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  • Molecular Sequence Data  (14)
  • Male  (12)
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  • 1
    Publication Date: 2011-05-10
    Description: Vascular plants appeared ~410 million years ago, then diverged into several lineages of which only two survive: the euphyllophytes (ferns and seed plants) and the lycophytes. We report here the genome sequence of the lycophyte Selaginella moellendorffii (Selaginella), the first nonseed vascular plant genome reported. By comparing gene content in evolutionarily diverse taxa, we found that the transition from a gametophyte- to a sporophyte-dominated life cycle required far fewer new genes than the transition from a nonseed vascular to a flowering plant, whereas secondary metabolic genes expanded extensively and in parallel in the lycophyte and angiosperm lineages. Selaginella differs in posttranscriptional gene regulation, including small RNA regulation of repetitive elements, an absence of the trans-acting small interfering RNA pathway, and extensive RNA editing of organellar genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166216/" 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/PMC3166216/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Banks, Jo Ann -- Nishiyama, Tomoaki -- Hasebe, Mitsuyasu -- Bowman, John L -- Gribskov, Michael -- dePamphilis, Claude -- Albert, Victor A -- Aono, Naoki -- Aoyama, Tsuyoshi -- Ambrose, Barbara A -- Ashton, Neil W -- Axtell, Michael J -- Barker, Elizabeth -- Barker, Michael S -- Bennetzen, Jeffrey L -- Bonawitz, Nicholas D -- Chapple, Clint -- Cheng, Chaoyang -- Correa, Luiz Gustavo Guedes -- Dacre, Michael -- DeBarry, Jeremy -- Dreyer, Ingo -- Elias, Marek -- Engstrom, Eric M -- Estelle, Mark -- Feng, Liang -- Finet, Cedric -- Floyd, Sandra K -- Frommer, Wolf B -- Fujita, Tomomichi -- Gramzow, Lydia -- Gutensohn, Michael -- Harholt, Jesper -- Hattori, Mitsuru -- Heyl, Alexander -- Hirai, Tadayoshi -- Hiwatashi, Yuji -- Ishikawa, Masaki -- Iwata, Mineko -- Karol, Kenneth G -- Koehler, Barbara -- Kolukisaoglu, Uener -- Kubo, Minoru -- Kurata, Tetsuya -- Lalonde, Sylvie -- Li, Kejie -- Li, Ying -- Litt, Amy -- Lyons, Eric -- Manning, Gerard -- Maruyama, Takeshi -- Michael, Todd P -- Mikami, Koji -- Miyazaki, Saori -- Morinaga, Shin-ichi -- Murata, Takashi -- Mueller-Roeber, Bernd -- Nelson, David R -- Obara, Mari -- Oguri, Yasuko -- Olmstead, Richard G -- Onodera, Naoko -- Petersen, Bent Larsen -- Pils, Birgit -- Prigge, Michael -- Rensing, Stefan A -- Riano-Pachon, Diego Mauricio -- Roberts, Alison W -- Sato, Yoshikatsu -- Scheller, Henrik Vibe -- Schulz, Burkhard -- Schulz, Christian -- Shakirov, Eugene V -- Shibagaki, Nakako -- Shinohara, Naoki -- Shippen, Dorothy E -- Sorensen, Iben -- Sotooka, Ryo -- Sugimoto, Nagisa -- Sugita, Mamoru -- Sumikawa, Naomi -- Tanurdzic, Milos -- Theissen, Gunter -- Ulvskov, Peter -- Wakazuki, Sachiko -- Weng, Jing-Ke -- Willats, William W G T -- Wipf, Daniel -- Wolf, Paul G -- Yang, Lixing -- Zimmer, Andreas D -- Zhu, Qihui -- Mitros, Therese -- Hellsten, Uffe -- Loque, Dominique -- Otillar, Robert -- Salamov, Asaf -- Schmutz, Jeremy -- Shapiro, Harris -- Lindquist, Erika -- Lucas, Susan -- Rokhsar, Daniel -- Grigoriev, Igor V -- GM065383/GM/NIGMS NIH HHS/ -- GM84051/GM/NIGMS NIH HHS/ -- HG004164/HG/NHGRI NIH HHS/ -- R01 GM043644/GM/NIGMS NIH HHS/ -- R01 GM084051/GM/NIGMS NIH HHS/ -- R01 GM084051-01A1/GM/NIGMS NIH HHS/ -- R01 HG004164/HG/NHGRI NIH HHS/ -- R01 HG004164-02/HG/NHGRI NIH HHS/ -- R01 HG004164-03/HG/NHGRI NIH HHS/ -- R01 HG004164-04/HG/NHGRI NIH HHS/ -- T32 GM007757/GM/NIGMS NIH HHS/ -- T32-HG00035/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2011 May 20;332(6032):960-3. doi: 10.1126/science.1203810. Epub 2011 May 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany and Plant Pathology, Purdue University, West Lafayette, IN 47907, USA. banksj@purdue.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21551031" target="_blank"〉PubMed〈/a〉
