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  • American Association for the Advancement of Science (AAAS)  (20)
  • English  (20)
  • 1995-1999  (20)
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  • American Association for the Advancement of Science (AAAS)  (20)
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  • English  (20)
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  • 1995-1999  (20)
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  • 1
    Online Resource
    Online Resource
    Terminating SMAD Signals
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 11 ( 1999-12-07)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 11 ( 1999-12-07)
    Abstract: SMADs function with other proteins to mediate transcriptional activation in response to transforming growth factor β and related proteins. SMADs are activated when phosphorylated by the TGF-β receptor, so one might have thought that the easy way to inactivate SMADs would be to dephosphorylate them. Although dephosphorylation might be a factor, new evidence points instead to a major role for ubiquitin-dependent degradation in termination of SMAD signaling. Lo and Massagué find that degradation of SMAD2 is increased in response to activation of the TGF-β receptor. Unlike regulation of some other transcription factors for which phosphorylation is a key tag that leads to ubiquitination and destruction, the essential event that leads to degradation of SMAD2 appears to be its translocation to the nucleus. The regulation of SMAD2 is also distinct from that recently described by Zhu et al. for SMAD1 and SMAD5, which appears to rely not on nuclear localization, but rather a cytoplasmic event that depends on a Pro-Tyr (PY) motif in the SMAD proteins. All the findings are summarized in an insightful "News and Views" by Heldin and ten Dijke. Lo, R.S., and Massagué, J. (1999) Ubiquitin-dependent degradation of TGF-β-activated Smad2. Nature Cell Biol. 1 : 472-478. [Online Journal] Zhu, H., Kavsak, P., Abdollah, S., Wrana, J.L., and Thomsen, G.H. (1999) A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400 : 687-693. [Online Journal] Heldin, C.-H., and ten Dijke, P. (1999) SMAD destruction turns off signalling. Nature Cell Biol. 1 : E195 - E197. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.11.tw4
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 2
    Online Resource
    Online Resource
    Evidence for Life on Earth More Than 3850 Million Years Ago
    American Association for the Advancement of Science (AAAS) ; 1997
    In:  Science Vol. 275, No. 5296 ( 1997-01-03), p. 38-39
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 275, No. 5296 ( 1997-01-03), p. 38-39
    Abstract: When did life first appear on Earth? Previous efforts to answer this fundamental question have found early life as far back as 3450 million years ago, in rock formations in Australia. In his Perspective, Holland discusses data recently published by Mojzsis et al . in the journal Nature that pushes the earliest life back to more than 3850 million years ago.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.275.5296.38
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1997
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
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  • 3
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    Online Resource
    Shaker Channels do the Twist
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 13 ( 1999-12-21)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 13 ( 1999-12-21)
    Abstract: Shaker K + channels from Drosophila are a well-studied example of voltage-gated channels that are essential for neuronal signal transduction. Two groups, Cha et al . and Glauner et al. , have now done experiments that move us a step closer to understanding the precise mechanism by which these channels are opened and closed in response to changes in membrane potential. A segment known as S4 is known to contain charged amino acids that participate in sensing voltage changes. These charged residues move across the electric field of the membrane as the channel is opened and closed. By tagging regions of the channel with donors and acceptors, the two groups used fluorescence resonance energy transfer to monitor movement between the subunits of the channel. As residues along the protein sequence near or in the S4 segment were probed, they appeared to alternately move closer or farther apart, suggesting that the S4 region may actually twist in response to voltage changes. Large changes in conformation of the subunits were not detected, and the twisting motion is an appealing model that would help explain how the series of charged residues in the S4 domain can be alternately exposed to the intracellular or extracellular face of the membrane through relatively small movements of regions within the channel subunits. Cha, A., Snyder, G.E., Selvin, P.R., and Bezanilla, F. (1999) Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature 402 : 809-813. [Online Journal] Glauner, K.S., Mannuzzu, L.M., Gandhi, C.S., and Isacoff, E.Y. (1999) Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel. Nature 402 : 813-817. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.13.tw2
