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  • American Association for the Advancement of Science (AAAS)  (10)
  • American Society of Hematology
  • PANGAEA
  • 2015-2019
  • 2000-2004
  • 1990-1994  (20)
  • 1945-1949
  • 1994  (20)
Collection
Keywords
Publisher
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  • 2015-2019
  • 2000-2004
  • 1990-1994  (20)
  • 1945-1949
Year
  • 1
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    Tetrad analysis possible in Arabidopsis with mutation of the QUARTET (QRT) genes (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-06-03
    Description: Two Arabidopsis thaliana genes, QRT1 and QRT2, are required for pollen separation during normal development. In qrt mutants, the outer walls of the four meiotic products of the pollen mother cell are fused, and pollen grains are released in tetrads. Pollen is viable and fertile, and the cytoplasmic pollen contents are discrete. Pollination with a single tetrad usually yields four seeds, and genetic analysis confirmed that marker loci segregate in a 2:2 ratio within these tetrads. These mutations allow tetrad analysis to be performed in Arabidopsis and define steps in pollen cell wall development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preuss, D -- Rhee, S Y -- Davis, R W -- New York, N.Y. -- Science. 1994 Jun 3;264(5164):1458-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Stanford University, CA 94305-5307.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8197459" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/physiology/ultrastructure ; Cell Wall/ultrastructure ; Chromosome Mapping ; *Genes, Plant ; Genetic Markers ; Glucuronidase/genetics ; Heterozygote ; Meiosis ; Microscopy, Electron, Scanning ; Mutation ; Phenotype ; Pollen/*physiology/ultrastructure
    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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    First images of asteroid 243 ida (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-09
    Description: The first images of the asteroid 243 Ida from Galileo show an irregular object measuring 56-kilometers by 24 kilometers by 21 kilometers. Its surface is rich in geologic features, including systems of grooves, blocks, chutes, albedo features, crater chains, and a full range of crater morphologies. The largest blocks may be distributed nonuniformly across the surface; lineaments and dark-floored craters also have preferential locations. Ida is interpreted to have a substantial regolith. The high crater density and size-frequency distribution (-3 differential power-law index) indicate a surface in equilibrium with saturated cratering. A minimum model crater age for Ida-and therefore for the Koronis family to which Ida belongs-is estimated at 1 billion years, older than expected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belton, M J -- Chapman, C R -- Veverka, J -- Klaasen, K P -- Harch, A -- Greeley, R -- Greenberg, R -- Head, J W 3rd -- McEwen, A -- Morrison, D -- Thomas, P C -- Davies, M E -- Carr, M H -- Neukum, G -- Fanale, F P -- Davis, D R -- Anger, C -- Gierasch, P J -- Ingersoll, A P -- Pilcher, C B -- New York, N.Y. -- Science. 1994 Sep 9;265(5178):1543-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17801529" target="_blank"〉PubMed〈/a〉
    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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  • 3
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    Epidermal cell fate determination in Arabidopsis: patterns defined by a steroid-inducible regulator (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-21
    Description: The Arabidopsis mutant ttg lacks both trichomes (epidermal hairs) and anthocyanin pigments. Trichomes and anthocyanins are restored by the constitutive expression of the maize transcriptional regulator (R). The expression of an R-glucocorticoid receptor chimeric protein results in a steroid hormone-dependent, conditional allele of R that functions in whole Arabidopsis plants. The response of the chimeric protein to pulses of hormone was used to define the pattern and timing of trichome formation on the developing leaf epidermis. Each adaxial epidermal leaf cell appears to have an equal probability of differentiating into a trichome; there is a temporal zone of decision for trichome cell fate that proceeds as a wave from the tip to the base of developing leaves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lloyd, A M -- Schena, M -- Walbot, V -- Davis, R W -- GM 32422/GM/NIGMS NIH HHS/ -- R37-H600198/PHS HHS/ -- New York, N.Y. -- Science. 1994 Oct 21;266(5184):436-9.