    Keywords: Angiosperms/chemistry/genetics ; *Biological Evolution ; Bryopsida/genetics ; Chlamydomonas/chemistry/genetics ; DNA Transposable Elements ; Evolution, Molecular ; Gene Expression Regulation, Plant ; Genes, Plant ; *Genome, Plant ; MicroRNAs/genetics ; Molecular Sequence Data ; Phylogeny ; Plant Proteins/genetics/metabolism ; Proteome/analysis ; RNA Editing ; RNA, Plant/genetics ; Repetitive Sequences, Nucleic Acid ; Selaginellaceae/*genetics/growth & development/metabolism ; Sequence Analysis, DNA
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  • 2
    Publication Date: 1999-04-16
    Description: A previously unknown giant sulfur bacterium is abundant in sediments underlying the oxygen minimum zone of the Benguela Current upwelling system. The bacterium has a spherical cell that exceeds by up to 100-fold the biovolume of the largest known prokaryotes. On the basis of 16S ribosomal DNA sequence data, these bacteria are closely related to the marine filamentous sulfur bacteria Thioploca, abundant in the upwelling area off Chile and Peru. Similar to Thioploca, the giant bacteria oxidize sulfide with nitrate that is accumulated to 〈/=800 millimolar in a central vacuole.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulz, H N -- Brinkhoff, T -- Ferdelman, T G -- Marine, M H -- Teske, A -- Jorgensen, B B -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):493-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Marine Microbiology, Celsiusstrasse, D-28359 Bremen, Germany. hschulz@mpi-bremen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205058" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/classification/cytology/*isolation & purification/*metabolism ; Cytoplasm/ultrastructure ; Genes, rRNA ; Geologic Sediments/*microbiology ; Microscopy, Electron ; Molecular Sequence Data ; Namibia ; Nitrates/analysis/*metabolism ; Oxidation-Reduction ; Phylogeny ; RNA, Bacterial/genetics ; RNA, Ribosomal, 16S/genetics ; Sulfides/*metabolism ; Sulfur/*analysis/metabolism ; Terminology as Topic ; Vacuoles/chemistry/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2001-07-14
    Description: Variation within genes has important implications for all biological traits. We identified 3899 single nucleotide polymorphisms (SNPs) that were present within 313 genes from 82 unrelated individuals of diverse ancestry, and we organized the SNPs into 4304 different haplotypes. Each gene had several variable SNPs and haplotypes that were present in all populations, as well as a number that were population-specific. Pairs of SNPs exhibited variability in the degree of linkage disequilibrium that was a function of their location within a gene, distance from each other, population distribution, and population frequency. Haplotypes generally had more information content (heterozygosity) than did individual SNPs. Our analysis of the pattern of variation strongly supports the recent expansion of the human population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stephens, J C -- Schneider, J A -- Tanguay, D A -- Choi, J -- Acharya, T -- Stanley, S E -- Jiang, R -- Messer, C J -- Chew, A -- Han, J H -- Duan, J -- Carr, J L -- Lee, M S -- Koshy, B -- Kumar, A M -- Zhang, G -- Newell, W R -- Windemuth, A -- Xu, C -- Kalbfleisch, T S -- Shaner, S L -- Arnold, K -- Schulz, V -- Drysdale, C M -- Nandabalan, K -- Judson, R S -- Ruano, G -- Vovis, G F -- New York, N.Y. -- Science. 2001 Jul 20;293(5529):489-93. Epub 2001 Jul 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genaissance Pharmaceuticals, Inc., Five Science Park, New Haven, CT 06511, USA. c.stephens@genaissance.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11452081" target="_blank"〉PubMed〈/a〉
