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  • Launch Vehicles and Launch Operations  (22)
  • Molecular Sequence Data  (22)
  • 2005-2009  (29)
  • 1990-1994  (15)
  • 1
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    Constellation Launch Vehicles Overview (2009)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: This slide presentation reviews the current status of the launch vehicles associated with the Constellation Program. These are the Ares I and the Ares V. An overview of the Ares launch vehicles is included. The presentation stresses that the major criteria for the Ares I launcher is the safety of the crew, and the presentation reviews the various features that are designed to assure that aim. The Ares I vehicle is being built on a foundation of proven technologies, and the Ares V will give NASA unprecedented performance and payload volume that can enable a range of future missions. The CDs contain videos of scenes from various activities surrounding the design, construction and testing of the vehicles.
    Keywords: Launch Vehicles and Launch Operations
    Type: Human Space Flight Review; Jul 29, 2009; Huntsville, AL; United States
    Format: text
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    NASA TECHNICAL REPORTS
  • 2
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    Expression of T cell antigen receptor heterodimers in a lipid-linked form (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-10
    Description: The interaction of the T cell receptor for antigen (TCR) with its antigen-major histocompatibility complex ligand is difficult to study because both are cell surface multimers. The TCR consists of two chains (alpha and beta) that are complexed to the five or more nonpolymorphic CD3 polypeptides. A soluble form of the TCR was engineered by replacing the carboxyl termini of alpha and beta with signal sequences from lipid-linked proteins, making them susceptible to enzymatic cleavage. In this manner, TCR heterodimers can be expressed independently of the CD3 polypeptides and in significant quantities (0.5 milligram per week). This technique seems generalizable to biochemical and structural studies of many other cell surface molecules as well.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, A Y -- Devaux, B -- Green, A -- Sagerstrom, C -- Elliott, J F -- Davis, M M -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):677-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305-5402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1696397" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaline Phosphatase/genetics ; Amino Acid Sequence ; Animals ; Antigens, CD3 ; Antigens, CD55 ; Antigens, Differentiation, T-Lymphocyte/genetics ; Cell Line ; Complement Inactivator Proteins/genetics ; Female ; Humans ; Macromolecular Substances ; Membrane Proteins/genetics ; Molecular Sequence Data ; Placenta/enzymology ; Pregnancy ; Protein Sorting Signals/genetics ; Receptors, Antigen, T-Cell/*genetics ; 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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    PAPER CURRENT
  • 3
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    Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-03-02
    Description: Cold-sensitive mutations in the SPB genes (spb1-spb7) of Saccharomyces cerevisiae suppress the inhibition of translation initiation resulting from deletion of the poly(A)-binding protein gene (PAB1). The SPB4 protein belongs to a family of adenosine triphosphate (ATP)-dependent RNA helicases. The aberrant production of 25S ribosomal RNA (rRNA) occurring in spb4-1 mutants or the deletion of SPB2 (RPL46) permits the deletion of PAB1. These data suggest that mutations affecting different steps of 60S subunit formation can allow PAB-independent translation, and they indicate that further characterization of the spb mutations could lend insight into the biogenesis of the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sachs, A B -- Davis, R W -- R37 GM 21891/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 2;247(4946):1077-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2408148" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Carrier Proteins/genetics/metabolism ; DEAD-box RNA Helicases ; Molecular Sequence Data ; Mutation ; Poly(A)-Binding Proteins ; *Protein Biosynthesis ; RNA Nucleotidyltransferases/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/genetics/metabolism ; RNA, Ribosomal/genetics/*metabolism ; Ribosomal Proteins/genetics/*metabolism ; Ribosomes/*metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    PAPER CURRENT
  • 4
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    Rel-associated pp40: an inhibitor of the rel family of transcription factors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-09-23
