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  • Cell Line  (25)
  • Base Sequence
  • American Association for the Advancement of Science (AAAS)  (40)
  • American Chemical Society
  • Springer
  • 2000-2004  (40)
  • 1980-1984
  • 2002  (40)
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  • American Association for the Advancement of Science (AAAS)  (40)
  • American Chemical Society
  • Springer
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  • 2000-2004  (40)
  • 1980-1984
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  • 1
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    The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-14
    Description: The first chordates appear in the fossil record at the time of the Cambrian explosion, nearly 550 million years ago. The modern ascidian tadpole represents a plausible approximation to these ancestral chordates. To illuminate the origins of chordate and vertebrates, we generated a draft of the protein-coding portion of the genome of the most studied ascidian, Ciona intestinalis. The Ciona genome contains approximately 16,000 protein-coding genes, similar to the number in other invertebrates, but only half that found in vertebrates. Vertebrate gene families are typically found in simplified form in Ciona, suggesting that ascidians contain the basic ancestral complement of genes involved in cell signaling and development. The ascidian genome has also acquired a number of lineage-specific innovations, including a group of genes engaged in cellulose metabolism that are related to those in bacteria and fungi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dehal, Paramvir -- Satou, Yutaka -- Campbell, Robert K -- Chapman, Jarrod -- Degnan, Bernard -- De Tomaso, Anthony -- Davidson, Brad -- Di Gregorio, Anna -- Gelpke, Maarten -- Goodstein, David M -- Harafuji, Naoe -- Hastings, Kenneth E M -- Ho, Isaac -- Hotta, Kohji -- Huang, Wayne -- Kawashima, Takeshi -- Lemaire, Patrick -- Martinez, Diego -- Meinertzhagen, Ian A -- Necula, Simona -- Nonaka, Masaru -- Putnam, Nik -- Rash, Sam -- Saiga, Hidetoshi -- Satake, Masanobu -- Terry, Astrid -- Yamada, Lixy -- Wang, Hong-Gang -- Awazu, Satoko -- Azumi, Kaoru -- Boore, Jeffrey -- Branno, Margherita -- Chin-Bow, Stephen -- DeSantis, Rosaria -- Doyle, Sharon -- Francino, Pilar -- Keys, David N -- Haga, Shinobu -- Hayashi, Hiroko -- Hino, Kyosuke -- Imai, Kaoru S -- Inaba, Kazuo -- Kano, Shungo -- Kobayashi, Kenji -- Kobayashi, Mari -- Lee, Byung-In -- Makabe, Kazuhiro W -- Manohar, Chitra -- Matassi, Giorgio -- Medina, Monica -- Mochizuki, Yasuaki -- Mount, Steve -- Morishita, Tomomi -- Miura, Sachiko -- Nakayama, Akie -- Nishizaka, Satoko -- Nomoto, Hisayo -- Ohta, Fumiko -- Oishi, Kazuko -- Rigoutsos, Isidore -- Sano, Masako -- Sasaki, Akane -- Sasakura, Yasunori -- Shoguchi, Eiichi -- Shin-i, Tadasu -- Spagnuolo, Antoinetta -- Stainier, Didier -- Suzuki, Miho M -- Tassy, Olivier -- Takatori, Naohito -- Tokuoka, Miki -- Yagi, Kasumi -- Yoshizaki, Fumiko -- Wada, Shuichi -- Zhang, Cindy -- Hyatt, P Douglas -- Larimer, Frank -- Detter, Chris -- Doggett, Norman -- Glavina, Tijana -- Hawkins, Trevor -- Richardson, Paul -- Lucas, Susan -- Kohara, Yuji -- Levine, Michael -- Satoh, Nori -- Rokhsar, Daniel S -- HD-37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2157-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481130" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Apoptosis ; Base Sequence ; Cellulose/metabolism ; Central Nervous System/physiology ; Ciona intestinalis/anatomy & histology/classification/*genetics/physiology ; Computational Biology ; Endocrine System/physiology ; Gene Dosage ; Gene Duplication ; Genes ; Genes, Homeobox ; *Genome ; Heart/embryology/physiology ; Immunity/genetics ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/genetics ; Organizers, Embryonic/physiology ; Phylogeny ; Polymorphism, Genetic ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Species Specificity ; Thyroid Gland/physiology ; Urochordata/genetics ; Vertebrates/anatomy & histology/classification/genetics/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Excess polymorphisms in genes for membrane proteins in Plasmodium falciparum (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-05
