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  • *Biological Evolution  (69)
  • Phosphorylation  (59)
  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (129)
  • 2000-2004  (129)
  • 1945-1949
  • 2004  (129)
  • 1945
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Keywords
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  • American Association for the Advancement of Science (AAAS)  (129)
  • Wiley-Blackwell  (263)
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  • 2000-2004  (129)
  • 1945-1949
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  • 1
    Publication Date: 2004-11-20
    Description: An autoregulatory transcription-translation feedback loop is thought to be essential in generating circadian rhythms in any model organism. In the cyanobacterium Synechococcus elongatus, the essential clock protein KaiC is proposed to form this type of transcriptional negative feedback. Nevertheless, we demonstrate here temperature-compensated, robust circadian cycling of KaiC phosphorylation even without kaiBC messenger RNA accumulation under continuous dark conditions. This rhythm persisted in the presence of a transcription or translation inhibitor. Moreover, kinetic profiles in the ratio of KaiC autophosphorylation-dephosphorylation were also temperature compensated in vitro. Thus, the cyanobacterial clock can keep time independent of de novo transcription and translation processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomita, Jun -- Nakajima, Masato -- Kondo, Takao -- Iwasaki, Hideo -- New York, N.Y. -- Science. 2005 Jan 14;307(5707):251-4. Epub 2004 Nov 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550625" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/biosynthesis/*metabolism ; *Circadian Rhythm ; Circadian Rhythm Signaling Peptides and Proteins ; Darkness ; Feedback, Physiological ; Light ; Mutation ; Operon ; Phosphorylation ; Protein Biosynthesis ; RNA, Bacterial/metabolism ; RNA, Messenger/metabolism ; Recombinant Proteins/metabolism ; Synechococcus/*genetics/*metabolism ; Temperature ; Transcription, Genetic
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  • 2
    Publication Date: 2004-10-02
    Description: Over the past 50 million years, successive clades of large carnivorous mammals diversified and then declined to extinction. In most instances, the cause of the decline remains a puzzle. Here we argue that energetic constraints and pervasive selection for larger size (Cope's rule) in carnivores lead to dietary specialization (hypercarnivory) and increased vulnerability to extinction. In two major clades of extinct North American canids, the evolution of large size was associated with a dietary shift to hypercarnivory and a decline in species durations. Thus, selection for attributes that promoted individual success resulted in progressive evolutionary failure of their clades.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Valkenburgh, Blaire -- Wang, Xiaoming -- Damuth, John -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):101-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolutionary Biology, University of California at Los Angeles, Los Angeles, CA 90095-1606, USA. bvanval@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459388" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Body Constitution ; Body Weight ; *Carnivora/anatomy & histology/classification/physiology ; Cuspid/anatomy & histology ; *Diet ; *Fossils ; Incisor/anatomy & histology ; Jaw/anatomy & histology ; Molar/anatomy & histology ; North America ; Paleodontology ; Population Density ; Population Dynamics ; Predatory Behavior ; Principal Component Analysis ; Selection, Genetic
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  • 3
    Publication Date: 2004-01-06
    Description: MDM2 binds the p53 tumor suppressor protein with high affinity and negatively modulates its transcriptional activity and stability. Overexpression of MDM2, found in many human tumors, effectively impairs p53 function. Inhibition of MDM2-p53 interaction can stabilize p53 and may offer a novel strategy for cancer therapy. Here, we identify potent and selective small-molecule antagonists of MDM2 and confirm their mode of action through the crystal structures of complexes. These compounds bind MDM2 in the p53-binding pocket and activate the p53 pathway in cancer cells, leading to cell cycle arrest, apoptosis, and growth inhibition of human tumor xenografts in nude mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vassilev, Lyubomir T -- Vu, Binh T -- Graves, Bradford -- Carvajal, Daisy -- Podlaski, Frank -- Filipovic, Zoran -- Kong, Norman -- Kammlott, Ursula -- Lukacs, Christine -- Klein, Christian -- Fotouhi, Nader -- Liu, Emily A -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):844-8. Epub 2004 Jan 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Discovery Oncology, Roche Research Center, Hoffmann-La Roche, Inc., Nutley, NJ 07110, USA. lyubomir.vassilev@roche.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/*drug effects ; Binding Sites ; Cell Cycle/drug effects ; Cell Division/*drug effects ; Cell Line ; Cell Line, Tumor ; Cell Survival/drug effects ; Crystallization ; Crystallography, X-Ray ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/metabolism ; Dose-Response Relationship, Drug ; Gene Expression ; Genes, p53 ; Humans ; Hydrophobic and Hydrophilic Interactions ; Imidazoles/chemistry/metabolism/*pharmacology ; Mice ; Mice, Nude ; Models, Molecular ; Molecular Weight ; NIH 3T3 Cells ; Neoplasm Transplantation ; Neoplasms, Experimental/drug therapy/metabolism/*pathology ; *Nuclear Proteins ; Phosphorylation ; Piperazines/chemistry/metabolism/*pharmacology ; Protein Conformation ; Proto-Oncogene Proteins/*antagonists & inhibitors/chemistry/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Stereoisomerism ; Transplantation, Heterologous ; Tumor Suppressor Protein p53/*metabolism
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-12-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2172.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618495" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Breeding ; Dogs/*anatomy & histology/*genetics/growth & development ; Genetic Variation ; Hindlimb ; Neoplasm Proteins/genetics ; Nose/anatomy & histology ; Phenotype ; Selection, Genetic ; Skull/anatomy & histology ; *Tandem Repeat Sequences ; Toes/anatomy & histology ; Transcription Factors/genetics
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  • 5
    Publication Date: 2004-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):796-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Brain/cytology ; Circadian Rhythm ; *Eye ; Gene Duplication ; Genome ; Homeodomain Proteins/*analysis ; Humans ; Light ; Photoreceptor Cells, Invertebrate/chemistry/*cytology ; Photoreceptor Cells, Vertebrate/chemistry/cytology ; Polychaeta/chemistry/*cytology/*genetics ; Retinal Ganglion Cells/cytology ; Rod Opsins/analysis/*chemistry/*genetics
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-05-08
    Description: I report on tiny skeletons of stem-group hummingbirds from the early Oligocene of Germany that are of essentially modern appearance and exhibit morphological specializations toward nectarivory and hovering flight. These are the oldest fossils of modern-type hummingbirds, which had not previously been reported from the Old World. The findings demonstrate that early hummingbird evolution was not restricted to the New World. They further suggest that bird-flower coevolution dates back to the early Oligocene and open another view on the origin of ornithophily in Old World plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayr, Gerald -- New York, N.Y. -- Science. 2004 May 7;304(5672):861-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Forschungsinstitut Senckenberg, Division of Ornithology, Senckenberganlage 25, D-60325 Frankfurt a.M., Germany. Gerald.Mayr@senckenberg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131303" target="_blank"〉PubMed〈/a〉
    Keywords: Americas ; Animals ; *Biological Evolution ; *Birds/anatomy & histology/classification ; Bone and Bones/anatomy & histology ; Europe ; Flight, Animal ; Flowers ; *Fossils ; Germany
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):37.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Awards and Prizes ; Berlin ; *Biological Evolution ; Biology/history ; Birds ; History, 20th Century ; History, 21st Century ; Museums/*history ; United States
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  • 8
    Publication Date: 2004-11-06
    Description: Phosphorylation of the human histone variant H2A.X and H2Av, its homolog in Drosophila melanogaster, occurs rapidly at sites of DNA double-strand breaks. Little is known about the function of this phosphorylation or its removal during DNA repair. Here, we demonstrate that the Drosophila Tip60 (dTip60) chromatin-remodeling complex acetylates nucleosomal phospho-H2Av and exchanges it with an unmodified H2Av. Both the histone acetyltransferase dTip60 as well as the adenosine triphosphatase Domino/p400 catalyze the exchange of phospho-H2Av. Thus, these data reveal a previously unknown mechanism for selective histone exchange that uses the concerted action of two distinct chromatin-remodeling enzymes within the same multiprotein complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kusch, Thomas -- Florens, Laurence -- Macdonald, W Hayes -- Swanson, Selene K -- Glaser, Robert L -- Yates, John R 3rd -- Abmayr, Susan M -- Washburn, Michael P -- Workman, Jerry L -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2084-7. Epub 2004 Nov 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA. tnk@stowers-institute.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528408" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/genetics/*metabolism ; Adenosine Triphosphatases/metabolism ; Animals ; Cell Line ; *DNA Damage ; DNA Repair ; Dimerization ; Drosophila Proteins/genetics/metabolism ; Drosophila melanogaster/embryology/genetics/*metabolism ; Embryo, Nonmammalian/metabolism ; Histone Acetyltransferases ; Histones/*metabolism ; Multiprotein Complexes/*metabolism ; Nucleosomes/*metabolism ; Phosphorylation ; RNA Interference ; Recombinant Proteins/metabolism ; Transcription Factors/metabolism
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-06-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1736.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15205506" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Alleles ; Animals ; *Biological Evolution ; Breeding ; Crosses, Genetic ; Environment ; Extremities/growth & development ; Fresh Water ; Gene Expression Regulation ; Genes ; Genome ; Homeodomain Proteins/*genetics/metabolism ; Mutation ; Paired Box Transcription Factors ; Seawater ; Selection, Genetic ; Smegmamorpha/*anatomy & histology/*genetics ; Transcription Factors/*genetics/metabolism
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  • 10
    Publication Date: 2004-09-11
    Description: The turnover of Jun proteins, like that of other transcription factors, is regulated through ubiquitin-dependent proteolysis. Usually, such processes are regulated by extracellular stimuli through phosphorylation of the target protein, which allows recognition by F box-containing E3 ubiquitin ligases. In the case of c-Jun and JunB, we found that extracellular stimuli also modulate protein turnover by regulating the activity of an E3 ligase by means of its phosphorylation. Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch. This pathway modulates cytokine production by effector T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Min -- Labuda, Tord -- Xia, Ying -- Gallagher, Ewen -- Fang, Deyu -- Liu, Yun-Cai -- Karin, Michael -- AI43477/AI/NIAID NIH HHS/ -- ES04151/ES/NIEHS NIH HHS/ -- ES06376/ES/NIEHS NIH HHS/ -- R21AI48542/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):271-5. Epub 2004 Sep 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0723, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15358865" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD28/immunology ; CD4-Positive T-Lymphocytes/immunology/*metabolism ; Interferon-gamma/metabolism ; Interleukins/metabolism ; Lymphocyte Activation ; *MAP Kinase Kinase Kinase 1 ; MAP Kinase Kinase Kinases/genetics/metabolism ; Mice ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinase 9 ; Mitogen-Activated Protein Kinases/*metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-jun/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Receptors, Antigen, T-Cell/immunology ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/*metabolism ; Th2 Cells/cytology/immunology/metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*metabolism
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  • 11
    Publication Date: 2004-05-25
    Description: Tyrosine phosphorylation, regulated by protein tyrosine phosphatases (PTPs) and kinases (PTKs), is important in signaling pathways underlying tumorigenesis. A mutational analysis of the tyrosine phosphatase gene superfamily in human cancers identified 83 somatic mutations in six PTPs (PTPRF, PTPRG, PTPRT, PTPN3, PTPN13, PTPN14), affecting 26% of colorectal cancers and a smaller fraction of lung, breast, and gastric cancers. Fifteen mutations were nonsense, frameshift, or splice-site alterations predicted to result in truncated proteins lacking phosphatase activity. Five missense mutations in the most commonly altered PTP (PTPRT) were biochemically examined and found to reduce phosphatase activity. Expression of wild-type but not a mutant PTPRT in human cancer cells inhibited cell growth. These observations suggest that the mutated tyrosine phosphatases are tumor suppressor genes, regulating cellular pathways that may be amenable to therapeutic intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Zhenghe -- Shen, Dong -- Parsons, D Williams -- Bardelli, Alberto -- Sager, Jason -- Szabo, Steve -- Ptak, Janine -- Silliman, Natalie -- Peters, Brock A -- van der Heijden, Michiel S -- Parmigiani, Giovanni -- Yan, Hai -- Wang, Tian-Li -- Riggins, Greg -- Powell, Steven M -- Willson, James K V -- Markowitz, Sanford -- Kinzler, Kenneth W -- Vogelstein, Bert -- Velculescu, Victor E -- CA 43460/CA/NCI NIH HHS/ -- CA 57345/CA/NCI NIH HHS/ -- CA 62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 May 21;304(5674):1164-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sidney Kimmel Comprehensive Cancer Center, Howard Hughes Medical Institute, Johns Hopkins University Medical Institutions, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155950" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Cell Division ; Codon, Nonsense ; Colorectal Neoplasms/*enzymology/*genetics ; Computational Biology ; *DNA Mutational Analysis ; Exons ; Frameshift Mutation ; Genes, Tumor Suppressor ; Humans ; Kinetics ; Markov Chains ; *Mutation ; Mutation, Missense ; Nerve Tissue Proteins/chemistry/genetics/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 13 ; Protein Tyrosine Phosphatase, Non-Receptor Type 3 ; Protein Tyrosine Phosphatases/chemistry/*genetics/metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 5 ; Signal Transduction ; Transfection ; Tyrosine/*metabolism
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  • 12
    Publication Date: 2004-09-18
    Description: Epidemiological observations have led to the hypothesis that the risk of developing some chronic noncommunicable diseases in adulthood is influenced not only by genetic and adult life-style factors but also by environmental factors acting in early life. Research in evolutionary biology, developmental biology, and animal and human physiology provides support for this idea and suggests that environmental processes influencing the propensity to disease in adulthood operate during the periconceptual, fetal, and infant phases of life. This "developmental origins of health and disease" concept may have important biological, medical, and socioeconomic implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gluckman, Peter D -- Hanson, Mark A -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1733-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Liggins Institute, University of Auckland and National Research Centre for Growth and Development, 2-6 Park Avenue, Grafton, Private Bag 92019, Auckland, New Zealand. pd.gluckman@auckland.ac.nz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375258" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birth Weight ; *Chronic Disease ; Cues ; Disease/*etiology ; *Disease Susceptibility ; *Embryonic and Fetal Development ; *Environment ; Female ; Humans ; Infant, Newborn ; Life Style ; Nutritional Physiological Phenomena ; Pregnancy ; Prenatal Exposure Delayed Effects ; Risk Factors
