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  • Kinetics  (55)
  • American Association for the Advancement of Science (AAAS)  (55)
  • American Institute of Physics (AIP)
  • Cambridge University Press
  • National Academy of Sciences
  • Wiley
  • 1985-1989  (55)
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (55)
  • American Institute of Physics (AIP)
  • Cambridge University Press
  • National Academy of Sciences
  • Wiley
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  • 1
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    Matrix-driven translocation of cells and nonliving particles (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-17
    Description: Cells of metazoan organisms produce and react to complex macromolecular microenvironments known as extracellular matrices. Assembly in vitro of native, compositionally nonuniform collagen-fibronectin matrices caused translocation of certain types of cells or polystyrene-latex beads from regions lacking fibronectin into regions containing it. The translocation process was not due to diffusion, convection, or electrostatic distribution effects, but may depend on nonequilibrium phenomena at the interface of contiguous collagen matrices formed in the presence and absence of fibronectin or particles. Extracellular matrix formation alone was sufficient to drive translocation by a biophysical process that may play a role in cellular migration during embryogenesis, as well as in other types of tissue reorganization such as inflammation, wound healing, and tumor invasion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Newman, S A -- Frenz, D A -- Tomasek, J J -- Rabuzzi, D D -- HD18148/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1985 May 17;228(4701):885-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4001925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cartilage/cytology/embryology ; *Cell Movement/drug effects ; Chick Embryo ; Collagen/*pharmacology ; Diffusion ; Extracellular Matrix/*physiology ; Fibroblasts/cytology ; Fibronectins/*pharmacology ; Humans ; In Vitro Techniques ; Kinetics ; Microspheres ; Movement
    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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    Potassium channels in cardiac cells activated by arachidonic acid and phospholipids (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-09
    Description: Two types of potassium-selective channels activated by intracellular arachidonic acid or phosphatidylcholine have been found in neonatal rat atrial cells. In inside-out patches, arachidonic acid and phosphatidylcholine each opened outwardly rectifying potassium-selective channels with conductances of 160 picosiemens (IK.AA) and 68 picosiemens (IK.PC), respectively. These potassium channels were not sensitive to internally applied adenosine triphosphate (ATP), magnesium, or calcium. Lowering the intracellular pH from 7.2 to 6.8 or 6.4 reversibly increased IK.AA channel activity three- or tenfold, respectively. A number of fatty acid derivatives were tested for their ability to activate IK.AA. These potassium-selective channels may help explain the increase in potassium conductance observed in ischemic cells and raise the possibility that fatty acid derivatives act as second messengers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, D -- Clapham, D E -- HL 34873/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1174-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mayo Foundation, Rochester, MN 55905.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727703" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Arachidonic Acids/*pharmacology ; Atrial Function ; Heart/*physiology ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Kinetics ; Membrane Potentials ; Phosphatidylcholines/*pharmacology ; Potassium Channels/drug effects/*physiology ; Rats
    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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  • 3
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    Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-09
    Description: Vasoactive intestinal peptide (VIP) labeled with 125I, [Tyr10-125I]VIP, can be hydrolyzed by immunoglobulin G (IgG) purified from a human subject, as judged by trichloroacetic acid precipitation and reversed-phase high-performance liquid chromatography (HPLC). The hydrolytic activity was precipitated by antibody to human IgG, it was bound by immobilized protein G and showed a molecular mass close to 150 kilodaltons by gel filtration chromatography, properties similar to those of authentic IgG. The Fab fragment, prepared from IgG by papain treatment, retained the VIP hydrolytic activity of the IgG. Peptide fragments produced by treatment of VIP with the antibody fraction were purified by reversed-phase HPLC and identified by fast atom bombardment-mass spectrometry and peptide sequencing. The scissile bond in VIP deduced from these experiments was Gln16-Met17. The antibody concentration (73.4 fmol per milligram of IgG) and the Kd (0.4 nM) were computed from analysis of VIP binding under conditions that did not result in peptide hydrolysis. Analysis of the antibody-mediated VIP hydrolysis at varying concentrations of substrate suggested conformity with Michaelis-Menton kinetics (Km). The values for Km (37.9 X 10(-9) M) and the turnover number kcat (15.6 min-1) suggested relatively tight VIP binding and a moderate catalytic efficiency of the antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S -- Volle, D J -- Beach, C M -- Johnson, D R -- Powell, M J -- Massey, R J -- HL 35506/HL/NHLBI NIH HHS/ -- HL 40348/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1158-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Nebraska Medical Center, Omaha 68105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727702" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Autoantibodies ; Catalysis ; Chromatography, High Pressure Liquid ; Humans ; Hydrolysis ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Kinetics ; Molecular Sequence Data ; Peptide Fragments/isolation & purification ; Vasoactive Intestinal Peptide/*immunology
    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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  • 4
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    Induction of an antibody that catalyzes the hydrolysis of an amide bond (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Catalysis of amide bond hydrolysis is of singular importance in enzymology. An antibody was induced to an analog of a high-energy intermediate anticipated along the reaction coordinate of amide hydrolysis. This antibody is an amidase with high specificity and a large rate enhancement (250,000) relative to the uncatalyzed reaction. This reaction represents the kinetically most difficult hydrolysis reaction yet catalyzed by an antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Schloeder, D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1188-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413482" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/metabolism ; Animals ; Antibodies, Monoclonal/biosynthesis/*physiology ; Antibody Specificity ; Antigens/immunology ; *Catalysis ; Chemical Phenomena ; Chemistry ; Hemocyanin/analogs & derivatives/immunology ; Hydrolysis ; Immunization ; Kinetics ; Mice ; Organophosphorus Compounds/immunology ; Substrate Specificity
