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  • 1
    Online Resource
    Online Resource
    Changing central Pacific El Niños reduce stability of North American salmon survival rates
    Proceedings of the National Academy of Sciences ; 2015
    In:  Proceedings of the National Academy of Sciences Vol. 112, No. 35 ( 2015-09), p. 10962-10966
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 112, No. 35 ( 2015-09), p. 10962-10966
    Abstract: Pacific salmon are a dominant component of the northeast Pacific ecosystem. Their status is of concern because salmon abundance is highly variable—including protected stocks, a recently closed fishery, and actively managed fisheries that provide substantial ecosystem services. Variable ocean conditions, such as the Pacific Decadal Oscillation (PDO), have influenced these fisheries, while diminished diversity of freshwater habitats have increased variability via the portfolio effect. We address the question of how recent changes in ocean conditions will affect populations of two salmon species. Since the 1980s, El Niño Southern Oscillation (ENSO) events have been more frequently associated with central tropical Pacific warming (CPW) rather than the canonical eastern Pacific warming ENSO (EPW). CPW is linked to the North Pacific Gyre Oscillation (NPGO), whereas EPW is linked to the PDO, different indicators of northeast Pacific Ocean ecosystem productivity. Here we show that both coho and Chinook salmon survival rates along western North America indicate that the NPGO, rather than the PDO, explains salmon survival since the 1980s. The observed increase in NPGO variance in recent decades was accompanied by an increase in coherence of local survival rates of these two species, increasing salmon variability via the portfolio effect. Such increases in coherence among salmon stocks are usually attributed to controllable freshwater influences such as hatcheries and habitat degradation, but the unknown mechanism underlying the ocean climate effect identified here is not directly subject to management actions.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.1503190112
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2015
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    α2-Chimaerin, a Cdc42/Rac1 Regulator, Is Selectively Expressed in the Rat Embryonic Nervous System and Is Involved in Neuritogenesis in N1E-115 Neuroblastoma Cells
    Society for Neuroscience ; 2001
    In:  The Journal of Neuroscience Vol. 21, No. 14 ( 2001-07-15), p. 5191-5202
    Details
    In: The Journal of Neuroscience, Society for Neuroscience, Vol. 21, No. 14 ( 2001-07-15), p. 5191-5202
    Abstract: Neuronal differentiation involves Rac and Cdc42 GTPases. α-Chimaerin, a Rac/Cdc42 regulator, occurs as α1- and alternatively spliced Src homology 2 (SH2) domain-containing α2-isoforms. α2-chimaerin mRNA was highly expressed in the rat embryonic nervous system, especially in early postmitotic neurons. α1-chimaerin mRNA was undetectable before embryonic day 16.5. Adult α2-chimaerin mRNA was restricted to neurons within specific brain regions, with highest expression in the entorhinal cortex. α2-chimaerin protein localized to neuronal perikarya, dendrites, and axons. The overall pattern of α2-chimaerin mRNA expression resembles that of cyclin-dependent kinase regulator p35 (CDK5/p35) which participates in neuronal differentiation and with which chimaerin interacts. To determine whether α2-chimaerin may have a role in neuronal differentiation and the relevance of the SH2 domain, the morphological effects of both chimaerin isoforms were investigated in N1E-115 neuroblastoma cells. When plated on poly-lysine, transient α2-chimaerin but not α1-chimaerin transfectants formed neurites. Permanent α2-chimaerin transfectants generated neurites whether or not they were stimulated by serum starvation, and many cells were enlarged. Permanent α1-chimaerin transfectants displayed numerous microspikes and contained F-actin clusters, a Cdc42-phenotype, but generated few neurites. In neuroblastoma cells, α2-chimaerin was predominantly soluble with some being membrane-associated, whereas α1-chimaerin was absent from the cytosol, being membrane- and cytoskeleton-associated, paralleling their subcellular distribution in brain. Transient transfection with α2-chimaerin mutated in the SH2 domain (N94H) generated an α1-chimaerin-like phenotype, protein partitioned in the particulate fraction, and in NGF-stimulated pheochromocytoma cell line 12 (PC12) cells, neurite formation was inhibited. These results indicate a role for α2-chimaerin in morphological differentiation for which its SH2 domain is vital.
    Type of Medium: Online Resource
    ISSN: 0270-6474 , 1529-2401
    URL: Article
    DOI: 10.1523/JNEUROSCI.21-14-05191.2001
    Language: English
    Publisher: Society for Neuroscience
    Publication Date: 2001
    detail.hit.zdb_id: 1475274-8
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    α2-Chimaerin, Cyclin-Dependent Kinase 5/p35, and Its Target Collapsin Response Mediator Protein-2 Are Essential Components in Semaphorin 3A-Induced Growth-Cone Collapse
    Society for Neuroscience ; 2004
    In:  The Journal of Neuroscience Vol. 24, No. 41 ( 2004-10-13), p. 8994-9004
    Details
    In: The Journal of Neuroscience, Society for Neuroscience, Vol. 24, No. 41 ( 2004-10-13), p. 8994-9004
    Abstract: Neurite outgrowth is influenced by positive and negative signals that include the semaphorins, an important family of axonal outgrowth inhibitors. Here we report that the Rac GTPase activating protein (GAP)α2-chimaerin is involved in Semaphorin 3A (Sema 3A) signaling. In dorsal root ganglion neurons, Sema 3A-induced growth cone collapse was inhibited by α2-chimaerin mutated to eliminate GAP activity or interaction with phosphotyrosine. Activation of α2-chimaerin by phorbol ester caused growth cone collapse. Active α2-chimaerin interacts with collapsin response mediator protein-2 (CRMP-2) and cyclin-dependent kinase (Cdk) 5/p35 kinase through its SH2 and GAP domains, respectively. Cdk5 phosphorylates CRMP-2 at serine 522, possibly facilitating phosphorylation of serine 518 and threonine 514 by glycogen synthase kinase 3β (GSK3β), a kinase previously implicated in Sema 3A signaling. Phosphorylation of CRMP-2 serine 522 was essential for Sema 3A-induced growth cone collapse, which is dependent on Cdk5 but not Rho kinase activity. α2-chimaerin, like CRMP-2, can associate with the Sema 3A receptor. These results indicate that active α2-chimaerin Rac GAP, Cdk5/p35, and its substrate CRMP-2, are implicated in the dynamics of growth cone guidance initiated through Sema 3A signaling.
    Type of Medium: Online Resource
    ISSN: 0270-6474 , 1529-2401
    URL: Article
    DOI: 10.1523/JNEUROSCI.3184-04.2004
    Language: English
    Publisher: Society for Neuroscience
    Publication Date: 2004
    detail.hit.zdb_id: 1475274-8
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Brazilian cave heritage under siege
    American Association for the Advancement of Science (AAAS) ; 2022
    In:  Science Vol. 375, No. 6586 ( 2022-03-18), p. 1238-1239
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 375, No. 6586 ( 2022-03-18), p. 1238-1239
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.abo1973
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2022
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
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