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  • Articles  (141)
  • *Biological Evolution  (49)
  • *Biodiversity  (47)
  • Protein Structure, Tertiary  (47)
  • 2015-2019
  • 2010-2014  (141)
  • 2010  (141)
  • Computer Science  (141)
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  • Articles  (141)
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  • 2015-2019
  • 2010-2014  (141)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-05-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2010 May 21;328(5981):969-71. doi: 10.1126/science.328.5981.969.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20489002" target="_blank"〉PubMed〈/a〉
    Keywords: *Animal Communication ; Animals ; *Biological Evolution ; Brain/anatomy & histology/physiology ; Child, Preschool ; Dominance, Cerebral ; *Gestures ; Hominidae/anatomy & histology/physiology ; Humans ; Infant ; *Language ; Language Development ; Sign Language ; Songbirds/anatomy & histology/physiology ; *Speech ; Vocalization, Animal
    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: 2010-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stroud, David A -- Meisinger, Chris -- Pfanner, Nikolaus -- Wiedemann, Nils -- New York, N.Y. -- Science. 2010 May 14;328(5980):831-2. doi: 10.1126/science.1190507.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biochemie und Molekularbiologie, ZBMZ, Trinationales Graduiertenkolleg 1478, Fakultat fur Biologie, and Centre for Biological Signalling Studies, Universitat Freiburg, 79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20466908" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/chemistry/*metabolism ; Carrier Proteins/metabolism ; Cell Membrane/*metabolism ; Chloroplasts/metabolism ; Escherichia coli/*metabolism ; Escherichia coli Proteins/chemistry/*metabolism ; Intracellular Membranes/metabolism ; Liposomes ; Mitochondria/metabolism ; Molecular Chaperones/chemistry/metabolism ; Multiprotein Complexes/chemistry/metabolism ; Peptidylprolyl Isomerase/metabolism ; Protein Folding ; Protein Precursors/chemistry/metabolism ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protein Transport
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tate, Christopher G -- New York, N.Y. -- Science. 2010 Jun 25;328(5986):1644-5. doi: 10.1126/science.1193065.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. cgt@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20576878" target="_blank"〉PubMed〈/a〉
    Keywords: Antiporters/*chemistry/genetics/metabolism ; Cell Membrane/*chemistry/metabolism ; Escherichia coli/*chemistry/metabolism ; Escherichia coli Proteins/chemistry/genetics/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Lipid Bilayers ; Membrane Transport Proteins/chemistry/metabolism ; Multiprotein Complexes/chemistry/metabolism ; Mutant Proteins/chemistry/metabolism ; Protein Engineering ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2010-11-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2010 Nov 5;330(6005):742-3. doi: 10.1126/science.330.6005.742.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21051603" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; Congresses as Topic ; Conservation of Natural Resources/economics ; Developing Countries ; Humans ; Intellectual Property ; *International Cooperation ; Policy ; Population Groups ; *United Nations
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2010-04-10
    Description: Arsenic, an ancient drug used in traditional Chinese medicine, has attracted worldwide interest because it shows substantial anticancer activity in patients with acute promyelocytic leukemia (APL). Arsenic trioxide (As2O3) exerts its therapeutic effect by promoting degradation of an oncogenic protein that drives the growth of APL cells, PML-RARalpha (a fusion protein containing sequences from the PML zinc finger protein and retinoic acid receptor alpha). PML and PML-RARalpha degradation is triggered by their SUMOylation, but the mechanism by which As2O3 induces this posttranslational modification is unclear. Here we show that arsenic binds directly to cysteine residues in zinc fingers located within the RBCC domain of PML-RARalpha and PML. Arsenic binding induces PML oligomerization, which increases its interaction with the small ubiquitin-like protein modifier (SUMO)-conjugating enzyme UBC9, resulting in enhanced SUMOylation and degradation. The identification of PML as a direct target of As2O3 provides new insights into the drug's mechanism of action and its specificity for APL.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Xiao-Wei -- Yan, Xiao-Jing -- Zhou, Zi-Ren -- Yang, Fei-Fei -- Wu, Zi-Yu -- Sun, Hong-Bin -- Liang, Wen-Xue -- Song, Ai-Xin -- Lallemand-Breitenbach, Valerie -- Jeanne, Marion -- Zhang, Qun-Ye -- Yang, Huai-Yu -- Huang, Qiu-Hua -- Zhou, Guang-Biao -- Tong, Jian-Hua -- Zhang, Yan -- Wu, Ji-Hui -- Hu, Hong-Yu -- de The, Hugues -- Chen, Sai-Juan -- Chen, Zhu -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):240-3. doi: 10.1126/science.1183424.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, Rui Jin Hospital affiliated to Shanghai Jiao Tong University School of Medicine, 197 Rui Jin Road II, Shanghai 200025, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378816" target="_blank"〉PubMed〈/a〉
    Keywords: Arsenic/*metabolism ; Arsenicals/*metabolism/*pharmacology ; Cell Line ; Humans ; Leukemia, Promyelocytic, Acute/drug therapy/genetics ; Mutant Proteins/chemistry/metabolism ; Mutation ; Nuclear Proteins/chemistry/genetics/*metabolism ; Oncogene Proteins, Fusion/chemistry/genetics/*metabolism ; Oxazines/metabolism ; Oxides/*metabolism/*pharmacology ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Retinoic Acid/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Transcription Factors/chemistry/genetics/*metabolism ; Tumor Suppressor Proteins/chemistry/genetics/*metabolism ; Ubiquitination ; Zinc Fingers
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beehler, Bruce M -- New York, N.Y. -- Science. 2010 Aug 20;329(5994):901. doi: 10.1126/science.329.5994.901-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20724618" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Wild ; *Biodiversity ; Indonesia ; Wit and Humor as Topic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Narbonne, Guy M -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):53-4. doi: 10.1126/science.1188688.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geological Sciences and Geological Engineering, Queen's University, Kingston, ON K7L 3N6, Canada. narbonne@geol.queensu.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20360098" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Carbon/analysis ; China ; Evolution, Chemical ; *Fossils ; Geologic Sediments/*chemistry ; Hydrogen Sulfide/analysis ; Iron/analysis ; Oceans and Seas ; Oxidation-Reduction ; Oxygen/analysis ; Seawater/*chemistry
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2010-10-12
    Description: Penguin feathers are highly modified in form and function, but there have been no fossils to inform their evolution. A giant penguin with feathers was recovered from the late Eocene (~36 million years ago) of Peru. The fossil reveals that key feathering features, including undifferentiated primary wing feathers and broad body contour feather shafts, evolved early in the penguin lineage. Analyses of fossilized color-imparting melanosomes reveal that their dimensions were similar to those of non-penguin avian taxa and that the feathering may have been predominantly gray and reddish-brown. In contrast, the dark black-brown color of extant penguin feathers is generated by large, ellipsoidal melanosomes previously unknown for birds. The nanostructure of penguin feathers was thus modified after earlier macrostructural modifications of feather shape linked to aquatic flight.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, Julia A -- Ksepka, Daniel T -- Salas-Gismondi, Rodolfo -- Altamirano, Ali J -- Shawkey, Matthew D -- D'Alba, Liliana -- Vinther, Jakob -- DeVries, Thomas J -- Baby, Patrice -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):954-7. doi: 10.1126/science.1193604. Epub 2010 Sep 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geological Sciences, University of Texas at Austin, Austin, TX 78712, USA. julia_clarke@jsg.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929737" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones/anatomy & histology ; Feathers/*anatomy & histology/ultrastructure ; *Fossils ; Melanosomes/ultrastructure ; Microscopy, Electron, Scanning ; Peru ; Phylogeny ; *Pigmentation ; Spheniscidae/*anatomy & histology/classification ; Wings, Animal/anatomy & histology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-07-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardenfors, Ulf -- New York, N.Y. -- Science. 2010 Jul 9;329(5988):140; author reply 141-2. doi: 10.1126/science.329.5988.140-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20616247" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Classification ; *Conservation of Natural Resources ; *Endangered Species ; Plants/*classification
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2010-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanukos, Anastasia -- Scotchmoor, Judith G -- Caldwell, Roy -- Lindberg, David R -- 51003439/Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Dec 24;330(6012):1764-5. doi: 10.1126/science.1186994. Epub 2010 Dec 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California Museum of Paleontology, University of California, Berkeley, Berkeley, CA 94720-4780, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21127217" target="_blank"〉PubMed〈/a〉
    Keywords: Awards and Prizes ; *Biological Evolution ; Biology/*education ; *Internet ; Science/*education ; Teaching ; *Teaching Materials
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
    Publication Date: 2010-02-13
    Description: The Ediacaran Period (635 to 542 million years ago) was a time of fundamental environmental and evolutionary change, culminating in the first appearance of macroscopic animals. Here, we present a detailed spatial and temporal record of Ediacaran ocean chemistry for the Doushantuo Formation in the Nanhua Basin, South China. We find evidence for a metastable zone of euxinic (anoxic and sulfidic) waters impinging on the continental shelf and sandwiched within ferruginous [Fe(II)-enriched] deep waters. A stratified ocean with coeval oxic, sulfidic, and ferruginous zones, favored by overall low oceanic sulfate concentrations, was maintained dynamically throughout the Ediacaran Period. Our model reconciles seemingly conflicting geochemical redox conditions proposed previously for Ediacaran deep oceans and helps to explain the patchy temporal record of early metazoan fossils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Chao -- Love, Gordon D -- Lyons, Timothy W -- Fike, David A -- Sessions, Alex L -- Chu, Xuelei -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):80-3. doi: 10.1126/science.1182369. Epub 2010 Feb 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, University of California, Riverside, CA 92521, USA. chaoli@ucr.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20150442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Carbonates/analysis ; China ; Ferrous Compounds/analysis ; *Fossils ; Geologic Sediments/*chemistry ; Hydrogen Sulfide ; Iron ; Oceans and Seas ; Oxidation-Reduction ; Oxygen/*analysis ; Seawater/*chemistry ; Sulfates/analysis
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):43. doi: 10.1126/science.328.5974.43.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20360089" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones/*anatomy & histology/radiography ; California ; Databases as Topic ; Humans ; Pan troglodytes/*anatomy & histology ; Skull/anatomy & histology ; Tomography, X-Ray Computed ; Universities
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-01-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Sebyung -- Douglas, Trevor -- New York, N.Y. -- Science. 2010 Jan 1;327(5961):42-3. doi: 10.1126/science.1184318.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and Center for Bio-Inspired Nanomaterials, Montana State University, Bozeman, MT 59717, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20044564" target="_blank"〉PubMed〈/a〉
    Keywords: Acetaldehyde/metabolism ; *Cell Compartmentation ; Crystallization ; Crystallography, X-Ray ; Cytosol/metabolism ; Escherichia coli/*chemistry/enzymology/*ultrastructure ; Escherichia coli Proteins/*chemistry/metabolism ; Ethanolamine/*metabolism ; Polyproteins/chemistry/metabolism ; Protein Folding ; Protein Structure, Tertiary
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 14
    Publication Date: 2010-02-06
    Description: Vesicular stomatitis virus (VSV) is a bullet-shaped rhabdovirus and a model system of negative-strand RNA viruses. Through direct visualization by means of cryo-electron microscopy, we show that each virion contains two nested, left-handed helices: an outer helix of matrix protein M and an inner helix of nucleoprotein N and RNA. M has a hub domain with four contact sites that link to neighboring M and N subunits, providing rigidity by clamping adjacent turns of the nucleocapsid. Side-by-side interactions between neighboring N subunits are critical for the nucleocapsid to form a bullet shape, and structure-based mutagenesis results support this description. Together, our data suggest a mechanism of VSV assembly in which the nucleocapsid spirals from the tip to become the helical trunk, both subsequently framed and rigidified by the M layer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2892700/" 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/PMC2892700/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Peng -- Tsao, Jun -- Schein, Stan -- Green, Todd J -- Luo, Ming -- Zhou, Z Hong -- AI050066/AI/NIAID NIH HHS/ -- AI069015/AI/NIAID NIH HHS/ -- GM071940/GM/NIGMS NIH HHS/ -- R01 AI050066/AI/NIAID NIH HHS/ -- R01 AI050066-08/AI/NIAID NIH HHS/ -- R01 AI069015/AI/NIAID NIH HHS/ -- R01 GM071940/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Feb 5;327(5966):689-93. doi: 10.1126/science.1181766.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Immunology, and Molecular Genetics, University of California at Los Angeles (UCLA), Los Angeles, CA 90095-7364, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20133572" target="_blank"〉PubMed〈/a〉
    Keywords: Cryoelectron Microscopy ; Crystallography, X-Ray ; Image Processing, Computer-Assisted ; Lipid Bilayers ; Models, Molecular ; Mutagenesis ; Nucleocapsid Proteins/*chemistry/genetics/ultrastructure ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; RNA, Viral/*chemistry/ultrastructure ; Vesiculovirus/*chemistry/physiology/*ultrastructure ; Viral Matrix Proteins/*chemistry/ultrastructure ; Virion/chemistry/ultrastructure ; Virus Assembly
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  • 15
    Publication Date: 2010-05-29
    Description: White and colleagues (Research Articles, 2 October 2009, pp. 64-106 and www.sciencemag.org/ardipithecus) reported Ardipithecus ramidus as an exclusive member of the human lineage post-African ape divergence. However, their analysis of shared-derived characters provides insufficient evidence of an ancestor-descendant relationship and exclusivity to the hominid lineage. Molecular and anatomical studies rather suggest that Ar. ramidus predates the human/African ape divergence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sarmiento, Esteban E -- New York, N.Y. -- Science. 2010 May 28;328(5982):1105; author reply 1105. doi: 10.1126/science.1184148.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Evolution Foundation, East Brunswick, NJ 08816, USA. este444@yahoo.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20508113" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bone and Bones/anatomy & histology ; *Fossils ; Hominidae/*anatomy & histology/*classification/physiology ; Humans ; Locomotion ; Paleodontology ; Time
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tirado, Reyes -- Johnston, Paul -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):170-1. doi: 10.1126/science.328.5975.170-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378798" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture/methods ; *Biodiversity ; Crops, Agricultural/*genetics ; Food Supply ; *Plants, Genetically Modified
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
    Publication Date: 2010-01-16