    Description: The detection of single-nucleotide polymorphisms in pathogenic microorganisms has normally been carried out by trial and error. Here we show that DNA hybridization with high-density oligonucleotide arrays provides rapid and convenient detection of single-nucleotide polymorphisms in Plasmodium falciparum, despite its exceptionally high adenine-thymine (AT) content (82%). A disproportionate number of polymorphisms are found in genes encoding proteins associated with the cell membrane. These genes are targets for only 22% of the oligonucleotide probes but account for 69% of the polymorphisms. Genetic variation is also enriched in subtelomeric regions, which account for 22% of the chromosome but 76% of the polymorphisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, Sarah K -- Hartl, Daniel L -- Wirth, Dyann F -- Nielsen, Kaare M -- Choi, Mehee -- Batalov, Serge -- Zhou, Yingyao -- Plouffe, David -- Le Roch, Karine G -- Abagyan, Ruben -- Winzeler, Elizabeth A -- GM61351/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):216-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364807" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosomes/genetics ; DNA, Protozoan/genetics ; *Genes, Protozoan ; Genetic Variation ; Genome, Protozoan ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Plasmodium falciparum/*genetics ; *Polymorphism, Single Nucleotide ; Protozoan Proteins/*genetics ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The hypoxia-inducible factors (HIFs) 1alpha and 2alpha are key mammalian transcription factors that exhibit dramatic increases in both protein stability and intrinsic transcriptional potency during low-oxygen stress. This increased stability is due to the absence of proline hydroxylation, which in normoxia promotes binding of HIF to the von Hippel-Lindau (VHL tumor suppressor) ubiquitin ligase. We now show that hypoxic induction of the COOH-terminal transactivation domain (CAD) of HIF occurs through abrogation of hydroxylation of a conserved asparagine in the CAD. Inhibitors of Fe(II)- and 2-oxoglutarate-dependent dioxygenases prevented hydroxylation of the Asn, thus allowing the CAD to interact with the p300 transcription coactivator. Replacement of the conserved Asn by Ala resulted in constitutive p300 interaction and strong transcriptional activity. Full induction of HIF-1alpha and -2alpha, therefore, relies on the abrogation of both Pro and Asn hydroxylation, which during normoxia occur at the degradation and COOH-terminal transactivation domains, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lando, David -- Peet, Daniel J -- Whelan, Dean A -- Gorman, Jeffrey J -- Whitelaw, Murray L -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):858-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biosciences (Biochemistry), Adelaide University, SA 5005, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823643" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Asparagine/*metabolism ; Basic Helix-Loop-Helix Transcription Factors ; Cell Hypoxia/*physiology ; Cell Line ; Humans ; Hydroxylation ; Hypoxia-Inducible Factor 1, alpha Subunit ; Mass Spectrometry ; Mice ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Mutation ; Oxygen/*physiology ; Proline/metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcriptional Activation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Comparative genome sequencing for discovery of novel polymorphisms in Bacillus anthracis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: Comparison of the whole-genome sequence of Bacillus anthracis isolated from a victim of a recent bioterrorist anthrax attack with a reference reveals 60 new markers that include single nucleotide polymorphisms (SNPs), inserted or deleted sequences, and tandem repeats. Genome comparison detected four high-quality SNPs between the two sequenced B. anthracis chromosomes and seven differences among different preparations of the reference genome. These markers have been tested on a collection of anthrax isolates and were found to divide these samples into distinct families. These results demonstrate that genome-based analysis of microbial pathogens will provide a powerful new tool for investigation of infectious disease outbreaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Read, Timothy D -- Salzberg, Steven L -- Pop, Mihai -- Shumway, Martin -- Umayam, Lowell -- Jiang, Lingxia -- Holtzapple, Erik -- Busch, Joseph D -- Smith, Kimothy L -- Schupp, James