    Keywords: African Continental Ancestry Group/genetics ; Alleles ; Animals ; Asian Continental Ancestry Group/genetics ; Dinucleoside Phosphates/genetics ; European Continental Ancestry Group/genetics ; Evolution, Molecular ; Female ; *Genetic Variation ; *Haplotypes ; Heterozygote ; Hispanic Americans/genetics ; Humans ; *Linkage Disequilibrium ; Male ; Mutation ; Pan troglodytes/genetics ; *Polymorphism, Single Nucleotide ; X Chromosome/genetics
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  • 4
    Publication Date: 2001-12-26
    Description: Stem cells generate many differentiated, short-lived cell types, such as blood, skin, and sperm, throughout adult life. Stem cells maintain a long-term capacity to divide, producing daughter cells that either self-renew or initiate differentiation. Although the surrounding microenvironment or "niche" influences stem cell fate decisions, few signals that emanate from the niche to specify stem cell self-renewal have been identified. Here we demonstrate that the apical hub cells in the Drosophila testis act as a cellular niche that supports stem cell self-renewal. Hub cells express the ligand Unpaired (Upd), which activates the Janus kinase-signal transducer and activator of transcription (JAK-STAT) pathway in adjacent germ cells to specify self-renewal and continual maintenance of the germ line stem cell population.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kiger, A A -- Jones, D L -- Schulz, C -- Rogers, M B -- Fuller, M T -- GM07790-22/GM/NIGMS NIH HHS/ -- HD07493/HD/NICHD NIH HHS/ -- P01-DK53074/DK/NIDDK NIH HHS/ -- R01 GM078176/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2542-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305-5329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752574" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cues ; DNA-Binding Proteins/genetics/*metabolism ; Drosophila/cytology/embryology/genetics/*physiology ; Drosophila Proteins/*metabolism ; Germ Cells/*physiology ; Glycoproteins/*metabolism ; Janus Kinases ; Ligands ; Male ; Mutation ; Protein-Tyrosine Kinases/genetics/*metabolism ; STAT Transcription Factors ; Signal Transduction ; Spermatocytes/cytology/physiology ; Spermatogenesis ; Stem Cells/cytology/*physiology ; Testis/cytology/metabolism ; Trans-Activators/genetics/*metabolism ; *Transcription Factors
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  • 5
    Publication Date: 1997-02-28
    Description: The leaf sucrose transporter SUT1 is essential for phloem loading and long-distance transport of assimilates. Both SUT1 messenger RNA (mRNA) and protein were shown to be diurnally regulated and to have high turnover rates. SUT1 protein was detected by immunolocalization in plasma membranes of enucleate sieve elements (SEs) in tobacco, potato, and tomato. Analysis by in situ hybridization showed that SUT1 mRNA localizes mainly to the SE and is preferentially associated with plasmodesmata. Antisense inhibition of SUT1 expression under control of a companion cell (CC)-specific promoter indicated synthesis of SUT1 mRNA in the CC. These results provide evidence for targeting of plant endogenous mRNA and potentially SUT1 protein through phloem plasmodesmata and for sucrose loading at the plasma membrane of SE.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, C -- Franceschi, V R -- Schulz, A -- Lemoine, R -- Frommer, W B -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1298-300.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Botanik, Eberhard-Karls-Universitat, Auf der Morgenstelle 1, D-72076 Tubingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036853" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport, Active ; Carrier Proteins/analysis/genetics/*metabolism ; Cell Membrane/chemistry/metabolism ; Fluorescent Antibody Technique ; Immunohistochemistry ; In Situ Hybridization ; Lycopersicon esculentum/metabolism ; Membrane Proteins/analysis/genetics/*metabolism ; *Membrane Transport Proteins ; Molecular Sequence Data ; Plant Leaves/chemistry/cytology/*metabolism ; Plant Proteins/analysis/genetics/*metabolism ; Plants, Toxic ; RNA, Messenger/analysis/genetics/metabolism ; RNA, Plant/analysis/genetics/metabolism ; Solanum tuberosum ; Sucrose/metabolism ; Tobacco/metabolism ; Transcription, Genetic