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  • 13
    Publication Date: 2004-02-07
    Description: Theory on the evolution of virulence generally predicts selection for an optimal level of virulence determined by trade-offs with transmission and/or recovery. Here we consider the evolution of pathogen virulence in hosts who acquire long-lived immunity and live in a spatially structured population. We show theoretically that large shifts in virulence may occur in pathogen populations as a result of a bistability in evolutionary dynamics caused by the local contact or social population structure of the host. This model provides an explanation for the rapid emergence of the highly virulent strains of rabbit hemorrhagic disease virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boots, M -- Hudson, P J -- Sasaki, A -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):842-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal and Plant Sciences, University of Sheffield, Western Bank, Sheffield S10 2TN, UK. m.boots@sheffield.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764881" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Caliciviridae Infections/epidemiology/*veterinary/virology ; *Communicable Diseases/epidemiology/immunology/transmission ; Disease Susceptibility ; Hemorrhagic Disease Virus, Rabbit/genetics/*pathogenicity ; Humans ; Immunity, Active ; Mathematics ; Models, Biological ; Molecular Epidemiology ; Mutation ; Recombination, Genetic ; *Virulence/genetics
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  • 14
    Publication Date: 2004-11-30
    Description: When exposed to increased dissolved solute in their environment (hyperosmotic stress), all eukaryotic cells respond by rapidly activating a conserved mitogen-activated protein kinase cascade, known in budding yeast Saccharomyces cerevisiae as the high osmolarity glycerol (HOG) pathway. Intensive genetic and biochemical analysis in this organism has revealed the presumptive osmosensors, downstream signaling components, and metabolic and transcriptional changes that allow cells to cope with this stressful condition. These findings have had direct application to understanding stress sensing and control of transcription by stress-activated mitogen-activated protein kinases in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westfall, Patrick J -- Ballon, Daniel R -- Thorner, Jeremy -- GM-21841/GM/NIGMS NIH HHS/ -- GM-68343/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1511-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biochemistry and Molecular Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567851" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; GTPase-Activating Proteins/metabolism ; Glycerol/*metabolism ; Intracellular Signaling Peptides and Proteins ; *MAP Kinase Signaling System ; Membrane Proteins/metabolism ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinases/*metabolism ; Osmolar Concentration ; Phosphorylation ; Protein Kinases/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*metabolism ; Transcription Factors/metabolism ; Transcription, Genetic
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Tomaso, Anthony W -- Weissman, Irving L -- AI10332/AI/NIAID NIH HHS/ -- AI41588/AI/NIAID NIH HHS/ -- R01 AI041588/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):977.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA. tdet@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963321" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Biological Evolution ; Cloning, Molecular ; Crosses, Genetic ; Heterozygote ; Homozygote ; Immunogenetics ; *Polymorphism, Genetic ; Urochordata/*genetics/growth & development/immunology
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  • 16
    Publication Date: 2004-02-21
    Description: PTEN is a tumor suppressor protein that dephosphorylates phosphatidylinositol 3,4,5 trisphosphate and antagonizes the phosphatidylinositol-3 kinase signaling pathway. We show here that PTEN can also inhibit cell migration through its C2 domain, independent of its lipid phosphatase activity. This activity depends on the protein phosphatase activity of PTEN and on dephosphorylation at a single residue, threonine(383). The ability of PTEN to control cell migration through its C2 domain is likely to be an important feature of its tumor suppressor activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftopoulou, Myrto -- Etienne-Manneville, Sandrine -- Self, Annette -- Nicholls, Sarah -- Hall, Alan -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1179-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory for Molecular Cell Biology and Cell Biology Unit, Cancer Research UK Oncogene and Signal Transduction Group, University College London, Gower Street, London WC1E 6BT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Catalysis ; Catalytic Domain ; Cell Line, Tumor ; Cell Movement/*physiology ; Cercopithecus aethiops ; Glioma ; Humans ; Mutation ; PTEN Phosphohydrolase ; Phosphoprotein Phosphatases/chemistry/metabolism ; Phosphoric Monoester Hydrolases/*chemistry/genetics/metabolism/*physiology ; Phosphorylation ; Phosphothreonine/metabolism ; Precipitin Tests ; Protein Structure, Tertiary ; Recombinant Proteins/pharmacology ; Sequence Deletion ; Transfection ; Tumor Suppressor Proteins/*chemistry/genetics/metabolism/*physiology
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  • 17
    Publication Date: 2004-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasmussen, Steen -- Chen, Liaohai -- Deamer, David -- Krakauer, David C -- Packard, Norman H -- Stadler, Peter F -- Bedau, Mark A -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):963-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Los Alamos National Laboratory, Los Alamos, NM 87545, USA. steen@lanl.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963315" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biopolymers ; Catalysis ; *Cells ; Combinatorial Chemistry Techniques ; Computer Simulation ; *Evolution, Chemical ; Genetic Engineering ; *Life ; Lipid Metabolism ; Lipids/chemistry ; Liposomes ; Mycoplasma genitalium/genetics/metabolism ; *Origin of Life ; Peptide Nucleic Acids/chemistry/metabolism ; RNA/chemistry/metabolism ; Selection, Genetic ; Thermodynamics
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  • 18
    Publication Date: 2004-12-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keeling, Patrick J -- Archibald, John M -- Fast, Naomi M -- Palmer, Jeffrey D -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2191; author reply 2191.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada. pkeeling@interchange.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618503" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; *Biological Evolution ; Chlorophyta/genetics/physiology ; *Eukaryota/genetics/physiology ; Gene Transfer, Horizontal ; Phylogeny ; *Phytoplankton/genetics ; Plastids/genetics/physiology ; Rhodophyta/genetics/physiology ; Symbiosis
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  • 19
    Publication Date: 2004-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1467.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Extremities/anatomy & histology ; Feeding Behavior ; *Fossils ; *Horses/anatomy & histology ; Paleodontology ; *Poaceae ; Time ; Tooth/*anatomy & histology ; Trees
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muoio, Deborah M -- Newgard, Christopher B -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):425-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486283" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cells, Cultured ; DNA-Binding Proteins/genetics/metabolism ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases ; Enzyme Activation ; Homeostasis ; Humans ; Insulin/*metabolism ; Insulin Receptor Substrate Proteins ; Insulin Resistance/*physiology ; Islets of Langerhans/metabolism ; Liver/metabolism ; Membrane Proteins/metabolism ; Mice ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinases/*metabolism ; Muscle, Skeletal/metabolism ; Nuclear Proteins/genetics/metabolism ; Obesity/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Transcription Factors ; eIF-2 Kinase/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-10-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, Alan -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):65-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory for Molecular Cell Biology & Cell Biology Unit, University College, London WC1E 6BT, UK. alan.hall@ucl. ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459376" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/metabolism/virology ; Actins/metabolism ; Catenins ; Cell Adhesion Molecules/metabolism ; Cell Membrane/metabolism/virology ; Enzyme Activation ; Kinesin/metabolism ; Membrane Fusion ; Membrane Glycoproteins/genetics/metabolism ; Microtubules/metabolism ; Mutation ; Phosphoproteins/metabolism ; Phosphorylation ; Vaccinia virus/genetics/growth & development/*metabolism ; Viral Envelope Proteins/genetics/*metabolism ; Viral Structural Proteins/*metabolism ; src-Family Kinases/*metabolism
    Print ISSN: 0036-8075
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  • 22
    Publication Date: 2004-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Witt, Christopher C -- Brumfield, Robb T -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):173; author reply 173.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences and, Museum of Natural Science, Louisiana State University, Baton Rouge, LA 70803, USA. cwitt@lsu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14715994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Evolution, Molecular ; Genes ; Genetics, Population ; Mathematics ; Models, Statistical ; *Phylogeny ; Plants/classification/genetics ; Sampling Studies ; Selection Bias
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  • 23
    Publication Date: 2004-10-23
    Description: Signaling by the transcription factor nuclear factor kappa B (NF-kappaB) involves its release from inhibitor kappa B (IkappaB) in the cytosol, followed by translocation into the nucleus. NF-kappaB regulation of IkappaBalpha transcription represents a delayed negative feedback loop that drives oscillations in NF-kappaB translocation. Single-cell time-lapse imaging and computational modeling of NF-kappaB (RelA) localization showed asynchronous oscillations following cell stimulation that decreased in frequency with increased IkappaBalpha transcription. Transcription of target genes depended on oscillation persistence, involving cycles of RelA phosphorylation and dephosphorylation. The functional consequences of NF-kappaB signaling may thus depend on number, period, and amplitude of oscillations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nelson, D E -- Ihekwaba, A E C -- Elliott, M -- Johnson, J R -- Gibney, C A -- Foreman, B E -- Nelson, G -- See, V -- Horton, C A -- Spiller, D G -- Edwards, S W -- McDowell, H P -- Unitt, J F -- Sullivan, E -- Grimley, R -- Benson, N -- Broomhead, D -- Kell, D B -- White, M R H -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):704-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Cell Imaging, School of Biological Sciences, Bioscience Research Building, Crown Street, Liverpool, L69 7ZB, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499023" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Computer Simulation ; Cytoplasm/metabolism ; Etoposide/pharmacology ; Feedback, Physiological ; *Gene Expression Regulation ; HeLa Cells ; Humans ; I-kappa B Proteins/genetics/metabolism ; Models, Biological ; NF-kappa B/*metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription Factor RelA ; Transcription, Genetic ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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  • 24
    Publication Date: 2004-09-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokstad, Erik -- New York, N.Y. -- Science. 2004 Sep 3;305(5689):1386.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15353767" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Echinodermata/*physiology ; Fishes ; *Fossils ; *Predatory Behavior ; *Regeneration
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  • 25
    Publication Date: 2004-01-24
    Description: Jun N-terminal kinases (JNKs) are essential for neuronal microtubule assembly and apoptosis. Phosphorylation of the activating protein 1 (AP1) transcription factor c-Jun, at multiple sites within its transactivation domain, is required for JNK-induced neurotoxicity. We report that in neurons the stability of c-Jun is regulated by the E3 ligase SCF(Fbw7), which ubiquitinates phosphorylated c-Jun and facilitates c-Jun degradation. Fbw7 depletion resulted in accumulation of phosphorylated c-Jun, stimulation of AP1 activity, and neuronal apoptosis. SCF(Fbw7) therefore antagonizes the apoptotic c-Jun-dependent effector arm of JNK signaling, allowing neurons to tolerate potentially neurotoxic JNK activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nateri, Abdolrahman S -- Riera-Sans, Lluis -- Da Costa, Clive -- Behrens, Axel -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1374-8. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mammalian Genetics Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739463" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Base Sequence ; Cell Cycle Proteins/genetics/*metabolism ; Cell Line ; F-Box Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Mice ; Mitogen-Activated Protein Kinases/*metabolism ; Molecular Sequence Data ; Neurons/*physiology ; PC12 Cells ; Phosphorylation ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Small Interfering/metabolism ; Rats ; Transcription Factor AP-1/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/genetics/*metabolism
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  • 26
    Publication Date: 2004-06-26
    Description: The nuclear factor-kappa B (NF-kappaB) family of transcription factors plays a seminal role in inflammation, apoptosis, development, and cancer. Modulation of NF-kappaB-mediated gene expression in response to diverse signals is coordinated by the IkappaB kinase (IKK) complex. We identified ELKS, an essential regulatory subunit of the IKK complex. Silencing ELKS expression by RNA interference blocked induced expression of NF-kappaB target genes, including the NF-kappaB inhibitor IkappaBalpha and proinflammatory genes such as cyclo-oxygenase 2 and interleukin 8. These cells were also not protected from apoptosis in response to cytokines. ELKS likely functions by recruiting IkappaBalpha to the IKK complex and thus serves a regulatory function for IKK activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ducut Sigala, Jeanette L -- Bottero, Virginie -- Young, David B -- Shevchenko, Andrej -- Mercurio, Frank -- Verma, Inder M -- New York, N.Y. -- Science. 2004 Jun 25;304(5679):1963-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Sciences, 10010 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/15218148" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Animals ; Apoptosis ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cyclooxygenase 2 ; Gene Expression ; Genes, Reporter ; HeLa Cells ; Humans ; I-kappa B Kinase ; I-kappa B Proteins/genetics/metabolism ; Interleukin-1/pharmacology ; Interleukin-8/genetics ; Isoenzymes/genetics ; Membrane Proteins ; Mice ; Mice, Knockout ; Mitogen-Activated Protein Kinases/metabolism ; Mutation ; NF-kappa B/*metabolism ; Nerve Tissue Proteins/genetics/*metabolism ; Phosphorylation ; Precipitin Tests ; Prostaglandin-Endoperoxide Synthases/genetics ; Protein-Serine-Threonine Kinases/*metabolism ; RNA Interference ; Tumor Necrosis Factor-alpha/pharmacology
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  • 27
    Publication Date: 2004-11-13
