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  • 1
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    Human lineage-specific amplification, selection, and neuronal expression of DUF1220 domains (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-02
    Description: Extreme gene duplication is a major source of evolutionary novelty. A genome-wide survey of gene copy number variation among human and great ape lineages revealed that the most striking human lineage-specific amplification was due to an unknown gene, MGC8902, which is predicted to encode multiple copies of a protein domain of unknown function (DUF1220). Sequences encoding these domains are virtually all primate-specific, show signs of positive selection, and are increasingly amplified generally as a function of a species' evolutionary proximity to humans, where the greatest number of copies (212) is found. DUF1220 domains are highly expressed in brain regions associated with higher cognitive function, and in brain show neuron-specific expression preferentially in cell bodies and dendrites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popesco, Magdalena C -- Maclaren, Erik J -- Hopkins, Janet -- Dumas, Laura -- Cox, Michael -- Meltesen, Lynne -- McGavran, Loris -- Wyckoff, Gerald J -- Sikela, James M -- AA11853/AA/NIAAA NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Human Medical Genetics, University of Colorado at Denver and Health Sciences Center, Aurora, CO 80045, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946073" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Evolution ; Brain/*metabolism ; Cognition ; Exons ; *Gene Amplification ; Gene Dosage ; Gene Duplication ; Gene Expression ; Genome, Human ; Humans ; Macaca mulatta/genetics ; Mice ; Molecular Sequence Data ; Neocortex/metabolism ; Neurons/*metabolism ; Pan troglodytes/genetics ; Phylogeny ; Polymerase Chain Reaction ; *Protein Structure, Tertiary ; Proteins/*chemistry/genetics ; Rats ; *Selection, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Preserved CD4+ central memory T cells and survival in vaccinated SIV-challenged monkeys (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-10
    Description: Vaccine-induced cellular immunity controls virus replication in simian immunodeficiency virus (SIV)-infected monkeys only transiently, leading to the question of whether such vaccines for AIDS will be effective. We immunized monkeys with plasmid DNA and replication-defective adenoviral vectors encoding SIV proteins and then challenged them with pathogenic SIV. Although these monkeys demonstrated a reduction in viremia restricted to the early phase of SIV infection, they showed a prolonged survival. This survival was associated with preserved central memory CD4+ T lymphocytes and could be predicted by the magnitude of the vaccine-induced cellular immune response. These immune correlates of vaccine efficacy should guide the evaluation of AIDS vaccines in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2365913/" 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/PMC2365913/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letvin, Norman L -- Mascola, John R -- Sun, Yue -- Gorgone, Darci A -- Buzby, Adam P -- Xu, Ling -- Yang, Zhi-Yong -- Chakrabarti, Bimal -- Rao, Srinivas S -- Schmitz, Jorn E -- Montefiori, David C -- Barker, Brianne R -- Bookstein, Fred L -- Nabel, Gary J -- Z99 AI999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 9;312(5779):1530-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. nletvin@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763152" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CD4-Positive T-Lymphocytes/*immunology ; Humans ; *Immunologic Memory ; Macaca mulatta ; Molecular Sequence Data ; Plasmids ; SAIDS Vaccines/*immunology ; Simian Acquired Immunodeficiency Syndrome/*immunology/prevention & control ; Simian Immunodeficiency Virus/*immunology ; Survival Analysis ; Vaccines, DNA/*immunology ; Vaccines, Synthetic/immunology ; Virus Replication
    Print ISSN: 0036-8075
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  • 3
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    Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-07