〈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/7939683" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Anthocyanins/*biosynthesis/genetics ; Arabidopsis/*cytology/genetics/growth & development/metabolism ; Dexamethasone/*pharmacology ; Gene Expression Regulation, Plant ; Microscopy, Electron, Scanning ; Plant Leaves/*cytology/growth & development/ultrastructure ; Receptors, Glucocorticoid/*physiology ; Recombinant Fusion Proteins ; Trans-Activators/*physiology ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    NMR solution structure of a peptide nucleic acid complexed with RNA (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Peptide nucleic acids (PNA) incorporating nucleic acid bases into an achiral polyamide backbone bind to DNA in a sequence-dependent manner. The structure of a PNA-ribonucleic acid (RNA) complex was determined with nuclear magnetic resonance methods. A hexameric PNA formed a 1:1 complex with a complementary RNA that is an antiparallel, right-handed double helix with Watson-Crick base pairing similar to the "A" form structure of RNA duplexes. The achiral PNA backbone assumed a distinct conformation upon binding that differed from previously proposed models and provides a basis for further structure-based design of antisense agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, S C -- Thomson, S A -- Veal, J M -- Davis, D G -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):777-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Research Institute, Research Triangle Park, NC 27709.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7519361" target="_blank"〉PubMed〈/a〉
    Keywords: Magnetic Resonance Spectroscopy ; Models, Molecular ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/*chemistry ; Peptides/*chemistry ; RNA/*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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  • 5
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    Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: Growth factors activate mitogen-activated protein kinases (MAPKs), including extracellular signal-regulated kinases (ERKs) and Jun kinases (JNKs). Although the signaling cascade from growth factor receptors to ERKs is relatively well understood, the pathway leading to JNK activation is more obscure. Activation of JNK by epidermal growth factor (EGF) or nerve growth factor (NGF) was dependent on H-Ras activation, whereas JNK activation by tumor necrosis factor alpha (TNF-alpha) was Ras-independent. Ras activates two protein kinases, Raf-1 and MEK (MAPK, or ERK, kinase) kinase (MEKK). Raf-1 contributes directly to ERK activation but not to JNK activation, whereas MEKK participated in JNK activation but caused ERK activation only after overexpression. These results demonstrate the existence of two distinct Ras-dependent MAPK cascades--one initiated by Raf-1 leading to ERK activation, and the other initiated by MEKK leading to JNK activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Minden, A -- Lin, A -- McMahon, M -- Lange-Carter, C -- Derijard, B -- Davis, R J -- Johnson, G L -- Karin, M -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1719-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California at San Diego, La Jolla 92093-0636.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992057" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Enzyme Activation/drug effects ; Epidermal Growth Factor/pharmacology ; Genes, ras ; HeLa Cells ; Humans ; JNK Mitogen-Activated Protein Kinases ; *MAP Kinase Kinase Kinase 1 ; Mice ; Mitogen-Activated Protein Kinase 1 ; *Mitogen-Activated Protein Kinases ; Nerve Growth Factors/pharmacology ; PC12 Cells ; Protein-Serine-Threonine Kinases/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Rats ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology ; ras Proteins/*pharmacology
    Print ISSN: 0036-8075
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  • 6
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    Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of beta-tubulin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-05-06
    Description: Microtubule dynamic instability underlies many cellular functions, including spindle morphogenesis and chromosome movement. The role of guanosine triphosphate (GTP) hydrolysis in dynamic instability was investigated by introduction of four mutations into yeast beta-tubulin at amino acids 103 to 109, a site thought to participate in GTP hydrolysis. Three of the mutations increased both the assembly-dependent rate of GTP hydrolysis and the average length of steady-state microtubules over time, a measure of dynamic instability. The fourth mutation did not substantially affect the rate of GTP hydrolysis or the steady-state microtubule lengths. These results demonstrate that the rate of GTP hydrolysis can modulate microtubule length and hence dynamic instability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, A -- Sage, C R -- Dougherty, C A -- Farrell, K W -- GM 41751/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 May 6;264(5160):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of California, Santa Barbara 93106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8171338" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; GTP Phosphohydrolases/*metabolism ; Guanosine Triphosphate/*metabolism ; Hydrolysis ; Microtubules/metabolism/*physiology/ultrastructure ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Saccharomyces cerevisiae/chemistry ; Tubulin/chemistry/genetics/*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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  • 7
