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  • Articles  (114)
  • Other Sources  (121)
  • GEOPHYSICS  (121)
  • Amino Acid Sequence  (58)
  • Biochemistry and Biotechnology
  • Physics
  • 1995-1999
  • 1990-1994  (235)
  • 1980-1984
  • 1993  (235)
Collection
  • Articles  (114)
  • Other Sources  (121)
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Years
  • 1995-1999
  • 1990-1994  (235)
  • 1980-1984
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  • 1
    Electronic Resource
    Electronic Resource
    Engineering cellulase mixtures by varying the mole fraction of Thermomonospora fusca E5 and E3, Trichoderma reesei CBHI, and Caldocellum saccharolyticum β-glucosidase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 1019-1028 
    Details
    ISSN: 0006-3592
    Keywords: Caldocellum saccharolyticum ; cellulose ; binding ; β-glucosidase ; hydrolysis ; mole fraction ; synergism ; Thermomonospora fusca ; Trichoderma reesei ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In this study, different mole fractions of pure Thermomonospora fusca E5 and E3, plus Trichoderma reesei CBHI were studied for reducing sugar production at 2 h, degree of synergism, and cellulose binding. In addition, the effects of introducing the Caldocellum saccharolyticum β-glucosidase into this cellulase system were investigated. The cellulases used were purified to homogeneity. Avicel PH 102 (4% w/w solution in 0.05 sodium acetate pH 5.5 buffer) was the substrate. Reactions were run at 50°C for 2 h using total cellulase concentrations of 8.3 or 12.2 μM. A bimixture of T. fusca E3 and T. reesei CBHI was very effective in hydrolyzing microcrystalline cellulose (9.1% conversion). The addition of endoglucanase E5 to the mixture only increased conversion to 9.8%. However, when both E5 and β-glucosidase were added, conversion increased to 14%. It was also observed that increasing total cellulase concentration beyond 8.3 μM did little to increase percent conversion of cellulose into glucose. The results of the binding studies indicate no competition for binding sites between the endo- and exocellulases. © 1993 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420902
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    Paper (German National Licenses)
    Fulltext
  • 2
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    The Koshak section: Evidence for element fractionation and an oxidation event at the K/T boundary (1993)
    In:  Other Sources
    Details
    Publication Date: 2019-01-25
    Description: The Koshak site is a new K/T section located about 125 km EEN of the Fort Shevchenko city, Mangyshlak, Kazakhstan. In this paper, we report results of geochemical and mineralogical studies of this section which indicate a deep element fractionation and an oxidation event at the K/T boundary.
    Keywords: GEOPHYSICS
    Type: Lunar and Planetary Inst., Twenty-Fourth Lunar and Planetary Science Conference. Part 3: N-Z; p 1051-1052
    Format: text
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    NASA TECHNICAL REPORTS
  • 3
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    Zonal mean winds in the equatorial mesosphere and lower thermosphere observed by the High Resolution Doppler Imager (1993)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: This paper presents analyses of mesospheric and lower thermospheric zonal mean winds observed by the High Resolution Doppler Imager (HRDI) on the Upper Atmosphere Research Satellite (UARS). Monthly averages of the equatorial zonal mean zonal winds are presented for January 1992 through June 1993. Equatorial zonal winds in the 70-90 km region are dominated by a semiannual oscillation (SAO), ranging from 30 m/s (westerly) to -100 m/s (easterly). At high latitudes the zonal wind variations are predominantly annual. Above 90 km, the low-latitude flow is easterly at all times, punctuated by a small semiannual variation. This behavior may be related to the deposition of momentum by the diurnal tides.