    Description: We assess the phylogenetic potential of approximately 300,000 protein sequences sampled from Swiss-Prot and GenBank. Although only a small subset of these data was potentially phylogenetically informative, this subset retained a substantial fraction of the original taxonomic diversity. Sampling biases in the databases necessitate building phylogenetic data sets that have large numbers of missing entries. However, an analysis of two "supermatrices" suggests that even data sets with as much as 92% missing data can provide insights into broad sections of the tree of life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Driskell, Amy C -- Ane, Cecile -- Burleigh, J Gordon -- McMahon, Michelle M -- O'meara, Brian C -- Sanderson, Michael J -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1172-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Evolution and Ecology, University of California, One Shields Avenue, Davis, CA 95616, USA. acdriskell@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539599" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anopheles/classification/genetics ; Biodiversity ; *Biological Evolution ; Classification ; Computational Biology ; *Databases, Nucleic Acid ; *Databases, Protein ; Multigene Family ; *Phylogeny ; Plant Proteins/genetics ; Plants/classification/genetics ; Spodoptera/classification/genetics
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-06-19
    Description: The Hedgehog (Hh) signaling pathway is intimately linked to cell growth and differentiation, with normal roles in embryonic pattern formation and adult tissue homeostasis and pathological roles in tumor initiation and growth. Recent advances in our understanding of Hh response have resulted from the identification of new pathway components and new mechanisms of action for old pathway components. The most striking new finding is that signal transmission from membrane to cytoplasm proceeds through recruitment, by the seven-transmembrane protein Smoothened, of an atypical kinesin, which routes pathway activation by interaction with other components of a complex that includes the latent zinc finger transcription factor, Ci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lum, Lawrence -- Beachy, Philip A -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1755-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, 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/15205520" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; DNA-Binding Proteins/metabolism ; Drosophila/metabolism ; Drosophila Proteins/*metabolism ; Gene Expression Regulation ; Hedgehog Proteins ; Kinesin/metabolism ; Mammals/metabolism ; Membrane Proteins/metabolism ; Models, Biological ; Phosphorylation ; Protein Transport ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled/metabolism ; *Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors
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  • 29
    Publication Date: 2004-01-31
    Description: Protein tyrosine kinases and phosphatases cooperate to regulate normal immune cell function. We examined the role of PEST domain-enriched tyrosine phosphatase (PEP) in regulating T cell antigen-receptor function during thymocyte development and peripheral T cell differentiation. Although normal naive T cell functions were retained in pep-deficient mice, effector/memory T cells demonstrated enhanced activation of Lck. In turn, this resulted in increased expansion and function of the effector/memory T cell pool, which was also associated with spontaneous development of germinal centers and elevated serum antibody levels. These results revealed a central role for PEP in negatively regulating specific aspects of T cell development and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, Kiminori -- Martin, Flavius -- Huang, Guangming -- Tumas, Dan -- Diehl, Lauri -- Chan, Andrew C -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Genentech, Inc., One DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752163" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmunity ; B-Lymphocytes/physiology ; CD4-Positive T-Lymphocytes/immunology/physiology ; CD8-Positive T-Lymphocytes/immunology/physiology ; Cell Cycle ; Gene Targeting ; Germinal Center/physiology ; Hydrogen-Ion Concentration ; Immunoglobulins/blood ; *Immunologic Memory ; Lymphocyte Activation ; Lymphocyte Count ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 12 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Receptors, Antigen, T-Cell/genetics/immunology ; Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/*immunology/physiology
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  • 30
    Publication Date: 2004-08-07
    Description: The cascade of events that leads to vaccinia-induced actin polymerization requires Src-dependent tyrosine phosphorylation of the viral membrane protein A36R. We found that a localized outside-in signaling cascade induced by the viral membrane protein B5R is required to potently activate Src and induce A36R phosphorylation at the plasma membrane. In addition, Src-mediated phosphorylation of A36R regulated the ability of virus particles to recruit and release conventional kinesin. Thus, Src activity regulates the transition between cytoplasmic microtubule transport and actin-based motility at the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newsome, Timothy P -- Scaplehorn, Niki -- Way, Michael -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):124-9. Epub 2004 Aug 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Motility Laboratory, Room 529, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297625" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Cell Line ; Cell Membrane/metabolism/virology ; Chickens ; Consensus Sequence ; Enzyme Activation ; HeLa Cells ; Humans ; Kinesin/metabolism ; Membrane Glycoproteins/chemistry/metabolism ; Microtubules/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Recombinant Fusion Proteins/metabolism ; Vaccinia virus/genetics/*metabolism/physiology ; Viral Envelope Proteins/chemistry/metabolism ; Viral Structural Proteins/*metabolism ; Virion/metabolism ; src-Family Kinases/*metabolism
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  • 31
    Publication Date: 2004-05-08
    Description: Prostaglandin E2 (PGE2) is a crucial mediator of inflammatory pain sensitization. Here, we demonstrate that inhibition of a specific glycine receptor subtype (GlyR alpha3) by PGE2-induced receptor phosphorylation underlies central inflammatory pain sensitization. We show that GlyR alpha3 is distinctly expressed in superficial layers of the spinal cord dorsal horn. Mice deficient in GlyR alpha3 not only lack the inhibition of glycinergic neurotransmission by PGE2 seen in wild-type mice but also show a reduction in pain sensitization induced by spinal PGE2 injection or peripheral inflammation. Thus, GlyR alpha3 may provide a previously unrecognized molecular target in pain therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harvey, Robert J -- Depner, Ulrike B -- Wassle, Heinz -- Ahmadi, Seifollah -- Heindl, Cornelia -- Reinold, Heiko -- Smart, Trevor G -- Harvey, Kirsten -- Schutz, Burkhard -- Abo-Salem, Osama M -- Zimmer, Andreas -- Poisbeau, Pierrick -- Welzl, Hans -- Wolfer, David P -- Betz, Heinrich -- Zeilhofer, Hanns Ulrich -- Muller, Ulrike -- New York, N.Y. -- Science. 2004 May 7;304(5672):884-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, The School of Pharmacy, London WC1N 1AX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131310" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dinoprostone/administration & dosage/*metabolism/pharmacology ; Female ; Freund's Adjuvant ; Glycine/metabolism ; Humans ; Inflammation/metabolism/*physiopathology ; Male ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Neurons/metabolism ; Pain/*physiopathology ; Patch-Clamp Techniques ; Phosphorylation ; Posterior Horn Cells/*metabolism ; Receptors, Glycine/chemistry/genetics/*metabolism ; Signal Transduction ; Spinal Cord/*metabolism ; Synaptic Transmission ; Transfection ; Zymosan
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉York, John D -- Hunter, Tony -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2053-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Cancer Biology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA. yorkj@duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604398" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Inositol/chemistry ; Inositol Phosphates/*metabolism ; Models, Biological ; Molecular Conformation ; Nuclear Proteins/*metabolism ; Phosphates/*metabolism ; Phosphatidylinositols/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/*metabolism ; Second Messenger Systems ; Serine/metabolism ; *Signal Transduction
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  • 33
    Publication Date: 2004-01-24
    Description: Mammalian sex chromosomes have undergone profound changes since evolving from ancestral autosomes. By examining retroposed genes in the human and mouse genomes, we demonstrate that, during evolution, the mammalian X chromosome has generated and recruited a disproportionately high number of functional retroposed genes, whereas the autosomes experienced lower gene turnover. Most autosomal copies originating from X-linked genes exhibited testis-biased expression. Such export is incompatible with mutational bias and is likely driven by natural selection to attain male germline function. However, the excess recruitment is consistent with a combination of both natural selection and mutational bias.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Emerson, J J -- Kaessmann, Henrik -- Betran, Esther -- Long, Manyuan -- GM-065429-01A1/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jan 23;303(5657):537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Ecology and Evolution, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739461" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chromosomes, Human/genetics ; Chromosomes, Human, X/*genetics ; Chromosomes, Mammalian/genetics ; Computational Biology ; Dosage Compensation, Genetic ; Female ; Gene Expression Profiling ; Genes, Duplicate ; Genetic Linkage ; Genome ; Genome, Human ; Humans ; Introns ; Male ; Mice ; Monte Carlo Method ; Mutation ; Oligonucleotide Array Sequence Analysis ; Ovary/metabolism ; Pseudogenes/*genetics ; *Recombination, Genetic ; Retroelements/*genetics ; Selection, Genetic ; Sex Characteristics ; Testis/metabolism ; X Chromosome/*genetics
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  • 34
    Publication Date: 2004-12-14
    Description: Discussions of the evolution of intelligence have focused on monkeys and apes because of their close evolutionary relationship to humans. Other large-brained social animals, such as corvids, also understand their physical and social worlds. Here we review recent studies of tool manufacture, mental time travel, and social cognition in corvids, and suggest that complex cognition depends on a "tool kit" consisting of causal reasoning, flexibility, imagination, and prospection. Because corvids and apes share these cognitive tools, we argue that complex cognitive abilities evolved multiple times in distantly related species with vastly different brain structures in order to solve similar socioecological problems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Emery, Nathan J -- Clayton, Nicola S -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1903-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sub-Department of Animal Behaviour, University of Cambridge, CB3 8AA, UK. nje23@cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591194" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Biological Evolution ; Brain/anatomy & histology/physiology ; *Cognition ; *Crows/anatomy & histology/physiology ; Hominidae/physiology ; Imagination ; *Intelligence ; Memory ; Social Behavior
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  • 35
    Publication Date: 2004-12-18
    Description: The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiardi, Adolfo -- Bhandari, Rashna -- Resnick, Adam C -- Snowman, Adele M -- Snyder, Solomon H -- DA00074/DA/NIDA NIH HHS/ -- MH068830-02/MH/NIMH NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2101-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604408" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Escherichia coli Proteins/metabolism ; Humans ; Inositol Phosphates/*metabolism ; Kinetics ; Magnesium/metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/*metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Protein Kinases/genetics/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Serine/metabolism ; Signal Transduction ; Temperature
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  • 36
    Publication Date: 2004-01-13
    Description: We characterize the evolutionary radiation of planktic foraminifera by the test size distributions of entire assemblages in more than 500 Cenozoic marine sediment samples, including more than 1 million tests. Calibration of Holocene size patterns with environmental parameters and comparisons with Cenozoic paleoproxy data show a consistently positive correlation between test size and surface-water stratification intensity. We infer that the observed macroevolutionary increase in test size of planktic foraminifera through the Cenozoic was an adaptive response to intensifying surface-water stratification in low latitudes, which was driven by polar cooling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmidt, Daniela N -- Thierstein, Hans R -- Bollmann, Jorg -- Schiebel, Ralf -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth Sciences, Eidgenossische Technische Hochschule (ETH) Zurich, and University of Zurich, ETH-Zentrum, CH-8092 Zurich, Switzerland. d.schmidt@gl.rhul.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Climate ; Ecosystem ; Eukaryota/chemistry/cytology ; Geography ; Oxygen Isotopes/analysis ; *Plankton/chemistry/cytology ; Seawater ; Temperature ; Time ; Zooplankton/chemistry/cytology
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  • 37
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erwin, Douglas H -- Krakauer, David C -- New York, N.Y. -- Science. 2004 May 21;304(5674):1117-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Paleobiology, Smithsonian Institution, Washington, DC 20560, USA. erwin@santafe.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155937" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Diffusion of Innovation ; Economics ; Ecosystem ; *Engineering ; Environment ; Epigenesis, Genetic ; Gene Duplication ; Gene Transfer, Horizontal ; Genotype ; Mutation ; Phenotype ; Selection, Genetic ; *Technology
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  • 38
    Publication Date: 2004-11-20
    Description: Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a "patatin domain" common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmermann, Robert -- Strauss, Juliane G -- Haemmerle, Guenter -- Schoiswohl, Gabriele -- Birner-Gruenberger, Ruth -- Riederer, Monika -- Lass, Achim -- Neuberger, Georg -- Eisenhaber, Frank -- Hermetter, Albin -- Zechner, Rudolf -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1383-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biosciences, University of Graz, Graz, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550674" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3-L1 Cells ; Adipocytes/enzymology/*metabolism ; Adipose Tissue/enzymology/*metabolism ; Adipose Tissue, Brown/enzymology/metabolism ; Amino Acid Sequence ; Animals ; COS Cells ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytoplasm/enzymology ; DNA, Complementary ; Diglycerides/metabolism ; Fatty Acids/metabolism ; Gene Silencing ; Glycerol/metabolism ; Humans ; Isoproterenol/pharmacology ; *Lipid Mobilization ; Lipolysis ; Lipoprotein Lipase/chemistry/genetics/immunology/*metabolism ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; Sterol Esterase/genetics/*metabolism ; Substrate Specificity ; Transfection ; Triglycerides/metabolism
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  • 39
    Publication Date: 2004-11-30
    Description: Signaling pathways that are activated by epidermal growth factor (EGF) or fibroblast growth factor (FGF) receptors have been identified and compared (detailed Connections Maps are available at Science's Signal Transduction Knowledge Environment). Both receptors stimulate a similar complement of intracellular signaling pathways. However, whereas activated EGF receptors (EGFRs) function as the main platform for recruitment of signaling proteins, signaling through the FGF receptors (FGFRs) is mediated primarily by assembly of a multidocking protein complex. Moreover, FGFR signaling is subject to additional intracellular and extracellular control mechanisms that do not affect EGFR signaling. The differential circuitry of the intracellular networks that are activated by EGFR and FGFR may affect signal specificity and physiological responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlessinger, Joseph -- R01-AR051448-01/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1506-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA. joseph.schlessinger@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567848" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Binding Sites ; Dimerization ; Epidermal Growth Factor/metabolism ; Fibroblast Growth Factors/metabolism ; Heparan Sulfate Proteoglycans/metabolism ; Humans ; Ligands ; Phosphorylation ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Receptors, Fibroblast Growth Factor/chemistry/*metabolism ; Second Messenger Systems ; *Signal Transduction ; Tyrosine/metabolism