    Description: Integrins mediate cell adhesion to the extracellular matrix and transmit signals within the cell that stimulate cell spreading, retraction, migration, and proliferation. The mechanism of integrin outside-in signaling has been unclear. We found that the heterotrimeric guanine nucleotide-binding protein (G protein) Galpha13 directly bound to the integrin beta3 cytoplasmic domain and that Galpha13-integrin interaction was promoted by ligand binding to the integrin alphaIIbbeta3 and by guanosine triphosphate (GTP) loading of Galpha13. Interference of Galpha13 expression or a myristoylated fragment of Galpha13 that inhibited interaction of alphaIIbbeta3 with Galpha13 diminished activation of protein kinase c-Src and stimulated the small guanosine triphosphatase RhoA, consequently inhibiting cell spreading and accelerating cell retraction. We conclude that integrins are noncanonical Galpha13-coupled receptors that provide a mechanism for dynamic regulation of RhoA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2842917/" 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/PMC2842917/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, Haixia -- Shen, Bo -- Flevaris, Panagiotis -- Chow, Christina -- Lam, Stephen C-T -- Voyno-Yasenetskaya, Tatyana A -- Kozasa, Tohru -- Du, Xiaoping -- GM061454/GM/NIGMS NIH HHS/ -- GM074001/GM/NIGMS NIH HHS/ -- HL062350/HL/NHLBI NIH HHS/ -- HL068819/HL/NHLBI NIH HHS/ -- HL080264/HL/NHLBI NIH HHS/ -- R01 GM061454/GM/NIGMS NIH HHS/ -- R01 GM061454-09/GM/NIGMS NIH HHS/ -- R01 GM074001/GM/NIGMS NIH HHS/ -- R01 GM074001-02/GM/NIGMS NIH HHS/ -- R01 HL062350/HL/NHLBI NIH HHS/ -- R01 HL062350-09/HL/NHLBI NIH HHS/ -- R01 HL068819/HL/NHLBI NIH HHS/ -- R01 HL068819-08/HL/NHLBI NIH HHS/ -- R01 HL080264/HL/NHLBI NIH HHS/ -- R01 HL080264-04/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2010 Jan 15;327(5963):340-3. doi: 10.1126/science.1174779.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Illinois at Chicago, 835 South Wolcott Avenue, Room E403, Chicago, IL 60612, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20075254" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Blood Platelets/*physiology ; Clot Retraction ; Fibrinogen/metabolism ; GTP-Binding Protein alpha Subunits, G12-G13/genetics/*metabolism ; Humans ; Integrin beta3/*metabolism ; Ligands ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Platelet Adhesiveness ; Platelet Glycoprotein GPIIb-IIIa Complex/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; Proto-Oncogene Proteins pp60(c-src)/metabolism ; RNA, Small Interfering ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; rhoA GTP-Binding Protein/antagonists & inhibitors/metabolism
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  • 18
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghazoul, Jaboury -- New York, N.Y. -- Science. 2010 Sep 24;329(5999):1598. doi: 10.1126/science.329.5999.1598-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929828" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; New Guinea ; Trees/*classification ; Tropical Climate
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, Charles R -- New York, N.Y. -- Science. 2010 Sep 3;329(5996):1156-7. doi: 10.1126/science.1194924.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Biology, University of California Museum of Paleontology, University of California, Berkeley, Berkeley, CA 94720, USA. crmarshall@berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20813942" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Data Interpretation, Statistical ; *Databases, Factual ; *Ecosystem ; Extinction, Biological ; *Fossils ; Geography ; *Invertebrates ; Marine Biology ; Oceans and Seas ; *Paleontology ; Population Dynamics ; Time
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  • 20
    Publication Date: 2010-05-29
    Description: The mechanism by which multispanning helix-bundle membrane proteins are inserted into their target membrane remains unclear. In both prokaryotic and eukaryotic cells, membrane proteins are inserted cotranslationally into the lipid bilayer. Positively charged residues flanking the transmembrane helices are important topological determinants, but it is not known whether they act strictly locally, affecting only the nearest transmembrane helices, or can act globally, affecting the topology of the entire protein. Here we found that the topology of an Escherichia coli inner membrane protein with four or five transmembrane helices could be controlled by a single positively charged residue placed in different locations throughout the protein, including the very C terminus. This observation points to an unanticipated plasticity in membrane protein insertion mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seppala, Susanna -- Slusky, Joanna S -- Lloris-Garcera, Pilar -- Rapp, Mikaela -- von Heijne, Gunnar -- 232648/European Research Council/International -- New York, N.Y. -- Science. 2010 Jun 25;328(5986):1698-700. doi: 10.1126/science.1188950. Epub 2010 May 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20508091" target="_blank"〉PubMed〈/a〉
    Keywords: Antiporters/*chemistry/genetics/metabolism ; Cell Membrane/*chemistry ; Drug Resistance, Bacterial ; Escherichia coli/*chemistry/drug effects/growth & development/metabolism ; Escherichia coli Proteins/*chemistry/genetics/metabolism ; Ethidium/pharmacology ; Lipid Bilayers ; Membrane Transport Proteins/chemistry/metabolism ; Mutagenesis, Site-Directed ; Mutant Proteins/chemistry/metabolism ; Protein Conformation ; Protein Engineering ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 21
    Publication Date: 2010-11-13
    Description: CCA-adding enzymes [ATP(CTP):tRNA nucleotidyltransferases] add CCA onto the 3' end of transfer RNA (tRNA) precursors without using a nucleic acid template. Although the mechanism by which cytosine (C) is selected at position 75 of tRNA has been established, the mechanism by which adenine (A) is selected at position 76 remains elusive. Here, we report five cocrystal structures of the enzyme complexed with both a tRNA mimic and nucleoside triphosphates under catalytically active conditions. These structures suggest that adenosine 5'-monophosphate is incorporated onto the A76 position of the tRNA via a carboxylate-assisted, one-metal-ion mechanism with aspartate 110 functioning as a general base. The discrimination against incorporation of cytidine 5'-triphosphate (CTP) at position 76 arises from improper placement of the alpha phosphate of the incoming CTP, which results from the interaction of C with arginine 224 and prevents the nucleophilic attack by the 3' hydroxyl group of cytidine75.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087442/" 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/PMC3087442/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pan, Baocheng -- Xiong, Yong -- Steitz, Thomas A -- GM57510/GM/NIGMS NIH HHS/ -- R01 GM057510/GM/NIGMS NIH HHS/ -- R01 GM057510-13/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):937-40. doi: 10.1126/science.1194985.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21071662" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/chemistry/*metabolism ; Adenosine Monophosphate/metabolism ; Adenosine Triphosphate/chemistry/metabolism ; Archaeoglobus fulgidus/*enzymology ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Cytidine Triphosphate/metabolism ; Cytosine/chemistry/*metabolism ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; RNA Nucleotidyltransferases/*chemistry/*metabolism ; RNA, Transfer/chemistry/*metabolism
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohannon, John -- New York, N.Y. -- Science. 2010 Apr 2;328(5974):23-5. doi: 10.1126/science.328.5974.23.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20360072" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Commerce/legislation & jurisprudence ; *Conservation of Natural Resources/legislation & jurisprudence ; *Ecosystem ; Endangered Species ; Madagascar ; *Trees ; Wood
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  • 23
    Publication Date: 2010-06-26
    Description: The factors determining species commonness and rarity are poorly understood, particularly in highly diverse communities. Theory predicts that interactions with neighbors of the same (conspecific) and other (heterospecific) species can influence a species' relative abundance, but empirical tests are lacking. By using a hierarchical model of survival for more than 30,000 seedlings of 180 tropical tree species on Barro Colorado Island, Panama, we tested whether species' sensitivity to neighboring individuals relates to their relative abundance in the community. We found wide variation among species in the effect of conspecific, but not heterospecific, neighbors on survival, and we found a significant relationship between the strength of conspecific neighbor effects and species abundance. Specifically, rare species suffered more from the presence of conspecific neighbors than common species did, suggesting that conspecific density dependence shapes species abundances in diverse communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Comita, Liza S -- Muller-Landau, Helene C -- Aguilar, Salomon -- Hubbell, Stephen P -- New York, N.Y. -- Science. 2010 Jul 16;329(5989):330-2. doi: 10.1126/science.1190772. Epub 2010 Jun 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Ecological Analysis and Synthesis, 735 State Street, Suite 300, Santa Barbara, CA 93101, USA. comita@nceas.ucsb.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20576853" target="_blank"〉PubMed〈/a〉
    Keywords: Bayes Theorem ; *Biodiversity ; *Ecosystem ; Panama ; Population Density ; Seedlings/growth & development ; Species Specificity ; *Trees/growth & development ; *Tropical Climate
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  • 24
    Publication Date: 2010-09-18
    Description: Hybrids between species are often sterile or inviable because the long-diverged genomes of their parents cause developmental problems when they come together in a single individual. According to the Dobzhansky-Muller (DM) model, the number of genes involved in these "intrinsic postzygotic incompatibilities" should increase faster than linearly with the divergence time between species. This straightforward prediction of the DM model has remained contentious owing to a lack of explicit tests. Examining two pairs of Drosophila species, we show that the number of genes involved in postzygotic isolation increases at least as fast as the square of the number of substitutions (an index of divergence time) between species. This observation verifies a key prediction of the DM model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matute, Daniel R -- Butler, Ian A -- Turissini, David A -- Coyne, Jerry A -- R01GM058260/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Sep 17;329(5998):1518-21. doi: 10.1126/science.1193440.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolution, The University of Chicago, 1101 East 57th Street, Chicago, IL 60637, USA. dmatute@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20847270" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Crosses, Genetic ; Drosophila/*genetics/physiology ; Drosophila melanogaster/genetics/physiology ; Epistasis, Genetic ; Female ; *Genes, Insect ; *Genetic Speciation ; *Hybridization, Genetic ; Infertility ; Male ; Models, Genetic ; Reproduction ; Species Specificity
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-01-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boomsma, Jacobus J -- Pamilo, Pekka -- New York, N.Y. -- Science. 2010 Jan 1;327(5961):45. doi: 10.1126/science.1185061.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Copenhagen, Universitetsparken 15, 2100 Copenhagen, Denmark. jjboomsma@bio.ku.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20044566" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Australia ; Behavior, Animal ; *Biological Evolution ; History, 20th Century ; History, 21st Century ; *Insects/genetics/physiology ; Social Behavior
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, Robert M -- New York, N.Y. -- Science. 2010 Jul 2;329(5987):41-2. doi: 10.1126/science.1191058.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoology Department, University of Oxford, Oxford OX1 3PS, UK. robert.may@zoo.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20595603" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/*classification ; Beetles/classification ; *Biodiversity ; Classification/methods ; Genetic Speciation ; Models, Statistical ; New Guinea ; Probability ; Trees/classification ; *Tropical Climate ; Uncertainty
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  • 27
    Publication Date: 2010-10-23
    Description: The M2 protein from the influenza A virus, an acid-activated proton-selective channel, has been the subject of numerous conductance, structural, and computational studies. However, little is known at the atomic level about the heart of the functional mechanism for this tetrameric protein, a His(37)-Trp(41) cluster. We report the structure of the M2 conductance domain (residues 22 to 62) in a lipid bilayer, which displays the defining features of the native protein that have not been attainable from structures solubilized by detergents. We propose that the tetrameric His(37)-Trp(41) cluster guides protons through the channel by forming and breaking hydrogen bonds between adjacent pairs of histidines and through specific interactions of the histidines with the tryptophan gate. This mechanism explains the main observations on M2 proton conductance.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384994/" 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/PMC3384994/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharma, Mukesh -- Yi, Myunggi -- Dong, Hao -- Qin, Huajun -- Peterson, Emily -- Busath, David D -- Zhou, Huan-Xiang -- Cross, Timothy A -- AI023007/AI/NIAID NIH HHS/ -- R01 AI023007/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2010 Oct 22;330(6003):509-12. doi: 10.1126/science.1191750.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20966252" target="_blank"〉PubMed〈/a〉
    Keywords: Histidine/chemistry ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Influenza A virus/*chemistry/physiology ; Ion Channels/*chemistry ; Ion Transport ; Lipid Bilayers ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Conformation ; Protein Structure, Tertiary ; *Protons ; Tryptophan/chemistry ; Viral Matrix Proteins/*chemistry
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  • 28
    Publication Date: 2010-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kettle, Chris J -- Ghazoul, Jaboury -- Ashton, Peter S -- Cannon, Charles H -- Chong, Lucy -- Diway, Bibia -- Faridah, Eny -- Harrison, Rhett -- Hector, Andrew -- Hollingsworth, Pete -- Koh, Lian Pin -- Khoo, Eyen -- Kitayama, Kanehiro -- Kartawinata, Kuswata -- Marshall, Andrew J -- Maycock, Colin R -- Nanami, Satoshi -- Paoli, Gary -- Potts, Matthew D -- Sheil, Douglas -- Tan, Sylvester -- Tomoaki, Ichie -- Webb, Campbell -- Yamakura, Takuo -- Burslem, David F R P -- New York, N.Y. -- Science. 2010 Oct 29;330(6004):584. doi: 10.1126/science.330.6004.584-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21030629" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; Borneo ; *Conservation of Natural Resources/economics ; Endangered Species ; Financial Support ; *Seeds ; *Trees
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  • 29
    Publication Date: 2010-06-26
    Description: The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buschmann, Sabine -- Warkentin, Eberhard -- Xie, Hao -- Langer, Julian D -- Ermler, Ulrich -- Michel, Hartmut -- New York, N.Y. -- Science. 2010 Jul 16;329(5989):327-30. doi: 10.1126/science.1187303. Epub 2010 Jun 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biophysik, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20576851" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalytic Domain ; Crystallography, X-Ray ; Cytoplasm/metabolism ; Electron Transport ; Electron Transport Complex IV/*chemistry/*metabolism ; Heme/chemistry ; Histidine/chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Oxygen/metabolism ; Periplasm/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proton Pumps/*chemistry/*metabolism ; *Protons ; Pseudomonas stutzeri/*enzymology ; Tyrosine/chemistry
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2010 Oct 1;330(6000):24. doi: 10.1126/science.330.6000.24.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929783" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Birds ; *Conservation of Natural Resources/statistics & numerical data ; *Endangered Species/statistics & numerical data ; *Plants ; Sample Size ; Sampling Studies
