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  • 1
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    A model for the mechanism of human topoisomerase I (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The three-dimensional structure of a 70-kilodalton amino terminally truncated form of human topoisomerase I in complex with a 22-base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact DNA. The linker region that connects the central core of the enzyme to the carboxyl-terminal domain assumes a coiled-coil configuration and protrudes away from the remainder of the enzyme. The positively charged DNA-proximal surface of the linker makes only a few contacts with the DNA downstream of the cleavage site. In combination with the crystal structures of the reconstituted human topoisomerase I before and after DNA cleavage, this information suggests which amino acid residues are involved in catalyzing phosphodiester bond breakage and religation. The structures also lead to the proposal that the topoisomerization step occurs by a mechanism termed "controlled rotation."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stewart, L -- Redinbo, M R -- Qiu, X -- Hol, W G -- Champoux, J J -- CA65656/CA/NCI NIH HHS/ -- GM16713/GM/NIGMS NIH HHS/ -- GM49156/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 6;279(5356):1534-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biomolecular Structure Center and Department of Biological Structure, School of Medicine, University of Washington, Seattle, WA 98195-7742, USA. emerald_biostructures@rocketmail.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9488652" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/chemistry/metabolism ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; DNA/chemistry/*metabolism ; DNA Topoisomerases, Type I/*chemistry/*metabolism ; Humans ; Hydrogen Bonding ; *Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligodeoxyribonucleotides/chemistry/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Tyrosine/chemistry/metabolism
    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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    Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-16
    Description: Mutation of the VHL tumor suppressor is associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site. The structure extends the similarities to the SCF (Skp1-Cul1-F-box protein) complex that targets proteins for degradation, supporting the hypothesis that VHL may function in an analogous pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stebbins, C E -- Kaelin, W G Jr -- Pavletich, N P -- New York, N.Y. -- Science. 1999 Apr 16;284(5413):455-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Structural Biology, Joan and Sanford I. Weill Graduate School of Medical Sciences, Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10205047" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Cycle Proteins/chemistry/metabolism ; Cloning, Molecular ; Crystallography, X-Ray ; *Genes, Tumor Suppressor ; Humans ; Hydrogen Bonding ; *Ligases ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Mutation, Missense ; Neoplasms/genetics ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/*chemistry/genetics/metabolism ; S-Phase Kinase-Associated Proteins ; Surface Properties ; Transcription Factors/*chemistry/metabolism ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*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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  • 3
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    Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-24
    Description: The von Hippel-Lindau (VHL) tumor suppressor gene is mutated in most human kidney cancers. The VHL protein is part of a complex that includes Elongin B, Elongin C, and Cullin-2, proteins associated with transcriptional elongation and ubiquitination. Here it is shown that the endogenous VHL complex in rat liver also includes Rbx1, an evolutionarily conserved protein that contains a RING-H2 fingerlike motif and that interacts with Cullins. The yeast homolog of Rbx1 is a subunit and potent activator of the Cdc53-containing SCFCdc4 ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor Sic1 and for the G1 to S cell cycle transition. These findings provide a further link between VHL and the cellular ubiquitination machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamura, T -- Koepp, D M -- Conrad, M N -- Skowyra, D -- Moreland, R J -- Iliopoulos, O -- Lane, W S -- Kaelin, W G Jr -- Elledge, S J -- Conaway, R C -- Harper, J W -- Conaway, J W -- AG-11085/AG/NIA NIH HHS/ -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 23;284(5414):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10213691" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Line ; *Cullin Proteins ; Cyclin-Dependent Kinase Inhibitor Proteins ; *F-Box Proteins ; Fungal Proteins/metabolism ; *Ligases ; Liver ; Male ; Molecular Sequence Data ; Peptide Synthases/*metabolism ; Proteins/*metabolism ; Rats ; Rats, Sprague-Dawley ; Recombinant Fusion Proteins/metabolism ; S-Phase Kinase-Associated Proteins ; SKP Cullin F-Box Protein Ligases ; Saccharomyces cerevisiae/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transcription Factors/metabolism ; *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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  • 4