    Keywords: GEOPHYSICS
    Type: Geophysical Research Letters (ISSN 0094-8276); 20; 24; p. 2849-2852
    Format: text
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    NASA TECHNICAL REPORTS
  • 4
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    Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS carbohydrate transport systems by binding to diverse target proteins. The crystal structure at 2.6 A resolution of one of the targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined. GK contains a region that is topologically identical to the adenosine triphosphate binding domains of hexokinase, the 70-kD heat shock cognate, and actin. IIIGlc binds far from the catalytic site of GK, indicating that long-range conformational changes mediate the inhibition of GK by IIIGlc. GK and IIIGlc are bound by hydrophobic and electrostatic interactions, with only one hydrogen bond involving an uncharged group. The phosphorylation site of IIIGlc, His90, is buried in a hydrophobic environment formed by the active site region of IIIGlc and a 3(10) helix of GK, suggesting that phosphorylation prevents IIIGlc binding to GK by directly disrupting protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, J H -- Faber, H R -- Worthylake, D -- Meadow, N D -- Roseman, S -- Pettigrew, D W -- Remington, S J -- 5-R37 GM38759/GM/NIGMS NIH HHS/ -- GM 42618-01A1/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):673-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430315" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Amino Acid Sequence ; Binding Sites ; Escherichia coli/*enzymology ; Escherichia coli Proteins ; Glycerol Kinase/*chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Models, Structural ; Phosphoenolpyruvate Sugar Phosphotransferase System/*chemistry/*metabolism ; *Protein Structure, Secondary
    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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  • 5
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    Genotypic and phenotypic characterization of HIV-1 patients with primary infection (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-08-27
    Description: Better characterization of human immunodeficiency virus-type 1 (HIV-1) in patients with primary infection has important implications for the development of an acquired immunodeficiency syndrome (AIDS) vaccine because vaccine strategies should target viral isolates with the properties of transmitted viruses. In five HIV-1 seroconverters, the viral phenotype was found to be uniformly macrophage-tropic and non-syncytium-inducing. Furthermore, the viruses were genotypically homogeneous within each patient, but a common signature sequence was not discernible among transmitted viruses. In the two cases where the sexual partners were also studied, the sequences of the transmitted viruses matched best with minor variants in the blood of the transmitters. There was also a stronger pressure to conserve sequences in gp120 than in gp41, nef, and p17, suggesting that a selective mechanism is involved in transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, T -- Mo, H -- Wang, N -- Nam, D S -- Cao, Y -- Koup, R A -- Ho, D D -- AI24030/AI/NIAID NIH HHS/ -- AI25541/AI/NIAID NIH HHS/ -- AI27742/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, New York University School of Medicine, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356453" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; Female ; Gene Products, gag/chemistry/genetics ; Genes, Viral ; Genotype ; Giant Cells/physiology ; HIV Antigens/chemistry/genetics ; HIV Envelope Protein gp120/chemistry/*genetics ; HIV Envelope Protein gp41/chemistry/genetics ; HIV Infections/*microbiology/transmission ; HIV Seropositivity/microbiology ; HIV-1/chemistry/*genetics/*physiology ; Humans ; Macrophages ; Male ; Molecular Sequence Data ; Phenotype ; Sequence Alignment ; Sexual Partners ; *Viral Proteins ; Virus Replication ; gag Gene Products, Human Immunodeficiency Virus
    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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  • 6
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    WT1-mediated growth suppression of Wilms tumor cells expressing a WT1 splicing variant (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-24
    Description: A human Wilms tumor cell line (RM1) was developed to test the tumor suppressor activity of WT1, a zinc finger transcription factor that is expressed in the developing human kidney and is mutationally inactivated in a subset of Wilms tumors. Transfection of each of four wild-type WT1 isoforms suppressed the growth of RM1 cells. The endogenous WT1 transcript in these cells was devoid of exon 2 sequences, a splicing alteration that was also detected in varying amounts in all Wilms tumors tested but not in normal kidney. Production of this abnormal transcript, which encodes a functionally altered protein, may represent a distinct mechanism for inactivating WT1 in Wilms tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haber, D A -- Park, S -- Maheswaran, S -- Englert, C -- Re, G G -- Hazen-Martin, D J -- Sens, D A -- Garvin, A J -- CA37887/CA/NCI NIH HHS/ -- CA58596/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 24;262(5142):2057-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Massachusetts General Hospital Cancer Center, Boston 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266105" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division/genetics ; DNA-Binding Proteins/biosynthesis/*genetics/physiology ; Genes, Wilms Tumor/genetics/*physiology ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Neoplasm Transplantation ; RNA, Messenger/genetics ; Tumor Cells, Cultured ; WT1 Proteins ; Wilms Tumor/*genetics/*pathology