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  • 31
    Publication Date: 2010-01-09
    Description: Large-scale biodiversity gradients among environments and habitats are usually attributed to a complex array of ecological and evolutionary factors. We tested the evolutionary component of such gradients by compiling the environments of the geologically oldest occurrences of marine genera and using sampling standardization to assess if originations tended to be clustered in particular environments. Shallow, tropical environments and carbonate substrates all tend to have harbored high origination rates. Diversity within these environments tended to be preferentially generated in reefs, probably because of their habitat complexity. Reefs were also prolific at exporting diversity to other environments, which might be a consequence of low-diversity habitats being more susceptible to invasions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kiessling, Wolfgang -- Simpson, Carl -- Foote, Michael -- New York, N.Y. -- Science. 2010 Jan 8;327(5962):196-8. doi: 10.1126/science.1182241.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum fur Naturkunde, Leibniz Institute for Research on Evolution and Biodiversity at the Humboldt University Berlin, 10115 Berlin, Germany. wolfgang.kiessling@mfn-berlin.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20056888" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa ; *Biodiversity ; *Biological Evolution ; Calcium Carbonate ; *Ecosystem ; Environment ; Fishes ; *Fossils ; Geography ; *Invertebrates/classification
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  • 32
    Publication Date: 2010-07-22
    Description: A substantial proportion of eukaryotic transcripts are considered to be noncoding RNAs because they contain only short open reading frames (sORFs). Recent findings suggest, however, that some sORFs encode small bioactive peptides. Here, we show that peptides of 11 to 32 amino acids encoded by the polished rice (pri) sORF gene control epidermal differentiation in Drosophila by modifying the transcription factor Shavenbaby (Svb). Pri peptides trigger the amino-terminal truncation of the Svb protein, which converts Svb from a repressor to an activator. Our results demonstrate that during Drosophila embryogenesis, Pri sORF peptides provide a strict temporal control to the transcriptional program of epidermal morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kondo, T -- Plaza, S -- Zanet, J -- Benrabah, E -- Valenti, P -- Hashimoto, Y -- Kobayashi, S -- Payre, F -- Kageyama, Y -- New York, N.Y. -- Science. 2010 Jul 16;329(5989):336-9. doi: 10.1126/science.1188158.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Okazaki Institute for Integrative Bioscience, National Institute for Basic Biology (NIBB), National Institutes of Natural Sciences, 5-1 Myodaiji-Higashiyama, Okazaki 444-8787, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20647469" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/embryology/*genetics/metabolism ; Embryo, Nonmammalian/cytology/*metabolism ; Embryonic Development ; Epidermis/cytology/metabolism ; *Gene Expression Regulation, Developmental ; Genes, Insect ; Mutation ; Open Reading Frames ; Peptides/genetics/*metabolism ; Protein Isoforms/chemistry/genetics/metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; RNA, Untranslated/genetics ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcription, Genetic
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  • 33
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1274-7. doi: 10.1126/science.329.5997.1274.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829463" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Conservation of Natural Resources ; Databases, Factual ; Ecosystem ; *Endangered Species ; International Cooperation ; Plant Development ; *Plants/classification ; Seeds ; *Terminology as Topic
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  • 34
    Publication Date: 2010-11-06
    Description: Protein synthesis requires several guanosine triphosphatase (GTPase) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-transfer RNAs (tRNAs) to the ribosome. To understand how the ribosome triggers GTP hydrolysis in translational GTPases, we have determined the crystal structure of EF-Tu and aminoacyl-tRNA bound to the ribosome with a GTP analog, to 3.2 angstrom resolution. EF-Tu is in its active conformation, the switch I loop is ordered, and the catalytic histidine is coordinating the nucleophilic water in position for inline attack on the gamma-phosphate of GTP. This activated conformation is due to a critical and conserved interaction of the histidine with A2662 of the sarcin-ricin loop of the 23S ribosomal RNA. The structure suggests a universal mechanism for GTPase activation and hydrolysis in translational GTPases on the ribosome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3763471/" 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/PMC3763471/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Voorhees, Rebecca M -- Schmeing, T Martin -- Kelley, Ann C -- Ramakrishnan, V -- 082086/Wellcome Trust/United Kingdom -- MC_U105184332/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2010 Nov 5;330(6005):835-8. doi: 10.1126/science.1194460.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21051640" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Guanosine Triphosphate/analogs & derivatives/*metabolism ; Hydrolysis ; Hydrophobic and Hydrophilic Interactions ; Nucleic Acid Conformation ; Paromomycin/metabolism ; Peptide Elongation Factor Tu/*chemistry/*metabolism ; Phosphates/metabolism ; Protein Structure, Tertiary ; RNA, Bacterial/chemistry/*metabolism ; RNA, Ribosomal, 23S/chemistry/metabolism ; RNA, Transfer, Amino Acyl/chemistry/*metabolism ; Ribosomes/*metabolism ; Thermus thermophilus/chemistry/*metabolism/ultrastructure
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  • 35
    Publication Date: 2010-05-08
    Description: Clathrin-mediated endocytosis, the major pathway for ligand internalization into eukaryotic cells, is thought to be initiated by the clustering of clathrin and adaptors around receptors destined for internalization. However, here we report that the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2) were required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. Changes in FCHo1/2 expression levels correlated directly with numbers of CCV budding events, ligand endocytosis, and synaptic vesicle marker recycling. FCHo1/2 proteins bound specifically to the plasma membrane and recruited the scaffold proteins eps15 and intersectin, which in turn engaged the adaptor complex AP2. The FCHo F-BAR membrane-bending activity was required, leading to the proposal that FCHo1/2 sculpt the initial bud site and recruit the clathrin machinery for CCV formation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883440/" 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/PMC2883440/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henne, William Mike -- Boucrot, Emmanuel -- Meinecke, Michael -- Evergren, Emma -- Vallis, Yvonne -- Mittal, Rohit -- McMahon, Harvey T -- MC_U105178795/Medical Research Council/United Kingdom -- U.1051.02.007(78795)/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2010 Jun 4;328(5983):1281-4. doi: 10.1126/science.1188462. Epub 2010 May 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council, Laboratory of Molecular Biology (MRC-LMB), Hills Road, Cambridge CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20448150" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Protein Complex 2/metabolism ; Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport/metabolism ; Animals ; Calcium-Binding Proteins/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; Clathrin/*metabolism ; Clathrin-Coated Vesicles/*metabolism ; *Endocytosis ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins ; Mice ; Models, Molecular ; Neurons/cytology/metabolism ; Phosphoproteins/metabolism ; Protein Multimerization ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; RNA Interference ; Rats ; Rats, Sprague-Dawley ; Recombinant Fusion Proteins/metabolism ; Synaptic Vesicles/metabolism
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  • 36
    Publication Date: 2010-11-27
    Description: The extinction of dinosaurs at the Cretaceous/Paleogene (K/Pg) boundary was the seminal event that opened the door for the subsequent diversification of terrestrial mammals. Our compilation of maximum body size at the ordinal level by sub-epoch shows a near-exponential increase after the K/Pg. On each continent, the maximum size of mammals leveled off after 40 million years ago and thereafter remained approximately constant. There was remarkable congruence in the rate, trajectory, and upper limit across continents, orders, and trophic guilds, despite differences in geological and climatic history, turnover of lineages, and ecological variation. Our analysis suggests that although the primary driver for the evolution of giant mammals was diversification to fill ecological niches, environmental temperature and land area may have ultimately constrained the maximum size achieved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Felisa A -- Boyer, Alison G -- Brown, James H -- Costa, Daniel P -- Dayan, Tamar -- Ernest, S K Morgan -- Evans, Alistair R -- Fortelius, Mikael -- Gittleman, John L -- Hamilton, Marcus J -- Harding, Larisa E -- Lintulaakso, Kari -- Lyons, S Kathleen -- McCain, Christy -- Okie, Jordan G -- Saarinen, Juha J -- Sibly, Richard M -- Stephens, Patrick R -- Theodor, Jessica -- Uhen, Mark D -- New York, N.Y. -- Science. 2010 Nov 26;330(6008):1216-9. doi: 10.1126/science.1194830.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, MSC03 2020, University of New Mexico, Albuquerque, NM 87131, USA. fasmith@unm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21109666" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atmosphere ; *Biological Evolution ; *Body Size ; Ecosystem ; Environment ; Extinction, Biological ; Fossils ; Geography ; Mammals/*anatomy & histology/classification/growth & development ; Models, Biological ; Oxygen ; Phylogeny ; Temperature
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  • 37
    Publication Date: 2010-01-16
    Description: We report here genome sequences and comparative analyses of three closely related parasitoid wasps: Nasonia vitripennis, N. giraulti, and N. longicornis. Parasitoids are important regulators of arthropod populations, including major agricultural pests and disease vectors, and Nasonia is an emerging genetic model, particularly for evolutionary and developmental genetics. Key findings include the identification of a functional DNA methylation tool kit; hymenopteran-specific genes including diverse venoms; lateral gene transfers among Pox viruses, Wolbachia, and Nasonia; and the rapid evolution of genes involved in nuclear-mitochondrial interactions that are implicated in speciation. Newly developed genome resources advance Nasonia for genetic research, accelerate mapping and cloning of quantitative trait loci, and will ultimately provide tools and knowledge for further increasing the utility of parasitoids as pest insect-control agents.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2849982/" 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/PMC2849982/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Werren, John H -- Richards, Stephen -- Desjardins, Christopher A -- Niehuis, Oliver -- Gadau, Jurgen -- Colbourne, John K -- Nasonia Genome Working Group -- Beukeboom, Leo W -- Desplan, Claude -- Elsik, Christine G -- Grimmelikhuijzen, Cornelis J P -- Kitts, Paul -- Lynch, Jeremy A -- Murphy, Terence -- Oliveira, Deodoro C S G -- Smith, Christopher D -- van de Zande, Louis -- Worley, Kim C -- Zdobnov, Evgeny M -- Aerts, Maarten -- Albert, Stefan -- Anaya, Victor H -- Anzola, Juan M -- Barchuk, Angel R -- Behura, Susanta K -- Bera, Agata N -- Berenbaum, May R -- Bertossa, Rinaldo C -- Bitondi, Marcia M G -- Bordenstein, Seth R -- Bork, Peer -- Bornberg-Bauer, Erich -- Brunain, Marleen -- Cazzamali, Giuseppe -- Chaboub, Lesley -- Chacko, Joseph -- Chavez, Dean -- Childers, Christopher P -- Choi, Jeong-Hyeon -- Clark, Michael E -- Claudianos, Charles -- Clinton, Rochelle A -- Cree, Andrew G -- Cristino, Alexandre S -- Dang, Phat M -- Darby, Alistair C -- de Graaf, Dirk C -- Devreese, Bart -- Dinh, Huyen H -- Edwards, Rachel -- Elango, Navin -- Elhaik, Eran -- Ermolaeva, Olga -- Evans, Jay D -- Foret, Sylvain -- Fowler, Gerald R -- Gerlach, Daniel -- Gibson, Joshua D -- Gilbert, Donald G -- Graur, Dan -- Grunder, Stefan -- Hagen, Darren E -- Han, Yi -- Hauser, Frank -- Hultmark, Da -- Hunter, Henry C 4th -- Hurst, Gregory D D -- Jhangian, Shalini N -- Jiang, Huaiyang -- Johnson, Reed M -- Jones, Andrew K -- Junier, Thomas -- Kadowaki, Tatsuhiko -- Kamping, Albert -- Kapustin, Yuri -- Kechavarzi, Bobak -- Kim, Jaebum -- Kim, Jay -- Kiryutin, Boris -- Koevoets, Tosca -- Kovar, Christie L -- Kriventseva, Evgenia V -- Kucharski, Robert -- Lee, Heewook -- Lee, Sandra L -- Lees, Kristin -- Lewis, Lora R -- Loehlin, David W -- Logsdon, John M Jr -- Lopez, Jacqueline A -- Lozado, Ryan J -- Maglott, Donna -- Maleszka, Ryszard -- Mayampurath, Anoop -- Mazur, Danielle J -- McClure, Marcella A -- Moore, Andrew D -- Morgan, Margaret B -- Muller, Jean -- Munoz-Torres, Monica C -- Muzny, Donna M -- Nazareth, Lynne V -- Neupert, Susanne -- Nguyen, Ngoc B -- Nunes, Francis M F -- Oakeshott, John G -- Okwuonu, Geoffrey O -- Pannebakker, Bart A -- Pejaver, Vikas R -- Peng, Zuogang -- Pratt, Stephen C -- Predel, Reinhard -- Pu, Ling-Ling -- Ranson, Hilary -- Raychoudhury, Rhitoban -- Rechtsteiner, Andreas -- Reese, Justin T -- Reid, Jeffrey G -- Riddle, Megan -- Robertson, Hugh M -- Romero-Severson, Jeanne -- Rosenberg, Miriam -- Sackton, Timothy B -- Sattelle, David B -- Schluns, Helge -- Schmitt, Thomas -- Schneider, Martina -- Schuler, Andreas -- Schurko, Andrew M -- Shuker, David M -- Simoes, Zila L P -- Sinha, Saurabh -- Smith, Zachary -- Solovyev, Victor -- Souvorov, Alexandre -- Springauf, Andreas -- Stafflinger, Elisabeth -- Stage, Deborah E -- Stanke, Mario -- Tanaka, Yoshiaki -- Telschow, Arndt -- Trent, Carol -- Vattathil, Selina -- Verhulst, Eveline C -- Viljakainen, Lumi -- Wanner, Kevin W -- Waterhouse, Robert M -- Whitfield, James B -- Wilkes, Timothy E -- Williamson, Michael -- Willis, Judith H -- Wolschin, Florian -- Wyder, Stefan -- Yamada, Takuji -- Yi, Soojin V -- Zecher, Courtney N -- Zhang, Lan -- Gibbs, Richard A -- 5R01GM070026-04/GM/NIGMS NIH HHS/ -- 5R01HG000747-14/HG/NHGRI NIH HHS/ -- 5R24GM084917-02/GM/NIGMS NIH HHS/ -- AI028309-13A2/AI/NIAID NIH HHS/ -- R01 AI055624/AI/NIAID NIH HHS/ -- R01 GM064864/GM/NIGMS NIH HHS/ -- R01 GM064864-04/GM/NIGMS NIH HHS/ -- R01 GM064864-05A2/GM/NIGMS NIH HHS/ -- R01 GM070026/GM/NIGMS NIH HHS/ -- R01 GM070026-04S1/GM/NIGMS NIH HHS/ -- R01 GM079484/GM/NIGMS NIH HHS/ -- R01 GM085163/GM/NIGMS NIH HHS/ -- R01 GM085163-01/GM/NIGMS NIH HHS/ -- R01 GM085233/GM/NIGMS NIH HHS/ -- R01 HG000747/HG/NHGRI NIH HHS/ -- R01 HG000747-14/HG/NHGRI NIH HHS/ -- R01GM064864/GM/NIGMS NIH HHS/ -- R24 GM084917/GM/NIGMS NIH HHS/ -- R24 GM084917-01/GM/NIGMS NIH HHS/ -- R24 GM084917-02/GM/NIGMS NIH HHS/ -- U54 HG003273/HG/NHGRI NIH HHS/ -- U54 HG003273-03/HG/NHGRI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 Jan 15;327(5963):343-8. doi: 10.1126/science.1178028.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20075255" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arthropods/parasitology ; *Biological Evolution ; DNA Methylation ; DNA Transposable Elements ; Female ; Gene Transfer, Horizontal ; Genes, Insect ; Genetic Speciation ; Genetic Variation ; *Genome, Insect ; Host-Parasite Interactions ; Insect Proteins/genetics/metabolism ; Insect Viruses/genetics ; Insects/genetics ; Male ; Molecular Sequence Data ; Quantitative Trait Loci ; Recombination, Genetic ; Sequence Analysis, DNA ; Wasp Venoms/chemistry/toxicity ; Wasps/*genetics/physiology ; Wolbachia/genetics
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  • 38
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poiner, Ian -- New York, N.Y. -- Science. 2010 Oct 1;330(6000):25. doi: 10.1126/science.330.6000.25.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929784" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Biomass ; *Ecosystem ; Marine Biology ; Oceans and Seas
