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  • 1
    Online Resource
    Online Resource
    Synaptic Protein Degradation Underlies Destabilization of Retrieved Fear Memory
    American Association for the Advancement of Science (AAAS) ; 2008
    In:  Science Vol. 319, No. 5867 ( 2008-02-29), p. 1253-1256
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 319, No. 5867 ( 2008-02-29), p. 1253-1256
    Abstract: Reactivated memory undergoes a rebuilding process that depends on de novo protein synthesis. This suggests that retrieval is dynamic and serves to incorporate new information into preexisting memories. However, little is known about whether or not protein degradation is involved in the reorganization of retrieved memory. We found that postsynaptic proteins were degraded in the hippocampus by polyubiquitination after retrieval of contextual fear memory. Moreover, the infusion of proteasome inhibitor into the CA1 region immediately after retrieval prevented anisomycin-induced memory impairment, as well as the extinction of fear memory. This suggests that ubiquitin- and proteasome-dependent protein degradation underlies destabilization processes after fear memory retrieval. It also provides strong evidence for the existence of reorganization processes whereby preexisting memory is disrupted by protein degradation, and updated memory is reconsolidated by protein synthesis.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.1150541
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2008
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  • 2
    Online Resource
    Online Resource
    The Orientia tsutsugamushi genome reveals massive proliferation of conjugative type IV secretion system and host–cell interaction genes
    Proceedings of the National Academy of Sciences ; 2007
    In:  Proceedings of the National Academy of Sciences Vol. 104, No. 19 ( 2007-05-08), p. 7981-7986
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 104, No. 19 ( 2007-05-08), p. 7981-7986
    Abstract: Scrub typhus is caused by the obligate intracellular rickettsia Orientia tsutsugamushi (previously called Rickettsia tsutsugamushi ). The bacterium is maternally inherited in trombicuid mites and transmitted to humans by feeding larvae. We report here the 2,127,051-bp genome of the Boryong strain, which represents the most highly repeated bacterial genome sequenced to date. The repeat density of the scrub typhus pathogen is 200-fold higher than that of its close relative Rickettsia prowazekii , the agent of epidemic typhus. A total of 359 tra genes for components of conjugative type IV secretion systems were identified at 79 sites in the genome. Associated with these are 〉 200 genes for signaling and host–cell interaction proteins, such as histidine kinases, ankyrin-repeat proteins, and tetratrico peptide-repeat proteins. Additionally, the O. tsutsugamushi genome contains 〉 400 transposases, 60 phage integrases, and 70 reverse transcriptases. Deletions and rearrangements have yielded unique gene combinations as well as frequent pseudogenization in the tra clusters. A comparative analysis of the tra clusters within the genome and across strains indicates sequence homogenization by gene conversion, whereas complexity, diversity, and pseudogenization are acquired by duplications, deletions, and transposon integrations into the amplified segments. The results suggest intragenomic duplications or multiple integrations of a massively proliferating conjugative transfer system. Diversifying selection on host–cell interaction genes along with repeated population bottlenecks may drive rare genome variants to fixation, thereby short-circuiting selection for low complexity in bacterial genomes.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.0611553104
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2007
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    SSG: 11
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Effects of Exercise on Cyclooxygenase‐2 Expression and Nuclear Factor‐κB DNA Binding in Human Peripheral Blood Mononuclear Cells
    Wiley ; 2009
    In:  Annals of the New York Academy of Sciences Vol. 1171, No. 1 ( 2009-08), p. 464-471
    Details
    In: Annals of the New York Academy of Sciences, Wiley, Vol. 1171, No. 1 ( 2009-08), p. 464-471
    Abstract: There are multiple lines of compelling evidence supporting the beneficial effect of exercise on the prevention and/or improvement of certain chronic diseases. However, exhaustive or intense exercise causes oxygen free radical generation and oxidative stress, which can lead to injuries and chronic fatigue as well as inflammation. Abnormal upregulation of cyclooxygenase‐2 (COX‐2), a rate‐limiting enzyme in prostaglandin biosynthesis, has been implicated in many inflammation‐associated chronic disorders. Nuclear factor‐κB (NF‐κB) is a major transcription factor involved in regulation of COX‐2 gene expression. To determine whether inflammation induction is dependent on intensity of exercise, COX‐2 expression and NF‐κB activation were adopted as the main targets. Thirteen volunteers who participated in the exercise program were subject to four exercise intensities [40, 60, 80, and 100% of heart rate reserve (HRR)] on a treadmill and to resting conditions. Isolated human peripheral blood mononuclear cells (PBMCs) were collected during the resting state and immediately after exercise and subjected to the electrophoretic mobility gel shift assay and Western blot analysis. As exercise intensity increased, both COX‐2 expression and NF‐κB DNA‐binding activity were enhanced. The expression of IκB kinase α (IKKα) and IκBα were not significantly altered. However, exhaustive/vigorous exercise (100% HRR) could induce the phosphorylation of both IKKα and IκBα. In conclusion, a single bout of exercise induced COX‐2 expression and DNA‐binding activity of NF‐κB in human PBMCs, and both COX‐2 expression and DNA‐binding activity of NF‐κB were dependent on exercise intensity.