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    Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The EPH-related transmembrane tyrosine kinases constitute the largest known family of receptor-like tyrosine kinases, with many members displaying specific patterns of expression in the developing and adult nervous system. A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified. These ligands were unable to act as conventional soluble factors. However, they did function when presented in membrane-bound form, suggesting that they require direct cell-to-cell contact to activate their receptors. Membrane attachment may serve to facilitate ligand dimerization or aggregation, because antibody-mediated clustering activated previously inactive soluble forms of these ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Gale, N W -- Aldrich, T H -- Maisonpierre, P C -- Lhotak, V -- Pawson, T -- Goldfarb, M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/*metabolism ; *DNA-Binding Proteins ; Ephrin-A1 ; Ephrin-B1 ; Humans ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Neurons/metabolism ; Phosphorylation ; Proteins/chemistry/*metabolism ; *Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; *Receptor, EphA5 ; Recombinant Fusion Proteins/metabolism ; Retroviridae Proteins, Oncogenic/*metabolism ; Solubility ; *Transcription Factors ; Transfection ; Tumor Cells, Cultured ; ets-Domain Protein Elk-1
    Print ISSN: 0036-8075
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  • 8
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    Association and activation of Jak-Tyk kinases by CNTF-LIF-OSM-IL-6 beta receptor components (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-01-07
    Description: A recently defined family of cytokines, consisting of ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), oncostatin M (OSM), and interleukin-6 (IL-6), utilize the Jak-Tyk family of cytoplasmic tyrosine kinases. The beta receptor components for this cytokine family, gp130 and LIF receptor beta, constitutively associate with Jak-Tyk kinases. Activation of these kinases occurs as a result of ligand-induced dimerization of the receptor beta components. Unlike other cytokine receptors studied to date, the receptors for the CNTF cytokine family utilize all known members of the Jak-Tyk family, but induce distinct patterns of Jak-Tyk phosphorylation in different cell lines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stahl, N -- Boulton, T G -- Farruggella, T -- Ip, N Y -- Davis, S -- Witthuhn, B A -- Quelle, F W -- Silvennoinen, O -- Barbieri, G -- Pellegrini, S -- P30 CA21765/CA/NCI NIH HHS/ -- R01 DK42932/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Jan 7;263(5143):92-5.〈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/8272873" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Cell Line ; Ciliary Neurotrophic Factor ; Cytokine Receptor gp130 ; Cytokines/metabolism/*pharmacology ; Enzyme Activation ; *Growth Inhibitors ; *Interleukin-6 ; Janus Kinase 1 ; Janus Kinase 2 ; Leukemia Inhibitory Factor ; *Lymphokines ; Membrane Glycoproteins/*metabolism ; Nerve Tissue Proteins/metabolism/pharmacology ; Oncostatin M ; Peptides/metabolism/pharmacology ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Proteins/metabolism ; *Proto-Oncogene Proteins ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cytokine/*metabolism ; Receptors, Growth Factor/metabolism ; Receptors, Interleukin/metabolism ; Receptors, Interleukin-6 ; Receptors, OSM-LIF ; Receptors, Oncostatin M ; Tyrosine/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    An osmosensing signal transduction pathway in mammalian cells (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: The osmotic balance between the cytoplasmic and extracellular compartments of cells is critical for the control of cell volume. A mammalian protein kinase, Jnk, which is a distant relative of the mitogen-activated protein kinase group, was activated by phosphorylation on threonine and tyrosine in osmotically shocked cells. The activation of Jnk may be relevant to the biological response to osmotic shock because the expression of human Jnk in the yeast Saccharomyces cerevisiae rescued a defect in growth on hyper-osmolar media. These data indicate that related protein kinases may mediate osmosensing signal transduction in yeast and mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Derijard, B -- Wu, I H -- Davis, R J -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):806-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047888" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium-Calmodulin-Dependent Protein Kinases/genetics ; Cricetinae ; Cricetulus ; Enzyme Activation ; Genetic Complementation Test ; JNK Mitogen-Activated Protein Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Osmotic Pressure ; Protein-Serine-Threonine Kinases/*physiology ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; Signal Transduction/*physiology ; Water-Electrolyte Balance/*physiology
    Print ISSN: 0036-8075
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  • 10
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    Federal funding obligations in astronomy (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M -- McCray, R -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1625.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17775611" target="_blank"〉PubMed〈/a〉
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