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  • 1
    Publication Date: 2014-04-05
    Description: A correlation between allochthonous units exposed in the NW Iberian Massif and the southern Armorican Massif is carried out based on lithological associations, structural position, age and geochemistry of protoliths and tectonometamorphic evolution. The units on both sides of the Bay of Biscay are grouped into Upper, Middle and Lower allochthons, whereas an underlying allochthonous thrust sheet identified in both massifs is referred to as the Parautochthon. The Lower Allochthon represents a fragment of the outermost edge of Gondwana that underwent continental subduction shortly after the closure of a Palaeozoic ocean which, in turn, is represented by the Middle Allochthon. The latter consists of supra-subduction ophiolites and metasedimentary sequences alternating with basic, mid-ocean ridge basalt (MORB)-type volcanics, with inheritances suggesting the proximity of a continental domain. Seafloor spreading began at the Cambro-Ordovician boundary and oceanic crust was still formed during the Late Devonian, covering the lifetime of the Rheic Ocean, which is possibly represented by the Middle Allochthon. The opening of the oceanic domain was related to pulling apart the peri-Gondwanan continental magmatic arc, which is represented by the Upper Allochthon.
    Print ISSN: 0305-8719
    Electronic ISSN: 2041-4927
    Topics: Geosciences
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  • 2
    Publication Date: 2002-06-01
    Description: The high degree of similarity between the mouse and human genomes is demonstrated through analysis of the sequence of mouse chromosome 16 (Mmu 16), which was obtained as part of a whole-genome shotgun assembly of the mouse genome. The mouse genome is about 10% smaller than the human genome, owing to a lower repetitive DNA content. Comparison of the structure and protein-coding potential of Mmu 16 with that of the homologous segments of the human genome identifies regions of conserved synteny with human chromosomes (Hsa) 3, 8, 12, 16, 21, and 22. Gene content and order are highly conserved between Mmu 16 and the syntenic blocks of the human genome. Of the 731 predicted genes on Mmu 16, 509 align with orthologs on the corresponding portions of the human genome, 44 are likely paralogous to these genes, and 164 genes have homologs elsewhere in the human genome; there are 14 genes for which we could find no human counterpart.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mural, Richard J -- Adams, Mark D -- Myers, Eugene W -- Smith, Hamilton O -- Miklos, George L Gabor -- Wides, Ron -- Halpern, Aaron -- Li, Peter W -- Sutton, Granger G -- Nadeau, Joe -- Salzberg, Steven L -- Holt, Robert A -- Kodira, Chinnappa D -- Lu, Fu -- Chen, Lin -- Deng, Zuoming -- Evangelista, Carlos C -- Gan, Weiniu -- Heiman, Thomas J -- Li, Jiayin -- Li, Zhenya -- Merkulov, Gennady V -- Milshina, Natalia V -- Naik, Ashwinikumar K -- Qi, Rong -- Shue, Bixiong Chris -- Wang, Aihui -- Wang, Jian -- Wang, Xin -- Yan, Xianghe -- Ye, Jane -- Yooseph, Shibu -- Zhao, Qi -- Zheng, Liansheng -- Zhu, Shiaoping C -- Biddick, Kendra -- Bolanos, Randall -- Delcher, Arthur L -- Dew, Ian M -- Fasulo, Daniel -- Flanigan, Michael J -- Huson, Daniel H -- Kravitz, Saul A -- Miller, Jason R -- Mobarry, Clark M -- Reinert, Knut -- Remington, Karin A -- Zhang, Qing -- Zheng, Xiangqun H -- Nusskern, Deborah R -- Lai, Zhongwu -- Lei, Yiding -- Zhong, Wenyan -- Yao, Alison -- Guan, Ping -- Ji, Rui-Ru -- Gu, Zhiping -- Wang, Zhen-Yuan -- Zhong, Fei -- Xiao, Chunlin -- Chiang, Chia-Chien -- Yandell, Mark -- Wortman, Jennifer R -- Amanatides, Peter G -- Hladun, Suzanne L -- Pratts, Eric C -- Johnson, Jeffery E -- Dodson, Kristina L -- Woodford, Kerry J -- Evans, Cheryl A -- Gropman, Barry -- Rusch, Douglas B -- Venter, Eli -- Wang, Mei -- Smith, Thomas J -- Houck, Jarrett T -- Tompkins, Donald E -- Haynes, Charles -- Jacob, Debbie -- Chin, Soo H -- Allen, David R -- Dahlke, Carl E -- Sanders, Robert -- Li, Kelvin -- Liu, Xiangjun -- Levitsky, Alexander A -- Majoros, William H -- Chen, Quan -- Xia, Ashley