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  • 6
    Publication Date: 2009-12-18
    Description: All cancers carry somatic mutations. A subset of these somatic alterations, termed driver mutations, confer selective growth advantage and are implicated in cancer development, whereas the remainder are passengers. Here we have sequenced the genomes of a malignant melanoma and a lymphoblastoid cell line from the same person, providing the first comprehensive catalogue of somatic mutations from an individual cancer. The catalogue provides remarkable insights into the forces that have shaped this cancer genome. The dominant mutational signature reflects DNA damage due to ultraviolet light exposure, a known risk factor for malignant melanoma, whereas the uneven distribution of mutations across the genome, with a lower prevalence in gene footprints, indicates that DNA repair has been preferentially deployed towards transcribed regions. The results illustrate the power of a cancer genome sequence to reveal traces of the DNA damage, repair, mutation and selection processes that were operative years before the cancer became symptomatic.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145108/" 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/PMC3145108/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pleasance, Erin D -- Cheetham, R Keira -- Stephens, Philip J -- McBride, David J -- Humphray, Sean J -- Greenman, Chris D -- Varela, Ignacio -- Lin, Meng-Lay -- Ordonez, Gonzalo R -- Bignell, Graham R -- Ye, Kai -- Alipaz, Julie -- Bauer, Markus J -- Beare, David -- Butler, Adam -- Carter, Richard J -- Chen, Lina -- Cox, Anthony J -- Edkins, Sarah -- Kokko-Gonzales, Paula I -- Gormley, Niall A -- Grocock, Russell J -- Haudenschild, Christian D -- Hims, Matthew M -- James, Terena -- Jia, Mingming -- Kingsbury, Zoya -- Leroy, Catherine -- Marshall, John -- Menzies, Andrew -- Mudie, Laura J -- Ning, Zemin -- Royce, Tom -- Schulz-Trieglaff, Ole B -- Spiridou, Anastassia -- Stebbings, Lucy A -- Szajkowski, Lukasz -- Teague, Jon -- Williamson, David -- Chin, Lynda -- Ross, Mark T -- Campbell, Peter J -- Bentley, David R -- Futreal, P Andrew -- Stratton, Michael R -- 077012/Z/05/Z/Wellcome Trust/United Kingdom -- 088340/Wellcome Trust/United Kingdom -- 093867/Wellcome Trust/United Kingdom -- England -- Nature. 2010 Jan 14;463(7278):191-6. doi: 10.1038/nature08658. Epub 2009 Dec 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Sanger Institute, Hinxton CB10 1SA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20016485" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Cell Line, Tumor ; DNA Damage/genetics ; DNA Mutational Analysis ; DNA Repair/genetics ; Gene Dosage/genetics ; Genes, Neoplasm/*genetics ; Genome, Human/*genetics ; Humans ; Loss of Heterozygosity/genetics ; Male ; Melanoma/etiology/genetics ; MicroRNAs/genetics ; Mutagenesis, Insertional/genetics ; Mutation/*genetics ; Neoplasms/etiology/*genetics ; Polymorphism, Single Nucleotide/genetics ; Precision Medicine ; Sequence Deletion/genetics ; Ultraviolet Rays
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
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  • 7
    Publication Date: 2008-08-23