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  • 39
    Publication Date: 2010-08-21
    Description: Multicellular organisms activate immunity upon recognition of pathogen-associated molecular patterns (PAMPs). Chitin is the major component of fungal cell walls, and chitin oligosaccharides act as PAMPs in plant and mammalian cells. Microbial pathogens deliver effector proteins to suppress PAMP-triggered host immunity and to establish infection. Here, we show that the LysM domain-containing effector protein Ecp6 of the fungal plant pathogen Cladosporium fulvum mediates virulence through perturbation of chitin-triggered host immunity. During infection, Ecp6 sequesters chitin oligosaccharides that are released from the cell walls of invading hyphae to prevent elicitation of host immunity. This may represent a common strategy of host immune suppression by fungal pathogens, because LysM effectors are widely conserved in the fungal kingdom.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Jonge, Ronnie -- van Esse, H Peter -- Kombrink, Anja -- Shinya, Tomonori -- Desaki, Yoshitake -- Bours, Ralph -- van der Krol, Sander -- Shibuya, Naoto -- Joosten, Matthieu H A J -- Thomma, Bart P H J -- New York, N.Y. -- Science. 2010 Aug 20;329(5994):953-5. doi: 10.1126/science.1190859.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Phytopathology, Wageningen University, Droevendaalsesteeg 1, 6708 PB Wageningen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20724636" target="_blank"〉PubMed〈/a〉
    Keywords: Chitin/metabolism ; Chitinase/metabolism ; Cladosporium/immunology/*pathogenicity ; Fungal Proteins/chemistry/immunology/*physiology ; Lycopersicon esculentum/*immunology/microbiology ; Plant Diseases/immunology/microbiology ; Protein Binding ; Protein Structure, Tertiary ; Trichoderma/physiology
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  • 40
    Publication Date: 2010-10-30
    Description: Prions are an unusual form of epigenetics: Their stable inheritance and complex phenotypes come about through protein folding rather than nucleic acid-associated changes. With intimate ties to protein homeostasis and a remarkable sensitivity to stress, prions are a robust mechanism that links environmental extremes with the acquisition and inheritance of new traits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halfmann, Randal -- Lindquist, Susan -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Oct 29;330(6004):629-32. doi: 10.1126/science.1191081.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21030648" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Biological Evolution ; *Epigenesis, Genetic ; Genetic Variation ; Homeostasis ; Peptide Termination Factors/chemistry/metabolism/physiology ; Phenotype ; Prions/*chemistry/metabolism/*physiology ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/metabolism/physiology ; Stress, Physiological
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  • 41
    Publication Date: 2010-02-13
    Description: Microorganisms can switch from a planktonic, free-swimming life-style to a sessile, colonial state, called a biofilm, which confers resistance to environmental stress. Conversion between the motile and biofilm life-styles has been attributed to increased levels of the prokaryotic second messenger cyclic di-guanosine monophosphate (c-di-GMP), yet the signaling mechanisms mediating such a global switch are poorly understood. Here we show that the transcriptional regulator VpsT from Vibrio cholerae directly senses c-di-GMP to inversely control extracellular matrix production and motility, which identifies VpsT as a master regulator for biofilm formation. Rather than being regulated by phosphorylation, VpsT undergoes a change in oligomerization on c-di-GMP binding.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2828054/" 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/PMC2828054/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasteva, Petya V -- Fong, Jiunn C N -- Shikuma, Nicholas J -- Beyhan, Sinem -- Navarro, Marcos V A S -- Yildiz, Fitnat H -- Sondermann, Holger -- 1R01GM081373/GM/NIGMS NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 AI055987/AI/NIAID NIH HHS/ -- R01 AI055987-06A1/AI/NIAID NIH HHS/ -- R01 GM081373/GM/NIGMS NIH HHS/ -- R01 GM081373-03/GM/NIGMS NIH HHS/ -- R01AI055987/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2010 Feb 12;327(5967):866-8. doi: 10.1126/science.1181185.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20150502" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Biofilms/*growth & development ; Crystallography, X-Ray ; Cyclic GMP/*analogs & derivatives/metabolism ; DNA, Bacterial/metabolism ; Dimerization ; Extracellular Matrix/*metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Models, Molecular ; Movement ; Point Mutation ; Polysaccharides, Bacterial/genetics/metabolism ; Protein Folding ; Protein Multimerization ; Protein Structure, Tertiary ; Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic ; Vibrio cholerae O1/cytology/genetics/*physiology
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  • 42
    Publication Date: 2010-01-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whiten, Andrew -- McGrew, William C -- Aiello, Leslie C -- Boesch, Christophe -- Boyd, Robert -- Byrne, Richard W -- Dunbar, Robin I M -- Matsuzawa, Tetsuro -- Silk, Joan B -- Tomasello, Michael -- van Schaik, Carel P -- Wrangham, Richard -- New York, N.Y. -- Science. 2010 Jan 22;327(5964):410; author reply 410-1. doi: 10.1126/science.327.5964.410-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20093456" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior ; Behavior, Animal ; *Biological Evolution ; Cognition ; Female ; *Hominidae/classification ; Humans ; Male ; *Pan troglodytes/classification
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  • 43
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-01-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2010 Jan 29;327(5965):519. doi: 10.1126/science.327.5965.519.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110481" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthozoa/classification/genetics ; Biodiversity ; *Biological Evolution ; Cnidaria/classification/genetics ; *Ecosystem ; Genes ; Genetic Speciation ; Geologic Sediments ; Phylogeny ; *Seawater
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  • 44
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-02-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2010 Feb 5;327(5966):633. doi: 10.1126/science.327.5966.633-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20133547" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; *Bufonidae/anatomy & histology/classification/physiology ; Genetic Speciation ; Population Dynamics ; South America
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, Stephen C -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Aug 27;329(5995):1026-7. doi: 10.1126/science.1194922.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Jack and Eileen Connors Laboratory of Structural Biology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA. harrison@crystal.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20798308" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*chemistry/*ultrastructure ; Capsid Proteins/*chemistry/ultrastructure ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Image Processing, Computer-Assisted ; Protein Structure, Tertiary ; Virion/chemistry/ultrastructure
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-01-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, Terry -- New York, N.Y. -- Science. 2010 Jan 29;327(5965):532-4. doi: 10.1126/science.1184703.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for the Study of Human Origins, Department of Anthropology, New York University, New York, NY 10003, USA. terry.harrison@nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110491" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; Asia ; *Biological Evolution ; Cercopithecidae/classification ; Climate ; Europe ; Extinction, Biological ; Fossils ; *Hominidae/classification ; Humans ; Paleontology ; Pan troglodytes ; Phylogeny ; Seasons ; Time
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  • 47
    Publication Date: 2010-11-26
    Description: Genomes of animals as different as sponges and humans show conservation of global architecture. Here we show that multiple genomic features including transposon diversity, developmental gene repertoire, physical gene order, and intron-exon organization are shattered in the tunicate Oikopleura, belonging to the sister group of vertebrates and retaining chordate morphology. Ancestral architecture of animal genomes can be deeply modified and may therefore be largely nonadaptive. This rapidly evolving animal lineage thus offers unique perspectives on the level of genome plasticity. It also illuminates issues as fundamental as the mechanisms of intron gain.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3760481/" 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/PMC3760481/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Denoeud, France -- Henriet, Simon -- Mungpakdee, Sutada -- Aury, Jean-Marc -- Da Silva, Corinne -- Brinkmann, Henner -- Mikhaleva, Jana -- Olsen, Lisbeth Charlotte -- Jubin, Claire -- Canestro, Cristian -- Bouquet, Jean-Marie -- Danks, Gemma -- Poulain, Julie -- Campsteijn, Coen -- Adamski, Marcin -- Cross, Ismael -- Yadetie, Fekadu -- Muffato, Matthieu -- Louis, Alexandra -- Butcher, Stephen -- Tsagkogeorga, Georgia -- Konrad, Anke -- Singh, Sarabdeep -- Jensen, Marit Flo -- Huynh Cong, Evelyne -- Eikeseth-Otteraa, Helen -- Noel, Benjamin -- Anthouard, Veronique -- Porcel, Betina M -- Kachouri-Lafond, Rym -- Nishino, Atsuo -- Ugolini, Matteo -- Chourrout, Pascal -- Nishida, Hiroki -- Aasland, Rein -- Huzurbazar, Snehalata -- Westhof, Eric -- Delsuc, Frederic -- Lehrach, Hans -- Reinhardt, Richard -- Weissenbach, Jean -- Roy, Scott W -- Artiguenave, Francois -- Postlethwait, John H -- Manak, J Robert -- Thompson, Eric M -- Jaillon, Olivier -- Du Pasquier, Louis -- Boudinot, Pierre -- Liberles, David A -- Volff, Jean-Nicolas -- Philippe, Herve -- Lenhard, Boris -- Roest Crollius, Hugues -- Wincker, Patrick -- Chourrout, Daniel -- Z01 LM000073-12/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 Dec 3;330(6009):1381-5. doi: 10.1126/science.1194167. Epub 2010 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commissariat a l'Energie Atomique, Institut de Genomique, Genoscope, Evry, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21097902" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA Transposable Elements ; DNA, Intergenic ; Exons ; Gene Order ; Genes, Duplicate ; Genes, Homeobox ; *Genome ; Introns ; Invertebrates/classification/genetics ; Molecular Sequence Data ; Recombination, Genetic ; Spliceosomes/metabolism ; Synteny ; Urochordata/anatomy & histology/classification/*genetics/immunology ; Vertebrates/classification/genetics
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  • 48
    Publication Date: 2010-10-28
    Description: Quantitative scenarios are coming of age as a tool for evaluating the impact of future socioeconomic development pathways on biodiversity and ecosystem services. We analyze global terrestrial, freshwater, and marine biodiversity scenarios using a range of measures including extinctions, changes in species abundance, habitat loss, and distribution shifts, as well as comparing model projections to observations. Scenarios consistently indicate that biodiversity will continue to decline over the 21st century. However, the range of projected changes is much broader than most studies suggest, partly because there are major opportunities to intervene through better policies, but also because of large uncertainties in projections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pereira, Henrique M -- Leadley, Paul W -- Proenca, Vania -- Alkemade, Rob -- Scharlemann, Jorn P W -- Fernandez-Manjarres, Juan F -- Araujo, Miguel B -- Balvanera, Patricia -- Biggs, Reinette -- Cheung, William W L -- Chini, Louise -- Cooper, H David -- Gilman, Eric L -- Guenette, Sylvie -- Hurtt, George C -- Huntington, Henry P -- Mace, Georgina M -- Oberdorff, Thierry -- Revenga, Carmen -- Rodrigues, Patricia -- Scholes, Robert J -- Sumaila, Ussif Rashid -- Walpole, Matt -- New York, N.Y. -- Science. 2010 Dec 10;330(6010):1496-501. doi: 10.1126/science.1196624. Epub 2010 Oct 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centro de Biologia Ambiental, Faculdade de Ciencias da Universidade de Lisboa, 1749-016 Lisboa, Portugal. hpereira@fc.ul.pt〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20978282" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquatic Organisms ; *Biodiversity ; Conservation of Natural Resources ; *Ecosystem ; Extinction, Biological ; Forecasting ; Models, Biological ; Plants ; Policy ; Population Dynamics
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  • 49
    Publication Date: 2010-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perrings, C -- Naeem, S -- Ahrestani, F -- Bunker, D E -- Burkill, P -- Canziani, G -- Elmqvist, T -- Ferrati, R -- Fuhrman, J -- Jaksic, F -- Kawabata, Z -- Kinzig, A -- Mace, G M -- Milano, F -- Mooney, H -- Prieur-Richard, A-H -- Tschirhart, J -- Weisser, W -- New York, N.Y. -- Science. 2010 Oct 15;330(6002):323-4. doi: 10.1126/science.1196431.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arizona State University, Tempe, AZ 85287, USA. Charles.Perrings@asu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20947748" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Conservation of Natural Resources/trends ; *Ecosystem ; Environment ; Forecasting ; International Cooperation
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  • 50
    Publication Date: 2010-09-11
    Description: Many bacteria and archaea contain clustered regularly interspaced short palindromic repeats (CRISPRs) that confer resistance to invasive genetic elements. Central to this immune system is the production of CRISPR-derived RNAs (crRNAs) after transcription of the CRISPR locus. Here, we identify the endoribonuclease (Csy4) responsible for CRISPR transcript (pre-crRNA) processing in Pseudomonas aeruginosa. A 1.8 angstrom crystal structure of Csy4 bound to its cognate RNA reveals that Csy4 makes sequence-specific interactions in the major groove of the crRNA repeat stem-loop. Together with electrostatic contacts to the phosphate backbone, these enable Csy4 to bind selectively and cleave pre-crRNAs using phylogenetically conserved serine and histidine residues in the active site. The RNA recognition mechanism identified here explains sequence- and structure-specific processing by a large family of CRISPR-specific endoribonucleases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3133607/" 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/PMC3133607/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haurwitz, Rachel E -- Jinek, Martin -- Wiedenheft, Blake -- Zhou, Kaihong -- Doudna, Jennifer A -- 5 T32 GM08295/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1355-8. doi: 10.1126/science.1192272.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Bacterial Proteins/*chemistry/*metabolism ; Base Pairing ; Base Sequence ; CRISPR-Associated Proteins ; Crystallization ; Crystallography, X-Ray ; Endoribonucleases/*chemistry/*metabolism ; Genes, Bacterial ; Hydrogen Bonding ; Models, Molecular ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Tertiary ; Pseudomonas aeruginosa/*enzymology/*genetics ; *RNA Processing, Post-Transcriptional ; RNA, Bacterial/chemistry/genetics/*metabolism ; *Repetitive Sequences, Nucleic Acid ; Static Electricity
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-07-31
    Description: Barton et al. (Reports, 19 March 2010, p. 1509) argued that stable conditions enable neutral coexistence of many phytoplankton species in the tropical oceans, whereas seasonal variation causes low biodiversity in subpolar oceans. However, their model prediction is not robust. A minor deviation from the neutrality assumption favors coexistence in fluctuating rather than stable environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huisman, Jef -- New York, N.Y. -- Science. 2010 Jul 30;329(5991):512; author reply 512. doi: 10.1126/science.1189880.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aquatic Microbiology, Institute for Biodiversity and Ecosystem Dynamics, University of Amsterdam, Post Office Box 94248, 1090 GE Amsterdam, Netherlands. j.huisman@uva.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20671171" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; *Ecosystem ; Environment ; Geography ; Models, Biological ; Oceans and Seas ; *Phytoplankton/growth & development/physiology ; Population Dynamics ; Seasons ; *Seawater