    Description: The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, N -- Ghosh, S -- Simmons, D L -- Tempst, P -- Liou, H C -- Baltimore, D -- Bose, H R Jr -- CA09583/CA/NCI NIH HHS/ -- CA2616/CA/NCI NIH HHS/ -- CA33192/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Sep 13;253(5025):1268-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Texas, Austin 78712.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1891714" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; Cloning, Molecular ; DNA Probes ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotide Probes ; Oncogene Proteins v-rel ; Open Reading Frames ; Phosphoproteins/*genetics/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; RNA, Messenger/genetics ; Retroviridae Proteins, Oncogenic/*antagonists & inhibitors ; Sequence Homology, Nucleic Acid ; Transcription Factors/*antagonists & inhibitors
    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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    Presence of an SH2 domain in the actin-binding protein tensin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-03
    Description: The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-gamma 1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Lu, M L -- Lo, S H -- Lin, S -- Butler, J A -- Druker, B J -- Roberts, T M -- An, Q -- Chen, L B -- GM 22289/GM/NIGMS NIH HHS/ -- GM 38318/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):712-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1708917" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Chick Embryo ; Cloning, Molecular ; Cytoskeletal Proteins/*chemistry/genetics/metabolism ; DNA/genetics ; Fluorescent Antibody Technique ; Immunoblotting ; *Microfilament Proteins ; Molecular Sequence Data ; Peptide Fragments/genetics ; Phosphotyrosine ; Protein-Tyrosine Kinases/genetics ; Sequence Homology, Nucleic Acid ; Signal Transduction ; Tyrosine/analogs & derivatives/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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  • 6
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    The receptor for ciliary neurotrophic factor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-07-05
    Description: Although neurotrophic factors were originally isolated on the basis of their ability to support the survival of neurons, these molecules are now thought to influence many aspects of the development and maintenance of the nervous system. Identifying the receptors for these neurotrophic factors should aid in identifying the cells on which these factors act and in understanding their precise mechanisms of action. A "tagged-ligand panning" procedure was used to clone a receptor for ciliary neurotrophic factor (CNTF). This receptor is expressed exclusively within the nervous system and skeletal muscle. The CNTF receptor has a structure unrelated to the receptors utilized by the nerve growth factor family of neurotrophic molecules, but instead is most homologous to the receptor for a cytokine, interleukin-6. This similarity suggestes that the CNTF receptor, like the interleukin-6 receptor, requires a second, signal-transducing component. In contrast to all known receptors, the CNTF receptor is anchored to cell membranes by a glycosyl-phosphatidylinositol linkage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Valenzuela, D M -- Wong, V V -- Furth, M E -- Squinto, S P -- Yancopoulos, G D -- New York, N.Y. -- Science. 1991 Jul 5;253(5015):59-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648265" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; Electrophoresis, Agar Gel ; Gene Expression ; Humans ; In Vitro Techniques ; Molecular Sequence Data ; Muscles/metabolism ; Nervous System/metabolism ; Neuroblastoma/metabolism ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/blood/*genetics ; Sequence Homology, Nucleic Acid ; 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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  • 7
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    Arabidopsis and Nicotiana anthocyanin production activated by maize regulators R and C1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Anthocyanin pathway-specific transcriptional activators R and C1 from the monocot maize were expressed in two dicots, Arabidopsis thaliana and Nicotiana tabacum. Expression of R caused augmented anthocyanin pigmentation in both plant species and augmented trichome (hair) production in Arabidopsis. Alone, C1 had no effect. Hybrid transgenic Arabidopsis expressing both C1 and R produced anthocyanins in root, petal, and stamen tissues that normally never express anthrocyanins. When R was expressed in the transparent testa glabrous (without anthocyanins and trichomes) mutant of Arabidopsis, the deficiency was complemented and both anthocyanins and trichomes were restored.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lloyd, A M -- Walbot, V -- Davis, R W -- GM 32422/GM/NIGMS NIH HHS/ -- R37-H600198/PHS HHS/ -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1773-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465611" target="_blank"〉PubMed〈/a〉