    Type of Medium: Online Resource
    ISSN: 0077-8923 , 1749-6632
    URL: Issue
    URL: Article
    DOI: 10.1111/nyas.2009.1171.issue-1
    DOI: 10.1111/j.1749-6632.2009.04915.x
    RVK:
    TD 7650
    Language: English
    Publisher: Wiley
    Publication Date: 2009
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  • 4
    Online Resource
    Online Resource
    Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD + Biosynthesis
    American Association for the Advancement of Science (AAAS) ; 2009
    In:  Science Vol. 324, No. 5927 ( 2009-05), p. 651-654
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 324, No. 5927 ( 2009-05), p. 651-654
    Abstract: The circadian clock is encoded by a transcription-translation feedback loop that synchronizes behavior and metabolism with the light-dark cycle. Here we report that both the rate-limiting enzyme in mammalian nicotinamide adenine dinucleotide (NAD + ) biosynthesis, nicotinamide phosphoribosyltransferase (NAMPT), and levels of NAD + display circadian oscillations that are regulated by the core clock machinery in mice. Inhibition of NAMPT promotes oscillation of the clock gene Per2 by releasing CLOCK:BMAL1 from suppression by SIRT1. In turn, the circadian transcription factor CLOCK binds to and up-regulates Nampt , thus completing a feedback loop involving NAMPT/NAD + and SIRT1/CLOCK:BMAL1.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.1171641
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2009
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    SSG: 11
    Location Call Number Limitation Availability
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  • 5
    Online Resource
    Online Resource
    CIB1 functions as a Ca 2+ -sensitive modulator of stress-induced signaling by targeting ASK1
    Proceedings of the National Academy of Sciences ; 2009
    In:  Proceedings of the National Academy of Sciences Vol. 106, No. 41 ( 2009-10-13), p. 17389-17394
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 106, No. 41 ( 2009-10-13), p. 17389-17394
    Abstract: Calcium and integrin binding protein 1 (CIB1) is a Ca 2+ -binding protein of 22 kDa that was initially identified as a protein that interacts with integrin α IIb . Although it interacts with various proteins and has been implicated in diverse cellular functions, the molecular mechanism by which CIB1 regulates intracellular signaling networks has remained unclear. We now show that, by targeting apoptosis signal-regulating kinase 1 (ASK1), CIB1 negatively regulates stress-activated MAPK signaling pathways. CIB1 was thus shown to bind to ASK1, to interfere with the recruitment of TRAF2 to ASK1, and to inhibit the autophosphorylation of ASK1 on threonine-838, thereby blocking ASK1 activation. Furthermore, CIB1 mitigated apoptotic cell death initiated either by TNF-α in breast cancer MCF7 cells or by 6-hydroxydopamine (6-OHDA) in dopaminergic cells. Ca 2+ influx induced by membrane depolarization reversed the inhibitory effect of CIB1 on 6-OHDA-induced ASK1 activation and cell death in dopaminergic neurons. These observations thus suggest that CIB1 functions as a Ca 2+ -sensitive negative regulator of ASK1-mediated signaling events.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.0812259106
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2009
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    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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