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  • 1
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    Heterogeneity of cellular circadian clocks in intact plants and its correction under light-dark cycles (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-07-17
    Description: Recent advances in single-cell analysis have revealed the stochasticity and nongenetic heterogeneity inherent to cellular processes. However, our knowledge of the actual cellular behaviors in a living multicellular organism is still limited. By using a single-cell bioluminescence imaging technique on duckweed, Lemna gibba , we demonstrate that, under constant conditions, cells in the intact plant work as individual circadian clocks that oscillate with their own frequencies and respond independently to external stimuli. Quantitative analysis uncovered the heterogeneity and instability of cellular clocks and partial synchronization between neighboring cells. Furthermore, we found that cellular clocks in the plant body under light-dark cycles showed a centrifugal phase pattern in which the effect of cell-to-cell heterogeneity in period lengths was almost masked. The inherent heterogeneity in the properties of cellular clocks observed under constant conditions is corrected under light-dark cycles to coordinate the daily rhythms of the plant body. These findings provide a novel perspective of spatiotemporal architectures in the plant circadian system.
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Reciprocal regulation between TOC1 and LHY/CCA1 within the Arabidopsis circadian clock (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-04
    Description: The interactive regulation between clock genes is central for oscillator function. Here, we show interactions between the Arabidopsis clock genes LATE ELONGATED HYPOCOTYL (LHY), CIRCADIAN CLOCK ASSOCIATED 1 (CCA1), and TIMING OF CAB EXPRESSION 1 (TOC1). The MYB transcription factors LHY and CCA1 negatively regulate TOC1 expression. We show that both proteins bind to a region in the TOC1 promoter that is critical for its clock regulation. Conversely, TOC1 appears to participate in the positive regulation of LHY and CCA1 expression. Our results indicate that these interactions form a loop critical for clock function in Arabidopsis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alabadi, D -- Oyama, T -- Yanovsky, M J -- Harmon, F G -- Mas, P -- Kay, S A -- GM56006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 3;293(5531):880-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11486091" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*genetics/physiology ; *Arabidopsis Proteins ; Biological Clocks/genetics ; Circadian Rhythm/*genetics ; DNA-Binding Proteins/*genetics/metabolism ; *Gene Expression Regulation, Plant ; Genes, Plant ; Models, Genetic ; Plant Proteins/*genetics/metabolism ; Promoter Regions, Genetic ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Transcription Factors/*genetics/metabolism
    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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  • 3
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    Cloning of the Arabidopsis clock gene TOC1, an autoregulatory response regulator homolog (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: The toc1 mutation causes shortened circadian rhythms in light-grown Arabidopsis plants. Here, we report the same toc1 effect in the absence of light input to the clock. We also show that TOC1 controls photoperiodic flowering response through clock function. The TOC1 gene was isolated and found to encode a nuclear protein containing an atypical response regulator receiver domain and two motifs that suggest a role in transcriptional regulation: a basic motif conserved within the CONSTANS family of transcription factors and an acidic domain. TOC1 is itself circadianly regulated and participates in a feedback loop to control its own expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strayer, C -- Oyama, T -- Schultz, T F -- Raman, R -- Somers, D E -- Mas, P -- Panda, S -- Kreps, J A -- Kay, S A -- GM 56006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):768-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Arabidopsis/*genetics/physiology ; *Arabidopsis Proteins ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Cloning, Molecular ; DNA-Binding Proteins/chemistry/genetics/physiology ; Feedback ; Gene Expression Regulation, Plant ; Genes, Plant ; Molecular Sequence Data ; Mutation, Missense ; Phenotype ; Photoperiod ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Repetitive Sequences, Amino Acid ; Transcription Factors/chemistry/genetics/physiology ; Transcription, Genetic
    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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  • 4
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    Jet-launching structure resolved near the supermassive black hole in M87 (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-29
