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  • *Biodiversity  (1)
  • *Unfolded Protein Response  (1)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 2010-2014  (2)
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Publisher
  • American Association for the Advancement of Science (AAAS)  (2)
Years
  • 2010-2014  (2)
Year
  • 1
    Publication Date: 2012-06-30
    Description: Ricklefs and Renner (Reports, 27 January 2012, p. 464) found significant correlations for abundances and species diversities of families and orders of trees on different continents, which they suggested falsifies the neutral theory of biodiversity (NTB). We argue that the correlations among families and orders and the lack of correlations among genera can be explained by the NTB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Anping -- Wang, Shaopeng -- Pacala, Stephen W -- New York, N.Y. -- Science. 2012 Jun 29;336(6089):1639; author reply 1639. doi: 10.1126/science.1222534.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544, USA. anpingc@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22745403" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Biological Evolution ; *Ecosystem ; *Trees
    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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  • 2
    Publication Date: 2013-05-25
    Description: Newly synthesized polypeptides fold and assemble with assistance from protein chaperones. Full maturation can take multiple attempts, exchanging chaperones at each round. Improperly folded molecules must exit folding cycles and be degraded. In the endoplasmic reticulum (ER), prolonged substrate cycling is detrimental because it expends chaperone and energy resources and increases toxic reactive oxygen species. In budding yeast, we found that unfolded protein O-mannosylation terminated failed folding attempts through the Pmt1/Pmt2 complex. O-mannosylation incapacitated target molecule folding and removed them from folding cycles by reducing engagement with the Kar2 chaperone. In an in vitro protein refolding assay, the modification intrinsically and irreversibly disabled the folding potential of the substrate. Thus, protein folding termination can involve a covalent glycosylation event.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Chengchao -- Wang, Songyu -- Thibault, Guillaume -- Ng, Davis T W -- New York, N.Y. -- Science. 2013 May 24;340(6135):978-81. doi: 10.1126/science.1234055.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Temasek Life Sciences Laboratory, National University of Singapore, Singapore.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704572" target="_blank"〉PubMed〈/a〉
    Keywords: Endoplasmic Reticulum/*metabolism ; Fungal Proteins/*metabolism ; Glycosylation ; Green Fluorescent Proteins/metabolism ; HSP70 Heat-Shock Proteins/*metabolism ; Mannose/*metabolism ; Mannosyltransferases/genetics/metabolism ; *Protein Folding ; Saccharomyces cerevisiae/*metabolism ; *Unfolded Protein Response
    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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