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  • Articles  (7)
  • Animals  (3)
  • Templates, Genetic  (2)
  • [abr] ARS; autonomous replication sequence  (2)
  • 1
    Publication Date: 2002-11-02
    Description: The interaction of climate and the timing of low tides along the West Coast of the United States creates a complex mosaic of thermal environments, in which northern sites can be more thermally stressful than southern sites. Thus, climate change may not lead to a poleward shift in the distribution of intertidal organisms, as has been proposed, but instead will likely cause localized extinctions at a series of "hot spots." Patterns of exposure to extreme climatic conditions are temporally variable, and tidal predictions suggest that in the next 3 to 5 years "hot spots" are likely to appear at several northern sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmuth, Brian -- Harley, Christopher D G -- Halpin, Patricia M -- O'Donnell, Michael -- Hofmann, Gretchen E -- Blanchette, Carol A -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1015-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of South Carolina, Department of Biological Sciences and Marine Sciences Program, Columbia, SC 29208, USA. helmuth@biol.sc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411702" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bivalvia/*physiology ; *Body Temperature ; *Climate ; *Ecosystem ; Environment ; Geography ; Pacific Ocean ; Pacific States ; Seasons ; *Seawater ; Temperature ; *Water Movements
    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: 2010-01-30
    Description: In vivo studies suggest that replication forks are arrested by encounters with head-on transcription complexes. Yet, the fate of the replisome and RNA polymerase (RNAP) after a head-on collision is unknown. We found that the Escherichia coli replisome stalls upon collision with a head-on transcription complex, but instead of collapsing, the replication fork remains highly stable and eventually resumes elongation after displacing the RNAP from DNA. We also found that the transcription-repair coupling factor Mfd promotes direct restart of the fork after the collision by facilitating displacement of the RNAP. These findings demonstrate the intrinsic stability of the replication apparatus and a previously unknown role for the transcription-coupled repair pathway in promoting replication past a RNAP block.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2861996/" 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/PMC2861996/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pomerantz, Richard T -- O'Donnell, Mike -- R01 GM038839/GM/NIGMS NIH HHS/ -- R01 GM038839-23/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Jan 29;327(5965):590-2. doi: 10.1126/science.1179595.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110508" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/metabolism ; DNA Repair ; *DNA Replication ; DNA, Bacterial/*metabolism ; DNA-Directed DNA Polymerase/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/metabolism ; Templates, Genetic ; Transcription Factors/metabolism ; Transcription, Genetic
    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: 2011-12-24
    Description: Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the open clamp so that both the loader and the clamp match the helical symmetry of DNA. One structure reveals that ATP has been hydrolyzed in one subunit and suggests that clamp closure and ejection of the loader involves disruption of the ATP-dependent match in symmetry. The structures explain how synergy among the loader, the clamp, and DNA can trigger ATP hydrolysis and release of the closed clamp on DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281585/" 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/PMC3281585/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelch, Brian A -- Makino, Debora L -- O'Donnell, Mike -- Kuriyan, John -- F32 GM087888/GM/NIGMS NIH HHS/ -- F32 GM087888-02/GM/NIGMS NIH HHS/ -- F32-087888/PHS HHS/ -- R01 GM038839/GM/NIGMS NIH HHS/ -- R01 GM038839-26/GM/NIGMS NIH HHS/ -- R01 GM045547/GM/NIGMS NIH HHS/ -- R01 GM045547-20/GM/NIGMS NIH HHS/ -- R01-GM308839/GM/NIGMS NIH HHS/ -- R01-GM45547/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Dec 23;334(6063):1675-80. doi: 10.1126/science.1211884.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22194570" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Bacteriophage T4 ; Binding Sites ; Crystallography, X-Ray ; DNA, A-Form/*chemistry/metabolism ; DNA, Viral/*chemistry/metabolism ; DNA-Directed DNA Polymerase/chemistry/*metabolism ; Hydrolysis ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Static Electricity ; Templates, Genetic ; Trans-Activators/*chemistry/metabolism ; Viral Proteins/*chemistry/metabolism
    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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  • 4
    Publication Date: 2012-03-20