    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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  • 7
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    The crystal structure of lysin, a fertilization protein (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-17
    Description: Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, A -- McRee, D E -- Vacquier, V D -- Stout, C D -- HD12986/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 17;262(5141):1864-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037-1093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8266073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Computer Graphics ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Mollusca ; Mucoproteins/*chemistry/metabolism ; Protein Structure, Secondary ; Vitelline Membrane/metabolism
    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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  • 8
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    Crystal structure of a synthetic triple-stranded alpha-helical bundle (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: The x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple-stranded coiled coil formed by three alpha-helices. Unlike the designed parallel coiled coil, the helices run up-up-down. The structure is stabilized by a distinctive hydrophobic interface consisting of eight layers. As in the design, each alpha-helix in the coiled coil contributes one leucine side chain to each layer. The structure suggests that hydrophobic interactions are a dominant factor in the stabilization of coiled coils. The stoichiometry and geometry of coiled coils are primarily determined by side chain packing in the solvent-inaccessible interior, but electrostatic interactions also contribute.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lovejoy, B -- Choe, S -- Cascio, D -- McRorie, D K -- DeGrado, W F -- Eisenberg, D -- 31299/PHS HHS/ -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1288-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024-1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8446897" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography ; *DNA-Binding Proteins ; Fungal Proteins/chemistry/ultrastructure ; Hydrogen Bonding ; Leucine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Protein Kinases/chemistry/ultrastructure ; *Protein Structure, Secondary ; *Saccharomyces cerevisiae Proteins ; Tropomyosin/chemistry/ultrastructure
    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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    Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-16
    Description: The cytoplasmic tyrosine kinase, Bruton's tyrosine kinase (Btk, formerly bpk or atk), is crucial for B cell development. Loss of kinase activity results in the human immunodeficiency, X-linked agammaglobulinemia, characterized by a failure to produce B cells. In the murine X-linked immunodeficiency (XID), B cells are present but respond abnormally to activating signals. The Btk gene, btk, was mapped to the xid region of the mouse X chromosome by interspecific backcross analysis. A single conserved residue within the amino terminal unique region of Btk was mutated in XID mice. This change in xid probably interferes with normal B cell signaling mediated by Btk protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawlings, D J -- Saffran, D C -- Tsukada, S -- Largaespada, D A -- Grimaldi, J C -- Cohen, L -- Mohr, R N -- Bazan, J F -- Howard, M -- Copeland, N G -- AR36834/AR/NIAMS NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 16;261(5119):358-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332901" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*enzymology/immunology ; Base Sequence ; Cell Line ; Chromosome Mapping ; Crosses, Genetic ; Exons ; Female ; Genetic Linkage ; Immunologic Deficiency Syndromes/enzymology/*genetics/immunology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Inbred DBA ; Mice, Mutant Strains ; Molecular Sequence Data ; Protein-Tyrosine Kinases/chemistry/*genetics/metabolism ; *X Chromosome
    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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    Ar-39 - Ar-40 ages of acapulcoites and lodranites: Evidence for early parent body heating (1993)
    In:  Other Sources
    Details
    Publication Date: 2019-01-25
    Description: New age dating of acapulcoites (Acapulco, Monument Draw) and lodranites (Gibson) allow us to reconstruct the history of their parent body in a chronological framework. These meteorites originated on a common parent body -4.55 Ga ago. Non-collisional heating caused partial melting, with lodranites having been heated slightly higher than acapulcoites. This parent body cooled to the Ar closure temperature at -4.51 Ga for acapulcoites and -4.48 Ga for lodranites. The difference in ages is consistent with the higher temperature and longer cooling time for lodranites. Cooling probably occurred at a few to tens of deg C/Ma, with slower cooling rates at lower temperatures.
    Keywords: GEOPHYSICS
    Type: Lunar and Planetary Inst., Twenty-fourth Lunar and Planetary Science Conference. Part 1: A-F; p 141-142
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    NASA TECHNICAL REPORTS
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