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 4
    Online Resource
    Online Resource
    Glutamate Signals Insulin Secretion
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 12 ( 1999-12-14)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 12 ( 1999-12-14)
    Abstract: Release of insulin from pancreatic βcells in response to glucose is thought to be signaled by generation of ATP and consequent influx of calcium into the cell. However, evidence indicates that a factor besides ATP is released from mitochondria that is necessary for secretion. Maechler and Wollheim provide evidence that this messenger is glutamate. Glutamate is shown to be generated by mitochondria in response to glucose and directly stimulates exocytosis in permeabilized cells in which the concentration of calcium is held constant. Uptake of glutamate by secretory granules appears to be required for its effects. Thus, glutamate, well known as an intercellular messenger in the nervous system, appears to also function as an intracellular messenger that controls insulin secretion. Maechler, P., and Wollheim, C.B. (1999) Mitochondial glutamate acts as a messenger in glucose-induced insulin exocytosis. Nature 402 : 685-689. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.12.tw5
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 5
    Online Resource
    Online Resource
    Releasing the block
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 1 ( 1999-09-28)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 1 ( 1999-09-28)
    Abstract: The inhibitory effect of cyclic adenosine 3',5'-monophosphate (cAMP) on lymphocyte activation is mediated through cAMP-dependent protein kinase (protein kinase A/PKA). Lymphocyte activation is also negatively regulated by a subgroup of protein tyrosine phosphatases (PTPases) that inactivate MAP kinases. The hematopoietic PTPase, HePTP, is known to bind to and rapidly deactivate the MAP kinases Erk1, Erk2, and p38. Hence, HePTP reduces transcription activation from Erk/p38-dependent promoters. Saxena et al. now report that HePTP is phosphorylated by PKA. This phosphorylation event reduced HePTP interaction with its bound MAP kinase. Release from this inhibition resulted in MAP kinase activation and transcription from the c-fos promoter. Hence, crosstalk between the cAMP/PKA pathway and MAP kinase activation pathways may occur through PTPases in immune cells. Saxena, M., Williams, S., Tasken, K., Mustelin, T. (1999) Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase. Nature Cell Biol . 1 : 305-310. Online Journal
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.1.tw5
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 6
    Online Resource
    Online Resource
    From Ras to Rac
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 1 ( 1999-09-28)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 1 ( 1999-09-28)
    Abstract: Cytoskeletal rearrangements can occur when cells respond to certain extracellular stimuli. One of the signaling cascades implicated in this process involves communication between the small GTP-binding proteins Ras and Rac. Scita et al. now show that fibroblast cell lines derived from knockout mice that lack the protein Eps8 do not remodel actin when treated with growth factors. Rac activity was regulated by a complex containing the proteins Eps8, E3b1, and Sos-1. The authors suggest that the formation of this complex stimulates the Rac-GEF activity of Sos-1. In addition, Eps8 activity was localized downstream of phosphatidylinositol 3-phosphate kinase, an immediate downstream effector of Ras. Hence, this complex may facilitate the transfer of signals between Ras and Rac. Scita, G., Nordstrom, J., Carbone, R., Tenca, P., Giardina, G., Gutkind, S., Bjarnegard, M., Betsholtz, C., and Di Fiore, P.P. (1999) EPS8 and E3B1 transduce signals from Ras to Rac. Nature 401 : 290-293. Online Journal
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.1.tw4
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 7
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    Online Resource
    Receptors: GCSF Receptors, Two by Two
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 4 ( 1999-10-19)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 4 ( 1999-10-19)
    Abstract: Aritomi et al . report the crystal structure of the cytokine granulocyte colony-stimulating factor (GCSF) with the main ligand-binding domain of the GCSF receptor. GCSF is related to growth hormone and erythropoietin, and when the latter molecules bind their receptors, one cytokine molecule interacts with two receptor molecules. However, in the GCSF complexes with the receptor domain, two cytokine molecules interacted with a pair of receptor molecules. The structure shows two regions of interaction: one interface is formed by a one-to-one interaction between GCSF and the receptor domain but the other results from interaction between the two one-to-one complexes. Thus, there appears to be more than one way for cytokine ligands to interact with and activate their receptors. Citation: Aritomi, M., Kunishima, N., Okamoto, T., Kuroki, R., Ota, Y., and Morikawa, K. (1999) Atomic structure of the GCSF-receptor complex showing a new ctyokine-receptor scheme. Nature 401 : 713-717. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.4.tw1