    Keywords: Anthocyanins/*biosynthesis ; Arabidopsis/*genetics/*metabolism ; Base Sequence ; Genes, Plant ; Genetic Vectors ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Plants, Genetically Modified ; *Plants, Toxic ; Plasmids ; Promoter Regions, Genetic ; Restriction Mapping ; Rhizobium/genetics ; Tobacco/*genetics/*metabolism ; Trans-Activators/*genetics/*metabolism ; Transcription, Genetic ; Zea mays/*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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  • 8
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    A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-05-25
    Description: Tumor necrosis factor alpha and beta (TNF-alpha and TNF-beta) bind surface receptors on a variety of cell types to mediate a wide range of immunological responses, inflammatory reactions, and anti-tumor effects. A cDNA clone encoding an integral membrane protein of 461 amino acids was isolated from a human lung fibroblast library by direct expression screening with radiolabeled TNF-alpha. The encoded receptor was also able to bind TNF-beta. The predicted cysteine-rich extracellular domain has extensive sequence similarity with five proteins, including nerve growth factor receptor and a transcriptionally active open reading frame from Shope fibroma virus, and thus defines a family of receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C A -- Davis, T -- Anderson, D -- Solam, L -- Beckmann, M P -- Jerzy, R -- Dower, S K -- Cosman, D -- Goodwin, R G -- New York, N.Y. -- Science. 1990 May 25;248(4958):1019-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2160731" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Cloning, Molecular ; DNA/genetics ; Humans ; Membrane Proteins/genetics ; Molecular Sequence Data ; Multigene Family ; Receptors, Cell Surface/*genetics ; Receptors, Tumor Necrosis Factor ; Tumor Necrosis Factor-alpha/*physiology
    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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    Low affinity interaction of peptide-MHC complexes with T cell receptors (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-20
    Description: The interaction of antigen-specific T cell receptors (TCRs) with their ligands, peptides bound to molecules of the major histocompatibility complex (MHC), is central to most immune responses, yet little is known about its chemical characteristics. The binding to T cells of a labeled monoclonal antibody to the TCR was inhibited by soluble class II MHC heterodimers complexed to different peptides. Inhibition was both peptide- and TCR-specific and of low affinity, with a KD = 4 x 10(-5) to 6 x 10(-5) M, orders of magnitude weaker than comparable antibody-antigen interactions. This finding is consistent with the scanning nature of T cell recognition and suggests that antigen-independent adhesion precedes TCR engagement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsui, K -- Boniface, J J -- Reay, P A -- Schild, H -- Fazekas de St Groth, B -- Davis, M M -- AI19512/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1788-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763329" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Antigen-Presenting Cells/immunology ; Cell Line ; Genetic Variation ; Immunoglobulin Fab Fragments/immunology ; Kinetics ; Macromolecular Substances ; *Major Histocompatibility Complex ; Models, Biological ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Protein Binding ; Receptors, Antigen, T-Cell/immunology/*physiology ; T-Lymphocytes/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transfected with class II DR3 genes, DR molecules were produced in normal amounts. However, the DR molecules were abnormally conformed and unstable because deletion of an antigen-processing gene had impaired intracellular formation of most class II-peptide complexes. Yet, 70 percent of the DR molecules still bore peptides, 80 percent of which were 21- to 24-amino acid fragments of the class II-associated invariant chain. These peptides were rare on DR3 from control cells. Thus, a defect in the main antigen-processing pathway revealed a process in which DR molecules bind long peptides derived from proteins present in the same compartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sette, A -- Ceman, S -- Kubo, R T -- Sakaguchi, K -- Appella, E -- Hunt, D F -- Davis, T A -- Michel, H -- Shabanowitz, J -- Rudersdorf, R -- AI15486/AI/NIAID NIH HHS/ -- AI18634/AI/NIAID NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1801-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465617" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Gene Deletion ; *Genes, MHC Class II ; HLA-DR Antigens/*genetics/*metabolism ; HLA-DR3 Antigen/*genetics/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Peptides/*metabolism ; 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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