)J recombination, a series of genomic rearrangements that occur specifically in developing lymphocytes. The recombination activating gene, RAG-1, which is a gene expressed exclusively in maturing lymphoid cells, was previously isolated. RAG-1 inefficiently induced V(D)J recombinase activity when transfected into fibroblasts, but cotransfection with an adjacent gene, RAG-2, has resulted in at least a 1000-fold increase in the frequency of recombination. The 2.1-kilobase RAG-2 complementary DNA encodes a putative protein of 527 amino acids whose sequence is unrelated to that of RAG-1. Like RAG-1, RAG-2 is conserved between species that carry out V(D)J recombination, and its expression pattern correlates precisely with that of V(D)J recombinase activity. In addition to being located just 8 kilobases apart, these convergently transcribed genes are unusual in that most, if not all, of their coding and 3' untranslated sequences are contained in single exons. RAG-1 and RAG-2 might activate the expression of the V(D)J recombinase but, more likely, they directly participate in the recombination reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oettinger, M A -- Schatz, D G -- Gorka, C -- Baltimore, D -- GM39458/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 22;248(4962):1517-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2360047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Evolution ; Cattle ; Cell Line ; Chickens ; Cricetinae ; DNA/*genetics ; DNA Nucleotidyltransferases/*genetics ; *DNA-Binding Proteins ; Dogs ; Female ; *Gene Rearrangement, B-Lymphocyte ; *Gene Rearrangement, T-Lymphocyte ; *Homeodomain Proteins ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Multigene Family ; Nuclear Proteins ; Nucleic Acid Hybridization ; Opossums ; Proteins/*genetics ; Rabbits ; Recombination, Genetic/*genetics ; Restriction Mapping ; Transfection ; Turtles ; VDJ Recombinases
    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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  • 10
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    Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-11
    Description: Protease nexin-II (PN-II) [amyloid beta-protein precursor (APP)] and the amyloid beta-protein are major constituents of neuritic plaques and cerebrovascular deposits in individuals with Alzheimer's disease and Down syndrome. Both the brain and the circulation have been implicated as sources of these molecules, although they have not been detected in blood. Human platelets have now been found to contain relatively large amounts of PN-II/APP. Platelet PN-II/APP was localized in platelet alpha-granules and was secreted upon platelet activation. Because PN-II/APP is a potent protease inhibitor and possesses growth factor activity, these results implicate PN-II/APP in wound repair. In certain disease states, alterations in platelet release and processing and clearance of PN-II/APP and its derived fragments could lead to pathological accumulation of these proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Nostrand, W E -- Schmaier, A H -- Farrow, J S -- Cunningham, D D -- GM-31609/GM/NIGMS NIH HHS/ -- HL01615/HL/NHLBI NIH HHS/ -- HL35553/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 May 11;248(4956):745-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2110384" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*blood/isolation & purification ; Amyloid beta-Peptides/*blood/isolation & purification ; Amyloid beta-Protein Precursor ; Antibodies, Monoclonal ; Blood Platelets/*chemistry ; Cell Fractionation ; Cytoplasmic Granules/*chemistry ; Epidermal Growth Factor/blood ; Humans ; Immunoblotting ; Plasminogen Inactivators/blood ; Platelet Activation ; Protein Precursors/*blood/isolation & purification
    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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