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  • 52
    Publication Date: 2010-07-03
    Description: Proton-pumping respiratory complex I is one of the largest and most complicated membrane protein complexes. Its function is critical for efficient energy supply in aerobic cells, and malfunctions are implicated in many neurodegenerative disorders. Here, we report an x-ray crystallographic analysis of mitochondrial complex I. The positions of all iron-sulfur clusters relative to the membrane arm were determined in the complete enzyme complex. The ubiquinone reduction site resides close to 30 angstroms above the membrane domain. The arrangement of functional modules suggests conformational coupling of redox chemistry with proton pumping and essentially excludes direct mechanisms. We suggest that a approximately 60-angstrom-long helical transmission element is critical for transducing conformational energy to proton-pumping elements in the distal module of the membrane arm.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hunte, Carola -- Zickermann, Volker -- Brandt, Ulrich -- New York, N.Y. -- Science. 2010 Jul 23;329(5990):448-51. doi: 10.1126/science.1191046. Epub 2010 Jul 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Biochemistry and Molecular Biology, Centre for Biological Signalling Studies (BIOSS), University of Freiburg, D-79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20595580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Electron Transport Complex I/*chemistry/*metabolism ; Fungal Proteins/chemistry/metabolism ; Iron/chemistry ; Mitochondria/enzymology ; Mitochondrial Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protons ; Sulfur/chemistry ; Ubiquinone/chemistry/metabolism ; Yarrowia/*enzymology
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  • 53
    Publication Date: 2010-08-28
    Description: Rational development of adenovirus vectors for therapeutic gene transfer is hampered by the lack of accurate structural information. Here, we report the x-ray structure at 3.5 angstrom resolution of the 150-megadalton adenovirus capsid containing nearly 1 million amino acids. We describe interactions between the major capsid protein (hexon) and several accessory molecules that stabilize the capsid. The virus structure also reveals an altered association between the penton base and the trimeric fiber protein, perhaps reflecting an early event in cell entry. The high-resolution structure provides a substantial advance toward understanding the assembly and cell entry mechanisms of a large double-stranded DNA virus and provides new opportunities for improving adenovirus-mediated gene transfer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2929978/" 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/PMC2929978/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, Vijay S -- Natchiar, S Kundhavai -- Stewart, Phoebe L -- Nemerow, Glen R -- AI042929/AI/NIAID NIH HHS/ -- EY011431/EY/NEI NIH HHS/ -- HL054352/HL/NHLBI NIH HHS/ -- R01 AI070771/AI/NIAID NIH HHS/ -- R01 AI070771-03/AI/NIAID NIH HHS/ -- R01 EY011431/EY/NEI NIH HHS/ -- R01 EY011431-13/EY/NEI NIH HHS/ -- R01 HL054352/HL/NHLBI NIH HHS/ -- R01 HL054352-17/HL/NHLBI NIH HHS/ -- R29 AI042929/AI/NIAID NIH HHS/ -- R29 AI042929-06/AI/NIAID NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Aug 27;329(5995):1071-5. doi: 10.1126/science.1187292.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. reddyv@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20798318" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*chemistry/physiology/*ultrastructure ; Capsid/*chemistry/*ultrastructure ; Capsid Proteins/*chemistry/ultrastructure ; Crystallography, X-Ray ; Genetic Vectors ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Virus Internalization
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  • 54
    Publication Date: 2010-10-12
    Description: Marx and Uhen (Reports, 19 February 2010, p. 993) suggested that correlated diversity changes in the fossil record of whales and diatoms reflects secular evolutionary signals of underlying ecological drivers. We question the meaning of this association and outline avenues for more complete testing of correlations between productivity and marine consumers through geologic time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pyenson, Nicholas D -- Irmis, Randall B -- Lipps, Jere H -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):178; author reply 178. doi: 10.1126/science.1189866.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, 6270 University Boulevard, University of British Columbia, Vancouver, BC V6T 1Z4, Canada. pyensonn@si.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Biological Evolution ; Climate ; *Diatoms ; *Ecosystem ; Food Chain ; *Fossils ; Geologic Sediments ; Oceans and Seas ; *Whales
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  • 55
    Publication Date: 2010-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regalado, Antonio -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1270-1. doi: 10.1126/science.329.5997.1270-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829459" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; Brazil ; Conservation of Natural Resources/*statistics & numerical data
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  • 56
    Publication Date: 2010-11-13
    Description: The Amazonian rainforest is arguably the most species-rich terrestrial ecosystem in the world, yet the timing of the origin and evolutionary causes of this diversity are a matter of debate. We review the geologic and phylogenetic evidence from Amazonia and compare it with uplift records from the Andes. This uplift and its effect on regional climate fundamentally changed the Amazonian landscape by reconfiguring drainage patterns and creating a vast influx of sediments into the basin. On this "Andean" substrate, a region-wide edaphic mosaic developed that became extremely rich in species, particularly in Western Amazonia. We show that Andean uplift was crucial for the evolution of Amazonian landscapes and ecosystems, and that current biodiversity patterns are rooted deep in the pre-Quaternary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoorn, C -- Wesselingh, F P -- ter Steege, H -- Bermudez, M A -- Mora, A -- Sevink, J -- Sanmartin, I -- Sanchez-Meseguer, A -- Anderson, C L -- Figueiredo, J P -- Jaramillo, C -- Riff, D -- Negri, F R -- Hooghiemstra, H -- Lundberg, J -- Stadler, T -- Sarkinen, T -- Antonelli, A -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):927-31. doi: 10.1126/science.1194585.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Paleoecology and Landscape Ecology, Institute for Biodiversity and Ecosystem Dynamics (IBED), University of Amsterdam, Science Park 904, 1098 XH Amsterdam, Netherlands. carina.hoorn@milne.cc〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21071659" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Climate Change ; Ecosystem ; Fossils ; Geography ; *Geological Phenomena ; Phylogeny ; Rivers ; South America ; Time ; Trees ; Wetlands
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-02-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alcock, Felicity -- Clements, Abigail -- Webb, Chaille -- Lithgow, Trevor -- New York, N.Y. -- Science. 2010 Feb 5;327(5966):649-50. doi: 10.1126/science.1182129.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne 3800, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20133559" target="_blank"〉PubMed〈/a〉
    Keywords: Alphaproteobacteria/genetics/*metabolism ; Amino Acid Transport Systems/chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; *Biological Evolution ; *Eukaryotic Cells/metabolism/ultrastructure ; Evolution, Molecular ; *Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/chemistry/*metabolism ; *Protein Transport ; *Symbiosis
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  • 58
    Publication Date: 2010-11-27
    Description: The brain's circuitry is established by directed migration and synaptogenesis of neurons during development. Although neurons mature and migrate in specific patterns, little is known about how neurons exit their germinal zone niche. We found that cerebellar granule neuron germinal zone exit is regulated by proteasomal degradation of Pard3A by the Seven in Absentia homolog (Siah) E3 ubiquitin ligase. Pard3A gain of function and Siah loss of function induce precocious radial migration. Time-lapse imaging using a probe to measure neuronal cell contact reveals that Pard3A promotes adhesive interactions needed for germinal zone exit by recruiting the epithelial tight junction adhesion molecule C to the neuronal cell surface. Our findings define a Siah-Pard3A signaling pathway that controls adhesion-dependent exit of neuronal progenitors or immature neurons from a germinal zone niche.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3065828/" 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/PMC3065828/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Famulski, Jakub K -- Trivedi, Niraj -- Howell, Danielle -- Yang, Yuan -- Tong, Yiai -- Gilbertson, Richard -- Solecki, David J -- P01 CA096832/CA/NCI NIH HHS/ -- P01 CA096832-07/CA/NCI NIH HHS/ -- P30 CA021765/CA/NCI NIH HHS/ -- P30 CA021765-33/CA/NCI NIH HHS/ -- R01 CA129541/CA/NCI NIH HHS/ -- R01 CA129541-04/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2010 Dec 24;330(6012):1834-8. doi: 10.1126/science.1198480. Epub 2010 Nov 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Neurobiology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21109632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Adhesion ; Cell Adhesion Molecules/chemistry/*metabolism ; Cell Line ; *Cell Movement ; Cell Polarity ; Cerebellum/*cytology/embryology/*metabolism ; Dogs ; Humans ; Immunoglobulins/chemistry/metabolism ; Mice ; Morphogenesis ; Neurons/cytology/*physiology ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; RNA Interference ; Signal Transduction ; Stem Cells/physiology ; Transfection ; Ubiquitin-Protein Ligases/genetics/*metabolism ; Ubiquitination
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  • 59
    Publication Date: 2010-09-11
    Description: The continued growth of human populations and of per capita consumption have resulted in unsustainable exploitation of Earth's biological diversity, exacerbated by climate change, ocean acidification, and other anthropogenic environmental impacts. We argue that effective conservation of biodiversity is essential for human survival and the maintenance of ecosystem processes. Despite some conservation successes (especially at local scales) and increasing public and government interest in living sustainably, biodiversity continues to decline. Moving beyond 2010, successful conservation approaches need to be reinforced and adequately financed. In addition, however, more radical changes are required that recognize biodiversity as a global public good, that integrate biodiversity conservation into policies and decision frameworks for resource production and consumption, and that focus on wider institutional and societal changes to enable more effective implementation of policy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rands, Michael R W -- Adams, William M -- Bennun, Leon -- Butchart, Stuart H M -- Clements, Andrew -- Coomes, David -- Entwistle, Abigail -- Hodge, Ian -- Kapos, Valerie -- Scharlemann, Jorn P W -- Sutherland, William J -- Vira, Bhaskar -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1298-303. doi: 10.1126/science.1189138.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Conservation Initiative, Judge Business School, University of Cambridge, Cambridge CB2 1AG, UK. mr494@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829476" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Conservation of Natural Resources/trends ; Decision Making ; Ecosystem ; Environment ; Humans ; International Cooperation ; Plants ; Population Dynamics ; Public Policy
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  • 60
    Publication Date: 2010-03-27
    Description: Phosphoinositide 3-kinases (PI3Ks) are lipid kinases with diverse roles in health and disease. The primordial PI3K, Vps34, is present in all eukaryotes and has essential roles in autophagy, membrane trafficking, and cell signaling. We solved the crystal structure of Vps34 at 2.9 angstrom resolution, which revealed a constricted adenine-binding pocket, suggesting the reason that specific inhibitors of this class of PI3K have proven elusive. Both the phosphoinositide-binding loop and the carboxyl-terminal helix of Vps34 mediate catalysis on membranes and suppress futile adenosine triphosphatase cycles. Vps34 appears to alternate between a closed cytosolic form and an open form on the membrane. Structures of Vps34 complexes with a series of inhibitors reveal the reason that an autophagy inhibitor preferentially inhibits Vps34 and underpin the development of new potent and specific Vps34 inhibitors.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860105/" 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/PMC2860105/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Simon -- Tavshanjian, Brandon -- Oleksy, Arkadiusz -- Perisic, Olga -- Houseman, Benjamin T -- Shokat, Kevan M -- Williams, Roger L -- MC_U105184308/Medical Research Council/United Kingdom -- U.1051.03.014(78824)/Medical Research Council/United Kingdom -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Mar 26;327(5973):1638-42. doi: 10.1126/science.1184429.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20339072" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/*analogs & derivatives/metabolism/pharmacology ; Adenosine Triphosphatases/metabolism ; Animals ; Autophagy/*drug effects ; Binding Sites ; Catalysis ; Catalytic Domain ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Drosophila Proteins/*antagonists & inhibitors/*chemistry/genetics/metabolism ; Drosophila melanogaster ; Enzyme Inhibitors/chemical synthesis/chemistry/*metabolism/pharmacology ; Furans/chemistry/metabolism/pharmacology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Phosphatidylinositol 3-Kinases/*antagonists & ; inhibitors/*chemistry/genetics/metabolism ; Phosphatidylinositols/metabolism ; Point Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pyridines/chemistry/metabolism/pharmacology ; Pyrimidines/chemistry/metabolism/pharmacology
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mindell, Joseph A -- New York, N.Y. -- Science. 2010 Oct 29;330(6004):601-2. doi: 10.1126/science.1198306.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Membrane Transport Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. mindellj@ninds.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21030639" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/*chemistry/metabolism ; Antiporters/*chemistry/metabolism ; Binding Sites ; Chloride Channels/*chemistry/metabolism ; Chlorides/*metabolism ; Crystallization ; Crystallography, X-Ray ; Cytoplasm/chemistry ; Eukaryota/*chemistry ; Glutamic Acid/metabolism ; Ion Channel Gating ; Ion Transport ; Models, Molecular ; Protein Structure, Tertiary ; Protons
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-09-04
    Description: The fossil record demonstrates that each major taxonomic group has a consistent net rate of diversification and a limit to its species richness. It has been thought that long-term changes in the dominance of major taxonomic groups can be predicted from these characteristics. However, new analyses show that diversity limits may rise or fall in response to adaptive radiations or extinctions. These changes are idiosyncratic and occur at different times in each taxa. For example, the end-Permian mass extinction permanently reduced the diversity of important, previously dominant groups such as brachiopods and crinoids. The current global crisis may therefore permanently alter the biosphere's taxonomic composition by changing the rules of evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alroy, J -- New York, N.Y. -- Science. 2010 Sep 3;329(5996):1191-4. doi: 10.1126/science.1189910.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Paleobiology Database, University of California, 735 State Street, Santa Barbara, CA 93101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20813951" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; Anthozoa ; *Biodiversity ; Biological Evolution ; Data Interpretation, Statistical ; *Databases, Factual ; Extinction, Biological ; *Fossils ; *Invertebrates ; Marine Biology ; Models, Biological ; *Mollusca ; Oceans and Seas ; Paleontology ; Population Dynamics ; Statistics as Topic ; Time