C -- Lopez, John R -- Donnelly, Michael T -- Newman, Matthew H -- Glodek, Anna -- Kraft, Cheryl L -- Nodell, Marc -- Ali, Feroze -- An, Hui-Jin -- Baldwin-Pitts, Danita -- Beeson, Karen Y -- Cai, Shuang -- Carnes, Mark -- Carver, Amy -- Caulk, Parris M -- Center, Angela -- Chen, Yen-Hui -- Cheng, Ming-Lai -- Coyne, My D -- Crowder, Michelle -- Danaher, Steven -- Davenport, Lionel B -- Desilets, Raymond -- Dietz, Susanne M -- Doup, Lisa -- Dullaghan, Patrick -- Ferriera, Steven -- Fosler, Carl R -- Gire, Harold C -- Gluecksmann, Andres -- Gocayne, Jeannine D -- Gray, Jonathan -- Hart, Brit -- Haynes, Jason -- Hoover, Jeffery -- Howland, Tim -- Ibegwam, Chinyere -- Jalali, Mena -- Johns, David -- Kline, Leslie -- Ma, Daniel S -- MacCawley, Steven -- Magoon, Anand -- Mann, Felecia -- May, David -- McIntosh, Tina C -- Mehta, Somil -- Moy, Linda -- Moy, Mee C -- Murphy, Brian J -- Murphy, Sean D -- Nelson, Keith A -- Nuri, Zubeda -- Parker, Kimberly A -- Prudhomme, Alexandre C -- Puri, Vinita N -- Qureshi, Hina -- Raley, John C -- Reardon, Matthew S -- Regier, Megan A -- Rogers, Yu-Hui C -- Romblad, Deanna L -- Schutz, Jakob -- Scott, John L -- Scott, Richard -- Sitter, Cynthia D -- Smallwood, Michella -- Sprague, Arlan C -- Stewart, Erin -- Strong, Renee V -- Suh, Ellen -- Sylvester, Karena -- Thomas, Reginald -- Tint, Ni Ni -- Tsonis, Christopher -- Wang, Gary -- Wang, George -- Williams, Monica S -- Williams, Sherita M -- Windsor, Sandra M -- Wolfe, Keriellen -- Wu, Mitchell M -- Zaveri, Jayshree -- Chaturvedi, Kabir -- Gabrielian, Andrei E -- Ke, Zhaoxi -- Sun, Jingtao -- Subramanian, Gangadharan -- Venter, J Craig -- Pfannkoch, Cynthia M -- Barnstead, Mary -- Stephenson, Lisa D -- New York, N.Y. -- Science. 2002 May 31;296(5573):1661-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Celera Genomics, 45 West Gude Drive, Rockville, MD 20850, USA. richard.mural@celera.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040188" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Chromosomes/*genetics ; Chromosomes, Human/genetics ; Computational Biology ; Conserved Sequence ; Databases, Nucleic Acid ; Evolution, Molecular ; Genes ; Genetic Markers ; *Genome ; *Genome, Human ; Genomics ; Humans ; Mice ; Mice, Inbred A/genetics ; Mice, Inbred DBA/genetics ; Mice, Inbred Strains/*genetics ; Molecular Sequence Data ; Physical Chromosome Mapping ; Proteins/chemistry/genetics ; Sequence Alignment ; *Sequence Analysis, DNA ; Species Specificity ; *Synteny
    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: 2002-10-05
    Description: Anopheles gambiae is the principal vector of malaria, a disease that afflicts more than 500 million people and causes more than 1 million deaths each year. Tenfold shotgun sequence coverage was obtained from the PEST strain of A. gambiae and assembled into scaffolds that span 278 million base pairs. A total of 91% of the genome was organized in 303 scaffolds; the largest scaffold was 23.1 million base pairs. There was substantial genetic variation within this strain, and the apparent existence of two haplotypes of approximately equal frequency ("dual haplotypes") in a substantial fraction of the genome likely reflects the outbred nature of the PEST strain. The sequence produced a conservative inference of more than 400,000 single-nucleotide polymorphisms that showed a markedly bimodal density distribution. Analysis of the genome sequence revealed strong evidence for about 14,000 protein-encoding transcripts. Prominent expansions in specific families of proteins likely involved in cell adhesion and immunity were noted. An expressed sequence tag analysis of genes regulated by blood feeding provided insights into the physiological adaptations of a hematophagous insect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holt, Robert A -- Subramanian, G Mani -- Halpern, Aaron -- Sutton, Granger G -- Charlab, Rosane -- Nusskern, Deborah R -- Wincker, Patrick -- Clark, Andrew G -- Ribeiro, Jose M C -- Wides, Ron -- Salzberg, Steven L -- Loftus, Brendan -- Yandell, Mark -- Majoros, William H -- Rusch, Douglas B -- Lai, Zhongwu -- Kraft, Cheryl L -- Abril, Josep F -- Anthouard, Veronique -- Arensburger, Peter -- Atkinson, Peter W -- Baden, Holly -- de Berardinis, Veronique -- Baldwin, Danita -- Benes, Vladimir -- Biedler, Jim -- Blass, Claudia -- Bolanos, Randall -- Boscus, Didier -- Barnstead, Mary -- Cai, Shuang -- Center, Angela -- Chaturverdi, Kabir -- Christophides, George K -- Chrystal, Mathew A -- Clamp, Michele -- Cravchik, Anibal -- Curwen, Val -- Dana, Ali -- Delcher, Art -- Dew, Ian -- Evans, Cheryl A -- Flanigan, Michael -- Grundschober-Freimoser, Anne -- Friedli, Lisa -- Gu, Zhiping -- Guan, Ping -- Guigo, Roderic -- Hillenmeyer, Maureen E -- Hladun, Susanne L -- Hogan, James R -- Hong, Young S -- Hoover, Jeffrey -- Jaillon, Olivier -- Ke, Zhaoxi -- Kodira, Chinnappa -- Kokoza, Elena -- Koutsos, Anastasios -- Letunic, Ivica -- Levitsky, Alex -- Liang, Yong -- Lin, Jhy-Jhu -- Lobo, Neil F -- Lopez, John R -- Malek, Joel A -- McIntosh, Tina C -- Meister, Stephan -- Miller, Jason -- Mobarry, Clark -- Mongin, Emmanuel -- Murphy, Sean D -- O'Brochta, David A -- Pfannkoch, Cynthia -- Qi, Rong -- Regier, Megan A -- Remington, Karin -- Shao, Hongguang -- Sharakhova, Maria V -- Sitter, Cynthia D -- Shetty, Jyoti -- Smith, Thomas J -- Strong, Renee -- Sun, Jingtao -- Thomasova, Dana -- Ton, Lucas Q -- Topalis, Pantelis -- Tu, Zhijian -- Unger, Maria F -- Walenz, Brian -- Wang, Aihui -- Wang, Jian -- Wang, Mei -- Wang, Xuelan -- Woodford, Kerry J -- Wortman, Jennifer R -- Wu, Martin -- Yao, Alison -- Zdobnov, Evgeny M -- Zhang, Hongyu -- Zhao, Qi -- Zhao, Shaying -- Zhu, Shiaoping C -- Zhimulev, Igor -- Coluzzi, Mario -- della Torre, Alessandra -- Roth, Charles W -- Louis, Christos -- Kalush, Francis -- Mural, Richard J -- Myers, Eugene W -- Adams, Mark D -- Smith, Hamilton O -- Broder, Samuel -- Gardner, Malcolm J -- Fraser, Claire M -- Birney, Ewan -- Bork, Peer -- Brey, Paul T -- Venter, J Craig -- Weissenbach, Jean -- Kafatos, Fotis C -- Collins, Frank H -- Hoffman, Stephen L -- R01AI44273/AI/NIAID NIH HHS/ -- U01AI48846/AI/NIAID NIH HHS/ -- U01AI50687/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):129-49.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Celera Genomics, 45 West Gude Drive, Rockville, MD 20850, USA. robert.holt@celera.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364791" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles/classification/*genetics/parasitology/physiology ; Biological Evolution ; Blood ; Chromosome Inversion ; Chromosomes, Artificial, Bacterial ; Computational Biology ; DNA Transposable Elements ; Digestion ; Drosophila melanogaster/genetics ; Enzymes/chemistry/genetics/metabolism ; Expressed Sequence Tags ; Feeding Behavior ; Gene Expression Regulation ; *Genes, Insect ; Genetic Variation ; *Genome ; Haplotypes ; Humans ; Insect Proteins/chemistry/genetics/physiology ; Insect Vectors/genetics/parasitology/physiology ; Malaria, Falciparum/transmission ; Molecular Sequence Data ; Mosquito Control ; Physical Chromosome Mapping ; Plasmodium falciparum/growth & development ; Polymorphism, Single Nucleotide ; Proteome ; *Sequence Analysis, DNA ; Species Specificity ; Transcription Factors/chemistry/genetics/physiology
    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: 2012-12-14
    Description: Highly charged iron (Fe(16+), here referred to as Fe XVII) produces some of the brightest X-ray emission lines from hot astrophysical objects, including galaxy clusters and stellar coronae, and it dominates the emission of the Sun at wavelengths near 15 angstroms. The Fe XVII spectrum is, however, poorly fitted by even the best astrophysical models. A particular problem has been that the intensity of the strongest Fe XVII line is generally weaker than predicted. This has affected the interpretation of observations by the Chandra and XMM-Newton orbiting X-ray missions, fuelling a continuing controversy over whether this discrepancy is caused by incomplete modelling of the plasma environment in these objects or by shortcomings in the treatment of the underlying atomic physics. Here we report the results of an experiment in which a target of iron ions was induced to fluoresce by subjecting it to femtosecond X-ray