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  • 1
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    Asef, a link between the tumor suppressor APC and G-protein signaling (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-19
    Description: The adenomatous polyposis coli gene (APC) is mutated in familial adenomatous polyposis and in sporadic colorectal tumors. Here the APC gene product is shown to bind through its armadillo repeat domain to a Rac-specific guanine nucleotide exchange factor (GEF), termed Asef. Endogenous APC colocalized with Asef in mouse colon epithelial cells and neuronal cells. Furthermore, APC enhanced the GEF activity of Asef and stimulated Asef-mediated cell flattening, membrane ruffling, and lamellipodia formation in MDCK cells. These results suggest that the APC-Asef complex may regulate the actin cytoskeletal network, cell morphology and migration, and neuronal function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawasaki, Y -- Senda, T -- Ishidate, T -- Koyama, R -- Morishita, T -- Iwayama, Y -- Higuchi, O -- Akiyama, T -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Genetic Information, Institute for Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947987" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Brain/metabolism ; Cell Line ; Cell Membrane/ultrastructure ; Cell Size ; Colon/cytology/metabolism ; Cytoplasm/metabolism ; Cytoskeletal Proteins/*metabolism ; Guanine Nucleotide Exchange Factors/chemistry/genetics/*metabolism ; Guanosine Diphosphate/metabolism ; Humans ; Immunoblotting ; Intestinal Mucosa/cytology/metabolism ; Mice ; Molecular Sequence Data ; Neurons/metabolism ; Precipitin Tests ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/metabolism ; Rho Guanine Nucleotide Exchange Factors ; Signal Transduction ; *Trans-Activators ; Transfection ; Two-Hybrid System Techniques ; beta Catenin ; rac GTP-Binding Proteins/*metabolism
    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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  • 2
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    Control of doublesex alternative splicing by transformer and transformer-2 in Drosophila (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-10
    Description: Sex-specific alternative processing of doublesex (dsx) precursor messenger RNA (pre-mRNA) regulates somatic sexual differentiation in Drosophila melanogaster. Cotransfection analyses in which the dsx gene and the female-specific transformer (tra) and transformer-2 (tra-2) complementary DNAs were expressed in Drosophila Kc cells revealed that female-specific splicing of the dsx transcript was positively regulated by the products of the tra and tra-2 genes. Furthermore, analyses of mutant constructs of dsx showed that a portion of the female-specific exon sequence was required for regulation of dsx pre-messenger RNA splicing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshijima, K -- Inoue, K -- Higuchi, I -- Sakamoto, H -- Shimura, Y -- New York, N.Y. -- Science. 1991 May 10;252(5007):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Faculty of Science, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1902987" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; Drosophila melanogaster/*genetics ; Gene Expression Regulation ; Genes/physiology ; Genes, Regulator/physiology ; Molecular Sequence Data ; *RNA Splicing ; RNA, Messenger/biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sex Differentiation/*physiology ; 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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  • 3
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    Platelet coagulation factor XIa-inhibitor, a form of Alzheimer amyloid precursor protein (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-01
    Description: An inhibitor of coagulation factor XIa was purified from serum-free conditioned medium of HepG2 liver cells. Platelets stimulated with thrombin or calcium ionophore (A23187) secrete a protein functionally and immunologically identical to the inhibitor, implying a role for this inhibitor in hemostasis. Analysis of the amino-terminal amino acid sequence and immunologic reactivity showed the inhibitor to be a truncated form of the Alzheimer's amyloid precursor protein that contains a Kunitz-type serine protease inhibitor domain and at least a portion of the amyloid beta protein. It inhibits factor XIa and trypsin with a Ki of 450 +/- 50 pM and 20 +/- 10 pM, respectively. Heparin (1 unit/ml) did not significantly effect inhibition of trypsin, but inhibition of XIa was 15 times greater (Ki = 25 +/- 15 pM) in the presence of heparin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, R P -- Higuchi, D A -- Broze, G J Jr -- New York, N.Y. -- Science. 1990 Jun 1;248(4959):1126-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Jewish Hospital, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2111585" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amyloid/immunology ; Amyloid beta-Protein Precursor ; Blood Platelets/*analysis ; Blood Proteins/immunology/*isolation & purification/physiology ; Cross Reactions ; Factor XIa/*antagonists & inhibitors ; Humans ; Molecular Sequence Data ; Protein Precursors/immunology ; Serine Proteinase Inhibitors/blood/*isolation & purification
    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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    Heteromeric NMDA receptors: molecular and functional distinction of subtypes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monyer, H -- Sprengel, R -- Schoepfer, R -- Herb, A -- Higuchi, M -- Lomeli, H -- Burnashev, N -- Sakmann, B -- Seeburg, P H -- New York, N.Y. -- Science. 1992 May 22;256(5060):1217-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Glutamates/pharmacology ; Glutamic Acid ; Glycine/pharmacology ; Macromolecular Substances ; Magnesium/pharmacology ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Multigene Family ; N-Methylaspartate/pharmacology ; Oligonucleotide Probes ; Organ Specificity ; Peptides ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*genetics/*metabolism ; Recombinant Proteins/drug effects/metabolism ; Sequence Homology, Nucleic Acid ; 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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  • 5