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    Mutation in the alpha-synuclein gene identified in families with Parkinson's disease (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: Parkinson's disease (PD) is a common neurodegenerative disorder with a lifetime incidence of approximately 2 percent. A pattern of familial aggregation has been documented for the disorder, and it was recently reported that a PD susceptibility gene in a large Italian kindred is located on the long arm of human chromosome 4. A mutation was identified in the alpha-synuclein gene, which codes for a presynaptic protein thought to be involved in neuronal plasticity, in the Italian kindred and in three unrelated families of Greek origin with autosomal dominant inheritance for the PD phenotype. This finding of a specific molecular alteration associated with PD will facilitate the detailed understanding of the pathophysiology of the disorder.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Polymeropoulos, M H -- Lavedan, C -- Leroy, E -- Ide, S E -- Dehejia, A -- Dutra, A -- Pike, B -- Root, H -- Rubenstein, J -- Boyer, R -- Stenroos, E S -- Chandrasekharappa, S -- Athanassiadou, A -- Papapetropoulos, T -- Johnson, W G -- Lazzarini, A M -- Duvoisin, R C -- Di Iorio, G -- Golbe, L I -- Nussbaum, R L -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2045-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetic Disease Research, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD 20892-1430, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197268" target="_blank"〉PubMed〈/a〉
    Keywords: Age of Onset ; Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Female ; Genes, Dominant ; Genetic Markers ; Greece ; Humans ; Italy ; Male ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics/physiology ; Parkinson Disease/*genetics ; Pedigree ; Phenotype ; *Point Mutation ; Polymerase Chain Reaction ; Protein Structure, Secondary ; Synucleins ; alpha-Synuclein
    Print ISSN: 0036-8075
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  • 5
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    A neuropeptide gene defined by the Drosophila memory mutant amnesiac (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Mutations in genes required for associative learning and memory in Drosophila exist, but isolation of the genes has been difficult because most are defined by a single, chemically induced allele. Here, a simplified genetic screen was used to identify candidate genes involved in learning and memory. Second site suppressors of the dunce (dnc) female sterility phenotype were isolated with the use of transposon mutagenesis. One suppressor mutation that was recovered mapped in the amnesiac (amn) gene. Cloning of the locus revealed that amn encodes a previously uncharacterized neuropeptide gene. Thus, with the cloning of amn, specific neuropeptides are implicated in the memory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feany, M B -- Quinn, W G -- New York, N.Y. -- Science. 1995 May 12;268(5212):869-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Codon ; DNA Transposable Elements ; DNA, Complementary/genetics ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; Female ; *Genes, Insect ; Growth Hormone-Releasing Hormone/chemistry/genetics ; Male ; Memory/*physiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Neuropeptides/chemistry/*genetics ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Sequence Homology, Amino Acid ; Suppression, Genetic
    Print ISSN: 0036-8075
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  • 6
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    Inhibitors of HIV nucleocapsid protein zinc fingers as candidates for the treatment of AIDS (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: Strategies for the treatment of human immunodeficiency virus-type 1 (HIV-1) infection must contend with the obstacle of drug resistance. HIV-1 nucleocapsid protein zinc fingers are prime antiviral targets because they are mutationally intolerant and are required both for acute infection and virion assembly. Nontoxic disulfide-substituted benzamides were identified that attack the zinc fingers, inactivate cell-free virions, inhibit acute and chronic infections, and exhibit broad antiretroviral activity. The compounds were highly synergistic with other antiviral agents, and resistant mutants have not been detected. Zinc finger-reactive compounds may offer an anti-HIV strategy that restricts drug-resistance development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, W G -- Supko, J G -- Malspeis, L -- Buckheit, R W Jr -- Clanton, D -- Bu, M -- Graham, L -- Schaeffer, C A -- Turpin, J A -- Domagala, J -- Gogliotti, R -- Bader, J P -- Halliday, S M -- Coren, L -- Sowder, R C 2nd -- Arthur, L O -- Henderson, L E -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Antiviral Drug Mechanisms, PRI/DynCorp., National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502043" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antiviral Agents/chemistry/pharmacokinetics/*pharmacology ; Benzamides/chemistry/pharmacokinetics/*pharmacology ; Biological Availability ; Capsid/chemistry/*metabolism ; *Capsid Proteins ; Cell Line ; Disulfides/chemistry/pharmacokinetics/*pharmacology ; Drug Resistance, Microbial ; Drug Synergism ; Gene Products, gag/*antagonists & inhibitors/chemistry ; HIV-1/*drug effects/physiology ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Viral Proteins ; Zinc Fingers/*drug effects ; gag Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
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  • 7
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    Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germ-line mutations of the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of human tumors, and somatic mutations of this gene have been identified in sporadic renal cell carcinomas and cerebellar hemangioblastomas. Two transcriptional elongation factors, Elongin B and C, were shown to bind in vitro and in vivo to a short, colinear region of the VHL protein (pVHL) that is frequently mutated in human tumors. A peptide replica of this region inhibited binding of pVHL to Elongin B and C whereas a point-mutant derivative, corresponding to a naturally occurring VHL missense mutation, had no effect. These results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kibel, A -- Iliopoulos, O -- DeCaprio, J A -- Kaelin, W G Jr -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1444-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660130" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carcinoma, Renal Cell ; *Genes, Tumor Suppressor ; Germ-Line Mutation ; Humans ; *Ligases ; Mice ; Molecular Sequence Data ; Nuclear Proteins/genetics/*metabolism ; Point Mutation ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/*metabolism ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/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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  • 8