pulses from a free-electron laser; our aim was to isolate a key aspect of the quantum mechanical description of the line emission. Surprisingly, we find a relative oscillator strength that is unexpectedly low, differing by 3.6sigma from the best quantum mechanical calculations. Our measurements suggest that the poor agreement is rooted in the quality of the underlying atomic wavefunctions rather than in insufficient modelling of collisional processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernitt, S -- Brown, G V -- Rudolph, J K -- Steinbrugge, R -- Graf, A -- Leutenegger, M -- Epp, S W -- Eberle, S -- Kubicek, K -- Mackel, V -- Simon, M C -- Trabert, E -- Magee, E W -- Beilmann, C -- Hell, N -- Schippers, S -- Muller, A -- Kahn, S M -- Surzhykov, A -- Harman, Z -- Keitel, C H -- Clementson, J -- Porter, F S -- Schlotter, W -- Turner, J J -- Ullrich, J -- Beiersdorfer, P -- Lopez-Urrutia, J R Crespo -- England -- Nature. 2012 Dec 13;492(7428):225-8. doi: 10.1038/nature11627.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Kernphysik, 69117 Heidelberg, Germany. sven.bernitt@mpi-hd.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23235875" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2014-03-29
    Description: The preparation of cold molecules is of great importance in many contexts, such as fundamental physics investigations, high-resolution spectroscopy of complex molecules, cold chemistry and astrochemistry. One versatile and widely applied method to cool molecules is helium buffer-gas cooling in either a supersonic beam expansion or a cryogenic trap environment. Another more recent method applicable to trapped molecular ions relies on sympathetic translational cooling, through collisional interactions with co-trapped, laser-cooled atomic ions, into spatially ordered structures called Coulomb crystals, combined with laser-controlled internal-state preparation. Here we present experimental results on helium buffer-gas cooling of the rotational degrees of freedom of MgH(+) molecular ions, which have been trapped and sympathetically cooled in a cryogenic linear radio-frequency quadrupole trap. With helium collision rates of only about ten per second--that is, four to five orders of magnitude lower than in typical buffer-gas cooling settings--we have cooled a single molecular ion to a rotational temperature of 7.5(+0.9)(-0.7) kelvin, the lowest such temperature so far measured. In addition, by varying the shape of, or the number of atomic and molecular ions in, larger Coulomb crystals, or both, we have tuned the effective rotational temperature from about 7 kelvin to about 60 kelvin by changing the translational micromotion energy of the ions. The extremely low helium collision rate may allow for sympathetic sideband cooling of single molecular ions, and eventually make quantum-logic spectroscopy of buffer-gas-cooled molecular ions feasible. Furthermore, application of the present cooling scheme to complex molecular ions should enable single- or few-state manipulations of individual molecules of biological interest.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hansen, A K -- Versolato, O O -- Klosowski, L -- Kristensen, S B -- Gingell, A -- Schwarz, M -- Windberger, A -- Ullrich, J -- Lopez-Urrutia, J R Crespo -- Drewsen, M -- England -- Nature. 2014 Apr 3;508(7494):76-9. doi: 10.1038/nature12996. Epub 2014 Mar 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Danish National Research Foundation Center for Quantum Optics - QUANTOP, Department of Physics and Astronomy, Aarhus University, DK-8000 Aarhus C, Denmark. ; Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, D-69117 Heidelberg, Germany. ; Institute of Physics, Faculty of Physics, Astronomy and Informatics, Nicolaus Copernicus University, Grudziadzka 5, 87-100 Torun, Poland. ; 1] Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, D-69117 Heidelberg, Germany [2] Physikalisch-Technische Bundesanstalt, Bundesallee 100, D-38116 Braunschweig, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24670662" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
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  • 6