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    Structural basis for the drug extrusion mechanism by a MATE multidrug transporter (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-03-29
    Description: Multidrug and toxic compound extrusion (MATE) family transporters are conserved in the three primary domains of life (Archaea, Bacteria and Eukarya), and export xenobiotics using an electrochemical gradient of H(+) or Na(+) across the membrane. MATE transporters confer multidrug resistance to bacterial pathogens and cancer cells, thus causing critical reductions in the therapeutic efficacies of antibiotics and anti-cancer drugs, respectively. Therefore, the development of MATE inhibitors has long been awaited in the field of clinical medicine. Here we present the crystal structures of the H(+)-driven MATE transporter from Pyrococcus furiosus in two distinct apo-form conformations, and in complexes with a derivative of the antibacterial drug norfloxacin and three in vitro selected thioether-macrocyclic peptides, at 2.1-3.0 A resolutions. The structures, combined with functional analyses, show that the protonation of Asp 41 on the amino (N)-terminal lobe induces the bending of TM1, which in turn collapses the N-lobe cavity, thereby extruding the substrate drug to the extracellular space. Moreover, the macrocyclic peptides bind the central cleft in distinct manners, which correlate with their inhibitory activities. The strongest inhibitory peptide that occupies the N-lobe cavity may pave the way towards the development of efficient inhibitors against MATE transporters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanaka, Yoshiki -- Hipolito, Christopher J -- Maturana, Andres D -- Ito, Koichi -- Kuroda, Teruo -- Higuchi, Takashi -- Katoh, Takayuki -- Kato, Hideaki E -- Hattori, Motoyuki -- Kumazaki, Kaoru -- Tsukazaki, Tomoya -- Ishitani, Ryuichiro -- Suga, Hiroaki -- Nureki, Osamu -- England -- Nature. 2013 Apr 11;496(7444):247-51. doi: 10.1038/nature12014. Epub 2013 Mar 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23535598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antiporters/*chemistry/*metabolism ; Apoproteins/chemistry/metabolism ; Archaeal Proteins/*chemistry/*metabolism ; Aspartic Acid/chemistry ; Crystallography, X-Ray ; DNA Mutational Analysis ; Macrocyclic Compounds/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Norfloxacin/chemistry/metabolism ; Peptides/chemistry/metabolism ; Protein Conformation ; Protons ; Pyrococcus furiosus/*chemistry ; Structure-Activity Relationship ; Sulfides/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Control of kinetic properties of AMPA receptor channels by nuclear RNA editing (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor channels mediate the fast component of excitatory postsynaptic currents in the central nervous system. Site-selective nuclear RNA editing controls the calcium permeability of these channels, and RNA editing at a second site is shown here to affect the kinetic aspects of these channels in rat brain. In three of the four AMPA receptor subunits (GluR-B, -C, and -D), intronic elements determine a codon switch (AGA, arginine, to GGA, glycine) in the primary transcripts in a position termed the R/G site, which immediately precedes the alternatively spliced modules "flip" and "flop." The extent of editing at this site progresses with brain development in a manner specific for subunit and splice form, and edited channels possess faster recovery rates from desensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lomeli, H -- Mosbacher, J -- Melcher, T -- Hoger, T -- Geiger, J R -- Kuner, T -- Monyer, H -- Higuchi, M -- Bach, A -- Seeburg, P H -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1709-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992055" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brain/embryology/*metabolism ; Cell Nucleus/metabolism ; Exons ; Glutamic Acid/pharmacology ; Glycine/genetics ; Introns ; Kinetics ; Membrane Potentials ; Molecular Sequence Data ; Oocytes ; PC12 Cells ; Patch-Clamp Techniques ; *RNA Editing ; Rats ; Rats, Wistar ; Receptors, AMPA/*genetics/*metabolism ; Recombinant Proteins/metabolism ; Xenopus
    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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    The muscle protein Dok-7 is essential for neuromuscular synaptogenesis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-24
    Description: The formation of the neuromuscular synapse requires muscle-specific receptor kinase (MuSK) to orchestrate postsynaptic differentiation, including the clustering of receptors for the neurotransmitter acetylcholine. Upon innervation, neural agrin activates MuSK to establish the postsynaptic apparatus, although agrin-independent formation of neuromuscular synapses can also occur experimentally in the absence of neurotransmission. Dok-7, a MuSK-interacting cytoplasmic protein, is essential for MuSK activation in cultured myotubes; in particular, the Dok-7 phosphotyrosine-binding domain and its target in MuSK are indispensable. Mice lacking Dok-7 formed neither acetylcholine receptor clusters nor neuromuscular synapses. Thus, Dok-7 is essential for neuromuscular synaptogenesis through its interaction with MuSK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Okada, Kumiko -- Inoue, Akane -- Okada, Momoko -- Murata, Yoji -- Kakuta, Shigeru -- Jigami, Takafumi -- Kubo, Sachiko -- Shiraishi, Hirokazu -- Eguchi, Katsumi -- Motomura, Masakatsu -- Akiyama, Tetsu -- Iwakura, Yoichiro -- Higuchi, Osamu -- Yamanashi, Yuji -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1802-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Regulation, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794080" target="_blank"〉PubMed〈/a〉
    Keywords: Agrin/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Differentiation ; Cell Line ; Down-Regulation ; Enzyme Activation ; Humans ; In Situ Hybridization ; Mice ; Molecular Sequence Data ; Motor Endplate/embryology/metabolism ; Muscle Denervation ; Muscle Fibers, Skeletal/cytology/metabolism ; Muscle Proteins/chemistry/genetics/*metabolism ; Muscle, Skeletal/embryology/*innervation/metabolism ; Mutation ; Neuromuscular Junction/*physiology ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Cholinergic/genetics/*metabolism ; Synapses/*physiology ; Synaptic Transmission
    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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