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  • 1
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    Cytoplasmic volume modulates spindle size during embryogenesis (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-11-16
    Description: Rapid and reductive cell divisions during embryogenesis require that intracellular structures adapt to a wide range of cell sizes. The mitotic spindle presents a central example of this flexibility, scaling with the dimensions of the cell to mediate accurate chromosome segregation. To determine whether spindle size regulation is achieved through a developmental program or is intrinsically specified by cell size or shape, we developed a system to encapsulate cytoplasm from Xenopus eggs and embryos inside cell-like compartments of defined sizes. Spindle size was observed to shrink with decreasing compartment size, similar to what occurs during early embryogenesis, and this scaling trend depended on compartment volume rather than shape. Thus, the amount of cytoplasmic material provides a mechanism for regulating the size of intracellular structures.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4094345/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4094345/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Good, Matthew C -- Vahey, Michael D -- Skandarajah, Arunan -- Fletcher, Daniel A -- Heald, Rebecca -- GM074751/GM/NIGMS NIH HHS/ -- GM098766/GM/NIGMS NIH HHS/ -- R01 GM074751/GM/NIGMS NIH HHS/ -- R01 GM098766/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Nov 15;342(6160):856-60. doi: 10.1126/science.1243147.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California-Berkeley, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24233724" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cell Size ; Cytoplasm/chemistry/*physiology/ultrastructure ; *Embryonic Development ; Ovum ; Spindle Apparatus/chemistry/*physiology/ultrastructure ; Xenopus laevis
    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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    The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-21
    Description: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharyya, Roby P -- Remenyi, Attila -- Good, Matthew C -- Bashor, Caleb J -- Falick, Arnold M -- Lim, Wendell A -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424299" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*chemistry/genetics/*metabolism ; Allosteric Regulation ; Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; Down-Regulation ; Enzyme Activation ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Biological ; Models, Molecular ; Mutation ; Pheromones/*physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; 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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  • 3
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    Scaffold proteins: hubs for controlling the flow of cellular information (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-05-10
    Description: The spatial and temporal organization of molecules within a cell is critical for coordinating the many distinct activities carried out by the cell. In an increasing number of biological signaling processes, scaffold proteins have been found to play a central role in physically assembling the relevant molecular components. Although most scaffolds use a simple tethering mechanism to increase the efficiency of interaction between individual partner molecules, these proteins can also exert complex allosteric control over their partners and are themselves the target of regulation. Scaffold proteins offer a simple, flexible strategy for regulating selectivity in pathways, shaping output behaviors, and achieving new responses from preexisting signaling components. As a result, scaffold proteins have been exploited by evolution, pathogens, and cellular engineers to reshape cellular behavior.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117218/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117218/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Good, Matthew C -- Zalatan, Jesse G -- Lim, Wendell A -- P50 GM081879/GM/NIGMS NIH HHS/ -- P50 GM081879-01A2/GM/NIGMS NIH HHS/ -- P50 GM081879-02/GM/NIGMS NIH HHS/ -- P50GM081879/GM/NIGMS NIH HHS/ -- PN2 EY016546/EY/NEI NIH HHS/ -- PN2 EY016546-08/EY/NEI NIH HHS/ -- PN2EY016546/EY/NEI NIH HHS/ -- R01 GM055040/GM/NIGMS NIH HHS/ -- R01 GM055040-12/GM/NIGMS NIH HHS/ -- R01 GM062583/GM/NIGMS NIH HHS/ -- R01 GM062583-08/GM/NIGMS NIH HHS/ -- R01GM055040/GM/NIGMS NIH HHS/ -- R01GM062583/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 May 6;332(6030):680-6. doi: 10.1126/science.1198701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21551057" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Evolution, Molecular ; Feedback, Physiological ; Intracellular Signaling Peptides and Proteins/chemistry/*metabolism ; *Metabolic Networks and Pathways ; Protein Binding ; Protein Engineering ; Protein Folding ; Proteins/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction ; Synapses/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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  • 4
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    Observations of fast radio bursts at frequencies down to 400 megahertz (2019)
    Springer Nature
    In: Nature
    Details
    Publication Date: 2019
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 5
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    The form drag of two-dimensional bluff-plates immersed in turbulent boundary layers (1968)
    Cambridge University Press
    Details
    Publication Date: 1968-02-26
    Description: Measurements of the distributions of pressure on a bluff flat plate (fence) have been correlated with the characteristics of the smooth-wall boundary layer in which it is immersed. For zero pressure-gradient flows, correlations are obtained for the variation of form drag with plate heighthwhich are analogous in form to the ‘law of the wall’ and the ‘velocity-defect law’ for the boundary-layer velocity profile. The data for adverse pressure-gradient flows is suggestive of a ‘law of the wake’ type correlation. Pressures on the upstream face of the bluff-plate are determined by a wall-similarity law, even forh/δ 〉 1, and are independent of the pressure-gradient history of the flow; the separation induced upstream is apparently of the Stratford-Townsend type. The effects of the history of the boundary layer are manifested only in the flow in the rear separation bubble, and then only forh/δ 〉 ½. The base pressure is also sensitive to free-stream pressure gradients downstream of the bluff-plate. The relative extent of upstream influence of the bluff-plate on the boundary layer is found to increase rapidly ash/δ decreases. One set of measurements of the mean flow field is also presented.
    Print ISSN: 0022-1120
    Electronic ISSN: 1469-7645
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Published by Cambridge University Press
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