    Publication Date: 1995-05-19
    Description: Excitation-contraction coupling was studied in mammalian cardiac cells in which the opening probability of L-type calcium (Ca2+) channels was reduced. Confocal microscopy during voltage-clamp depolarization revealed distinct local transients in the concentration of intracellular calcium ions ([Ca2+]i). When voltage was varied, the latency to occurrence and the relative probability of occurrence of local [Ca2+]i transients varied as predicted if Ca2+ release from the sarcoplasmic reticulum (SR) was linked tightly to Ca2+ flux through L-type Ca2+ channels but not to that through the Na-Ca exchanger or to average [Ca2+]i. Voltage had no effect on the amplitude of local [Ca2+]i transients. Thus, the most efficacious "Ca2+ signal" for activating Ca2+ release from the SR may be a transient microdomain of high [Ca2+]i beneath an individual, open L-type Ca2+ channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez-Lopez, J R -- Shacklock, P S -- Balke, C W -- Wier, W G -- HL02466/HL/NHLBI NIH HHS/ -- HL29473/HL/NHLBI NIH HHS/ -- HL50435/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 May 19;268(5213):1042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Maryland, School of Medicine, Baltimore 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium Channels/drug effects/*physiology ; Electric Stimulation ; Guinea Pigs ; In Vitro Techniques ; Ion Channel Gating/physiology ; Membrane Potentials/physiology ; Microscopy, Confocal ; Myocardium/*metabolism ; Patch-Clamp Techniques ; Probability ; Sarcoplasmic Reticulum/metabolism ; Verapamil/pharmacology
    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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  • 7
    Publication Date: 2015-03-15
    Description: Control over the motional degrees of freedom of atoms, ions, and molecules in a field-free environment enables unrivalled measurement accuracies but has yet to be applied to highly charged ions (HCIs), which are of particular interest to future atomic clock designs and searches for physics beyond the Standard Model. Here, we report on the Coulomb crystallization of HCIs (specifically (40)Ar(13+)) produced in an electron beam ion trap and retrapped in a cryogenic linear radiofrequency trap by means of sympathetic motional cooling through Coulomb interaction with a directly laser-cooled ensemble of Be(+) ions. We also demonstrate cooling of a single Ar(13+) ion by a single Be(+) ion-the prerequisite for quantum logic spectroscopy with a potential 10(-19) accuracy level. Achieving a seven-orders-of-magnitude decrease in HCI temperature starting at megakelvin down to the millikelvin range removes the major obstacle for HCI investigation with high-precision laser spectroscopy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmoger, L -- Versolato, O O -- Schwarz, M -- Kohnen, M -- Windberger, A -- Piest, B -- Feuchtenbeiner, S -- Pedregosa-Gutierrez, J -- Leopold, T -- Micke, P -- Hansen, A K -- Baumann, T M -- Drewsen, M -- Ullrich, J -- Schmidt, P O -- Lopez-Urrutia, J R Crespo -- New York, N.Y. -- Science. 2015 Mar 13;347(6227):1233-6. doi: 10.1126/science.aaa2960.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, 69117 Heidelberg, Germany. Physikalisch-Technische Bundesanstalt, Bundesallee 100, 38116 Braunschweig, Germany. ; Physikalisch-Technische Bundesanstalt, Bundesallee 100, 38116 Braunschweig, Germany. ; Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, 69117 Heidelberg, Germany. ; Physique des Interactions Ioniques et Moleculaires, Aix-Marseille Universite, 13397 Marseille, France. ; Department of Physics and Astronomy, Aarhus University, 8000 Aarhus C, Denmark. ; National Superconducting Cyclotron Laboratory (NSCL), Michigan State University, 640 S. Shaw Lane, East Lansing, MI 48824, USA. ; Physikalisch-Technische Bundesanstalt, Bundesallee 100, 38116 Braunschweig, Germany. Institut fur Quantenoptik, Leibniz Universitat Hannover, Welfengarten 1, 30167 Hannover, Germany. ; Max-Planck-Institut fur Kernphysik, Saupfercheckweg 1, 69117 Heidelberg, Germany. jose.crespo@mpi-hd.mpg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25766230" target="_blank"〉PubMed〈/a〉