M -- Solomon, Daniel -- Keim, Paul -- Fraser, Claire M -- R01-LM06845/LM/NLM NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2028-33. Epub 2002 May 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Institute for Genomic Research, 9712 Medical Center Drive, Rockville, MD 20850, USA., Department of Biological Sciences, Northern Arizona University, Flagstaff, AZ 86011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004073" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/microbiology ; Bacillus anthracis/classification/*genetics/isolation & ; purification/pathogenicity ; Bacterial Typing Techniques ; Base Sequence ; Bioterrorism ; Chromosome Inversion ; Computational Biology ; Disease Outbreaks ; Genetic Markers ; *Genetic Variation ; *Genome, Bacterial ; Genomics ; Humans ; Minisatellite Repeats ; Molecular Sequence Data ; Mutation ; Phenotype ; Phylogeny ; Plasmids ; *Polymorphism, Single Nucleotide ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Sequence Deletion ; Species Specificity ; Transposases/genetics ; Virulence/genetics
    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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  • 5
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    Production of alpha 1,3-galactosyltransferase-deficient pigs (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-21
    Description: The enzyme alpha1,3-galactosyltransferase (alpha1,3GT or GGTA1) synthesizes alpha1,3-galactose (alpha1,3Gal) epitopes (Galalpha1,3Galbeta1,4GlcNAc-R), which are the major xenoantigens causing hyperacute rejection in pig-to-human xenotransplantation. Complete removal of alpha1,3Gal from pig organs is the critical step toward the success of xenotransplantation. We reported earlier the targeted disruption of one allele of the alpha1,3GT gene in cloned pigs. A selection procedure based on a bacterial toxin was used to select for cells in which the second allele of the gene was knocked out. Sequencing analysis demonstrated that knockout of the second allele of the alpha1,3GT gene was caused by a T-to-G single point mutation at the second base of exon 9, which resulted in inactivation of the alpha1,3GT protein. Four healthy alpha1,3GT double-knockout female piglets were produced by three consecutive rounds of cloning. The piglets carrying a point mutation in the alpha1,3GT gene hold significant value, as they would allow production of alpha1,3Gal-deficient pigs free of antibiotic-resistance genes and thus have the potential to make a safer product for human use.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154759/" 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/PMC3154759/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Phelps, Carol J -- Koike, Chihiro -- Vaught, Todd D -- Boone, Jeremy -- Wells, Kevin D -- Chen, Shu-Hung -- Ball, Suyapa -- Specht, Susan M -- Polejaeva, Irina A -- Monahan, Jeff A -- Jobst, Pete M -- Sharma, Sugandha B -- Lamborn, Ashley E -- Garst, Amy S -- Moore, Marilyn -- Demetris, Anthony J -- Rudert, William A -- Bottino, Rita -- Bertera, Suzanne -- Trucco, Massimo -- Starzl, Thomas E -- Dai, Yifan -- Ayares, David L -- DK29961/DK/NIDDK NIH HHS/ -- R01 AM007772/AM/NIADDK NIH HHS/ -- R01 DK029961-19/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):411-4. Epub 2002 Dec 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉PPL Therapeutics Inc., 1700 Kraft Drive, Blacksburg, VA 24060, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493821" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Bacterial Toxins/pharmacology ; Cell Line ; Cloning, Molecular ; Cloning, Organism ; DNA, Complementary ; Embryo Transfer ; Enterotoxins/pharmacology ; Female ; Fibroblasts ; Galactosyltransferases/*deficiency/*genetics ; *Gene Targeting ; Genetic Vectors ; HeLa Cells ; Humans ; Immunoglobulin M/blood ; Islets of Langerhans Transplantation ; Mice ; Mice, Knockout ; *Point Mutation ; Pregnancy ; Swine/*genetics ; Transfection ; Transplantation, Heterologous ; Trisaccharides/*analysis/biosynthesis/immunology
    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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  • 6
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    Genomic instability in mice lacking histone H2AX (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-06