    Description: Ubiquitin-positive, tau- and alpha-synuclein-negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic lateral sclerosis. Although the identity of the ubiquitinated protein specific to either disorder was unknown, we showed that TDP-43 is the major disease protein in both disorders. Pathologic TDP-43 was hyper-phosphorylated, ubiquitinated, and cleaved to generate C-terminal fragments and was recovered only from affected central nervous system regions, including hippocampus, neocortex, and spinal cord. TDP-43 represents the common pathologic substrate linking these neurodegenerative disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, Manuela -- Sampathu, Deepak M -- Kwong, Linda K -- Truax, Adam C -- Micsenyi, Matthew C -- Chou, Thomas T -- Bruce, Jennifer -- Schuck, Theresa -- Grossman, Murray -- Clark, Christopher M -- McCluskey, Leo F -- Miller, Bruce L -- Masliah, Eliezer -- Mackenzie, Ian R -- Feldman, Howard -- Feiden, Wolfgang -- Kretzschmar, Hans A -- Trojanowski, John Q -- Lee, Virginia M-Y -- AG10124/AG/NIA NIH HHS/ -- AG17586/AG/NIA NIH HHS/ -- T32 AG00255/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023659" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/*metabolism/pathology ; Antibodies, Monoclonal ; *Brain Chemistry ; Cerebral Cortex/chemistry/pathology ; DNA-Binding Proteins/*analysis/chemistry/genetics/immunology ; Dementia/genetics/*metabolism/pathology ; Fluorescent Antibody Technique ; Hippocampus/chemistry/pathology ; Humans ; Immunoblotting ; Molecular Sequence Data ; Motor Neurons/chemistry/pathology ; Neurons/chemistry/pathology ; Peptide Fragments/chemistry ; Phosphorylation ; Spinal Cord/*chemistry/pathology ; Ubiquitin/*analysis
    Print ISSN: 0036-8075
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  • 4
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    From the genome to the proteome: uncovering peptides in the Apis brain (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-28
    Description: Neuropeptides, critical brain peptides that modulate animal behavior by affecting the activity of almost every neuronal circuit, are inherently difficult to predict directly from a nascent genome sequence because of extensive posttranslational processing. The combination of bioinformatics and proteomics allows unprecedented neuropeptide discovery from an unannotated genome. Within the Apis mellifera genome, we have inferred more than 200 neuropeptides and have confirmed the sequences of 100 peptides. This study lays the groundwork for future molecular studies of Apis neuropeptides with the identification of 36 genes, 33 of which were previously unreported.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hummon, Amanda B -- Richmond, Timothy A -- Verleyen, Peter -- Baggerman, Geert -- Huybrechts, Jurgen -- Ewing, Michael A -- Vierstraete, Evy -- Rodriguez-Zas, Sandra L -- Schoofs, Liliane -- Robinson, Gene E -- Sweedler, Jonathan V -- DC006395/DC/NIDCD NIH HHS/ -- GM068946/GM/NIGMS NIH HHS/ -- NS31609/NS/NINDS NIH HHS/ -- P30 DA01830/DA/NIDA NIH HHS/ -- P30 DA018310/DA/NIDA NIH HHS/ -- R01 GM068946/GM/NIGMS NIH HHS/ -- R01 NS031609/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):647-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Illinois, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068263" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Bees/*chemistry/*genetics ; Brain Chemistry ; Codon ; Computational Biology ; *Genes, Insect ; Genome, Insect ; Insect Proteins/*chemistry/*genetics ; Mass Spectrometry ; Molecular Sequence Data ; Neuropeptides/*chemistry/*genetics ; Protein Precursors/chemistry/genetics ; Proteome
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  • 5
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    A secreted serine-threonine kinase determines virulence in the eukaryotic pathogen Toxoplasma gondii (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-16
    Description: Toxoplasma gondii strains differ dramatically in virulence despite being genetically very similar. Genetic mapping revealed two closely adjacent quantitative trait loci on parasite chromosome VIIa that control the extreme virulence of the type I lineage. Positional cloning identified the candidate virulence gene ROP18, a highly polymorphic serine-threonine kinase that was secreted into the host cell during parasite invasion. Transfection of the virulent ROP18 allele into a nonpathogenic type III strain increased growth and enhanced mortality by 4 to 5 logs. These attributes of ROP18 required kinase activity, which revealed that secretion of effectors is a major component of parasite virulence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taylor, S -- Barragan, A -- Su, C -- Fux, B -- Fentress, S J -- Tang, K -- Beatty, W L -- Hajj, H El -- Jerome, M -- Behnke, M S -- White, M -- Wootton, J C -- Sibley, L D -- AI059176/AI/NIAID NIH HHS/ -- AI36629/AI/NIAID NIH HHS/ -- AI44600/AI/NIAID NIH HHS/ -- P20 RR-020185/RR/NCRR NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 15;314(5806):1776-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63130, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17170305" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Catalytic Domain ; Chromosome Mapping ; Chromosomes/genetics ; Cloning, Molecular ; Genes, Protozoan ; Mice ; Molecular Sequence Data ; Movement ; Point Mutation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Protozoan Proteins/chemistry/genetics/*metabolism ; Quantitative Trait Loci ; Toxoplasma/*enzymology/genetics/growth & development/*pathogenicity ; Toxoplasmosis, Animal/mortality/parasitology ; Transfection ; Virulence/genetics ; Virulence Factors/chemistry/genetics/*metabolism