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, Haigen -- Ding, Hui -- Wu, Jun -- New York, N.Y. -- Science. 2010 Aug 20;329(5994):900; author reply 900-1. doi: 10.1126/science.329.5994.900-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20724616" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; China ; *Conservation of Natural Resources ; Environmental Pollution/prevention & control ; Trees
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  • 64
    Publication Date: 2010-05-29
    Description: High-conductance voltage- and Ca2+-activated K+ (BK) channels encode negative feedback regulation of membrane voltage and Ca2+ signaling, playing a central role in numerous physiological processes. We determined the x-ray structure of the human BK Ca2+ gating apparatus at a resolution of 3.0 angstroms and deduced its tetrameric assembly by solving a 6 angstrom resolution structure of a Na+-activated homolog. Two tandem C-terminal regulator of K+ conductance (RCK) domains from each of four channel subunits form a 350-kilodalton gating ring at the intracellular membrane surface. A sequence of aspartic amino acids that is known as the Ca2+ bowl, and is located within the second of the tandem RCK domains, creates four Ca2+ binding sites on the outer perimeter of the gating ring at the "assembly interface" between RCK domains. Functionally important mutations cluster near the Ca2+ bowl, near the "flexible interface" between RCK domains, and on the surface of the gating ring that faces the voltage sensors. The structure suggests that the Ca2+ gating ring, in addition to regulating the pore directly, may also modulate the voltage sensor.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022345/" 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/PMC3022345/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, Peng -- Leonetti, Manuel D -- Pico, Alexander R -- Hsiung, Yichun -- MacKinnon, Roderick -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM043949/GM/NIGMS NIH HHS/ -- R01 GM043949-20/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Jul 9;329(5988):182-6. doi: 10.1126/science.1190414. Epub 2010 May 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20508092" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/*metabolism ; Crystallography, X-Ray ; Humans ; *Ion Channel Gating ; Large-Conductance Calcium-Activated Potassium Channel alpha ; Subunits/*chemistry/genetics/*metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Patch-Clamp Techniques ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Sodium/metabolism
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  • 65
    Publication Date: 2010-10-12
    Description: CLC proteins transport chloride (Cl(-)) ions across cell membranes to control the electrical potential of muscle cells, transfer electrolytes across epithelia, and control the pH and electrolyte composition of intracellular organelles. Some members of this protein family are Cl(-) ion channels, whereas others are secondary active transporters that exchange Cl(-) ions and protons (H(+)) with a 2:1 stoichiometry. We have determined the structure of a eukaryotic CLC transporter at 3.5 angstrom resolution. Cytoplasmic cystathionine beta-synthase (CBS) domains are strategically positioned to regulate the ion-transport pathway, and many disease-causing mutations in human CLCs reside on the CBS-transmembrane interface. Comparison with prokaryotic CLC shows that a gating glutamate residue changes conformation and suggests a basis for 2:1 Cl(-)/H(+) exchange and a simple mechanistic connection between CLC channels and transporters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079386/" 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/PMC3079386/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Liang -- Campbell, Ernest B -- Hsiung, Yichun -- MacKinnon, Roderick -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM043949/GM/NIGMS NIH HHS/ -- R01 GM043949-20/GM/NIGMS NIH HHS/ -- R01 GM043949-21/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Oct 29;330(6004):635-41. doi: 10.1126/science.1195230. Epub 2010 Sep 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, Howard Hughes Medical Institute, 1230 York Avenue, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929736" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/chemistry/metabolism ; Animals ; Antiporters/*chemistry/metabolism ; Binding Sites ; Cell Line ; Cell Membrane/chemistry ; Chloride Channels/*chemistry/metabolism ; Chlorides/*metabolism ; Crystallization ; Crystallography, X-Ray ; Cystathionine beta-Synthase/chemistry ; Cytoplasm/chemistry ; Glutamic Acid/metabolism ; Ion Channel Gating ; Ion Transport ; Models, Biological ; Models, Molecular ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Protons ; Rhodophyta/*chemistry/metabolism
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-12-18
    Description: Carbon and water flow between plants and the atmosphere is regulated by the opening and closing of minute stomatal pores in surfaces of leaves. By changing the aperture of stomata, plants regulate water loss and photosynthetic carbon gain in response to many environmental stimuli, but stomatal movements cannot yet be reliably predicted. We found that the complexity that characterizes stomatal control in seed plants is absent in early-diverging vascular plant lineages. Lycophyte and fern stomata are shown to lack key responses to abscisic acid and epidermal cell turgor, making their behavior highly predictable. These results indicate that a fundamental transition from passive to active metabolic control of plant water balance occurred after the divergence of ferns about 360 million years ago.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brodribb, Tim J -- McAdam, Scott A M -- New York, N.Y. -- Science. 2011 Feb 4;331(6017):582-5. doi: 10.1126/science.1197985. Epub 2010 Dec 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Plant Science, University of Tasmania, Private Bag 55, Hobart, Tasmania 7001, Australia. timothyb@utas.edu.au〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21163966" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/metabolism/pharmacology ; Angiosperms/metabolism/*physiology ; *Biological Evolution ; Ferns/metabolism/*physiology ; Gymnosperms/metabolism/*physiology ; Light ; Lycopodiaceae/metabolism/*physiology ; Plant Epidermis/metabolism ; Plant Leaves/*metabolism ; Plant Stomata/cytology/*physiology ; Plant Transpiration ; Vapor Pressure ; Water/metabolism
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  • 67
    Publication Date: 2010-02-27
    Description: Spatial diversity gradients are a pervasive feature of life on Earth. We examined a global ocean circulation, biogeochemistry, and ecosystem model that indicated a decrease in phytoplankton diversity with increasing latitude, consistent with observations of many marine and terrestrial taxa. In the modeled subpolar oceans, seasonal variability of the environment led to competitive exclusion of phytoplankton with slower growth rates and lower diversity. The relatively weak seasonality of the stable subtropical and tropical oceans in the global model enabled long exclusion time scales and prolonged coexistence of multiple phytoplankton with comparable fitness. Superimposed on the decline in diversity seen from equator to pole were "hot spots" of enhanced diversity in some regions of energetic ocean circulation, which reflected lateral dispersal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barton, Andrew D -- Dutkiewicz, Stephanie -- Flierl, Glenn -- Bragg, Jason -- Follows, Michael J -- New York, N.Y. -- Science. 2010 Mar 19;327(5972):1509-11. doi: 10.1126/science.1184961. Epub 2010 Feb 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. adbarton@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20185684" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; Biomass ; Climate ; *Ecosystem ; Environment ; Geography ; Models, Biological ; Oceans and Seas ; *Phytoplankton/growth & development/physiology ; Population Dynamics ; Seasons ; *Seawater
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-11-26
    Description: The last common ancestor of plants and animals may have lived 1 billion years ago. Plants and animals have occasionally exchanged genes but, for the most part, have countered selective pressures independently. Microbes (bacteria, eukaryotes, and viruses) were omnipresent threats, influencing the direction of multicellular evolution. Receptors that detect molecular signatures of infectious organisms mediate awareness of nonself and are integral to host defense in plants and animals alike. The discoveries leading to elucidation of these receptors and their ligands followed a similar logical and methodological pathway in both plant and animal research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ronald, Pamela C -- Beutler, Bruce -- New York, N.Y. -- Science. 2010 Nov 19;330(6007):1061-4. doi: 10.1126/science.1189468.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, University of California, Davis, CA 95616, USA. pcronald@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21097929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Humans ; *Immunity/genetics ; Immunity, Innate ; Plant Proteins/genetics/immunology ; Plants/genetics/*immunology/microbiology ; *Receptors, Immunologic/physiology
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  • 69
    Publication Date: 2010-01-02
    Description: Many bacterial cells contain proteinaceous microcompartments that act as simple organelles by sequestering specific metabolic processes involving volatile or toxic metabolites. Here we report the three-dimensional (3D) crystal structures, with resolutions between 1.65 and 2.5 angstroms, of the four homologous proteins (EutS, EutL, EutK, and EutM) that are thought to be the major shell constituents of a functionally complex ethanolamine utilization (Eut) microcompartment. The Eut microcompartment is used to sequester the metabolism of ethanolamine in bacteria such as Escherichia coli and Salmonella enterica. The four Eut shell proteins share an overall similar 3D fold, but they have distinguishing structural features that help explain the specific roles they play in the microcompartment. For example, EutL undergoes a conformational change that is probably involved in gating molecular transport through shell protein pores, whereas structural evidence suggests that EutK might bind a nucleic acid component. Together these structures give mechanistic insight into bacterial microcompartments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, Shiho -- Sawaya, Michael R -- Yeates, Todd O -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 Jan 1;327(5961):81-4. doi: 10.1126/science.1179513.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California Los Angeles, 611 Charles Young Drive East, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20044574" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Compartmentation ; Crystallography, X-Ray ; Escherichia coli K12/*chemistry/*metabolism/ultrastructure ; Escherichia coli Proteins/*chemistry/metabolism ; Ethanolamine/*metabolism ; Metabolic Networks and Pathways ; Models, Molecular ; Molecular Sequence Data ; Polyproteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism
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  • 70
    Publication Date: 2010-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stuart, S N -- Wilson, E O -- McNeely, J A -- Mittermeier, R A -- Rodriguez, J P -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):177. doi: 10.1126/science.1188606.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉International Union for Conservation of Nature (IUCN) Species Survival Commission, 1196 Gland, Switzerland. simon.stuart@iucn.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378803" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Classification ; *Conservation of Natural Resources/economics/statistics & numerical data ; *Ecology/economics/methods ; *Endangered Species/statistics & numerical data ; *Plants/classification ; Public Policy
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  • 71
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):162. doi: 10.1126/science.328.5975.162.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378789" target="_blank"〉PubMed〈/a〉
    Keywords: *Behavior ; *Biological Evolution ; Brain/physiology ; Humans ; *Memory, Short-Term ; *Models, Psychological
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 72
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):160-3. doi: 10.1126/science.328.5975.160.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Art ; *Biological Evolution ; *Cognition ; Creativity ; Cultural Evolution ; Executive Function ; Hominidae ; Humans ; *Memory, Short-Term ; Models, Psychological ; Symbolism
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  • 73
    Publication Date: 2010-03-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2010 Mar 26;327(5973):1566-7. doi: 10.1126/science.327.5973.1566-b.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20339040" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA, Mitochondrial/chemistry/*genetics ; Finger Phalanges ; Genome, Mitochondrial ; Hominidae/*classification/genetics ; Humans ; Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Siberia ; Time
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  • 74
    Publication Date: 2010-02-27
    Description: In the past, explanations for high species diversity have been sought at the species level. Theory shows that coexistence requires substantial differences between species, but species-level data rarely provide evidence for such differences. Using data from forests in the southeastern United States, I show here that variation evident at the individual level provides for coexistence of large numbers of competitors. Variation among individuals within populations allows species to differ in their distributions of responses to the environment, despite the fact that the populations to which they belong do not differ, on average. Results are consistent with theory predicting that coexistence depends on competition being stronger within than between species, shown here by analysis of individual-level responses to environmental fluctuation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, James S -- New York, N.Y. -- Science. 2010 Feb 26;327(5969):1129-32. doi: 10.1126/science.1183506.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nicholas School of the Environment, Department of Biology, Duke University, Durham, NC 27708, USA. jimclark@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20185724" target="_blank"〉PubMed〈/a〉
    Keywords: Acer/growth & development/physiology ; *Biodiversity ; Computer Simulation ; *Ecosystem ; Environment ; Nyssa/growth & development/physiology ; Population Dynamics ; Southeastern United States ; *Trees/growth & development/physiology
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  • 75
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stuessy, Tod -- New York, N.Y. -- Science. 2010 Sep 24;329(5999):1605-6. doi: 10.1126/science.1195336.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Systematic and Evolutionary Botany, Biodiversity Center, University of Vienna, Rennweg 14, A-1030 Vienna, Austria. tod.stuessy@univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929832" target="_blank"〉PubMed〈/a〉
    Keywords: *Asteraceae/anatomy & histology/classification ; *Biological Evolution ; Flowers/anatomy & histology ; *Fossils ; *Helianthus/anatomy & histology/classification/genetics ; Phylogeny ; South America
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beattie, Andrew -- Ehrlich, Paul -- New York, N.Y. -- Science. 2010 Apr 16;328(5976):307-8. doi: 10.1126/science.328.5976.307-c.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20395493" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bacteria ; *Biodiversity ; *Conservation of Natural Resources ; Ecosystem ; *Invertebrates