    Description: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage. Double-strand breaks (DSBs) induce histone H2AX phosphorylation, which is associated with the recruitment of repair factors to damaged DNA. To help clarify the physiological role of H2AX, we targeted H2AX in mice. Although H2AX is not essential for irradiation-induced cell-cycle checkpoints, H2AX-/- mice were radiation sensitive, growth retarded, and immune deficient, and mutant males were infertile. These pleiotropic phenotypes were associated with chromosomal instability, repair defects, and impaired recruitment of Nbs1, 53bp1, and Brca1, but not Rad51, to irradiation-induced foci. Thus, H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" 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/PMC4721576/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celeste, Arkady -- Petersen, Simone -- Romanienko, Peter J -- Fernandez-Capetillo, Oscar -- Chen, Hua Tang -- Sedelnikova, Olga A -- Reina-San-Martin, Bernardo -- Coppola, Vincenzo -- Meffre, Eric -- Difilippantonio, Michael J -- Redon, Christophe -- Pilch, Duane R -- Olaru, Alexandru -- Eckhaus, Michael -- Camerini-Otero, R Daniel -- Tessarollo, Lino -- Livak, Ferenc -- Manova, Katia -- Bonner, William M -- Nussenzweig, Michel C -- Nussenzweig, Andre -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):922-7. Epub 2002 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934988" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology/physiology ; Base Sequence ; Cell Aging ; Cell Cycle ; Cells, Cultured ; *Chromosome Aberrations ; DNA Damage ; *DNA Repair ; Female ; Gene Targeting ; Histones/chemistry/*genetics/*physiology ; Immunoglobulin Class Switching ; Infertility, Male/genetics/physiopathology ; Lymphocyte Count ; Male ; Meiosis ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Phosphorylation ; *Recombination, Genetic ; Spermatocytes/physiology ; T-Lymphocytes/immunology/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: The presence of galactose alpha-1,3-galactose residues on the surface of pig cells is a major obstacle to successful xenotransplantation. Here, we report the production of four live pigs in which one allele of the alpha-1,3-galactosyltransferase locus has been knocked out. These pigs were produced by nuclear transfer technology; clonal fetal fibroblast cell lines were used as nuclear donors for embryos reconstructed with enucleated pig oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, Liangxue -- Kolber-Simonds, Donna -- Park, Kwang-Wook -- Cheong, Hee-Tae -- Greenstein, Julia L -- Im, Gi-Sun -- Samuel, Melissa -- Bonk, Aaron -- Rieke, August -- Day, Billy N -- Murphy, Clifton N -- Carter, David B -- Hawley, Robert J -- Prather, Randall S -- R44 RR15198/RR/NCRR NIH HHS/ -- T32 RR07004/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1089-92. Epub 2002 Jan 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Science, University of Missouri, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778012" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Animals, Genetically Modified ; Cell Line ; *Cloning, Organism ; Embryo Transfer ; Female ; Fetus ; Fibroblasts ; Galactosyltransferases/*genetics ; *Gene Targeting ; Genetic Vectors ; Male ; Mutagenesis, Insertional ; Nuclear Transfer Techniques ; Pregnancy ; Recombination, Genetic ; Swine ; Swine, Miniature/embryology/*genetics ; Transfection
    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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  • 8
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    Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Obligate intracellular apicomplexan parasites rely on gliding motion powered by their actomyosin system to disperse throughout tissues and to penetrate host cells. Toxoplasma gondii myosin A has been implicated in this process, but direct proof has been lacking. We designed a genetic screen to generate a tetracycline-inducible transactivator system in T. gondii. The MyoA gene was disrupted in the presence of a second regulatable copy of MyoA. Conditional removal of this myosin caused severe impairment in host cell invasion and parasite spreading in cultured cells, and unambiguously established the pathogenic function of this motor in an animal model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meissner, Markus -- Schluter, Dirk -- Soldati, Dominique -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):837-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Imperial College Road, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399593" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcimycin/pharmacology ; Calcium/metabolism ; Cell Line ; Cells, Cultured ; Exocytosis ; Genetic Vectors ; Humans ; Mice ; Movement ; Nonmuscle Myosin Type IIA/genetics/*physiology ; Organelles/metabolism ; Protozoan Proteins/genetics/physiology ; Tetracycline/pharmacology ; Toxoplasma/genetics/growth & development/*pathogenicity/*physiology ; Toxoplasmosis, Animal/*parasitology ; Trans-Activators/metabolism ; Transfection ; Transgenes ; Virulence ; Virulence Factors/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Huntington's disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. Transcriptional dysregulation has been implicated in HD pathogenesis. Here, we report that huntingtin interacts with the transcriptional activator Sp1 and coactivator TAFII130. Coexpression of Sp1 and TAFII130 in cultured striatal cells from wild-type and HD transgenic mice reverses the transcriptional inhibition of the dopamine D2 receptor gene caused by mutant huntingtin, as well as protects neurons from huntingtin-induced cellular toxicity. Furthermore, soluble mutant huntingtin inhibits Sp1 binding to DNA in postmortem brain tissues of both presymptomatic and affected HD patients. Understanding these early molecular events in HD may provide an opportunity to interfere with the effects of mutant huntingtin before the development of disease symptoms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunah, Anthone W -- Jeong, Hyunkyung -- Griffin, April -- Kim, Yong-Man -- Standaert, David G -- Hersch, Steven M -- Mouradian, M Maral -- Young, Anne B -- Tanese, Naoko -- Krainc, Dimitri -- 5R37AG13617/AG/NIA NIH HHS/ -- AT00613/AT/NCCIH NIH HHS/ -- NS02174/NS/NINDS NIH HHS/ -- NS34361/NS/NINDS NIH HHS/ -- NS35255/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2238-43. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Center for Aging, Genetics and Neurodegeneration, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Caudate Nucleus/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Corpus Striatum/cytology/embryology/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Down-Regulation ; Gene Expression Regulation ; Humans ; Huntington Disease/*genetics/metabolism ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/physiology ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides ; Promoter Regions, Genetic ; Rats ; Receptors, Dopamine D2/genetics ; Solubility ; Sp1 Transcription Factor/chemistry/*metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; Transfection ; Trinucleotide Repeat Expansion ; Two-Hybrid System Techniques
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Many proteins associated with the plasma membrane are known to partition into submicroscopic sphingolipid- and cholesterol-rich domains called lipid rafts, but the determinants dictating this segregation of proteins in the membrane are poorly understood. We suppressed the tendency of Aequorea fluorescent proteins to dimerize and targeted these variants to the plasma membrane using several different types of lipid anchors. Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts. Thus the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zacharias, David A -- Violin, Jonathan D -- Newton, Alexandra C -- Tsien, Roger Y -- 2T32 GM07752/GM/NIGMS NIH HHS/ -- DK54441/DK/NIDDK NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):913-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Biomedical Sciences Graduate Program, and, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0647, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988576" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Animals ; Bacterial Proteins/chemistry/*metabolism ; Caveolin 1 ; Caveolins/metabolism ; Cell Line ; Detergents ; Dimerization ; Dogs ; Energy Transfer ; Fluorescence ; Green Fluorescent Proteins ; Luminescent Proteins/chemistry/*metabolism ; Membrane Microdomains/*metabolism ; Myristic Acid/metabolism ; Oligopeptides/chemistry/*metabolism ; Palmitic Acid/metabolism ; Protein Prenylation ; Recombinant Fusion Proteins/metabolism ; Solubility ; Spectrometry, Fluorescence ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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