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  • 6
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    Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-26
    Description: In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersen, Christian B F -- Ballut, Lionel -- Johansen, Jesper S -- Chamieh, Hala -- Nielsen, Klaus H -- Oliveira, Cristiano L P -- Pedersen, Jan Skov -- Seraphin, Bertrand -- Le Hir, Herve -- Andersen, Gregers Rom -- New York, N.Y. -- Science. 2006 Sep 29;313(5795):1968-72. Epub 2006 Aug 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Aarhus, DK-8000 Aarhus, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931718" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/analogs & derivatives/metabolism ; Adenylyl Imidodiphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; DEAD-box RNA Helicases ; Dimerization ; Drosophila Proteins/chemistry/metabolism ; Eukaryotic Initiation Factor-4A/*chemistry/metabolism ; *Exons ; Humans ; Hydrogen Bonding ; Hydrolysis ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*chemistry/metabolism ; Nuclear Proteins/*chemistry/metabolism ; Nucleic Acid Conformation ; Poly U/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Helicases/chemistry/metabolism ; RNA, Messenger/*chemistry/metabolism ; RNA-Binding Proteins/*chemistry/metabolism
    Print ISSN: 0036-8075
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  • 7
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    A gain-of-function mutation in a cytokinin receptor triggers spontaneous root nodule organogenesis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-18
    Description: Legume root nodules originate from differentiated cortical cells that reenter the cell cycle and form organ primordia. We show that perception of the phytohormone cytokinin is a key element in this switch. Mutation of a Lotus japonicus cytokinin receptor gene leads to spontaneous development of root nodules in the absence of rhizobia or rhizobial signal molecules. The mutant histidine kinase receptor has cytokinin-independent activity and activates an Escherichia coli two-component phosphorelay system in vivo. Mutant analysis shows that cytokinin signaling is required for cell divisions that initiate nodule development and defines an autoregulated process where cytokinin induction of nodule stem cells is controlled by shoots.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tirichine, Leila -- Sandal, Niels -- Madsen, Lene H -- Radutoiu, Simona -- Albrektsen, Anita S -- Sato, Shusei -- Asamizu, Erika -- Tabata, Satoshi -- Stougaard, Jens -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):104-7. Epub 2006 Nov 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Gene Expression, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10, DK-8000 Aarhus C, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110537" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Amino Acid Sequence ; Calcium/metabolism ; Cell Division ; Cytokinins/*metabolism/pharmacology ; Escherichia coli/genetics ; Gene Expression Regulation, Plant ; Genes, Plant ; Kinetin/pharmacology ; Lipopolysaccharides/metabolism ; Lotus/genetics/metabolism/*physiology ; Meristem/cytology ; Molecular Sequence Data ; Mutation ; Nitrogen Fixation ; Plant Roots/cytology/metabolism ; Plants, Genetically Modified ; Protein Kinases/chemistry/*genetics/*metabolism ; Receptors, Cell Surface/chemistry/genetics/metabolism ; Root Nodules, Plant/cytology/*growth & development/metabolism ; *Signal Transduction ; Transformation, Genetic
    Print ISSN: 0036-8075
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  • 8
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    Tequila, a neurotrypsin ortholog, regulates long-term memory formation in Drosophila (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-12
    Description: Mutations in the human neurotrypsin gene are associated with autosomal recessive mental retardation. To further understand the pathophysiological consequences of the lack of this serine protease, we studied Tequila (Teq), the Drosophila neurotrypsin ortholog, using associative memory as a behavioral readout. We found that teq inactivation resulted in a long-term memory (LTM)-specific defect. After LTM conditioning of wild-type flies, teq expression transiently increased in the mushroom bodies. Moreover, specific inhibition of teq expression in adult mushroom bodies resulted in a reversible LTM defect. Hence, the Teq pathway is essential for information processing in Drosophila.