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  • Chemistry  (61)
  • Humans  (27)
  • AIRCRAFT DESIGN, TESTING AND PERFORMANCE  (12)
  • 2000-2004  (13)
  • 1980-1984  (86)
  • 1
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    HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-09
    Description: HIF (hypoxia-inducible factor) is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability. In the presence of oxygen, HIF is targeted for destruction by an E3 ubiquitin ligase containing the von Hippel-Lindau tumor suppressor protein (pVHL). We found that human pVHL binds to a short HIF-derived peptide when a conserved proline residue at the core of this peptide is hydroxylated. Because proline hydroxylation requires molecular oxygen and Fe(2+), this protein modification may play a key role in mammalian oxygen sensing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivan, M -- Kondo, K -- Yang, H -- Kim, W -- Valiando, J -- Ohh, M -- Salic, A -- Asara, J M -- Lane, W S -- Kaelin , W G Jr -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):464-8. Epub 2001 Apr 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Brigham and Women's Hospital, Howard Hughes Medical Institute, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Hypoxia ; Cell Line ; Cobalt/pharmacology ; Deferoxamine/pharmacology ; Humans ; Hydroxylation ; Hydroxyproline/*metabolism ; *Ligases ; Mass Spectrometry ; Mice ; Molecular Sequence Data ; Oxygen/*physiology ; Protein Structure, Tertiary ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factors/*metabolism ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Von Hippel-Lindau Tumor Suppressor Protein
    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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    Parasitology. Drugs to combat tropical protozoan parasites (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelb, Michael H -- Hol, Wim G J -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):343-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Chemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130767" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antimalarials/chemistry/pharmacology/therapeutic use ; *Antiprotozoal Agents/chemistry/pharmacology/therapeutic use ; Chagas Disease/drug therapy/parasitology ; Chemistry, Pharmaceutical ; Combinatorial Chemistry Techniques ; Computational Biology ; Databases, Factual ; Drug Design ; Drug Resistance ; Genomics ; Humans ; Leishmania/drug effects/genetics/metabolism ; Leishmaniasis/drug therapy/parasitology ; Malaria/drug therapy/parasitology ; Plasmodium falciparum/drug effects/genetics/metabolism ; Plasmodium vivax/drug effects/genetics ; *Trypanocidal Agents/chemistry/pharmacology/therapeutic use ; Trypanosoma brucei brucei/drug effects/genetics/metabolism ; Trypanosoma cruzi/drug effects/genetics/metabolism ; Trypanosomiasis, African/drug therapy/parasitology
    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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    Location of a major susceptibility locus for familial schizophrenia on chromosome 1q21-q22 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-28
    Description: Schizophrenia is a complex disorder, and there is substantial evidence supporting a genetic etiology. Despite this, prior attempts to localize susceptibility loci have produced predominantly suggestive findings. A genome-wide scan for schizophrenia susceptibility loci in 22 extended families with high rates of schizophrenia provided highly significant evidence of linkage to chromosome 1 (1q21-q22), with a maximum heterogeneity logarithm of the likelihood of linkage (lod) score of 6.50. This linkage result should provide sufficient power to allow the positional cloning of the underlying susceptibility gene.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3787922/" 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/PMC3787922/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brzustowicz, L M -- Hodgkinson, K A -- Chow, E W -- Honer, W G -- Bassett, A S -- 53216/Canadian Institutes of Health Research/Canada -- K08 MH01392/MH/NIMH NIH HHS/ -- N01-HG-65403/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):678-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular and Behavioral Neuroscience, Rutgers University, Newark, NJ 07102, USA. brzustowicz@axon.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10784452" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Computer Simulation ; Female ; Genes, Dominant ; Genes, Recessive ; Genetic Heterogeneity ; Genetic Linkage ; Genetic Markers ; *Genetic Predisposition to Disease ; Humans ; Likelihood Functions ; Lod Score ; Male ; Models, Genetic ; Pedigree ; Schizophrenia/*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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  • 4
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    Predictive identification of exonic splicing enhancers in human genes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-13
    Description: Specific short oligonucleotide sequences that enhance pre-mRNA splicing when present in exons, termed exonic splicing enhancers (ESEs), play important roles in constitutive and alternative splicing. A computational method, RESCUE-ESE, was developed that predicts which sequences have ESE activity by statistical analysis of exon-intron and splice site composition. When large data sets of human gene sequences were used, this method identified 10 predicted ESE motifs. Representatives of all 10 motifs were found to display enhancer activity in vivo, whereas point mutants of these sequences exhibited sharply reduced activity. The motifs identified enable prediction of the splicing phenotypes of exonic mutations in human genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fairbrother, William G -- Yeh, Ru-Fang -- Sharp, Phillip A -- Burge, Christopher B -- 1 R01 HG02439-01/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1007-13. Epub 2002 Jul 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114529" target="_blank"〉PubMed〈/a〉
    Keywords: Computational Biology ; Consensus Sequence ; DNA, Complementary ; Databases, Nucleic Acid ; *Exons ; *Genes ; *Genome, Human ; Humans ; Hypoxanthine Phosphoribosyltransferase/genetics ; Introns ; Oligonucleotides/genetics ; Point Mutation ; *RNA Splicing ; *Regulatory Sequences, Nucleic Acid ; 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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  • 5
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    Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Min, Jung-Hyun -- Yang, Haifeng -- Ivan, Mircea -- Gertler, Frank -- Kaelin, William G Jr -- Pavletich, Nikola P -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1886-9. Epub 2002 May 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Hydroxylation ; Hydroxyproline/*metabolism ; Hypoxia-Inducible Factor 1, alpha Subunit ; Ligases/*chemistry/genetics/metabolism ; Macromolecular Substances ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; Transcription Factors/*chemistry/metabolism ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein
    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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  • 6
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    Asbestos surface charge heterogeneity and biological effects (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Light, W G -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280676" target="_blank"〉PubMed〈/a〉
    Keywords: *Asbestos ; Humans ; Occupational Diseases/chemically induced ; Structure-Activity Relationship
    Print ISSN: 0036-8075
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  • 7
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    The human homologs of the raf (mil) oncogene are located on human chromosomes 3 and 4 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-06
    Description: Two human genes that are homologous to both the murine transforming gene (oncogene) v-raf and the chicken transforming gene v-mil have been mapped by means of human-rodent somatic cell hybrids to human chromosomes previously devoid of known oncogenes. One gene, c-raf-2, which appears to be a processed pseudogene, is located on chromosome 4. The other gene, c-raf-1, which appears to be the active gene, is located on chromosome 3 and has been regionally mapped by chromosomal in situ hybridization to 3p25. This assignment correlates with specific chromosomal abnormalities associated with certain human malignancies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T -- O'Brien, S J -- Nash, W G -- Rapp, U R -- Morton, C C -- Leder, P -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):71-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6691137" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/genetics ; Animals ; Chromosome Aberrations ; Chromosome Mapping ; *Chromosomes, Human, 1-3 ; *Chromosomes, Human, 4-5 ; Cricetinae ; Humans ; Hybrid Cells ; Kidney Neoplasms/genetics ; Lung Neoplasms/genetics ; Male ; Mice ; Nucleic Acid Hybridization ; *Oncogenes
    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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    Gene for T-cell growth factor: location on human chromosome 4q and feline chromosome B1 (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: T-cell growth factor (TCGF) or interleukin-2 (IL-2), an immunoregulatory lymphokine, is produced by lectin- or antigen-activated mature T lymphocytes and in a constitutive manner by certain T-cell lymphoma cell lines. By means of a molecular clone of human TCGF and DNA extracted from a panel of somatic cell hybrids (rodent cells X normal human lymphocytes), the TCGF structural gene was identified on human chromosome 4. In situ hybridization of the TCGF clone to human chromosomes resulted in significant labeling of the midportion of the long arm of chromosome 4, indicating that the TCGF gene was located at band q26-28. Genomic DNA from a panel of hybrids prepared with HUT-102 B2 cells was examined with the same molecular clone. In this clone of cells, which produces human T-cell leukemia virus, the TCGF gene was also located on chromosome 4 and was apparently not rearranged. The homologous TCGF locus in the domestic cat was assigned to chromosome B1 by using a somatic cell hybrid panel that segregates cat chromosomes. Linkage studies as well as high-resolution G-trypsin banding indicate that this feline chromosome is partially homologous to human chromosome 4.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seigel, L J -- Harper, M E -- Wong-Staal, F -- Gallo, R C -- Nash, W G -- O'Brien, S J -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):175-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats/*genetics ; Chromosome Banding ; Chromosome Mapping ; *Chromosomes ; *Chromosomes, Human, 4-5 ; Cloning, Molecular ; Deltaretrovirus ; *Genes ; Genetic Linkage ; Humans ; Hybrid Cells ; Interleukin-2/*genetics ; Nucleic Acid Hybridization
    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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    Biologically active chorionic gonadotropin: synthesis by the human fetus (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-04-15
    Description: The kidney, and to a slight extent the liver, of human fetuses were found to synthesize and secrete the alpha subunit common to glycoprotein hormones. Fetal lung and muscle did not synthesize this protein. Since fetal kidney and liver were previously found to synthesize beta chorionic gonadotropin, their ability to synthesize bioactive chorionic gonadotropin was also determined. The newly synthesized hormone bound to mouse Leydig cells and elicited a biological response: namely, the synthesis of testosterone. These results suggest that the human fetus may participate in metabolic homeostasis during its development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGregor, W G -- Kuhn, R W -- Jaffe, R B -- HD08478/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1983 Apr 15;220(4594):306-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6682243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chorionic Gonadotropin/*biosynthesis ; Fetus/*metabolism ; Humans ; Kidney/embryology ; Leydig Cells/metabolism ; Liver/embryology ; Luteinizing Hormone/biosynthesis ; Male ; Mice ; Placenta/metabolism ; Testosterone/biosynthesis
    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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  • 10
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    Linkage analysis of nondeletion hereditary persistence of fetal hemoglobin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-19
    Description: Nondeletion forms of hereditary persistence of fetal hemoglobin may result from regulatory disorders of globin gene expression. The defects in two such conditions were localized by demonstrating a tight genetic linkage between the disorders and polymorphic restriction endonuclease sites within the beta-like globin gene complex. In one instance, the defect probably occurred outside the region of DNA between the epsilon- and beta-globin genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Old, J M -- Ayyub, H -- Wood, W G -- Clegg, J B -- Weatherall, D J -- New York, N.Y. -- Science. 1982 Feb 19;215(4535):981-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6186021" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosome Deletion ; DNA Restriction Enzymes ; Female ; Fetal Hemoglobin/*genetics ; Genetic Linkage ; Globins/genetics ; Humans ; Male ; Pedigree ; Polymorphism, Genetic ; Thalassemia/*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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