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balter, Michael -- New York, N.Y. -- Science. 2004 Nov 12;306(5699):1120-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15539578" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; Cooperative Behavior ; *Cultural Evolution ; Emotions ; Endorphins/physiology ; Female ; Humans ; Language ; Male ; Maternal Behavior ; *Music ; Nonverbal Communication ; Object Attachment ; Selection, Genetic ; Sexual Behavior ; *Social Behavior
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-05-15
    Description: The Red Queen hypothesis posits that sex has evolved in response to the shifting adaptive landscape generated by the evolution of interacting species. Previous studies supporting the Red Queen hypothesis have considered a narrow region of parameter space and only a subset of ecological and genetic interactions. Here, we develop a population genetics model that circumscribes a broad array of ecological and genetic interactions among species and derive the first general analytical conditions for the impact of species interactions on the evolution of sex. Our results show that species interactions typically select against sex. We conclude that, although the Red Queen favors sex under certain circumstances, it alone does not account for the ubiquity of sex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Otto, Sarah P -- Nuismer, Scott L -- F32 GM65620-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 14;304(5673):1018-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of British Columbia, Vancouver, BC V6T 1Z4, Canada. otto@zoology.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143283" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Biological Evolution ; Epistasis, Genetic ; Gene Frequency ; Genetic Linkage ; Genetics, Population ; Genotype ; Linkage Disequilibrium ; Mathematics ; Models, Genetic ; Recombination, Genetic ; Reproduction, Asexual ; Selection, Genetic ; *Sex
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1268.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988522" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Biological Science Disciplines/education ; *Curriculum ; Georgia ; Natural Science Disciplines/education ; *Religion and Science ; Textbooks as Topic ; United States
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  • 43
    Publication Date: 2004-07-17
    Description: The community structure and ecological function of contemporary marine ecosystems are critically dependent on eukaryotic phytoplankton. Although numerically inferior to cyanobacteria, these organisms are responsible for the majority of the flux of organic matter to higher trophic levels and the ocean interior. Photosynthetic eukaryotes evolved more than 1.5 billion years ago in the Proterozoic oceans. However, it was not until the Mesozoic Era (251 to 65 million years ago) that the three principal phytoplankton clades that would come to dominate the modern seas rose to ecological prominence. In contrast to their pioneering predecessors, the dinoflagellates, coccolithophores, and diatoms all contain plastids derived from an ancestral red alga by secondary symbiosis. Here we examine the geological, geochemical, and biological processes that contributed to the rise of these three, distantly related, phytoplankton groups.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falkowski, Paul G -- Katz, Miriam E -- Knoll, Andrew H -- Quigg, Antonietta -- Raven, John A -- Schofield, Oscar -- Taylor, F J R -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):354-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Marine and Coastal Sciences, Rutgers University, 71 Dudley Road, New Brunswick, NJ 08540, USA. falko@imcs.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15256663" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; *Biological Evolution ; *Ecosystem ; Fossils ; Phylogeny ; *Phytoplankton/classification/cytology/physiology ; Plastids/physiology
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  • 44
    Publication Date: 2004-02-07
    Description: Microtubule (MT) stabilization is regulated by the small guanosine triphosphate (GTP)-binding protein Rho and its effector, mammalian homolog of Diaphanous (mDia), in migrating cells, but factors responsible for localized stabilization at the leading edge are unknown. We report that integrin-mediated activation of focal adhesion kinase (FAK) at the leading edge is required for MT stabilization by the Rho-mDia signaling pathway in mouse fibroblasts. MT stabilization also involved FAK-regulated localization of a lipid raft marker, ganglioside GM1, to the leading edge. The integrin-FAK signaling pathway may facilitate Rho-mDia signaling through GM1, or through a specialized membrane domain containing GM1, to stabilize MTs in the leading edge of migrating cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palazzo, Alexander F -- Eng, Christina H -- Schlaepfer, David D -- Marcantonio, Eugene E -- Gundersen, Gregg G -- CA87038/CA/NCI NIH HHS/ -- GM 44585/GM/NIGMS NIH HHS/ -- GM 62939/GM/NIGMS NIH HHS/ -- GM 68695/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):836-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764879" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Carrier Proteins/metabolism ; Cell Adhesion ; Cell Line ; Cell Membrane/*metabolism ; Cholesterol/metabolism ; Fibronectins/metabolism/pharmacology ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; G(M1) Ganglioside/metabolism ; Glycosylphosphatidylinositols/metabolism ; Integrins/*metabolism ; Membrane Microdomains/*metabolism ; Mice ; Mice, Knockout ; Microtubules/*metabolism/ultrastructure ; NIH 3T3 Cells ; Phosphorylation ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Tubulin/metabolism ; rho GTP-Binding Proteins/*metabolism ; rhoA GTP-Binding Protein/genetics/metabolism
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  • 45
    Publication Date: 2004-09-09
    Description: Regenerating arms of crinoids represent direct evidence of nonlethal attacks by predators and provide an opportunity for exploring the importance of predation through geologic time. Analysis of 11 Paleozoic crinoid Lagerstatten revealed a significant increase in arm regeneration during the Siluro-Devonian. During this interval, referred to as the Middle Paleozoic Marine Revolution, the diversity of shell-crushing predators increased, and antipredatory morphologies among invertebrate prey, such as crinoids, became more common. Crinoid arm regeneration data suggest an increase in nonlethal attacks at this time and represent a causal link between those patterns, which implies an important role for predator-driven evolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baumiller, Tomasz K -- Gahn, Forest J -- New York, N.Y. -- Science. 2004 Sep 3;305(5689):1453-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Michigan Museum of Paleontology, Ann Arbor, MI 48105, USA. tomaszb@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15353799" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Echinodermata/*physiology ; Fishes ; *Fossils ; *Predatory Behavior ; *Regeneration
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  • 46
    Publication Date: 2004-10-23
    Description: Despite evidence that protein kinases are regulators of apoptosis, a specific role for phosphatases in regulating cell survival has not been established. Here we show that alpha4, a noncatalytic subunit of protein phosphatase 2A (PP2A), is required to repress apoptosis in murine cells. alpha4 is a nonredundant regulator of the dephosphorylation of the transcription factors c-Jun and p53. As a result of alpha4 deletion, multiple proapoptotic genes were transcribed. Either inhibition of new protein synthesis or Bcl-xL overexpression suppressed apoptosis initiated by alpha4 deletion. Thus, mammalian cell viability depends on repression of transcription-initiated apoptosis mediated by a component of PP2A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kong, Mei -- Fox, Casey J -- Mu, James -- Solt, Laura -- Xu, Anne -- Cinalli, Ryan M -- Birnbaum, Morris J -- Lindsten, Tullia -- Thompson, Craig B -- New York, N.Y. -- Science. 2004 Oct 22;306(5696):695-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15499020" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/cytology ; Animals ; *Apoptosis ; Cell Differentiation ; Cell Line ; Cell Survival ; Cells, Cultured ; Cycloheximide/pharmacology ; Gene Deletion ; Gene Expression Profiling ; Liver/cytology/metabolism ; Mice ; Mice, Transgenic ; Oligonucleotide Array Sequence Analysis ; PPAR gamma/metabolism ; Phosphoprotein Phosphatases/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein Phosphatase 2 ; Protein Synthesis Inhibitors/pharmacology ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Proto-Oncogene Proteins c-jun/metabolism ; Transcription, Genetic ; Tumor Suppressor Protein p53/metabolism ; bcl-X Protein
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  • 47
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-03-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Begun, David R -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1478-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anthropology, University of Toronto, Toronto, Ontario M5S 3G3, Canada. begun@chass.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001766" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuspid/anatomy & histology ; *Biological Evolution ; Cooperative Behavior ; Cuspid/anatomy & histology ; Dental Enamel/anatomy & histology ; Ethiopia ; *Fossils ; *Hominidae/anatomy & histology/classification ; Humans ; Locomotion ; Lower Extremity/anatomy & histology ; Molar/anatomy & histology ; Paleodontology ; Pan troglodytes/anatomy & histology ; Skull/anatomy & histology ; Tooth/*anatomy & histology
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  • 48
    Publication Date: 2004-07-27
    Description: Inherited channelopathies are at the origin of many neurological disorders. Here we report a form of channelopathy that is acquired in experimental temporal lobe epilepsy (TLE), the most common form of epilepsy in adults. The excitability of CA1 pyramidal neuron dendrites was increased in TLE because of decreased availability of A-type potassium ion channels due to transcriptional (loss of channels) and posttranslational (increased channel phosphorylation by extracellular signal-regulated kinase) mechanisms. Kinase inhibition partly reversed dendritic excitability to control levels. Such acquired channelopathy is likely to amplify neuronal activity and may contribute to the initiation and/or propagation of seizures in TLE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernard, Christophe -- Anderson, Anne -- Becker, Albert -- Poolos, Nicholas P -- Beck, Heinz -- Johnston, Daniel -- MH44754/MH/NIMH NIH HHS/ -- MH48432/MH/NIMH NIH HHS/ -- NS37444/NS/NINDS NIH HHS/ -- NS39943/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):532-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Baylor College of Medicine, Houston, TX 77030, USA. cbernard@inmed.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273397" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/pharmacology ; 4-Aminopyridine/pharmacology ; Action Potentials/drug effects ; Animals ; Butadienes/pharmacology ; Dendrites/*physiology ; Enzyme Inhibitors/pharmacology ; Epilepsy, Temporal Lobe/*physiopathology ; Hippocampus/cytology/*physiopathology ; Male ; Membrane Potentials ; Mitogen-Activated Protein Kinases/antagonists & inhibitors/metabolism ; Nitriles/pharmacology ; Phosphorylation ; Pilocarpine/administration & dosage ; Potassium Channel Blockers/pharmacology ; Potassium Channels/drug effects/metabolism/*physiology ; *Potassium Channels, Voltage-Gated ; Protein Kinase C/antagonists & inhibitors/metabolism ; Pyramidal Cells/*physiology ; Rats ; Rats, Sprague-Dawley ; Shal Potassium Channels
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  • 49
    Publication Date: 2004-02-14
    Description: The life cycles of sexually reproducing animals and flowering plants begin with male and female gametes and their fusion to form a zygote. Selection at this earliest stage is crucial for offspring quality and raises similar evolutionary issues, yet zoology and botany use dissimilar approaches. There are striking parallels in the role of prezygotic competition for sexual selection on males, cryptic female choice, sexual conflict, and against selfish genetic elements and genetic incompatibility. In both groups, understanding the evolution of sex-specific and reproductive traits will require an appreciation of the effects of prezygotic competition on fitness.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernasconi, G -- Ashman, T-L -- Birkhead, T R -- Bishop, J D D -- Grossniklaus, U -- Kubli, E -- Marshall, D L -- Schmid, B -- Skogsmyr, I -- Snook, R R -- Taylor, D -- Till-Bottraud, I -- Ward, P I -- Zeh, D W -- Hellriegel, B -- New York, N.Y. -- Science. 2004 Feb 13;303(5660):971-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Environmental Sciences, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. bernasco@uwinst.unizh.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14963320" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*physiology ; Animals ; *Biological Evolution ; Competitive Behavior ; Copulation ; Female ; Gene Expression ; Male ; Pollen/*physiology ; *Reproduction ; Selection, Genetic ; Sex Characteristics ; *Sexual Behavior, Animal ; Spermatozoa/*physiology
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-10-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472046" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA, Mitochondrial/*genetics ; Genetics, Population ; History, Ancient ; *Hominidae/classification/parasitology ; Humans ; Lice Infestations/history/transmission ; Pediculus/classification/*genetics/physiology ; Population Dynamics ; Species Specificity ; Time
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-07-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayr, Ernst -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):46-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum of Comparative Zoology, Harvard University, Cambridge, MA 02138, USA. emayr@oeb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232092" target="_blank"〉PubMed〈/a〉
    Keywords: Biodiversity ; *Biological Evolution ; Biology/*history ; Classification ; Genetics, Population ; Germany ; History, 20th Century ; History, 21st Century ; Mutation ; Selection, Genetic
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gadagkar, Raghavendra -- New York, N.Y. -- Science. 2004 Dec 3;306(5702):1694-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Ecological Sciences, Indian Institute of Science, 560 012 Bangalore, India. ragh@ces.iisc.ernet.in〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15576600" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Ants/genetics/*physiology ; Bees/genetics/physiology ; Behavior, Animal ; *Biological Evolution ; Diploidy ; Female ; Genes, Insect ; Genetic Variation ; Haploidy ; Male ; *Parthenogenesis ; Reproduction ; Sex Determination Processes ; Sexual Behavior, Animal ; Social Behavior
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  • 53
    Publication Date: 2004-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):384.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087524" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA-Binding Proteins/genetics/physiology ; *Developmental Biology ; Drosophila/embryology/genetics/physiology ; Drosophila Proteins ; *Genes ; Insects/embryology/genetics/physiology ; Nuclear Proteins ; Planarians/genetics/physiology ; *RNA Interference ; Regeneration ; Stem Cells/physiology ; Transcription Factors