    Description: Adipose tissue is central to the regulation of energy balance. Two functionally different types of fat are present in mammals: white adipose tissue, the primary site of triglyceride storage, and brown adipose tissue, which is specialized in energy expenditure and can counteract obesity. Factors that specify the developmental fate and function of white and brown adipose tissue remain poorly understood. Here we demonstrate that whereas some members of the family of bone morphogenetic proteins (BMPs) support white adipocyte differentiation, BMP7 singularly promotes differentiation of brown preadipocytes even in the absence of the normally required hormonal induction cocktail. BMP7 activates a full program of brown adipogenesis including induction of early regulators of brown fat fate PRDM16 (PR-domain-containing 16; ref. 4) and PGC-1alpha (peroxisome proliferator-activated receptor-gamma (PPARgamma) coactivator-1alpha; ref. 5), increased expression of the brown-fat-defining marker uncoupling protein 1 (UCP1) and adipogenic transcription factors PPARgamma and CCAAT/enhancer-binding proteins (C/EBPs), and induction of mitochondrial biogenesis via p38 mitogen-activated protein (MAP) kinase-(also known as Mapk14) and PGC-1-dependent pathways. Moreover, BMP7 triggers commitment of mesenchymal progenitor cells to a brown adipocyte lineage, and implantation of these cells into nude mice results in development of adipose tissue containing mostly brown adipocytes. Bmp7 knockout embryos show a marked paucity of brown fat and an almost complete absence of UCP1. Adenoviral-mediated expression of BMP7 in mice results in a significant increase in brown, but not white, fat mass and leads to an increase in energy expenditure and a reduction in weight gain. These data reveal an important role of BMP7 in promoting brown adipocyte differentiation and thermogenesis in vivo and in vitro, and provide a potential new therapeutic approach for the treatment of obesity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2745972/" 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/PMC2745972/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tseng, Yu-Hua -- Kokkotou, Efi -- Schulz, Tim J -- Huang, Tian Lian -- Winnay, Jonathon N -- Taniguchi, Cullen M -- Tran, T Thien -- Suzuki, Ryo -- Espinoza, Daniel O -- Yamamoto, Yuji -- Ahrens, Molly J -- Dudley, Andrew T -- Norris, Andrew W -- Kulkarni, Rohit N -- Kahn, C Ronald -- K08 DK064906/DK/NIDDK NIH HHS/ -- K08 DK64906/DK/NIDDK NIH HHS/ -- P30 DK040561/DK/NIDDK NIH HHS/ -- P30 DK040561-13/DK/NIDDK NIH HHS/ -- P30 DK46200/DK/NIDDK NIH HHS/ -- R01 DK 060837/DK/NIDDK NIH HHS/ -- R01 DK077097/DK/NIDDK NIH HHS/ -- R01 DK077097-01A1/DK/NIDDK NIH HHS/ -- R01 DK077097-02/DK/NIDDK NIH HHS/ -- R01 DK67536/DK/NIDDK NIH HHS/ -- R21 DK070722/DK/NIDDK NIH HHS/ -- R21 DK070722-01/DK/NIDDK NIH HHS/ -- R21 DK070722-02/DK/NIDDK NIH HHS/ -- England -- Nature. 2008 Aug 21;454(7207):1000-4. doi: 10.1038/nature07221.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Obesity and Hormone Action, Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215, USA. yu-hua.tseng@joslin.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18719589" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3-L1 Cells ; *Adipogenesis ; Adipose Tissue, Brown/*growth & development/*metabolism ; Adipose Tissue, White/growth & development ; Animals ; Bone Morphogenetic Protein 7 ; Bone Morphogenetic Proteins/*metabolism ; Cell Line ; *Energy Metabolism/genetics ; Male ; Mesenchymal Stromal Cells/cytology/physiology ; Mice ; Mice, Inbred C57BL ; Mice, Nude ; Mitochondria/physiology ; Thermogenesis ; Transforming Growth Factor beta/*metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
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  • 8
    Publication Date: 1991-02-08
    Description: The mos proto-oncogene product, pp39mos, is a protein kinase and has been equated with cytostatic factor (CSF), an activity in unfertilized eggs that is thought to be responsible for the arrest of meiosis at metaphase II. The biochemical properties and potential substrates of pp39mos were examined in unfertilized eggs and in transformed cells in order to study how the protein functions both as CSF and in transformation. The pp39mos protein associated with polymers under conditions that favor tubulin oligomerization and was present in an approximately 500-kilodalton "core" complex under