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, Jon -- New York, N.Y. -- Science. 2010 Sep 24;329(5999):1586-7. doi: 10.1126/science.329.5999.1586.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929818" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ape Diseases/parasitology ; *Biological Evolution ; DNA, Protozoan/analysis/genetics ; Feces/*parasitology ; Gorilla gorilla/*parasitology ; Humans ; Malaria/parasitology/veterinary ; Malaria, Falciparum/parasitology ; Pan paniscus/parasitology ; Pan troglodytes/*parasitology ; Plasmodium/classification/*genetics/isolation & purification ; Plasmodium falciparum/*genetics
    Print ISSN: 0036-8075
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  • 78
    Publication Date: 2010-08-28
    Description: Construction of a complex virus may involve a hierarchy of assembly elements. Here, we report the structure of the whole human adenovirus virion at 3.6 angstroms resolution by cryo-electron microscopy (cryo-EM), revealing in situ atomic models of three minor capsid proteins (IIIa, VIII, and IX), extensions of the (penton base and hexon) major capsid proteins, and interactions within three protein-protein networks. One network is mediated by protein IIIa at the vertices, within group-of-six (GOS) tiles--a penton base and its five surrounding hexons. Another is mediated by ropes (protein IX) that lash hexons together to form group-of-nine (GON) tiles and bind GONs to GONs. The third, mediated by IIIa and VIII, binds each GOS to five surrounding GONs. Optimization of adenovirus for cancer and gene therapy could target these networks.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412078/" 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/PMC3412078/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Hongrong -- Jin, Lei -- Koh, Sok Boon S -- Atanasov, Ivo -- Schein, Stan -- Wu, Lily -- Zhou, Z Hong -- 1S10RR23057/RR/NCRR NIH HHS/ -- AI069015/AI/NIAID NIH HHS/ -- CA101904/CA/NCI NIH HHS/ -- GM071940/GM/NIGMS NIH HHS/ -- R01 AI069015/AI/NIAID NIH HHS/ -- R01 CA101904/CA/NCI NIH HHS/ -- R01 GM071940/GM/NIGMS NIH HHS/ -- S10 RR023057/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2010 Aug 27;329(5995):1038-43. doi: 10.1126/science.1187433.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, CA 90095-7364, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20798312" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/*chemistry/genetics/metabolism/*ultrastructure ; Capsid/chemistry/ultrastructure ; Capsid Proteins/*chemistry/metabolism/ultrastructure ; Cryoelectron Microscopy ; Genome, Viral ; Image Processing, Computer-Assisted ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Virion/chemistry/ultrastructure
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1278-80. doi: 10.1126/science.329.5997.1278.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829464" target="_blank"〉PubMed〈/a〉
    Keywords: Agriculture ; Animals ; *Biodiversity ; Biological Evolution ; Borneo ; Endangered Species ; Geological Processes ; Indonesia ; International Cooperation ; New Guinea ; *Plants ; Politics ; *Trees
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  • 80
    Publication Date: 2010-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2010 Sep 10;329(5997):1270-1. doi: 10.1126/science.329.5997.1270-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20829460" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthozoa ; *Biodiversity ; Biological Evolution ; Crustacea ; Fishes ; Geologic Sediments ; Geological Processes ; Indian Ocean ; Indonesia ; International Cooperation ; Pacific Ocean ; Philippines ; *Volcanic Eruptions
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  • 81
    Publication Date: 2010-06-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joly, Carlos A -- Rodrigues, Ricardo R -- Metzger, Jean Paul -- Haddad, Celio F B -- Verdade, Luciano M -- Oliveira, Mariana C -- Bolzani, Vanderlan S -- New York, N.Y. -- Science. 2010 Jun 11;328(5984):1358-9. doi: 10.1126/science.1188639.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biolgy, Biology Institute, State University of Campinas, 13083-970 Campinas, Sao Paulo (SP), Brazil. cjoly@unicamp.br〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20538935" target="_blank"〉PubMed〈/a〉
    Keywords: *Biodiversity ; Brazil ; *Conservation of Natural Resources ; Education ; Foundations ; Periodicals as Topic ; Public Policy ; *Research
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  • 82
    Publication Date: 2010-07-10
    Description: During HIV-1 infection, antibodies are generated against the region of the viral gp120 envelope glycoprotein that binds CD4, the primary receptor for HIV-1. Among these antibodies, VRC01 achieves broad neutralization of diverse viral strains. We determined the crystal structure of VRC01 in complex with a human immunodeficiency virus HIV-1 gp120 core. VRC01 partially mimics CD4 interaction with gp120. A shift from the CD4-defined orientation, however, focuses VRC01 onto the vulnerable site of initial CD4 attachment, allowing it to overcome the glycan and conformational masking that diminishes the neutralization potency of most CD4-binding-site antibodies. To achieve this recognition, VRC01 contacts gp120 mainly through immunoglobulin V-gene regions substantially altered from their genomic precursors. Partial receptor mimicry and extensive affinity maturation thus facilitate neutralization of HIV-1 by natural human antibodies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2981354/" 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/PMC2981354/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Tongqing -- Georgiev, Ivelin -- Wu, Xueling -- Yang, Zhi-Yong -- Dai, Kaifan -- Finzi, Andres -- Kwon, Young Do -- Scheid, Johannes F -- Shi, Wei -- Xu, Ling -- Yang, Yongping -- Zhu, Jiang -- Nussenzweig, Michel C -- Sodroski, Joseph -- Shapiro, Lawrence -- Nabel, Gary J -- Mascola, John R -- Kwong, Peter D -- P30 AI060354/AI/NIAID NIH HHS/ -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 Aug 13;329(5993):811-7. doi: 10.1126/science.1192819. Epub 2010 Jul 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20616231" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/*immunology ; Antibody Affinity ; Antigenic Variation ; Antigens, CD4/chemistry/immunology/metabolism ; Base Sequence ; Binding Sites, Antibody ; Crystallography, X-Ray ; Epitopes/immunology ; HIV Antibodies/*chemistry/*immunology ; HIV Envelope Protein gp120/chemistry/genetics/*immunology ; HIV-1/*immunology ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Models, Molecular ; Molecular Mimicry ; Molecular Sequence Data ; Neutralization Tests ; Protein Conformation ; Protein Structure, Tertiary
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-01-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaston, Kevin J -- New York, N.Y. -- Science. 2010 Jan 8;327(5962):154-5. doi: 10.1126/science.1182818.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity and Macroecology Group, Department of Animal and Plant Sciences, University of Sheffield, Sheffield S10 2TN, UK. k.j.gaston@sheffi eld.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20056880" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Biomass ; Conservation of Natural Resources ; *Ecosystem ; Plants ; Population Dynamics
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  • 84
    Publication Date: 2010-10-12
    Description: Fossil capitula and pollen grains of Asteraceae from the Eocene of Patagonia, southern Argentina, exhibit morphological features recognized today in taxa, such as Mutisioideae and Carduoideae, that are phylogenetically close to the root of the asteracean tree. This fossil supports the hypothesis of a South American origin of Asteraceae and an Eocene age of divergence and suggests that an ancestral stock of Asteraceae may have formed part of a geoflora developed in southern Gondwana before the establishment of effective dispersal barriers within this landmass.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barreda, V D -- Palazzesi, L -- Telleria, M C -- Katinas, L -- Crisci, J V -- Bremer, K -- Passalia, M G -- Corsolini, R -- Rodriguez Brizuela, R -- Bechis, F -- New York, N.Y. -- Science. 2010 Sep 24;329(5999):1621. doi: 10.1126/science.1193108.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Seccion Paleopalinologia, Division Paleobotanica, Museo Argentino de Ciencias Naturales Bernardino Rivadavia, Avenida Angel Gallardo 470, C1405DJR Buenos Aires, Argentina. vbarreda@macn.gov.ar〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929840" target="_blank"〉PubMed〈/a〉
    Keywords: Argentina ; *Asteraceae/anatomy & histology/classification/genetics ; *Biological Evolution ; Climate ; Flowers/*anatomy & histology ; *Fossils ; Phylogeny ; Pollen ; South America
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  • 85
    Publication Date: 2010-04-17
    Description: SAGA is a transcriptional coactivator complex that is conserved across eukaryotes and performs multiple functions during transcriptional activation and elongation. One role is deubiquitination of histone H2B, and this activity resides in a distinct subcomplex called the deubiquitinating module (DUBm), which contains the ubiquitin-specific protease Ubp8, bound to Sgf11, Sus1, and Sgf73. The deubiquitinating activity depends on the presence of all four DUBm proteins. We report here the 1.90 angstrom resolution crystal structure of the DUBm bound to ubiquitin aldehyde, as well as the 2.45 angstrom resolution structure of the uncomplexed DUBm. The structure reveals an arrangement of protein domains that gives rise to a highly interconnected complex, which is stabilized by eight structural zinc atoms that are critical for enzymatic activity. The structure suggests a model for how interactions with the other DUBm proteins activate Ubp8 and allows us to speculate about how the DUBm binds to monoubiquitinated histone H2B in nucleosomes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220450/" 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/PMC4220450/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Samara, Nadine L -- Datta, Ajit B -- Berndsen, Christopher E -- Zhang, Xiangbin -- Yao, Tingting -- Cohen, Robert E -- Wolberger, Cynthia -- F32GM089037/GM/NIGMS NIH HHS/ -- R01 GM095822/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2010 May 21;328(5981):1025-9. doi: 10.1126/science.1190049. Epub 2010 Apr 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20395473" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehydes/chemistry/metabolism ; Crystallography, X-Ray ; Endopeptidases/*chemistry/metabolism ; Histone Acetyltransferases/*chemistry/metabolism ; Histones/metabolism ; Models, Biological ; Models, Molecular ; Nuclear Proteins/*chemistry/metabolism ; Nucleosomes/chemistry/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA-Binding Proteins/*chemistry/metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/metabolism ; Trans-Activators/*chemistry/metabolism ; Transcription Factors/*chemistry/metabolism ; Ubiquitin/chemistry/*metabolism ; Ubiquitinated Proteins/metabolism ; Ubiquitination ; Ubiquitins/chemistry/metabolism ; Zinc/chemistry/metabolism ; Zinc Fingers
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  • 86
    Publication Date: 2010-09-04
    Description: Mechanical stimuli drive many physiological processes, including touch and pain sensation, hearing, and blood pressure regulation. Mechanically activated (MA) cation channel activities have been recorded in many cells, but the responsible molecules have not been identified. We characterized a rapidly adapting MA current in a mouse neuroblastoma cell line. Expression profiling and RNA interference knockdown of candidate genes identified Piezo1 (Fam38A) to be required for MA currents in these cells. Piezo1 and related Piezo2 (Fam38B) are vertebrate multipass transmembrane proteins with homologs in invertebrates, plants, and protozoa. Overexpression of mouse Piezo1 or Piezo2 induced two kinetically distinct MA currents. Piezos are expressed in several tissues, and knockdown of Piezo2 in dorsal root ganglia neurons specifically reduced rapidly adapting MA currents. We propose that Piezos are components of MA cation channels.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3062430/" 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/PMC3062430/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coste, Bertrand -- Mathur, Jayanti -- Schmidt, Manuela -- Earley, Taryn J -- Ranade, Sanjeev -- Petrus, Matt J -- Dubin, Adrienne E -- Patapoutian, Ardem -- DE016927/DE/NIDCR NIH HHS/ -- NS046303/NS/NINDS NIH HHS/ -- R01 NS046303/NS/NINDS NIH HHS/ -- R01 NS046303-08/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2010 Oct 1;330(6000):55-60. doi: 10.1126/science.1193270. Epub 2010 Sep 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, The Scripps Research Institute (TSRI), La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20813920" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cations/*metabolism ; Cell Line, Tumor ; Cell Membrane/chemistry ; Cloning, Molecular ; Ganglia, Spinal/cytology ; Ion Channels/analysis/chemistry/genetics/*metabolism ; *Mechanotransduction, Cellular ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Neurons/*metabolism ; Patch-Clamp Techniques ; Pressure ; Protein Structure, Tertiary ; RNA Interference ; RNA, Small Interfering/genetics ; Transfection
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  • 87
    Publication Date: 2010-11-06
    Description: The brain's visual cortex processes information concerning form, pattern, and motion within functional maps that reflect the layout of neuronal circuits. We analyzed functional maps of orientation preference in the ferret, tree shrew, and galago--three species separated since the basal radiation of placental mammals more than 65 million years ago--and found a common organizing principle. A symmetry-based class of models for the self-organization of cortical networks predicts all essential features of the layout of these neuronal circuits, but only if suppressive long-range interactions dominate development. We show mathematically that orientation-selective long-range connectivity can mediate the required interactions. Our results suggest that self-organization has canalized the evolution of the neuronal circuitry underlying orientation preference maps into a single common design.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3138194/" 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/PMC3138194/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaschube, Matthias -- Schnabel, Michael -- Lowel, Siegrid -- Coppola, David M -- White, Leonard E -- Wolf, Fred -- EY06821/EY/NEI NIH HHS/ -- EY11488/EY/NEI NIH HHS/ -- P50 GM071508/GM/NIGMS NIH HHS/ -- P50 GM071508-08/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Nov 19;330(6007):1113-6. doi: 10.1126/science.1194869. Epub 2010 Nov 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institute for Dynamics and Self-Organization, Bernstein Center for Computational Neuroscience, Faculty of Physics, Gottingen University, D-37073 Gottingen, Germany. kaschube@princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21051599" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Ferrets/anatomy & histology ; Galago/anatomy & histology ; Neurons/*cytology ; Tupaiidae/anatomy & histology ; Visual Cortex/*anatomy & histology/cytology
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  • 88
    Publication Date: 2010-09-04