    Description: The conversion of chemical energy into mechanical force by AAA+ (ATPases associated with diverse cellular activities) ATPases is integral to cellular processes, including DNA replication, protein unfolding, cargo transport and membrane fusion. The AAA+ ATPase motor cytoplasmic dynein regulates ciliary trafficking, mitotic spindle formation and organelle transport, and dissecting its precise functions has been challenging because of its rapid timescale of action and the lack of cell-permeable, chemical modulators. Here we describe the discovery of ciliobrevins, the first specific small-molecule antagonists of cytoplasmic dynein. Ciliobrevins perturb protein trafficking within the primary cilium, leading to their malformation and Hedgehog signalling blockade. Ciliobrevins also prevent spindle pole focusing, kinetochore-microtubule attachment, melanosome aggregation and peroxisome motility in cultured cells. We further demonstrate the ability of ciliobrevins to block dynein-dependent microtubule gliding and ATPase activity in vitro. Ciliobrevins therefore will be useful reagents for studying cellular processes that require this microtubule motor and may guide the development of additional AAA+ ATPase superfamily inhibitors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3321072/" 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/PMC3321072/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Firestone, Ari J -- Weinger, Joshua S -- Maldonado, Maria -- Barlan, Kari -- Langston, Lance D -- O'Donnell, Michael -- Gelfand, Vladimir I -- Kapoor, Tarun M -- Chen, James K -- R01 CA136574/CA/NCI NIH HHS/ -- R01 GM038839/GM/NIGMS NIH HHS/ -- R01 GM052111/GM/NIGMS NIH HHS/ -- R01 GM052111-14/GM/NIGMS NIH HHS/ -- R01 GM065933/GM/NIGMS NIH HHS/ -- R01 GM52111/GM/NIGMS NIH HHS/ -- R01 GM65933/GM/NIGMS NIH HHS/ -- R01 GM71772/GM/NIGMS NIH HHS/ -- England -- Nature. 2012 Mar 18;484(7392):125-9. doi: 10.1038/nature10936.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, California 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22425997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cilia/drug effects/metabolism/pathology ; Cytoplasm/*enzymology ; Cytoplasmic Dyneins/*antagonists & inhibitors/metabolism ; Enzyme Inhibitors/*chemistry/*pharmacology ; Hedgehog Proteins/metabolism ; Kinetochores/drug effects/metabolism ; Kruppel-Like Transcription Factors/metabolism ; Melanosomes/drug effects/metabolism ; Mice ; Microtubules/drug effects/metabolism ; Molecular Weight ; Movement/drug effects ; NIH 3T3 Cells ; Peroxisomes/drug effects/physiology ; Protein Transport/drug effects ; Quinazolinones/*chemistry/*pharmacology ; Signal Transduction/drug effects ; Spindle Apparatus/drug effects/metabolism/pathology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1980-04-11
    Description: In cats anesthetized with chloralose-pentobarbital and artificially ventilated, electrical stimulation of the caudal end of the cut cervical vagus nerve has a biphasic effect on the bronchoconstriction induced by an intravenous infusion of serotonin. The response consists of a brief augmentation of bronchoconstriction followed by relatively prolonged bronchodilation. After muscarinic receptor blockade with atropine, vagal stimulation causes only bronchodilation. Vagally mediated bronchodilation is not affected by beta adrenergic blockade with propranolol, alpha adrenergic blockade with phenoxybenzamine, or adrenergic neuronal blockade with guanethidine, but is abolished by autonomic ganglionic blockade with hexamethonium. These findings support the conclusion that a nonadrenergic inhibitory nervous system is present in the pulmonary airways of the cat and that the system is supplied by preganglionic fibers in the cervical vagus nerves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diamond, L -- O'Donnell, M -- New York, N.Y. -- Science. 1980 Apr 11;208(4440):185-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7361114" target="_blank"〉PubMed〈/a〉
    Keywords: Airway Resistance/drug effects ; Animals ; Cats/anatomy & histology/*physiology ; Electric Stimulation ; Female ; Guanethidine/pharmacology ; Hexamethonium Compounds/pharmacology ; Lung/*innervation ; Lung Compliance/drug effects ; Neural Pathways/physiology ; Parasympathetic Nervous System/physiology ; Phenoxybenzamine/pharmacology ; Propranolol/pharmacology ; Serotonin/pharmacology ; Sympathetic Nervous System/physiology ; Vagotomy
    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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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Current Opinion in Genetics & Development 4 (1994), S. 185-195 
    ISSN: 0959-437X
    Keywords: [abr] ACS; ARS core consensus sequence ; [abr] ARS; autonomous replication sequence ; [abr] BPV; bovine papilloma virus ; [abr] HSV-1; herpes simplex virus 1 ; [abr] MCM; minichromosome maintenance ; [abr] ORC; origin recognition complex ; [abr] PCNA; proliferating cell nuclear antigen ; [abr] PP2A; protein phosphatase 2A ; [abr] RF-C; replication factor C ; [abr] RP-A; replication protein A ; [abr] SSB; single-stranded DNA-binding protein ; [abr] SV40; simian virus 40 ; [abr] pol/Pol; DNA polymerase ; [abr] snup; specialized nucleoprotein structure ; [abr] ssDNA; single-stranded DNA
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Current Opinion in Genetics & Development 4 (1994), S. 185-195 
    ISSN: 0959-437X
    Keywords: [abr] ACS; ARS core consensus sequence ; [abr] ARS; autonomous replication sequence ; [abr] BPV; bovine papilloma virus ; [abr] HSV-1; herpes simplex virus 1 ; [abr] MCM; minichromosome maintenance ; [abr] ORC; origin recognition complex ; [abr] PCNA; proliferating cell nuclear antigen ; [abr] PP2A; protein phosphatase 2A ; [abr] RF-C; replication factor C ; [abr] RP-A; replication protein A ; [abr] SSB; single-stranded DNA-binding protein ; [abr] SV40; simian virus 40 ; [abr] pol/Pol; DNA polymerase ; [abr] snup; specialized nucleoprotein structure ; [abr] ssDNA; single-stranded DNA
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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