conditions that favor depolymerization. beta-Tubulin was preferentially coprecipitated in pp39mos immunoprecipitates and was the major phosphorylated product in a pp39mos-dependent immune complex kinase assay. Immunofluorescence analysis of NIH 3T3 cells transformed with Xenopus c-mos showed that pp39mos colocalizes with tubulin in the spindle during metaphase and in the midbody and asters during telophase. Disruption of microtubules with nocodazole affected tubulin and pp39mos organization in the same way. It therefore appears that pp39mos is a tubulin-associated protein kinase and may thus participate in the modification of microtubules and contribute to the formation of the spindle. This activity expressed during interphase in somatic cells may be responsible for the transforming activity of pp39mos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, R P -- Oskarsson, M -- Paules, R S -- Schulz, N -- Cleveland, D -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):671-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825142" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Line ; Cell Transformation, Neoplastic/metabolism ; Macromolecular Substances ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-mos ; Tubulin/*metabolism
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2011-06-28
    Description: Sixteen-month-old infants (N = 83) rationally used sparse data about the distribution of outcomes among agents and objects to solve a fundamental inference problem: deciding whether event outcomes are due to themselves or the world. When infants experienced failed outcomes, their causal attributions affected whether they sought help or explored.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gweon, Hyowon -- Schulz, Laura -- New York, N.Y. -- Science. 2011 Jun 24;332(6037):1524. doi: 10.1126/science.1204493.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. hyora@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21700866" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; Humans ; Infant ; *Infant Behavior ; *Learning ; Male ; *Mental Processes ; *Problem Solving
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1997-09-20
    Description: The crystal structure of squalene-hopene cyclase from Alicyclobacillus acidocaldarius was determined at 2.9 angstrom resolution. The mechanism and sequence of this cyclase are closely related to those of 2,3-oxidosqualene cyclases that catalyze the cyclization step in cholesterol biosynthesis. The structure reveals a membrane protein with membrane-binding characteristics similar to those of prostaglandin-H2 synthase, the only other reported protein of this type. The active site of the enzyme is located in a large central cavity that is of suitable size to bind squalene in its required conformation and that is lined by aromatic residues. The structure supports a mechanism in which the acid starting the reaction by protonating a carbon-carbon double bond is an aspartate that is coupled to a histidine. Numerous surface alpha helices are connected by characteristic QW-motifs (Q is glutamine and W is tryptophan) that tighten the protein structure, possibly for absorbing the reaction energy without structural damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wendt, K U -- Poralla, K -- Schulz, G E -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Albertstrasse 21, D-79104 Freiburg im Breisgau, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295270" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillaceae/*enzymology ; Binding Sites ; Cell Membrane/enzymology ; Crystallization ; Crystallography, X-Ray ; Cyclization ; Dimerization ; Humans ; Hydrogen Bonding ; *Intramolecular Transferases ; Isomerases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment ; Squalene/metabolism ; Thermodynamics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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