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    Regulated subcellular distribution of the NR1 subunit of the NMDA receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: NMDA (N-methyl-D-aspartate) receptors are selectively localized at the postsynaptic membrane of excitatory synapses in the mammalian brain. The molecular mechanisms underlying this localization were investigated by expressing the NR1 subunit of the NMDA receptor in fibroblasts. NR1 splice variants containing the first COOH-terminal exon cassette (NR1A and NR1D) were located in discrete, receptor-rich domains associated with the plasma membrane. NR1 splice variants lacking this exon cassette (NR1C and NR1E) were distributed throughout the cell, with large amounts of NR1 protein present in the cell interior. Insertion of this exon cassette into the COOH-terminus of the GluR1 AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate) receptor was sufficient to cause GluR1 to be localized to discrete, receptor-rich domains. Furthermore, protein kinase C phosphorylation of specific serines within this exon disrupted the receptor-rich domains. These results demonstrate that amino acid sequences contained within the NR1 molecule serve to localize this receptor subunit to discrete membrane domains in a manner that is regulated by alternative splicing and protein phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehlers, M D -- Tingley, W G -- Huganir, R L -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1734-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569904" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Membrane/*metabolism ; Exons ; Fluorescent Antibody Technique ; Microscopy, Confocal ; Molecular Sequence Data ; Phosphorylation ; Protein Kinase C/metabolism ; Quail ; Receptors, AMPA/analysis ; Receptors, N-Methyl-D-Aspartate/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Serine/metabolism ; Subcellular Fractions/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
    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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  • 9
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    Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on both threonine-14 and tyrosine-15 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: Cdc2 is the cyclin-dependent kinase that controls entry of cells into mitosis. Phosphorylation of Cdc2 on threonine-14 and tyrosine-15 inhibits the activity of the enzyme and prevents premature initiation of mitosis. Although Wee1 has been identified as the kinase that phosphorylates tyrosine-15 in various organisms, the threonine-14-specific kinase has not been isolated. A complementary DNA was cloned from Xenopus that encodes Myt1, a member of the Wee1 family that was discovered to phosphorylate Cdc2 efficiently on both threonine-14 and tyrosine-15. Myt1 is a membrane-associated protein that contains a putative transmembrane segment. Immunodepletion studies suggested that Myt1 is the predominant threonine-14-specific kinase in Xenopus egg extracts. Myt1 activity is highly regulated during the cell cycle, suggesting that this relative of Wee1 plays a role in mitotic control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mueller, P R -- Coleman, T R -- Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):86-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569953" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/*metabolism ; *Cell Cycle Proteins ; Cell Membrane/enzymology ; Cloning, Molecular ; Cyclins/metabolism ; Interphase ; Mitosis ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Oocytes/enzymology ; Phosphorylation ; Phosphothreonine/metabolism ; Phosphotyrosine/metabolism ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins
    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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    Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Cdc2, the cyclin-dependent kinase that controls mitosis, is negatively regulated by phosphorylation on its threonine-14 and tyrosine-15 residues. Cdc25, the phosphatase that dephosphorylates both of these residues, undergoes activation and phosphorylation by multiple kinases at mitosis. Plx1, a kinase that associates with and phosphorylates the amino-terminal domain of Cdc25, was purified extensively from Xenopus egg extracts. Cloning of its complementary DNA revealed that Plx1 is related to the Polo family of protein kinases. Recombinant Plx1 phosphorylated Cdc25 and stimulated its activity in a purified system. Cdc25 phosphorylated by Plx1 reacted strongly with MPM-2, a monoclonal antibody to mitotic phosphoproteins. These studies indicate that Plx1 may participate in control of mitotic progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumagai, A -- Dunphy, W G -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1377-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, 216-76, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703070" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; Cloning, Molecular ; Cyclins/metabolism ; Enzyme Activation ; Molecular Sequence Data ; Mutation ; Oocytes/enzymology ; Peptide Mapping ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/analysis ; Phosphothreonine/analysis ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/metabolism ; Recombinant Proteins/metabolism ; Xenopus ; *Xenopus Proteins ; cdc25 Phosphatases
    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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