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  • 8
    Publication Date: 2016-03-24
    Description: The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the core promoter. TFIID comprises the TATA-binding protein (TBP) and 13 TBP-associated factors (TAF1-13), which specifically interact with a variety of core promoter DNA sequences. Here we present the structure of human TFIID in complex with TFIIA and core promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution. All core promoter elements are contacted by subunits of TFIID, with TAF1 and TAF2 mediating major interactions with the downstream promoter. TFIIA bridges the TBP-TATA complex with lobe B of TFIID. We also present the cryo-electron microscopy reconstruction of a fully assembled human TAF-less PIC. Superposition of common elements between the two structures provides novel insights into the general role of TFIID in promoter recognition, PIC assembly, and transcription initiation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4856295/" 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/PMC4856295/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Louder, Robert K -- He, Yuan -- Lopez-Blanco, Jose Ramon -- Fang, Jie -- Chacon, Pablo -- Nogales, Eva -- GM008295/GM/NIGMS NIH HHS/ -- GM63072/GM/NIGMS NIH HHS/ -- R01 GM063072/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2016 Mar 31;531(7596):604-9. doi: 10.1038/nature17394. Epub 2016 Mar 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biophysics Graduate Group, University of California, Berkeley, California 94720, USA. ; QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA. ; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. ; Department of Biological Physical Chemistry, Rocasolano Physical Chemistry Institute, CSIC, Serrano 119, Madrid 28006, Spain. ; Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27007846" target="_blank"〉PubMed〈/a〉
    Keywords: Cryoelectron Microscopy ; DNA/chemistry/metabolism/ultrastructure ; Humans ; Models, Molecular ; Promoter Regions, Genetic/*genetics ; Protein Binding ; Substrate Specificity ; TATA Box/genetics ; TATA-Binding Protein Associated Factors/chemistry/metabolism/ultrastructure ; TATA-Box Binding Protein/chemistry/metabolism/ultrastructure ; Transcription Factor TFIIA/chemistry/metabolism/ultrastructure ; Transcription Factor TFIID/chemistry/*metabolism/*ultrastructure ; *Transcription Initiation, Genetic
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2016-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Louder, Robert K -- He, Yuan -- Lopez-Blanco, Jose Ramon -- Fang, Jie -- Chacon, Pablo -- Nogales, Eva -- Nature. 2016 Apr 20. doi: 10.1038/nature17984.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27096372" target="_blank"〉PubMed〈/a〉
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    Electronic ISSN: 1476-4687
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-10-02
    Description: The ability of vertebrae skeletal muscle to contract more vigorously than normal in the presence of potentiating agents depends on the initial length of a muscle cell. Other factors such as the intracellular calcium ion transient, temperature, chemical nature of the potentiating agent, and the ratio of intrinsic twitch to tetanic force influence the degree of contractile potentiation but cannot account for the length dependence. At least part of a muscle cell seems normally less than fully active during contractions not only at short lengths but also at optimal sarcomere lengths.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez, J R -- Wanek, L A -- Taylor, S R -- NS 14268/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 2;214(4516):79-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6974399" target="_blank"〉PubMed〈/a〉
    Keywords: Aequorin ; Animals ; Calcium/*physiology ; In Vitro Techniques ; *Muscle Contraction/drug effects ; Muscles/*physiology/ultrastructure ; Rana temporaria ; Temperature ; Zinc/pharmacology
    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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