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Didelot, Gerard -- Molinari, Florence -- Tchenio, Paul -- Comas, Daniel -- Milhiet, Elodie -- Munnich, Arnold -- Colleaux, Laurence -- Preat, Thomas -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):851-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genes et Dynamique des Systemes de Memoire, UMR CNRS 7637, Ecole Superieure de Physique et de Chimie Industrielles, 10 Rue Vauquelin 75005 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Conditioning, Classical ; Drosophila Proteins/chemistry/genetics/*physiology ; Drosophila melanogaster/genetics/*physiology ; Gene Expression ; Gene Expression Regulation ; Humans ; Learning ; *Memory ; Mifepristone/pharmacology ; Models, Animal ; Molecular Sequence Data ; Mushroom Bodies/anatomy & histology/physiology ; Mutation ; Odors ; RNA Interference ; RNA, Messenger/genetics/metabolism ; Serine Endopeptidases/chemistry/genetics/*physiology
    Print ISSN: 0036-8075
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  • 9
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    A bacterial protein enhances the release and efficacy of liposomal cancer drugs (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-25
    Description: Clostridium novyi-NT is an anaerobic bacterium that can infect hypoxic regions within experimental tumors. Because C. novyi-NT lyses red blood cells, we hypothesized that its membrane-disrupting properties could be exploited to enhance the release of liposome-encapsulated drugs within tumors. Here, we show that treatment of mice bearing large, established tumors with C. novyi-NT plus a single dose of liposomal doxorubicin often led to eradication of the tumors. The bacterial factor responsible for the enhanced drug release was identified as a previously unrecognized protein termed liposomase. This protein could potentially be incorporated into diverse experimental approaches for the specific delivery of chemotherapeutic agents to tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheong, Ian -- Huang, Xin -- Bettegowda, Chetan -- Diaz, Luis A Jr -- Kinzler, Kenneth W -- Zhou, Shibin -- Vogelstein, Bert -- CA062924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1308-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and the Ludwig Center for Cancer Genetics and Therapeutics, Johns Hopkins Kimmel Comprehensive Cancer Center, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17124324" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antineoplastic Agents/*administration & dosage/pharmacokinetics/therapeutic use ; Bacterial Proteins/chemistry/genetics/*metabolism ; Base Sequence ; Camptothecin/administration & dosage/analogs & ; derivatives/pharmacokinetics/therapeutic use ; Cell Line, Tumor ; Cloning, Molecular ; Clostridium/*chemistry/genetics ; Colorectal Neoplasms/*drug therapy ; Doxorubicin/*administration & dosage/pharmacokinetics/therapeutic use ; Drug Carriers ; Humans ; Lipase/chemistry/genetics/*metabolism ; Lipid Bilayers/chemistry ; Liposomes/chemistry/*metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Protein Structure, Tertiary
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  • 10
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    Anaphase inactivation of the spindle checkpoint (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-11
    Description: The spindle checkpoint delays cell cycle progression until microtubules attach each pair of sister chromosomes to opposite poles of the mitotic spindle. Following sister chromatid separation, however, the checkpoint ignores chromosomes whose kinetochores are attached to only one spindle pole, a state that activates the checkpoint prior to metaphase. We demonstrate that, in budding yeast, mutual inhibition between the anaphase-promoting complex (APC) and Mps1, an essential component of the checkpoint, leads to sustained inactivation of the spindle checkpoint. Mps1 protein abundance decreases in anaphase, and Mps1 is a target of the APC. Furthermore, expression of Mps1 in anaphase, or repression of the APC in anaphase, reactivates the spindle checkpoint. This APC-Mps1 feedback circuit allows cells to irreversibly inactivate the checkpoint during anaphase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palframan, William J -- Meehl, Janet B -- Jaspersen, Sue L -- Winey, Mark -- Murray, Andrew W -- GM43987/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- R37 GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):680-4. Epub 2006 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase/*physiology ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/metabolism ; Chromosomes, Fungal/physiology ; Feedback, Physiological ; GTP-Binding Proteins/metabolism ; Kinetochores/physiology ; Mad2 Proteins ; Mitosis ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Securin ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/*metabolism
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