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 8
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    Neuroscience: Neurotrophins as Neurotransmitters
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 6 ( 1999-11-02)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 6 ( 1999-11-02)
    Abstract: Neurotrophins are secreted factors that influence growth, survival, and other functions of neurons. Kafitz et al. now report that two of these proteins, brain-derived neurotrophic factor (BDNF) and neurotrophin-4/5 (NT-4/5) can also function as a potent neurotransmitters. Application of BDNF or NT-4/5 to slices of hippocampus, cortex, or cerebellum from rat brain caused depolarization of neurons very similar to that caused by glutamate. The effects appear to result from stimulation of TrkB neurotrophin receptors and consequent activation of sodium channels. The very rapid effect on the channels is observer in recordings during which the concentration of cytoplasmic components is substantially reduced. Thus, it seems that direct interaction of neurotrophin receptors with sodium channels (rather than signaling through tyrosine kinase activity of the receptors) may mediate the depolarization. Kafitz, K.W., Rose, C.R., Thoenen, H.., and Konnerth, A. (1999) Neurotrophin-evoked rapid excitation through TrkB receptors. Nature 401 : 918-921. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.6.tw3
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 9
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    Online Resource
    Calcium signaling: Regulation of Gene Expression by Neuronal Calcium
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 4 ( 1999-10-19)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 4 ( 1999-10-19)
    Abstract: The control of gene expression by calcium and the NF-AT family of transcription factors may not just occur in lymphocytes. Graef et al . now report a similar pathway in neurons. Electrical activity or depolarization of hippocampal neurons stimulated the entry of calcium through L-type voltage-gated channels. This event resulted in a calcineurin-dependent dephosphorylation of the NF-ATc4 transcription factor and its subsequent relocalization to the nucleus. The serine-threonine kinase GSK-3 appeared to do just the opposite: The enzyme inhibited transcription in neurons by phosphorylating NF-ATc4. This modification promoted the nuclear export of the transcription factor. The authors suggest that this calcium-dependent mechanism of transcriptional control may be linked to the expression of the inositol 1,4,5-triphosphate receptor and regulation of synaptic plasticity in such neurons. Graef, I.A., Mermelstein, P.G., Stankunas, K., Nellson, J.R., Deisseroth, K., Tsien, R.W., and Crabtree, G. R. (1999) L-type calcium channels and GSK-3 regulate the activity of NF-Atc4 in hippocampal neurons. Nature 401 : 703-708. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.4.tw2
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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  • 10
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    Light response in plants: Nucleoside Diphosphate Kinase Sees the Light
    American Association for the Advancement of Science (AAAS) ; 1999
    In:  Science's STKE Vol. 1999, No. 3 ( 1999-10-12)
    Details
    In: Science's STKE, American Association for the Advancement of Science (AAAS), Vol. 1999, No. 3 ( 1999-10-12)
    Abstract: Plants respond to red light through receptors known as phytochromes, but the signaling mechanisms that mediate cellular responses to activated phytochromes are not well understood. Choi et al. therefore used a yeast two-hybrid screen to identify proteins that bound to phytochrome A. They came up with nucleoside diphosphate kinase 2 (NDPK2), a protein that acts as a tumor suppressor in mammalian cells. Arapidopsis plants lacking NDPK2 were insensitive to red and far-red light. NDPK2 preferentially bound to light-activated phytochrome A in vitro and gamma-phosphate exchange activity of NDPK2 was increased as a consequence. NDPK has been ascribed a number of different activities in various cell types from transcription factor to activator of G proteins. Exactly how NDPK2 acts to promote responses of plant cells to red light remains a mystery. Choi, G., Yi, H., Lee, J., Kwon, Y.-K., Soh, M.S., Shin, B., Luka, Z., Hahn, T.-R., and Song, P.-S. (1999) Phytochrome signalling is mediated through nucleoside diphosphate kinase 2. Nature 401 : 610-613. [Online Journal]
    Type of Medium: Online Resource
    ISSN: 1525-8882
    URL: Article
    DOI: 10.1126/stke.1999.3.tw5
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1999
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