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-03-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):1957.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044775" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Brain/anatomy & histology/*growth & development ; Gorilla gorilla/anatomy & histology/genetics/growth & development ; *Hominidae/anatomy & histology/genetics/growth & development ; Humans ; Macaca/anatomy & histology/genetics/growth & development ; Masticatory Muscles/anatomy & histology/growth & development ; Myosin Heavy Chains/*genetics ; Pan troglodytes/anatomy & histology/genetics/growth & development ; Primates/anatomy & histology/genetics/growth & development ; *Sequence Deletion ; Skull/anatomy & histology/growth & development
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  • 55
    Publication Date: 2004-10-30
    Description: The emergence of the seed habit in the Middle Paleozoic was a decisive evolutionary breakthrough. Today, seed plants are the most successful plant lineage, with more than 250,000 living species. We have identified a middle Givetian (385 million years ago) seed precursor from Belgium predating the earliest seeds by about 20 million years. Runcaria is a small, radially symmetrical, integumented megasporangium surrounded by a cupule. The megasporangium bears an unopened distal extension protruding above the multilobed integument. This extension is assumed to be involved in anemophilous pollination. Runcaria sheds new light on the sequence of character acquisition leading to the seed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerrienne, P -- Meyer-Berthaud, B -- Fairon-Demaret, M -- Streel, M -- Steemans, P -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):856-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Geologie, B18, Universite de Liege, Sart Tilman, Liege 1, Belgique. p.gerrienne@ulg.ac.be〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514154" target="_blank"〉PubMed〈/a〉
    Keywords: Belgium ; *Biological Evolution ; Fossils ; Plant Physiological Phenomena ; Plant Structures/*anatomy & histology ; Plants/*anatomy & histology/classification ; Pollen ; *Seeds ; Time
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-04-06
    Description: A tetrapod humerus from the Late Devonian of Pennsylvania has a novel mix of primitive and derived characters. A comparative analysis of this fossil and other relevant humeri from the Devonian shows that the role of the limb in propping the body arose first in fish fins, not tetrapod limbs. The functional diversity of the earliest known limbs includes several different kinds of appendage design. This functional diversity was achieved with a humeral architecture that was remarkably conserved during the Devonian.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shubin, Neil H -- Daeschler, Edward B -- Coates, Michael I -- New York, N.Y. -- Science. 2004 Apr 2;304(5667):90-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organismal Biology and Anatomy, University of Chicago, Chicago, IL 60637, USA. nshubin@uchicago.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15064415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Biomechanical Phenomena ; Extremities/*anatomy & histology ; Fishes/anatomy & histology/physiology ; *Fossils ; Humerus/*anatomy & histology ; Locomotion ; Movement ; Pennsylvania ; Vertebrates/*anatomy & histology/physiology
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  • 57
    Publication Date: 2004-06-26
    Description: Arrestin regulates almost all G protein-coupled receptor (GPCR)-mediated signaling and trafficking. We report that the multidomain protein, spinophilin, antagonizes these multiple arrestin functions. Through blocking G protein receptor kinase 2 (GRK2) association with receptor-Gbetagamma complexes, spinophilin reduces arrestin-stabilized receptor phosphorylation, receptor endocytosis, and the acceleration of mitogen-activated protein kinase (MAPK) activity following endocytosis. Spinophilin knockout mice were more sensitive than wild-type mice to sedation elicited by stimulation of alpha2 adrenergic receptors, whereas arrestin 3 knockout mice were more resistant, indicating that the signal-promoting, rather than the signal-terminating, roles of arrestin are more important for certain response pathways. The reciprocal interactions of GPCRs with spinophilin and arrestin represent a regulatory mechanism for fine-tuning complex receptor-orchestrated cell signaling and responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Qin -- Zhao, Jiali -- Brady, Ashley E -- Feng, Jian -- Allen, Patrick B -- Lefkowitz, Robert J -- Greengard, Paul -- Limbird, Lee E -- DA10044/DA/NIDA NIH HHS/ -- DK43879/DK/NIDDK NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- HL42671/HL/NHLBI NIH HHS/ -- MH40899/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 25;304(5679):1940-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Center of Molecular Neuroscience, Vanderbilt University Medical Center, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218143" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*analogs & derivatives/pharmacology ; Adrenergic alpha-Agonists/pharmacology ; Animals ; Arrestin/*antagonists & inhibitors/*metabolism ; Arrestins/genetics/metabolism ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Endocytosis ; Enzyme Activation ; Epinephrine/pharmacology ; G-Protein-Coupled Receptor Kinase 3 ; GTP-Binding Proteins/*metabolism ; Humans ; MAP Kinase Signaling System ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microfilament Proteins/genetics/*metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Motor Activity ; Nerve Tissue Proteins/genetics/*metabolism ; Phosphorylation ; Receptors, Adrenergic, alpha-2/*metabolism ; Rotarod Performance Test ; Signal Transduction ; Transfection ; beta-Adrenergic Receptor Kinases
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-30
    Description: The actions of many extracellular stimuli are elicited by complexes of cell surface receptors, heterotrimeric guanine nucleotide-binding proteins (G proteins), and mitogen-activated protein (MAP) kinase complexes. Analysis of haploid yeast cells and their response to peptide mating pheromones has produced important advances in our understanding of G protein and MAP kinase signaling mechanisms. Many of the components, their interrelationships, and their regulators were first identified in yeast. Current analysis of the pheromone response pathway (see the Connections Maps at Science's Signal Transduction Knowledge Environment) will benefit from new and powerful genomic, proteomic, and computational approaches that will likely reveal additional general principles that are applicable to more complex organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yuqi -- Dohlman, Henrik G -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1508-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567849" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle ; GTP-Binding Proteins/metabolism ; Lipoproteins/*metabolism ; *MAP Kinase Signaling System ; Mutation ; Pheromones/*metabolism ; Phosphorylation ; Protein Precursors/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism/physiology ; Saccharomyces cerevisiae Proteins/*metabolism ; *Signal Transduction
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  • 59
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-01-17
    Description: Communities arising through adaptive radiation are generally regarded as unique, with speciation and adaptation being quite different from immigration and ecological assortment. Here, I use the chronological arrangement of the Hawaiian Islands to visualize snapshots of evolutionary history and stages of community assembly. Analysis of an adaptive radiation of habitat-associated, polychromatic spiders shows that (i) species assembly is not random; (ii) within any community, similar sets of ecomorphs arise through both dispersal and evolution; and (iii) species assembly is dynamic with maximum species numbers in communities of intermediate age. The similar patterns of species accumulation through evolutionary and ecological processes suggest universal principles underlie community assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gillespie, Rosemary -- New York, N.Y. -- Science. 2004 Jan 16;303(5656):356-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Insect Biology, University of California, 201 Wellman Hall, Berkeley, CA94720-3112, USA. gillespi@nature.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14726588" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Biodiversity ; *Biological Evolution ; DNA, Mitochondrial/genetics ; DNA, Ribosomal/genetics ; *Ecosystem ; Electron Transport Complex IV/genetics ; Environment ; Feeding Behavior ; Hawaii ; Isoenzymes/genetics ; Phylogeny ; Population Density ; RNA, Ribosomal, 16S/genetics ; *Spiders/anatomy & histology/classification/genetics/physiology
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  • 60
    Publication Date: 2004-06-12
    Description: A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo)plasmic reticulum Ca2+-adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene)-triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca2-E1 approximately P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sorensen, Thomas Lykke-Moller -- Moller, Jesper Vuust -- Nissen, Poul -- New York, N.Y. -- Science. 2004 Jun 11;304(5677):1672-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15192230" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*analogs & derivatives/*metabolism ; Aluminum Compounds/metabolism ; Animals ; Binding Sites ; Calcium/*metabolism ; Calcium-Transporting ATPases/*chemistry/*metabolism ; Crystallization ; Crystallography, X-Ray ; Cytosol/metabolism ; Fluorides/metabolism ; Models, Molecular ; Muscle Fibers, Fast-Twitch/*enzymology ; Phosphorylation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rabbits ; Sarcoplasmic Reticulum Calcium-Transporting ATPases
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, Benjamin G -- New York, N.Y. -- Science. 2004 Jan 23;303(5657):480-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dyson Perrins Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QY, UK. ben.davis@chemistry.oxford.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739446" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemistry/*methods ; Drug Design ; Erythropoietin/chemistry/metabolism ; Glycosylation ; *Molecular Mimicry ; Molecular Structure ; Phosphorylation ; *Protein Processing, Post-Translational ; Recombinant Proteins/chemistry/metabolism ; ras Proteins/chemistry/metabolism
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  • 62
    Publication Date: 2004-04-10
    Description: Ventricular arrhythmias can cause sudden cardiac death (SCD) in patients with normal hearts and in those with underlying disease such as heart failure. In animals with heart failure and in patients with inherited forms of exercise-induced SCD, depletion of the channel-stabilizing protein calstabin2 (FKBP12.6) from the ryanodine receptor-calcium release channel (RyR2) complex causes an intracellular Ca2+ leak that can trigger fatal cardiac arrhythmias. A derivative of 1,4-benzothiazepine (JTV519) increased the affinity of calstabin2 for RyR2, which stabilized the closed state of RyR2 and prevented the Ca2+ leak that triggers arrhythmias. Thus, enhancing the binding of calstabin2 to RyR2 may be a therapeutic strategy for common ventricular arrhythmias.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wehrens, Xander H T -- Lehnart, Stephan E -- Reiken, Steven R -- Deng, Shi-Xian -- Vest, John A -- Cervantes, Daniel -- Coromilas, James -- Landry, Donald W -- Marks, Andrew R -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):292-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073377" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Arrhythmia Agents/*pharmacology/therapeutic use ; Calcium/metabolism ; Calcium-Transporting ATPases/metabolism ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Death, Sudden, Cardiac/prevention & control ; Electric Stimulation ; Electrocardiography ; Heart/*drug effects/physiology ; Humans ; Isoproterenol/pharmacology ; Mice ; Myocardial Contraction ; Phosphorylation ; Physical Exertion ; Protein Binding ; Ryanodine Receptor Calcium Release Channel/*metabolism ; Sarcoplasmic Reticulum/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases ; Tachycardia, Ventricular/metabolism/*prevention & control ; Tacrolimus Binding Proteins/deficiency/genetics/*metabolism ; Thiazepines/*pharmacology/therapeutic use
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  • 63
    Publication Date: 2004-07-31
    Description: Gefitinib (Iressa, Astra Zeneca Pharmaceuticals) is a tyrosine kinase inhibitor that targets the epidermal growth factor receptor (EGFR) and induces dramatic clinical responses in nonsmall cell lung cancers (NSCLCs) with activating mutations within the EGFR kinase domain. We report that these mutant EGFRs selectively activate Akt and signal transduction and activator of transcription (STAT) signaling pathways, which promote cell survival, but have no effect on extracellular signal-regulated kinase signaling, which induces proliferation. NSCLC cells expressing mutant EGFRs underwent extensive apoptosis after small interfering RNA-mediated knockdown of the mutant EGFR or treatment with pharmacological inhibitors of Akt and STAT signaling and were relatively resistant to apoptosis induced by conventional chemotherapeutic drugs. Thus, mutant EGFRs selectively transduce survival signals on which NSCLCs become dependent; inhibition of those signals by gefitinib may contribute to the drug's efficacy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sordella, Raffaella -- Bell, Daphne W -- Haber, Daniel A -- Settleman, Jeffrey -- P01 95281/PHS HHS/ -- New York, N.Y. -- Science. 2004 Aug 20;305(5687):1163-7. Epub 2004 Jul 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Therapeutics, Massachusetts General Hospital Cancer Center and Harvard Medical School, Building 149, 13th Street, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15284455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/pharmacology ; *Apoptosis ; Carcinoma, Non-Small-Cell Lung/drug therapy/*genetics/pathology ; Catalytic Domain ; Cell Line ; Cell Line, Tumor ; Cell Survival ; DNA-Binding Proteins/antagonists & inhibitors/metabolism ; Enzyme Activation ; Humans ; Lung Neoplasms/drug therapy/*genetics/pathology ; Mice ; *Milk Proteins ; Mitogen-Activated Protein Kinases/metabolism ; Mutation ; Mutation, Missense ; Phosphorylation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins c-akt ; Quinazolines/*pharmacology ; RNA, Small Interfering ; Receptor, Epidermal Growth Factor/*genetics/*metabolism ; STAT5 Transcription Factor ; Sequence Deletion ; Signal Transduction ; Trans-Activators/antagonists & inhibitors/metabolism ; Transfection ; Tyrosine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 64
    Publication Date: 2004-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Minna, John D -- Gazdar, Adi F -- Sprang, Stephen R -- Herz, Joachim -- P50CA70907/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. john.minna@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178790" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/drug therapy/genetics/metabolism ; Amino Acid Substitution ; Antineoplastic Agents/therapeutic use ; Carcinoma, Non-Small-Cell Lung/drug therapy/*genetics/metabolism ; Controlled Clinical Trials as Topic ; Enzyme Inhibitors/therapeutic use ; Epidermal Growth Factor/metabolism ; *Genes, erbB-1 ; Humans ; Japan ; Ligands ; Lung Neoplasms/*drug therapy/*genetics/metabolism ; *Mutation ; Phosphorylation ; Protein Structure, Tertiary ; Quinazolines/*therapeutic use ; Receptor, Epidermal Growth Factor/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Sequence Deletion ; Smoking ; Treatment Outcome ; United States
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  • 65
    Publication Date: 2004-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Proffitt, Fiona -- New York, N.Y. -- Science. 2004 Jun 25;304(5679):1894-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15218121" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; England ; History, 20th Century ; History, 21st Century ; *Moths/anatomy & histology/physiology ; Pigmentation ; Predatory Behavior ; *Selection, Genetic
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  • 66
    Publication Date: 2004-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brower, Andrew V Z -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):173; author reply 173.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, Oregon State University, Corvallis, OR 97331, USA. browera@science.oregonstate.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14715995" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Evolution, Molecular ; Genes ; Mathematics ; Models, Statistical ; *Phylogeny ; Sampling Studies
