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  • 1
    Publication Date: 2004-05-29
    Description: Cytokinesis is the essential process that partitions cellular contents into daughter cells. To identify and characterize cytokinesis proteins rapidly, we used a functional proteomic and comparative genomic strategy. Midbodies were isolated from mammalian cells, proteins were identified by multidimensional protein identification technology (MudPIT), and protein function was assessed in Caenorhabditis elegans. Of 172 homologs disrupted by RNA interference, 58% displayed defects in cleavage furrow formation or completion, or germline cytokinesis. Functional dissection of the midbody demonstrated the importance of lipid rafts and vesicle trafficking pathways in cytokinesis, and the utilization of common membrane cytoskeletal components in diverse morphogenetic events in the cleavage furrow, the germline, and neurons.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3679889/" 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/PMC3679889/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skop, Ahna R -- Liu, Hongbin -- Yates, John 3rd -- Meyer, Barbara J -- Heald, Rebecca -- F32 GM064159/GM/NIGMS NIH HHS/ -- F32 GM064159-01/GM/NIGMS NIH HHS/ -- F32 GM064159-02/GM/NIGMS NIH HHS/ -- F32 GM064159-03/GM/NIGMS NIH HHS/ -- F32 GM64159-01/GM/NIGMS NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- RR1823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):61-6. Epub 2004 May 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA. skop@wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Caenorhabditis elegans/cytology/genetics/physiology ; Carrier Proteins/analysis/isolation & purification/physiology ; Cell Cycle/physiology ; *Cell Division ; Cell Fractionation ; Cell Membrane/physiology ; Computational Biology ; Cricetinae ; Cytoskeletal Proteins/analysis/isolation & purification/physiology ; Cytoskeleton/physiology ; Germ Cells/physiology ; HeLa Cells ; Humans ; Membrane Microdomains/physiology ; Morphogenesis ; Organelles/chemistry/*physiology ; Protein Transport ; Proteins/analysis/isolation & purification/*physiology ; Proteome/*analysis ; Proteomics ; Signal Transduction ; Spindle Apparatus/physiology/ultrastructure
    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: 2003-11-01
    Description: We describe a new molecular class of genetic-pairing system that has a native DNA backbone but has all four base pairs replaced by new, larger pairs. The base pairs include size-expanded analogs of thymine and of adenine, both extended by the width of a benzene ring (2.4 A). The expanded-diameter double helices are more thermodynamically stable than the Watson-Crick helix, likely because of enhanced base stacking. Structural data confirm a right-handed, double-stranded, and base-paired helical form. Because of the larger base size, all the pairs of this helical system are fluorescent, which suggests practical applications in detection of natural DNA and RNA. Our findings establish that there is no apparent structural or thermodynamic prohibition against genetic systems having sizes different from the natural one.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Haibo -- Gao, Jianmin -- Lynch, Stephen R -- Saito, Y David -- Maynard, Lystranne -- Kool, Eric T -- GM52956/GM/NIGMS NIH HHS/ -- GM63587/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):868-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305-5080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593180" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*analogs & derivatives/chemistry ; *Base Pairing ; Base Sequence ; Benzene/chemistry ; Circular Dichroism ; Hydrogen Bonding ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; *Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Nucleic Acid Hybridization ; Oligodeoxyribonucleotides/*chemistry ; Temperature ; Thermodynamics ; Thymine/*analogs & derivatives/chemistry
    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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  • 3
    Publication Date: 2019-06-27
    Description: Crack growths were measured at elevated temperatures under four types of loading: pp, pc, cp, and cc. In H-13 steel, all these four types of loading gave nearly the same crack growth rates, and the length of hold time had negligible effects. In AISI 316 stainless steel, the hold time effects on crack growth rate were negligible if the loading was tension-tension type; however, these effects were significant in reversed bending load, and the crack growth rates under these four types of loading varied considerably. Both tensile and compressive hold times caused increased crack growth rate, but the compressive hold period was more deleterious than the tensile one. Metallographic examination showed that all the crack paths under different types of loading were largely transgranular for both CTS tension-tension specimens and SEN reversed cantilever bending specimens. In addition, an electric potential technique was used to monitor crack growth at elevated temperature.
    Keywords: METALLIC MATERIALS
    Type: NASA-CR-135105 , MTS-HWL-4116-776
    Format: application/pdf
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