    Description: Approximately 10% of active galactic nuclei exhibit relativistic jets, which are powered by the accretion of matter onto supermassive black holes. Although the measured width profiles of such jets on large scales agree with theories of magnetic collimation, the predicted structure on accretion disk scales at the jet launch point has not been detected. We report radio interferometry observations, at a wavelength of 1.3 millimeters, of the elliptical galaxy M87 that spatially resolve the base of the jet in this source. The derived size of 5.5 +/- 0.4 Schwarzschild radii is significantly smaller than the innermost edge of a retrograde accretion disk, suggesting that the M87 jet is powered by an accretion disk in a prograde orbit around a spinning black hole.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doeleman, Sheperd S -- Fish, Vincent L -- Schenck, David E -- Beaudoin, Christopher -- Blundell, Ray -- Bower, Geoffrey C -- Broderick, Avery E -- Chamberlin, Richard -- Freund, Robert -- Friberg, Per -- Gurwell, Mark A -- Ho, Paul T P -- Honma, Mareki -- Inoue, Makoto -- Krichbaum, Thomas P -- Lamb, James -- Loeb, Abraham -- Lonsdale, Colin -- Marrone, Daniel P -- Moran, James M -- Oyama, Tomoaki -- Plambeck, Richard -- Primiani, Rurik A -- Rogers, Alan E E -- Smythe, Daniel L -- SooHoo, Jason -- Strittmatter, Peter -- Tilanus, Remo P J -- Titus, Michael -- Weintroub, Jonathan -- Wright, Melvyn -- Young, Ken H -- Ziurys, Lucy M -- New York, N.Y. -- Science. 2012 Oct 19;338(6105):355-8. doi: 10.1126/science.1224768. Epub 2012 Sep 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MIT Haystack Observatory, Off Route 40, Westford, MA 01886, USA. sdoeleman@haystack.mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23019611" 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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  • 5
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    Reconstitution of circadian oscillation of cyanobacterial KaiC phosphorylation in vitro (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-04-16
    Description: Kai proteins globally regulate circadian gene expression of cyanobacteria. The KaiC phosphorylation cycle, which persists even without transcription or translation, is assumed to be a basic timing process of the circadian clock. We have reconstituted the self-sustainable oscillation of KaiC phosphorylation in vitro by incubating KaiC with KaiA, KaiB, and adenosine triphosphate. The period of the in vitro oscillation was stable despite temperature change (temperature compensation), and the circadian periods observed in vivo in KaiC mutant strains were consistent with those measured in vitro. The enigma of the circadian clock can now be studied in vitro by examining the interactions between three Kai proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakajima, Masato -- Imai, Keiko -- Ito, Hiroshi -- Nishiwaki, Taeko -- Murayama, Yoriko -- Iwasaki, Hideo -- Oyama, Tokitaka -- Kondo, Takao -- New York, N.Y. -- Science. 2005 Apr 15;308(5720):414-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15831759" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate ; Bacterial Proteins/chemistry/genetics/*metabolism ; *Circadian Rhythm ; Circadian Rhythm Signaling Peptides and Proteins ; Genes, Bacterial ; Luminescence ; Mutation ; Phosphorylation ; Recombinant Proteins/chemistry/metabolism ; Synechococcus/genetics/*metabolism ; Temperature
    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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  • 6
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    The 2.8 A crystal structure of the dynein motor domain (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-03-09
    Description: Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 A resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kon, Takahide -- Oyama, Takuji -- Shimo-Kon, Rieko -- Imamula, Kenji -- Shima, Tomohiro -- Sutoh, Kazuo -- Kurisu, Genji -- England -- Nature. 2012 Mar 7;484(7394):345-50. doi: 10.1038/nature10955.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. takahide.kon@protein.osaka-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22398446" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Allosteric Regulation ; Binding Sites ; Crystallography, X-Ray ; Cytoplasmic Dyneins/*chemistry/metabolism ; Dictyostelium/*chemistry ; Hydrolysis ; Microtubules/metabolism ; Models, Biological ; Models, Molecular ; Movement ; Protein Structure, Tertiary ; Structure-Activity Relationship
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 7
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    Stereocomplex Poly(lactic acid) Alloys with Superb Heat Resistance and Toughness (2015)
    American Chemical Society (ACS)
    Details
    Publication Date: 2015-11-14
    Description: ACS Sustainable Chemistry & Engineering DOI: 10.1021/acssuschemeng.5b00832
    Electronic ISSN: 2168-0485
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Published by American Chemical Society (ACS)
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  • 8
    Electronic Resource
    Electronic Resource
    c-erbB-2 Gene Product Associates with Catenins in Human Cancer Cells
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 205 (1994), S. 73-78 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/bbrc.1994.2631
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  • 9
    Electronic Resource
    Electronic Resource
    Determination of baicalin and baicalein in rat plasma by high-performance liquid chromatography with electrochemical detection
    Amsterdam : Elsevier
    Journal of Chromatography B: Biomedical Sciences and Applications 575 (1992), S. 131-136 
    Details
    ISSN: 0378-4347
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0378-4347(92)80513-P
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  • 10
    Electronic Resource
    Electronic Resource
    Extraction-photometric determination of nitrite in fresh and sea water
    Amsterdam : Elsevier
    Analytica Chimica Acta 58 (1972), S. 228-230 
    Details
    ISSN: 0003-2670
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0003-2670(00)86875-0
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