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  • 67
    Publication Date: 2004-05-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greenamyre, J Timothy -- Hastings, Teresa G -- New York, N.Y. -- Science. 2004 May 21;304(5674):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Emory University School of Medicine, Atlanta, GA 30322, USA. jgreena@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155938" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Dopamine/metabolism ; Electron Transport Complex I/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitochondria/enzymology/*metabolism ; Mutation ; Nerve Tissue Proteins/genetics/metabolism ; Neurons/metabolism ; Oncogene Proteins/genetics/metabolism ; Oxidative Stress ; Parkinson Disease/*etiology/*genetics/metabolism ; Phosphorylation ; Protein Kinases/*genetics/*metabolism ; Reactive Oxygen Species/metabolism ; Synucleins ; Ubiquitin Thiolesterase/genetics/metabolism ; Ubiquitin-Protein Ligases/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 68
    Publication Date: 2004-02-21
    Description: The Sir2 deacetylase modulates organismal life-span in various species. However, the molecular mechanisms by which Sir2 increases longevity are largely unknown. We show that in mammalian cells, the Sir2 homolog SIRT1 appears to control the cellular response to stress by regulating the FOXO family of Forkhead transcription factors, a family of proteins that function as sensors of the insulin signaling pathway and as regulators of organismal longevity. SIRT1 and the FOXO transcription factor FOXO3 formed a complex in cells in response to oxidative stress, and SIRT1 deacetylated FOXO3 in vitro and within cells. SIRT1 had a dual effect on FOXO3 function: SIRT1 increased FOXO3's ability to induce cell cycle arrest and resistance to oxidative stress but inhibited FOXO3's ability to induce cell death. Thus, one way in which members of the Sir2 family of proteins may increase organismal longevity is by tipping FOXO-dependent responses away from apoptosis and toward stress resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunet, Anne -- Sweeney, Lora B -- Sturgill, J Fitzhugh -- Chua, Katrin F -- Greer, Paul L -- Lin, Yingxi -- Tran, Hien -- Ross, Sarah E -- Mostoslavsky, Raul -- Cohen, Haim Y -- Hu, Linda S -- Cheng, Hwei-Ling -- Jedrychowski, Mark P -- Gygi, Steven P -- Sinclair, David A -- Alt, Frederick W -- Greenberg, Michael E -- NIHP30-HD18655/HD/NICHD NIH HHS/ -- P01 NS35138-17/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):2011-5. Epub 2004 Feb 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and Department of Neurobiology, Center for Blood Research (CBR) Institute for Biomedical Research, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976264" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Apoptosis ; Cell Cycle ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Cerebellum/cytology ; Forkhead Transcription Factors ; Gene Expression Profiling ; Gene Expression Regulation ; Histone Deacetylases/genetics/*metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Mice ; Mice, Knockout ; Neurons/cytology ; *Oxidative Stress ; Phosphorylation ; Proteins/genetics ; Recombinant Proteins/metabolism ; Sirtuin 1 ; Sirtuins/genetics/*metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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  • 69
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-05-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewontin, Richard -- New York, N.Y. -- Science. 2004 May 14;304(5673):979.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Museum of Comparative Zoology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143272" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; England ; Game Theory ; History, 20th Century ; History, 21st Century ; Selection, Genetic
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  • 70
    Publication Date: 2004-03-06
    Description: Late Miocene fossil hominid teeth recovered from Ethiopia's Middle Awash are assigned to Ardipithecus kadabba. Their primitive morphology and wear pattern demonstrate that A. kadabba is distinct from Ardipithecus ramidus. These fossils suggest that the last common ancestor of apes and humans had a functionally honing canine-third premolar complex. Comparison with teeth of Sahelanthropus and Orrorin, the two other named late Miocene hominid genera, implies that these putative taxa are very similar to A. kadabba. It is therefore premature to posit extensive late Miocene hominid diversity on the basis of currently available samples.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haile-Selassie, Yohannes -- Suwa, Gen -- White, Tim D -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1503-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cleveland Museum of Natural History, 1 Wade Oval Drive, Cleveland, OH 44106, USA. yhailese@cmnh.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001775" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bicuspid/*anatomy & histology ; *Biological Evolution ; Cuspid/*anatomy & histology ; Dental Enamel/anatomy & histology ; Dentition ; Ethiopia ; *Fossils ; *Hominidae/anatomy & histology/classification ; Humans ; Paleodontology
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  • 71
    Publication Date: 2004-03-06
    Description: Self-incompatibility (SI) response in Brassica is initiated by haplotype-specific interactions between the pollen-borne ligand S locus protein 11/SCR and its stigmatic S receptor kinase, SRK. This binding induces autophosphorylation of SRK, which is then thought to trigger a signaling cascade that leads to self-pollen rejection. A recessive mutation of the modifier (m) gene eliminates the SI response in stigma. Positional cloning of M has revealed that it encodes a membrane-anchored cytoplasmic serine/threonine protein kinase, designated M locus protein kinase (MLPK). Transient expression of MLPK restores the ability of mm papilla cells to reject self-pollen, suggesting that MLPK is a positive mediator of Brassica SI signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murase, Kohji -- Shiba, Hiroshi -- Iwano, Megumi -- Che, Fang-Sik -- Watanabe, Masao -- Isogai, Akira -- Takayama, Seiji -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1516-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Brassica rapa/enzymology/genetics/*physiology ; Cell Membrane/*enzymology ; Cloning, Molecular ; Cytoplasm/enzymology ; Flowers/enzymology/*physiology ; Genes, Plant ; Haplotypes ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Open Reading Frames ; Phosphorylation ; Physical Chromosome Mapping ; Plant Proteins ; Pollen/physiology ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction
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  • 72
    Publication Date: 2004-11-30
    Description: In vitro studies suggest a role for c-Jun N-terminal kinases (JNKs) in proatherogenic cellular processes. We show that atherosclerosis-prone ApoE-/- mice simultaneously lacking JNK2 (ApoE-/- JNK2-/- mice), but not ApoE-/- JNK1-/- mice, developed less atherosclerosis than do ApoE-/- mice. Pharmacological inhibition of JNK activity efficiently reduced plaque formation. Macrophages lacking JNK2 displayed suppressed foam cell formation caused by defective uptake and degradation of modified lipoproteins and showed increased amounts of the modified lipoprotein-binding and -internalizing scavenger receptor A (SR-A), whose phosphorylation was markedly decreased. Macrophage-restricted deletion of JNK2 was sufficient to decrease atherogenesis. Thus, JNK2-dependent phosphorylation of SR-A promotes uptake of lipids in macrophages, thereby regulating foam cell formation, a critical step in atherogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ricci, Romeo -- Sumara, Grzegorz -- Sumara, Izabela -- Rozenberg, Izabela -- Kurrer, Michael -- Akhmedov, Alexander -- Hersberger, Martin -- Eriksson, Urs -- Eberli, Franz R -- Becher, Burkhard -- Boren, Jan -- Chen, Mian -- Cybulsky, Myron I -- Moore, Kathryn J -- Freeman, Mason W -- Wagner, Erwin F -- Matter, Christian M -- Luscher, Thomas F -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1558-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Research, Institute of Physiology, and Division of Cardiology, University Hospital Zurich, CH-8057 Zurich, Switzerland. romeo.ricci@cell.biol.ethz.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567863" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD36/metabolism ; Aorta/chemistry/pathology ; Apolipoproteins E/genetics ; Arteriosclerosis/*metabolism/pathology ; Bone Marrow Transplantation ; Cells, Cultured ; Cholesterol/metabolism ; Cholesterol, Dietary/administration & dosage ; Diet, Atherogenic ; Endothelial Cells/physiology ; Foam Cells/*metabolism ; Lipoproteins, LDL/metabolism ; Macrophages/*metabolism ; Macrophages, Peritoneal/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitogen-Activated Protein Kinase 8/metabolism ; Mitogen-Activated Protein Kinase 9/genetics/*metabolism ; Muscle, Smooth, Vascular/cytology ; Myocytes, Smooth Muscle/physiology ; Phosphorylation ; Receptors, Immunologic/genetics/*metabolism ; Receptors, Scavenger ; Scavenger Receptors, Class A ; T-Lymphocytes/immunology
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  • 73
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-09-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahlberg, P E -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1715; author reply 1715.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Evolutionary Organismal Biology, Evolutionary Biology Centre, Uppsala University, Norbyvagen 18A752 36 Uppsala, Sweden. per.ahlberg@ebc.uu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375249" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Fossils ; Humerus/*anatomy & histology ; Scotland ; Vertebrates/*anatomy & histology
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  • 74
    Publication Date: 2004-03-20
    Description: The spatial organization of the microtubule cytoskeleton is thought to be directed by steady-state activity gradients of diffusible regulatory molecules. We visualized such intracellular gradients by monitoring the interaction between tubulin and a regulator of microtubule dynamics, stathmin, using a fluorescence resonance energy transfer (FRET) biosensor. These gradients were observed both during interphase in motile membrane protrusions and during mitosis around chromosomes, which suggests that a similar mechanism may contribute to the creation of polarized microtubule structures. These interaction patterns are likely to reflect phosphorylation of stathmin in these areas.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Niethammer, Philipp -- Bastiaens, Philippe -- Karsenti, Eric -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1862-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15031504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Binding Sites ; Cell Line ; *Cell Movement ; Chromosomes/metabolism ; Cytosol/metabolism ; Fluorescence Resonance Energy Transfer ; Green Fluorescent Proteins ; Interphase ; Luminescent Proteins ; *Microtubule Proteins ; Microtubules/metabolism/ultrastructure ; *Mitosis ; Mutation ; Phosphoprotein Phosphatases/metabolism ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Spindle Apparatus/ultrastructure ; Stathmin ; Swine ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection ; Tubulin/*metabolism ; Xenopus ; Xenopus Proteins
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  • 75
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-04-10
    Description: The acquisitions of mitochondria and plastids were important events in the evolution of the eukaryotic cell, supplying it with compartmentalized bioenergetic and biosynthetic factories. Ancient invasions by eubacteria through symbiosis more than a billion years ago initiated these processes. Advances in geochemistry, molecular phylogeny, and cell biology have offered insight into complex molecular events that drove the evolution of endosymbionts into contemporary organelles. In losing their autonomy, endosymbionts lost the bulk of their genomes, necessitating the evolution of elaborate mechanisms for organelle biogenesis and metabolite exchange. In the process, symbionts acquired many host-derived properties, lost much of their eubacterial identity, and were transformed into extraordinarily diverse organelles that reveal complex histories that we are only beginning to decipher.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dyall, Sabrina D -- Brown, Mark T -- Johnson, Patricia J -- AI27857/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 9;304(5668):253-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, 405 Hilgard Avenue, Los Angeles, CA 90095-1489, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073369" target="_blank"〉PubMed〈/a〉
    Keywords: Alphaproteobacteria/genetics/physiology ; *Bacterial Physiological Phenomena ; *Biological Evolution ; Chloroplasts/physiology ; Cyanobacteria/genetics/physiology ; Evolution, Molecular ; Genome ; Genome, Bacterial ; Mitochondria/*physiology ; Organelles/*physiology ; Origin of Life ; Plastids/*physiology ; Proteins/chemistry/metabolism ; *Symbiosis
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  • 76
    Publication Date: 2004-05-08
    Description: Self-regulating systems often use robust oscillatory circuits. One such system controls the chemotactic signaling mechanism of Dictyostelium, where pulses of adenosine 3',5'-monophosphate (cAMP) are generated with a periodicity of 7 minutes. We have observed spontaneous oscillations in activation of the mitogen-activated protein (MAP) kinase ERK2 that occur in phase with peaks of cAMP, and we show that ERK2 modulates cAMP levels through the phosphodiesterase RegA. Computer modeling and simulations of the underlying circuit faithfully account for the ability of the cells to spontaneously generate periodic pulses during specific stages of development. Similar oscillatory processes may occur in cells of many different species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maeda, Mineko -- Lu, Sijie -- Shaulsky, Gad -- Miyazaki, Yuji -- Kuwayama, Hidekazu -- Tanaka, Yoshimasa -- Kuspa, Adam -- Loomis, William F -- GM52359/GM/NIGMS NIH HHS/ -- GM62350/GM/NIGMS NIH HHS/ -- R01 GM052359/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 7;304(5672):875-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Graduate School of Science, Osaka University, Machikaneyama-cho 1-16, Toyonaka, Osaka 560-0043, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15131307" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases ; Adenylyl Cyclases/metabolism ; Animals ; Computer Simulation ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/genetics/*metabolism ; Dictyostelium/enzymology/genetics/growth & development/*metabolism ; Enzyme Activation ; Mitogen-Activated Protein Kinase 1/genetics/*metabolism ; Models, Biological ; Mutagenesis, Site-Directed ; Mutation ; Phosphorylation ; Protozoan Proteins/genetics/metabolism ; Receptors, Cyclic AMP/metabolism ; *Signal Transduction
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  • 77
    Publication Date: 2004-11-20
    Description: The observation of the regulation of fast protein dynamics in a cellular context requires the development of reliable technologies. Here, a signal regulation cascade reliant on the stimulus-dependent acceleration of the bidirectional flow of mitogen-activated protein kinase (extracellular signal-regulated kinase) across the nuclear envelope was visualized by reversible protein highlighting. Light-induced conversion between the bright and dark states of a monomeric fluorescent protein engineered from a novel coral protein was employed. Because of its photochromic properties, the protein could be highlighted, erased, and highlighted again in a nondestructive manner, allowing direct observation of regulated fast nucleocytoplasmic shuttling of key signaling molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ando, Ryoko -- Mizuno, Hideaki -- Miyawaki, Atsushi -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Function and Dynamics, Advanced Technology Development Group, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-city, Saitama, 351-0198, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550670" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Anthozoa ; COS Cells ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; Epidermal Growth Factor/pharmacology ; Fluorescence ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Light ; Luminescent Proteins/chemistry/*metabolism ; MAP Kinase Signaling System ; Microscopy, Confocal ; Mitogen-Activated Protein Kinase 3/*metabolism ; Molecular Sequence Data ; Nuclear Envelope/*metabolism ; Phosphorylation ; Protein Transport ; Recombinant Proteins/chemistry/metabolism ; Transfection ; beta Karyopherins/metabolism