    Description: Coxsackie and adenovirus receptor (CAR) is the primary cellular receptor for group B coxsackieviruses and most adenovirus serotypes and plays a crucial role in adenoviral gene therapy. Recent discovery of the interaction between junctional adhesion molecule-like protein (JAML) and CAR uncovered important functional roles in immunity, inflammation, and tissue homeostasis. Crystal structures of JAML ectodomain (2.2 angstroms) and its complex with CAR (2.8 angstroms) reveal an unusual immunoglobulin-domain assembly for JAML and a charged interface that confers high specificity. Biochemical and mutagenesis studies illustrate how CAR-mediated clustering of JAML recruits phosphoinositide 3-kinase (P13K) to a JAML intracellular sequence motif as delineated for the alphabeta T cell costimulatory receptor CD28. Thus, CAR and JAML are cell signaling receptors of the immune system with implications for asthma, cancer, and chronic nonhealing wounds.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2951132/" 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/PMC2951132/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verdino, Petra -- Witherden, Deborah A -- Havran, Wendy L -- Wilson, Ian A -- AI064811/AI/NIAID NIH HHS/ -- AI42266/AI/NIAID NIH HHS/ -- AI52257/AI/NIAID NIH HHS/ -- CA58896/CA/NCI NIH HHS/ -- R01 AI036964/AI/NIAID NIH HHS/ -- R01 AI052257/AI/NIAID NIH HHS/ -- R01 AI052257-05/AI/NIAID NIH HHS/ -- R01 AI064811/AI/NIAID NIH HHS/ -- R01 AI064811-01A1/AI/NIAID NIH HHS/ -- R01 CA058896/CA/NCI NIH HHS/ -- R01 CA058896-16A1/CA/NCI NIH HHS/ -- R01 GM080301/GM/NIGMS NIH HHS/ -- R37 AI042266/AI/NIAID NIH HHS/ -- R37 AI042266-13/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2010 Sep 3;329(5996):1210-4. doi: 10.1126/science.1187996.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20813955" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD28/metabolism ; Binding Sites ; CHO Cells ; Cell Adhesion Molecules/*chemistry/*metabolism ; Coxsackie and Adenovirus Receptor-Like Membrane Protein ; Cricetinae ; Cricetulus ; Crystallization ; Crystallography, X-Ray ; Epithelium/immunology ; Glycosylation ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Mice ; Phosphatidylinositol 3-Kinases/*metabolism ; Physicochemical Processes ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Structure, Tertiary ; Receptors, Antigen, T-Cell, gamma-delta/immunology/metabolism ; Receptors, Virus/*chemistry/*metabolism ; *Signal Transduction ; T-Lymphocyte Subsets/immunology/metabolism
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  • 89
    Publication Date: 2010-04-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharjee, Yudhijit -- New York, N.Y. -- Science. 2010 Apr 9;328(5975):150-1. doi: 10.1126/science.328.5975.150.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20378779" target="_blank"〉PubMed〈/a〉
    Keywords: Astronomical Phenomena ; *Biological Evolution ; Data Collection ; *Educational Status ; Humans ; Public Opinion ; Religion and Science ; *Science ; United States ; *United States Government Agencies
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-07-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collen, Ben -- Baillie, Jonathan E M -- New York, N.Y. -- Science. 2010 Jul 9;329(5988):140; author reply 141-2. doi: 10.1126/science.329.5988.140-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20616248" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Conservation of Natural Resources/*statistics & numerical data ; Endangered Species/*statistics & numerical data/trends ; Plants
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
    Publication Date: 2010-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gray, Michael W -- Lukes, Julius -- Archibald, John M -- Keeling, Patrick J -- Doolittle, W Ford -- New York, N.Y. -- Science. 2010 Nov 12;330(6006):920-1. doi: 10.1126/science.1198594.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21071654" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Cell Physiological Processes ; Genome, Mitochondrial ; Introns ; Mitochondria/genetics/physiology ; Models, Biological ; Mutation ; RNA Editing ; RNA Splicing ; Ribosomes/physiology ; Selection, Genetic ; Spliceosomes/genetics/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbons, Ann -- New York, N.Y. -- Science. 2010 Aug 13;329(5993):740-2. doi: 10.1126/science.329.5993.740.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20705825" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological/*genetics ; *Biological Evolution ; Gene Frequency ; Genetic Techniques ; Genetics, Population/*methods ; *Genome, Human ; Haplotypes ; Humans ; Models, Genetic ; Multifactorial Inheritance ; Mutation ; *Polymorphism, Single Nucleotide ; *Selection, Genetic
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  • 93
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-03-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marton-Lefevre, Julia -- New York, N.Y. -- Science. 2010 Mar 5;327(5970):1179. doi: 10.1126/science.1188424.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20203016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; Climate Change ; Conservation of Natural Resources ; Ecosystem ; Endangered Species ; Extinction, Biological ; International Cooperation
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  • 94
    Publication Date: 2010-10-12
    Description: Voltage- and store-operated calcium (Ca(2+)) channels are the major routes of Ca(2+) entry in mammalian cells, but little is known about how cells coordinate the activity of these channels to generate coherent calcium signals. We found that STIM1 (stromal interaction molecule 1), the main activator of store-operated Ca(2+) channels, directly suppresses depolarization-induced opening of the voltage-gated Ca(2+) channel Ca(V)1.2. STIM1 binds to the C terminus of Ca(V)1.2 through its Ca(2+) release-activated Ca(2+) activation domain, acutely inhibits gating, and causes long-term internalization of the channel from the membrane. This establishes a previously unknown function for STIM1 and provides a molecular mechanism to explain the reciprocal regulation of these two channels in cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Chan Young -- Shcheglovitov, Aleksandr -- Dolmetsch, Ricardo -- DP1 OD003889/OD/NIH HHS/ -- DP1OD003889/OD/NIH HHS/ -- R01 NS048564/NS/NINDS NIH HHS/ -- R21MH087898/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2010 Oct 1;330(6000):101-5. doi: 10.1126/science.1191027.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929812" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels, L-Type/chemistry/genetics/*metabolism ; Calcium Signaling ; Cell Line ; Cell Membrane/*metabolism ; Humans ; Ion Channel Gating ; Jurkat Cells ; Membrane Proteins/chemistry/genetics/*metabolism ; Models, Biological ; Neoplasm Proteins/chemistry/genetics/*metabolism ; Neurons/*metabolism ; Patch-Clamp Techniques ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Rats, Sprague-Dawley ; T-Lymphocytes/*metabolism
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  • 95
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-11-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Eric -- New York, N.Y. -- Science. 2010 Nov 26;330(6008):1170-1. doi: 10.1126/science.330.6008.1170.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21109644" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biodiversity ; *Conservation of Natural Resources/economics ; Ecuador ; *International Cooperation ; Petroleum ; *Trees
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  • 96
    Publication Date: 2010-02-20
    Description: Modern cetaceans, a poster child of evolution, play an important role in the ocean ecosystem as apex predators and nutrient distributors, as well as evolutionary "stepping stones" for the deep sea biota. Recent discussions on the impact of climate change and marine exploitation on current cetacean populations may benefit from insights into what factors have influenced cetacean diversity in the past. Previous studies suggested that the rise of diatoms as dominant marine primary producers and global temperature change were key factors in the evolution of modern whales. Based on a comprehensive diversity data set, we show that much of observed cetacean paleodiversity can indeed be explained by diatom diversity in conjunction with variations in climate as indicated by oxygen stable isotope records (delta18O).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Felix G -- Uhen, Mark D -- New York, N.Y. -- Science. 2010 Feb 19;327(5968):993-6. doi: 10.1126/science.1185581.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of Otago, 360 Leith Walk, Post Office Box 56, Dunedin, Otago 9016, New Zealand. f.g.marx@bristol.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20167785" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biodiversity ; *Biological Evolution ; *Cetacea/classification/physiology ; *Climate Change ; *Diatoms ; *Ecosystem ; Feeding Behavior ; Food Chain ; *Fossils ; Geologic Sediments ; Oceans and Seas ; Seawater ; Temperature ; *Whales/classification/physiology
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  • 97
    Publication Date: 2010-02-06
    Description: Recent studies have identified range expansion as a potential driver of speciation. Yet it remains poorly understood how, under identical extrinsic settings, differential tendencies for geographic movement of taxa originate and subsequently affect diversification. We identified multiple traits that predict large distributional ranges in extant species of toads (Bufonidae) and used statistical methods to define and phylogenetically reconstruct an optimal range-expansion phenotype. Our results indicate that lineage-specific range-shifting abilities increased through an accumulation of adaptive traits that culminated in such a phenotype. This initiated the episode of global colonization and triggered the major radiation of toads. Evolution toward a range-expansion phenotype might be crucial to understanding both ancient widespread radiations and the evolutionary background of contemporary invasive species such as the cane toad.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Bocxlaer, Ines -- Loader, Simon P -- Roelants, Kim -- Biju, S D -- Menegon, Michele -- Bossuyt, Franky -- New York, N.Y. -- Science. 2010 Feb 5;327(5966):679-82. doi: 10.1126/science.1181707.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Amphibian Evolution Lab, Unit of Ecology and Systematics, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20133569" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Biological ; Africa ; Animals ; Asia ; Australia ; Bayes Theorem ; *Biological Evolution ; *Bufonidae/anatomy & histology/classification/genetics/physiology ; Genetic Speciation ; Geography ; Likelihood Functions ; Molecular Sequence Data ; Phenotype ; Phylogeny ; Population Dynamics ; Reproduction ; South America ; Species Specificity
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  • 98
    Publication Date: 2010-02-13
    Description: Synaptic vesicle fusion in brain synapses occurs in phases that are either tightly coupled to action potentials (synchronous), immediately following action potentials (asynchronous), or as stochastic events in the absence of action potentials (spontaneous). Synaptotagmin-1, -2, and -9 are vesicle-associated Ca2+ sensors for synchronous release. Here we found that double C2 domain (Doc2) proteins act as Ca2+ sensors to trigger spontaneous release. Although Doc2 proteins are cytosolic, they function analogously to synaptotagmin-1 but with a higher Ca2+ sensitivity. Doc2 proteins bound to N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complexes in competition with synaptotagmin-1. Thus, different classes of multiple C2 domain-containing molecules trigger synchronous versus spontaneous fusion, which suggests a general mechanism for synaptic vesicle fusion triggered by the combined actions of SNAREs and multiple C2 domain-containing proteins.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846320/" 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/PMC2846320/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Groffen, Alexander J -- Martens, Sascha -- Diez Arazola, Rocio -- Cornelisse, L Niels -- Lozovaya, Natalia -- de Jong, Arthur P H -- Goriounova, Natalia A -- Habets, Ron L P -- Takai, Yoshimi -- Borst, J Gerard -- Brose, Nils -- McMahon, Harvey T -- Verhage, Matthijs -- MC_U105178795/Medical Research Council/United Kingdom -- U.1051.02.007(78795)/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2010 Mar 26;327(5973):1614-8. doi: 10.1126/science.1183765. Epub 2010 Feb 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Functional Genomics, CNCR, Neuroscience Campus Amsterdam, VU University and VU Medical Center, Amsterdam, 1081 HV, Netherlands. sander.groffen@cncr.vu.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20150444" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Binding Sites ; Calcium/*metabolism ; Calcium-Binding Proteins/chemistry/genetics/*metabolism ; Cells, Cultured ; Excitatory Postsynaptic Potentials ; Hippocampus/cytology ; Inhibitory Postsynaptic Potentials ; Membrane Fusion ; Mice ; Mice, Knockout ; Mutant Proteins/genetics/metabolism ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/physiology ; Neurotransmitter Agents/*metabolism ; Patch-Clamp Techniques ; Protein Structure, Tertiary ; Purkinje Cells/physiology ; Rats ; SNARE Proteins/metabolism ; *Synaptic Transmission ; Synaptic Vesicles/*physiology ; Synaptotagmin I/metabolism
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  • 99
    Publication Date: 2010-04-24
    Description: Bacterial NusG is a highly conserved transcription factor that is required for most Rho activity in vivo. We show by nuclear magnetic resonance spectroscopy that Escherichia coli NusG carboxyl-terminal domain forms a complex alternatively with Rho or with transcription factor NusE, a protein identical to 30S ribosomal protein S10. Because NusG amino-terminal domain contacts RNA polymerase and the NusG carboxy-terminal domain interaction site of NusE is accessible in the ribosomal 30S subunit, NusG may act as a link between transcription and translation. Uncoupling of transcription and translation at the ends of bacterial operons enables transcription termination by Rho factor, and competition between ribosomal NusE and Rho for NusG helps to explain why Rho cannot terminate translated transcripts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burmann, Bjorn M -- Schweimer, Kristian -- Luo, Xiao -- Wahl, Markus C -- Stitt, Barbara L -- Gottesman, Max E -- Rosch, Paul -- GM037219/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2010 Apr 23;328(5977):501-4. doi: 10.1126/science.1184953.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lehrstuhl Biopolymere und Forschungszentrum fur Bio-Makromolekule, Universitat Bayreuth, Universitatsstrasse 30, 95447 Bayreuth, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20413501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Binding, Competitive ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/biosynthesis/chemistry/*genetics/metabolism ; Hydrophobic and Hydrophilic Interactions ; Models, Molecular ; Molecular Sequence Data ; Nuclear Magnetic Resonance, Biomolecular ; Operon ; Peptide Elongation Factors/chemistry/*metabolism ; Protein Binding ; *Protein Biosynthesis ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Ribosomal Proteins/chemistry/*metabolism ; Ribosome Subunits, Small, Bacterial/metabolism ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic
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  • 100
    Publication Date: 2010-10-16
    Description: Molecular dynamics (MD) simulations are widely used to study protein motions at an atomic level of detail, but they have been limited to time scales shorter than those of many biologically critical conformational changes. We examined two fundamental processes in protein dynamics--protein folding and conformational change within the folded state--by means of extremely long all-atom MD simulations conducted on a special-purpose machine. Equilibrium simulations of a WW protein domain captured multiple folding and unfolding events that consistently follow a well-defined folding pathway; separate simulations of the protein's constituent substructures shed light on possible determinants of this pathway. A 1-millisecond simulation of the folded protein BPTI reveals a small number of structurally distinct conformational states whose reversible interconversion is slower than local relaxations within those states by a factor of more than 1000.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shaw, David E -- Maragakis, Paul -- Lindorff-Larsen, Kresten -- Piana, Stefano -- Dror, Ron O -- Eastwood, Michael P -- Bank, Joseph A -- Jumper, John M -- Salmon, John K -- Shan, Yibing -- Wriggers, Willy -- New York, N.Y. -- Science. 2010 Oct 15;330(6002):341-6. doi: 10.1126/science.1187409.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D. E. Shaw Research, 120 West 45th Street, New York, NY 10036, USA. David.Shaw@DEShawResearch.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20947758" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Aprotinin/*chemistry ; Computational Biology ; Computers ; Kinetics ; Microfilament Proteins/chemistry ; Models, Molecular ; *Molecular Dynamics Simulation ; Mutant Proteins/chemistry ; *Protein Conformation ; *Protein Folding ; Protein Structure, Tertiary ; Proteins/*chemistry ; Solvents ; Thermodynamics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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