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  • 78
    Publication Date: 2004-05-15
    Description: Dynamic changes in chromatin structure, induced by posttranslational modification of histones, play a fundamental role in regulating eukaryotic transcription. Here we report that histone H2B is phosphorylated at evolutionarily conserved Ser33 (H2B-S33) by the carboxyl-terminal kinase domain (CTK) of the Drosophila TFIID subunit TAF1. Phosphorylation of H2B-S33 at the promoter of the cell cycle regulatory gene string and the segmentation gene giant coincides with transcriptional activation. Elimination of TAF1 CTK activity in Drosophila cells and embryos reduces transcriptional activation and phosphorylation of H2B-S33. These data reveal that H2B-S33 is a physiological substrate for the TAF1 CTK and that H2B-S33 phosphorylation is essential for transcriptional activation events that promote cell cycle progression and development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maile, Tobias -- Kwoczynski, Simona -- Katzenberger, Rebeccah J -- Wassarman, David A -- Sauer, Frank -- GM066204-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 May 14;304(5673):1010-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California-Riverside, Riverside, CA 95121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15143281" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Cell Cycle ; Cell Cycle Proteins ; DNA-Binding Proteins/genetics ; Drosophila/embryology/*genetics/metabolism ; Drosophila Proteins/chemistry/genetics/*metabolism ; Embryo, Nonmammalian/physiology ; Genes, Insect ; Histone Acetyltransferases ; Histones/chemistry/*metabolism ; Homeodomain Proteins/genetics ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphoserine/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/genetics ; RNA Interference ; Recombinant Proteins/chemistry/metabolism ; Repressor Proteins/genetics ; TATA-Binding Protein Associated Factors ; Transcription Factor TFIID/chemistry/genetics/*metabolism ; Transcription Factors ; *Transcription, Genetic ; *Transcriptional Activation
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  • 79
    Publication Date: 2004-02-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ruby, Edward -- Henderson, Brian -- McFall-Ngai, Margaret -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1305-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pacific Biomedical Research Center, Kewalo Marine Laboratory, University of Hawaii, Honolulu, HI 96813, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14988540" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/genetics/pathogenicity ; Bacterial Infections/microbiology ; *Bacterial Physiological Phenomena ; *Biological Evolution ; *Ecosystem ; Humans ; Immune System/physiology ; Invertebrates/*microbiology/physiology ; Models, Biological ; Vertebrates/*microbiology/physiology ; Virulence Factors/physiology
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  • 80
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sack, Fred D -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1461-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Cellular and Molecular Biology, Ohio State University, Columbus, OH 43210, USA. sack.1@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178791" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/genetics/growth & development/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Cell Communication ; Cell Division ; Cell Membrane/metabolism ; Genes, Plant ; MAP Kinase Kinase Kinases/*metabolism ; MAP Kinase Signaling System ; Mutation ; Phosphorylation ; Plant Epidermis/*cytology/physiology ; Plant Leaves/*cytology/physiology ; Receptors, Cell Surface/metabolism ; Serine Endopeptidases/genetics/metabolism
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  • 81
    Publication Date: 2004-10-02
    Description: Diatoms are unicellular algae with plastids acquired by secondary endosymbiosis. They are responsible for approximately 20% of global carbon fixation. We report the 34 million-base pair draft nuclear genome of the marine diatom Thalassiosira pseudonana and its 129 thousand-base pair plastid and 44 thousand-base pair mitochondrial genomes. Sequence and optical restriction mapping revealed 24 diploid nuclear chromosomes. We identified novel genes for silicic acid transport and formation of silica-based cell walls, high-affinity iron uptake, biosynthetic enzymes for several types of polyunsaturated fatty acids, use of a range of nitrogenous compounds, and a complete urea cycle, all attributes that allow diatoms to prosper in aquatic environments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Armbrust, E Virginia -- Berges, John A -- Bowler, Chris -- Green, Beverley R -- Martinez, Diego -- Putnam, Nicholas H -- Zhou, Shiguo -- Allen, Andrew E -- Apt, Kirk E -- Bechner, Michael -- Brzezinski, Mark A -- Chaal, Balbir K -- Chiovitti, Anthony -- Davis, Aubrey K -- Demarest, Mark S -- Detter, J Chris -- Glavina, Tijana -- Goodstein, David -- Hadi, Masood Z -- Hellsten, Uffe -- Hildebrand, Mark -- Jenkins, Bethany D -- Jurka, Jerzy -- Kapitonov, Vladimir V -- Kroger, Nils -- Lau, Winnie W Y -- Lane, Todd W -- Larimer, Frank W -- Lippmeier, J Casey -- Lucas, Susan -- Medina, Monica -- Montsant, Anton -- Obornik, Miroslav -- Parker, Micaela Schnitzler -- Palenik, Brian -- Pazour, Gregory J -- Richardson, Paul M -- Rynearson, Tatiana A -- Saito, Mak A -- Schwartz, David C -- Thamatrakoln, Kimberlee -- Valentin, Klaus -- Vardi, Assaf -- Wilkerson, Frances P -- Rokhsar, Daniel S -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):79-86.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Oceanography, University of Washington, Seattle, WA 98195, USA. armbrust@ocean.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459382" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Algal Proteins/chemistry/genetics/physiology ; Animals ; *Biological Evolution ; Cell Nucleus/genetics ; Chromosomes ; DNA/genetics ; Diatoms/chemistry/cytology/*genetics/metabolism ; *Ecosystem ; Energy Metabolism ; *Genome ; Iron/metabolism ; Light ; Light-Harvesting Protein Complexes/chemistry/genetics/metabolism ; Mitochondria/genetics ; Molecular Sequence Data ; Nitrogen/metabolism ; Photosynthesis ; Plastids/genetics ; Restriction Mapping ; Sequence Alignment ; *Sequence Analysis, DNA ; Silicic Acid/metabolism ; Symbiosis ; Urea/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-02-07
    Description: Darwinian dynamics based on mutation and selection form the core of mathematical models for adaptation and coevolution of biological populations. The evolutionary outcome is often not a fitness-maximizing equilibrium but can include oscillations and chaos. For studying frequency-dependent selection, game-theoretic arguments are more appropriate than optimization algorithms. Replicator and adaptive dynamics describe short- and long-term evolution in phenotype space and have found applications ranging from animal behavior and ecology to speciation, macroevolution, and human language. Evolutionary game theory is an essential component of a mathematical and computational approach to biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, Martin A -- Sigmund, Karl -- New York, N.Y. -- Science. 2004 Feb 6;303(5659):793-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program for Evolutionary Dynamics, Department of Mathematics, Department of Organismic and Evolutionary Biology, Harvard University, 1 Brattle Square, Cambridge, MA 02138, USA. martin_nowak@harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14764867" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Algorithms ; Animals ; *Biological Evolution ; Ecosystem ; Evolution, Molecular ; Female ; *Game Theory ; Genetics, Population ; Humans ; Male ; Mathematics ; Selection, Genetic
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  • 83
    Publication Date: 2004-07-03
    Description: Species richness often peaks at intermediate productivity and decreases as resources become more or less abundant. The mechanisms that produce this pattern are not completely known, but several previous studies have suggested environmental heterogeneity as a cause. In experiments with evolving digital organisms and populations of fixed size, maximum species richness emerges at intermediate productivity, even in a spatially homogeneous environment, owing to frequency-dependent selection to exploit an influx of mixed resources. A diverse pool of limiting resources is sufficient to cause adaptive radiation, which is manifest by the origin and maintenance of phenotypically and phylogenetically distinct groups of organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, Stephanie S -- Wilke, Claus O -- Ofria, Charles -- Lenski, Richard E -- Adami, Christoph -- New York, N.Y. -- Science. 2004 Jul 2;305(5680):84-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Digital Life Laboratory 136-93, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15232105" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Biological ; Algorithms ; *Biodiversity ; *Biological Evolution ; *Computer Simulation ; Ecosystem ; Genome ; *Models, Biological ; Mutation ; Phylogeny ; *Software ; User-Computer Interface
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  • 84
    Publication Date: 2004-01-06
    Description: Interactions between ends from different DNA double-strand breaks (DSBs) can produce tumorigenic chromosome translocations. Two theories for the juxta-position of DSBs in translocations, the static "contact-first" and the dynamic "breakage-first" theory, differ fundamentally in their requirement for DSB mobility. To determine whether or not DSB-containing chromosome domains are mobile and can interact, we introduced linear tracks of DSBs in nuclei. We observed changes in track morphology within minutes after DSB induction, indicating movement of the domains. In a subpopulation of cells, the domains clustered. Juxtaposition of different DSB-containing chromosome domains through clustering, which was most extensive in G1 phase cells, suggests an adhesion process in which we implicate the Mre11 complex. Our results support the breakage-first theory to explain the origin of chromosomal translocations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aten, Jacob A -- Stap, Jan -- Krawczyk, Przemek M -- van Oven, Carel H -- Hoebe, Ron A -- Essers, Jeroen -- Kanaar, Roland -- New York, N.Y. -- Science. 2004 Jan 2;303(5654):92-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Microscopical Research, Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, P.O. Box 22700, 1100 DE Amsterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14704429" target="_blank"〉PubMed〈/a〉
    Keywords: Alpha Particles ; Animals ; Ataxia Telangiectasia/genetics/metabolism ; CHO Cells ; Cell Nucleus/metabolism/radiation effects ; *Chromosome Breakage ; Chromosomes, Human/*metabolism ; Chromosomes, Mammalian/metabolism ; Cricetinae ; Cricetulus ; DNA/*metabolism/radiation effects ; *DNA Damage ; DNA Repair ; DNA-Binding Proteins/metabolism ; Fibroblasts/metabolism ; G1 Phase ; G2 Phase ; HeLa Cells ; Histones/*metabolism ; Humans ; Phosphorylation ; Rad51 Recombinase ; S Phase ; Translocation, Genetic
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  • 85
    Publication Date: 2004-10-09
    Description: Little is known of the fate of viruses involved in long-term obligatory associations with eukaryotes. For example, many species of parasitoid wasps have symbiotic viruses to manipulate host defenses and to allow development of parasitoid larvae. The complete nucleotide sequence of the DNA enclosed in the virus particles injected by a parasitoid wasp revealed a complex organization, resembling a eukaryote genomic region more than a viral genome. Although endocellular symbiont genomes have undergone a dramatic loss of genes, the evolution of symbiotic viruses appears to be characterized by extensive duplication of virulence genes coding for truncated versions of cellular proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Espagne, Eric -- Dupuy, Catherine -- Huguet, Elisabeth -- Cattolico, Laurence -- Provost, Bertille -- Martins, Nathalie -- Poirie, Marylene -- Periquet, Georges -- Drezen, Jean Michel -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Recherche sur la Biologie de l'Insecte, CNRS UMR 6035, UFR Sciences et Techniques, Parc de Grandmont, 37200 Tours, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15472078" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Ankyrin Repeat ; Base Composition ; *Biological Evolution ; Cysteine Proteinase Inhibitors/genetics ; Genes, Viral ; *Genome, Viral ; Introns ; Manduca/parasitology/virology ; Molecular Sequence Data ; Polydnaviridae/*genetics ; Protein Tyrosine Phosphatases/genetics ; *Sequence Analysis, DNA ; *Symbiosis ; Viral Proteins/chemistry/genetics ; Virulence Factors/genetics ; Wasps/*virology
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  • 86
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zimmer, Carl -- New York, N.Y. -- Science. 2004 Nov 19;306(5700):1283.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15550638" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthropometry ; *Biological Evolution ; Biomechanical Phenomena ; Body Size ; Buttocks/anatomy & histology ; Hominidae/anatomy & histology/*physiology ; Humans ; Ligaments/anatomy & histology ; *Physical Endurance ; *Running/physiology ; Tendons/anatomy & histology
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  • 87
    Publication Date: 2004-12-25
    Description: The ablation of the protein kinase Raf-1 renders cells hypersensitive to apoptosis despite normal regulation of extracellular signal-regulated kinases, which suggests that apoptosis protection is mediated by a distinct pathway. We used proteomic analysis of Raf-1 signaling complexes to show that Raf-1 counteracts apoptosis by suppressing the activation of mammalian sterile 20-like kinase (MST2). Raf-1 prevents dimerization and phosphorylation of the activation loop of MST2 independently of its protein kinase activity. Depletion of MST2 from Raf-1-/- mouse or human cells abrogated sensitivity to apoptosis, whereas overexpression of MST2 induced apoptosis. Conversely, depletion of Raf-1 from Raf-1+/+ mouse or human cells led to MST2 activation and apoptosis. The concomitant depletion of both Raf-1 and MST2 prevented apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neill, Eric -- Rushworth, Linda -- Baccarini, Manuela -- Kolch, Walter -- New York, N.Y. -- Science. 2004 Dec 24;306(5705):2267-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15618521" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/metabolism ; *Apoptosis ; COS Cells ; Cell Line, Tumor ; Dimerization ; Humans ; Mice ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Proteomics ; Proto-Oncogene Proteins c-raf/genetics/*metabolism ; RNA, Small Interfering ; Signal Transduction ; Staurosporine/pharmacology ; Transfection
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  • 88
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scotland, Robert W -- Sanderson, Michael J -- New York, N.Y. -- Science. 2004 Jan 30;303(5658):643.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Sciences, Oxford University, Oxford, OX1 3RB, UK. robert.scotland@plants.ox.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14752153" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/*classification ; Animals ; *Biodiversity ; *Biological Evolution ; Birds/*classification ; Classification ; Computer Simulation ; Models, Biological ; *Phylogeny
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  • 89
    Publication Date: 2004-10-16
    Description: Obesity contributes to the development of type 2 diabetes, but the underlying mechanisms are poorly understood. Using cell culture and mouse models, we show that obesity causes endoplasmic reticulum (ER) stress. This stress in turn leads to suppression of insulin receptor signaling through hyperactivation of c-Jun N-terminal kinase (JNK) and subsequent serine phosphorylation of insulin receptor substrate-1 (IRS-1). Mice deficient in X-box-binding protein-1 (XBP-1), a transcription factor that modulates the ER stress response, develop insulin resistance. These findings demonstrate that ER stress is a central feature of peripheral insulin resistance and type 2 diabetes at the molecular, cellular, and organismal levels. Pharmacologic manipulation of this pathway may offer novel opportunities for treating these common diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozcan, Umut -- Cao, Qiong -- Yilmaz, Erkan -- Lee, Ann-Hwee -- Iwakoshi, Neal N -- Ozdelen, Esra -- Tuncman, Gurol -- Gorgun, Cem -- Glimcher, Laurie H -- Hotamisligil, Gokhan S -- AI32412/AI/NIAID NIH HHS/ -- DK52539/DK/NIDDK NIH HHS/ -- P05-CA100707/CA/NCI NIH HHS/ -- T32-DK07703/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 15;306(5695):457-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Complex Diseases, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15486293" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Cells, Cultured ; DNA-Binding Proteins/genetics/metabolism ; Diabetes Mellitus, Type 2/*metabolism ; Endoplasmic Reticulum/*metabolism ; Glucose/metabolism ; Homeostasis ; Insulin/*metabolism ; Insulin Receptor Substrate Proteins ; *Insulin Resistance ; Liver/metabolism ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred BALB C ; Mice, Obese ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinases/metabolism ; Muscle, Skeletal/metabolism ; Mutation ; Nuclear Proteins/genetics/metabolism ; Obesity/*metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Rats ; Receptor, Insulin/metabolism ; Signal Transduction ; Transcription Factors ; Tunicamycin/pharmacology ; eIF-2 Kinase/metabolism
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  • 90
    Publication Date: 2004-05-01
    Description: Receptor tyrosine kinase genes were sequenced in non-small cell lung cancer (NSCLC) and matched normal tissue. Somatic mutations of the epidermal growth factor receptor gene EGFR were found in 15of 58 unselected tumors from Japan and 1 of 61 from the United States. Treatment with the EGFR kinase inhibitor gefitinib (Iressa) causes tumor regression in some patients with NSCLC, more frequently in Japan. EGFR mutations were found in additional lung cancer samples from U.S. patients who responded to gefitinib therapy and in a lung adenocarcinoma cell line that was hypersensitive to growth inhibition by gefitinib, but not in gefitinib-insensitive tumors or cell lines. These results suggest that EGFR mutations may predict sensitivity to gefitinib.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paez, J Guillermo -- Janne, Pasi A -- Lee, Jeffrey C -- Tracy, Sean -- Greulich, Heidi -- Gabriel, Stacey -- Herman, Paula -- Kaye, Frederic J -- Lindeman, Neal -- Boggon, Titus J -- Naoki, Katsuhiko -- Sasaki, Hidefumi -- Fujii, Yoshitaka -- Eck, Michael J -- Sellers, William R -- Johnson, Bruce E -- Meyerson, Matthew -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1497-500. Epub 2004 Apr 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Medical Oncology and Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118125" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/drug therapy/genetics/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Antineoplastic Agents/pharmacology/therapeutic use ; Carcinoma, Non-Small-Cell Lung/drug therapy/*genetics/metabolism ; Cell Line, Tumor ; Controlled Clinical Trials as Topic ; Enzyme Inhibitors/pharmacology/therapeutic use ; Female ; *Genes, erbB-1 ; Humans ; Japan ; Lung Neoplasms/drug therapy/*genetics/metabolism ; Male ; Molecular Sequence Data ; *Mutation ; Mutation, Missense ; Phosphorylation ; Protein Conformation ; Protein Structure, Tertiary ; Quinazolines/pharmacology/*therapeutic use ; Receptor, Epidermal Growth Factor/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Sequence Deletion ; Treatment Outcome ; United States
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  • 91
    Publication Date: 2004-04-10
    Description: Chlamydiae are the major cause of preventable blindness and sexually transmitted disease. Genome analysis of a chlamydia-related symbiont of free-living amoebae revealed that it is twice as large as any of the pathogenic chlamydiae and had few signs of recent lateral gene acquisition. We showed that about 700 million years ago the last common ancestor of pathogenic and symbiotic chlamydiae was already adapted to intracellular survival in early eukaryotes and contained many virulence factors found in modern pathogenic chlamydiae, including a type III secretion system. Ancient chlamydiae appear to be the originators of mechanisms for the exploitation of eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horn, Matthias -- Collingro, Astrid -- Schmitz-Esser, Stephan -- Beier, Cora L -- Purkhold, Ulrike -- Fartmann, Berthold -- Brandt, Petra -- Nyakatura, Gerald J -- Droege, Marcus -- Frishman, Dmitrij -- Rattei, Thomas -- Mewes, Hans-Werner -- Wagner, Michael -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):728-30. Epub 2004 Apr 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbial Ecology, Institute of Ecology and Conservation Biology, University of Vienna, Althanstrasse 14, 1090 Vienna, Austria. horn@microbial-ecology.net〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073324" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthamoeba/microbiology ; Animals ; Bacterial Proteins/analysis/genetics/metabolism ; *Biological Evolution ; Cell Membrane/chemistry ; Cell Wall/chemistry ; Chlamydia/classification/genetics/metabolism/pathogenicity ; Chlamydiales/*classification/*genetics/metabolism/pathogenicity ; Chlamydophila/classification/genetics/metabolism/pathogenicity ; Electron Transport ; Gene Order ; Gene Transfer, Horizontal ; Genes, Bacterial ; *Genome, Bacterial ; Molecular Sequence Data ; Nucleotide Transport Proteins/metabolism ; Phylogeny ; Symbiosis ; Virulence ; Virulence Factors/genetics/metabolism
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  • 92
    Publication Date: 2004-10-30
    Description: Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frank, Rene A W -- Titman, Christopher M -- Pratap, J Venkatesh -- Luisi, Ben F -- Perham, Richard N -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):872-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514159" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Dihydrolipoyllysine-Residue Acetyltransferase ; Geobacillus stearothermophilus/*enzymology ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Models, Molecular ; Mutation ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry/metabolism ; Protons ; Pyruvate Dehydrogenase (Lipoamide)/*chemistry/genetics/*metabolism ; Pyruvate Dehydrogenase Complex/*chemistry/*metabolism ; Pyruvic Acid/metabolism ; Thiamine Pyrophosphate/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1454.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567821" target="_blank"〉PubMed〈/a〉
    Keywords: Alaska ; Animals ; *Biological Evolution ; *Bison/classification/genetics ; Canada ; *Climate ; DNA, Mitochondrial/genetics ; *Fossils ; Genetic Variation ; Human Activities ; Humans ; Population Dynamics ; Sequence Analysis, DNA ; Time
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  • 94
    Publication Date: 2004-06-05
    Description: Stomata are epidermal structures that modulate gas exchange between a plant and its environment. During development, stomata are specified and positioned nonrandomly by the integration of asymmetric cell divisions and intercellular signaling. The Arabidopsis mitogen-activated protein kinase kinase kinase gene, YODA, acts as part of a molecular switch controlling cell identities in the epidermis. Null mutations in YODA lead to excess stomata, whereas constitutive activation of YODA eliminated stomata. Transcriptome analysis of seedlings with altered YODA activity was used to identify potential stomatal regulatory genes. A putative transcription factor from this set was shown to regulate the developmental behavior of stomatal precursors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bergmann, Dominique C -- Lukowitz, Wolfgang -- Somerville, Chris R -- 5 F32GM064273-03/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1494-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Carnegie Institution, Department of Plant Biology, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178800" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*cytology/genetics/growth & development/metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Cell Differentiation ; Cell Division ; Cell Lineage ; DNA, Bacterial ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; Genes, Plant ; MAP Kinase Kinase Kinases/genetics/*metabolism ; MAP Kinase Signaling System ; Mutation ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Phosphorylation ; Plant Epidermis/*cytology/growth & development/physiology ; Plant Leaves/*cytology/growth & development/physiology ; Plants, Genetically Modified ; Receptors, Cell Surface/metabolism ; Serine Endopeptidases/metabolism ; Transcription Factors/genetics/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-30
    Description: Natural killer (NK) cells are lymphocytes of the innate immune system that are involved in the early defenses against foreign cells, as well as autologous cells undergoing various forms of stress, such as microbial infection or tumor transformation. NK cell activation is controlled by a dynamic balance between complementary and antagonistic pathways that are initiated upon interaction with potential target cells. NK cells express an array of activating cell surface receptors that can trigger cytolytic programs, as well as cytokine or chemokine secretion. Some of these activating cell surface receptors initiate protein tyrosine kinase (PTK)-dependent pathways through noncovalent associations with transmembrane signaling adaptors that harbor intracytoplasmic ITAMs (immunoreceptor tyrosine-based activation motifs). Additional cell surface receptors that are not directly coupled to ITAMs also participate in NK cell activation. These include NKG2D, which is noncovalently associated to the DAP10 transmembrane signaling adaptor, as well as integrins and cytokine receptors. NK cells also express cell surface inhibitory receptors that antagonize activating pathways through protein tyrosine phosphatases (PTPs). These inhibitory cell surface receptors are characterized by intracytoplasmic ITIMs (immunoreceptor tyrosine-based inhibition motifs). The tyrosine-phosphorylation status of several signaling components that are substrates for both PTKs and PTPs is thus key to the propagation of the NK cell effector pathways. Understanding the integration of these multiple signals is central to the understanding and manipulation of NK cell effector signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vivier, Eric -- Nunes, Jacques A -- Vely, Frederic -- New York, N.Y. -- Science. 2004 Nov 26;306(5701):1517-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre d'Immunologie de Marseille-Luminy, INSERM-CNRS-Univ. Mediterranee, Campus de Luminy, Case 906, 13288 Marseille cedex 09, France. vivier@ciml.univ-mrs.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15567854" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Motifs ; Animals ; Antibody-Dependent Cell Cytotoxicity ; Cytokines/metabolism ; Humans ; Killer Cells, Natural/immunology/*physiology ; Lymphocyte Activation ; Membrane Proteins/metabolism ; Mice ; Models, Immunological ; NK Cell Lectin-Like Receptor Subfamily K ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Receptors, Immunologic/chemistry/metabolism/physiology ; Receptors, Natural Killer Cell ; *Signal Transduction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):766-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297641" target="_blank"〉PubMed〈/a〉
    Keywords: Archaea/cytology/*physiology ; Bacteria/cytology/ultrastructure ; *Bacterial Physiological Phenomena ; *Biological Evolution ; *Cell Nucleus/metabolism/ultrastructure ; Eukaryotic Cells/*physiology/ultrastructure ; Genes, Archaeal ; Genes, Bacterial ; Intracellular Membranes/ultrastructure ; Myxococcales/cytology/physiology ; Nuclear Envelope/physiology/ultrastructure ; Symbiosis ; *Virus Physiological Phenomena ; Viruses/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 2004-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):383.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087522" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Cichlids/*anatomy & histology/*genetics/growth & development ; Crosses, Genetic ; *Genes ; Mandible/*anatomy & histology/growth & development ; *Quantitative Trait Loci
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2004 Feb 20;303(5661):1128-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14976292" target="_blank"〉PubMed〈/a〉
    Keywords: Altruism ; Animals ; *Biological Evolution ; Brain/*physiology ; *Cooperative Behavior ; Culture ; Games, Experimental ; Humans ; Magnetic Resonance Imaging ; Prefrontal Cortex/physiology ; Primates/psychology ; Punishment ; Reproductive Behavior ; Social Behavior
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  • 99
    Publication Date: 2004-05-29
    Description: Inherited defects in signaling pathways downstream of the insulin receptor have long been suggested to contribute to human type 2 diabetes mellitus. Here we describe a mutation in the gene encoding the protein kinase AKT2/PKBbeta in a family that shows autosomal dominant inheritance of severe insulin resistance and diabetes mellitus. Expression of the mutant kinase in cultured cells disrupted insulin signaling to metabolic end points and inhibited the function of coexpressed, wild-type AKT. These findings demonstrate the central importance of AKT signaling to insulin sensitivity in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2258004/" 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/PMC2258004/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉George, Stella -- Rochford, Justin J -- Wolfrum, Christian -- Gray, Sarah L -- Schinner, Sven -- Wilson, Jenny C -- Soos, Maria A -- Murgatroyd, Peter R -- Williams, Rachel M -- Acerini, Carlo L -- Dunger, David B -- Barford, David -- Umpleby, A Margot -- Wareham, Nicholas J -- Davies, Huw Alban -- Schafer, Alan J -- Stoffel, Markus -- O'Rahilly, Stephen -- Barroso, Ines -- 078986/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2004 May 28;304(5675):1325-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QQ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166380" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adipocytes/cytology/metabolism ; Adult ; Aged ; Amino Acid Motifs ; Amino Acid Sequence ; Amino Acid Substitution ; Catalytic Domain ; Cell Differentiation ; Cell Line ; Cell Nucleus/metabolism ; Cytosol/metabolism ; DNA-Binding Proteins/metabolism ; Diabetes Mellitus/*genetics/metabolism ; Female ; Genes, Dominant ; Hepatocyte Nuclear Factor 3-beta ; Humans ; Hyperinsulinism/genetics/metabolism ; Insulin/metabolism ; Insulin Resistance/*genetics ; Lipid Metabolism ; Male ; Middle Aged ; Molecular Sequence Data ; *Mutation, Missense ; Nuclear Proteins/metabolism ; Pedigree ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-akt ; Signal Transduction ; *Transcription Factors
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  • 100
    Publication Date: 2004-05-01
    Description: A general caging method for proteins that are regulated by phosphorylation was used to study the in vivo biochemical action of cofilin and the subsequent cellular response. By acute and local activation of a chemically engineered, light-sensitive phosphocofilin mimic, we demonstrate that cofilin polymerizes actin, generates protrusions, and determines the direction of cell migration. We propose a role for cofilin that is distinct from its role as an actin-depolymerizing factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, Mousumi -- Song, Xiaoyan -- Mouneimne, Ghassan -- Sidani, Mazen -- Lawrence, David S -- Condeelis, John S -- GM38511/GM/NIGMS NIH HHS/ -- GM61034/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Apr 30;304(5671):743-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15118165" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Depolymerizing Factors ; Actins/*metabolism ; Animals ; Biopolymers ; Cell Line, Tumor ; *Cell Movement ; Light ; Lim Kinases ; Microfilament Proteins/genetics/*physiology ; Microinjections ; Mutation ; Phenylacetates/chemistry ; Phosphorylation ; Protein Binding ; Protein Kinases/metabolism ; Pseudopodia/physiology/ultrastructure ; RNA, Small Interfering ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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