    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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  • 5
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    Genetic reconstitution of functional acetylcholine receptor channels in mouse fibroblasts (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-18
    Description: Foreign genes can be stably integrated into the genome of a cell by means of DNA-mediated gene transfer techniques, and large quantities of homogenous cells that continuously express these gene products can then be isolated. Such an expression system can be used to study the functional consequences of introducing specific mutations into genes and to study the expressed protein in the absence of cellular components with which it is normally in contact. All four Torpedo acetylcholine receptor (AChR) subunit complementary DNA's were introduced into the genome of a mouse fibroblast cell by DNA-mediated gene transfer. A clonal cell line that stably produced high concentrations of correctly assembled cell surface AChR's and formed proper ligand-gated ion channels was isolated. With this new expression system, recombinant DNA, biochemical, pharmacological, and electrophysiological techniques were combined to study Torpedo AChR's in a single intact system. The physiological and pharmacological profiles of Torpedo AChR's expressed in mouse fibroblast cells differ in some details from those described earlier, and may provide a more accurate reflection of the properties of this receptor in its natural environment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Claudio, T -- Green, W N -- Hartman, D S -- Hayden, D -- Paulson, H L -- Sigworth, F J -- Sine, S M -- Swedlund, A -- NS 07102/NS/NINDS NIH HHS/ -- NS 21501/NS/NINDS NIH HHS/ -- NS 21714/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1688-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3686008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/physiology ; Fibroblasts/metabolism ; *Genes ; Kinetics ; Mice ; Receptors, Cholinergic/*genetics/metabolism ; Torpedo ; *Transfection
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  • 6
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    Efflux of chloroquine from Plasmodium falciparum: mechanism of chloroquine resistance (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-27
    Description: Chloroquine-resistant Plasmodium falciparum accumulate significantly less chloroquine than susceptible parasites, and this is thought to be the basis of their resistance. However, the reason for the lower accumulation of chloroquine was unknown. The resistant parasite has now been found to release chloroquine 40 to 50 times more rapidly than the susceptible parasite, although their initial rates of chloroquine accumulation are the same. Verapamil and two other calcium channel blockers, as well as vinblastine and daunomycin, each slowed the release and increased the accumulation of chloroquine by resistant (but not susceptible) Plasmodium falciparum. These results suggest that a higher rate of chloroquine release explains the lower chloroquine accumulation, and thus the resistance observed in resistant Plasmodium falciparum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krogstad, D J -- Gluzman, I Y -- Kyle, D E -- Oduola, A M -- Martin, S K -- Milhous, W K -- Schlesinger, P H -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1283-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317830" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Calcium Channel Blockers/pharmacology ; Chloroquine/*metabolism/pharmacology ; Daunorubicin/pharmacology ; Drug Resistance ; Kinetics ; Plasmodium falciparum/drug effects/genetics/*metabolism ; Vinblastine/pharmacology
    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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  • 7
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    Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-22
    Description: The three-dimensional structure of most enzymes is unknown; however, many enzymes may have structural motifs similar to those in the known structures of functionally related enzymes. Evidence is presented that an enzyme of unknown structure [Ile-transfer RNA (tRNA) synthetase] may share a functionally important structural motif with an enzyme of related function (Tyr-tRNA synthetase). This approach involves (i) identifying segments of Ile-tRNA synthetase that have been unusually conserved during evolution, (ii) predicting the function of one such segment by assuming a structural relation between Ile-tRNA synthetase and Tyr-tRNA synthetase, and (iii) testing the predicted function by mutagenesis and subsequent biochemical analysis. Random mutations were introduced by cassette mutagenesis into a ten-amino-acid segment of Ile-tRNA synthetase that was predicted to be involved in the formation of the binding site for isoleucine. Few amino acid substitutions appear to be tolerated in this region. However, one substitution (independently isolated twice) increased the Michaelis constant Km for isoleucine in the adenylate synthesis reaction by greater than 6000-fold, but had little effect on the Km for adenosine triphosphate, the apparent Km for tRNA, or the rate constant kcat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, N D -- Lien, D C -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):521-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3282306" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acyl-tRNA Synthetases ; Binding Sites ; DNA Mutational Analysis ; Escherichia coli/enzymology ; *Isoleucine-tRNA Ligase ; Kinetics ; Protein Conformation ; Saccharomyces cerevisiae/enzymology ; Structure-Activity Relationship
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  • 8
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    Positron emission tomography reveals elevated D2 dopamine receptors in drug-naive schizophrenics (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: In postmortem studies of patients with schizophrenia, D2 dopamine receptors in the basal ganglia have been observed to be more numerous than in patients with no history of neurological or psychiatric disease. Because most patients with schizophrenia are treated with neuroleptic drugs that block D2 dopamine receptors in the caudate nucleus, it has been suggested that this increase in the number of receptors is a result of adaptation to these drugs rather than a biochemical abnormality intrinsic to schizophrenia. With positron emission tomography (PET), the D2 dopamine receptor density in the caudate nucleus of living human beings was measured in normal volunteers and in two groups of patients with schizophrenia--one group that had never been treated with neuroleptics and another group that had been treated with these drugs. D2 dopamine receptor densities in the caudate nucleus were higher in both groups of patients than in the normal volunteers. Thus, schizophrenia itself is associated with an increase in brain D2 dopamine receptor density.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, D F -- Wagner, H N Jr -- Tune, L E -- Dannals, R F -- Pearlson, G D -- Links, J M -- Tamminga, C A -- Broussolle, E P -- Ravert, H T -- Wilson, A A -- Toung, J K -- Malat, J -- Williams, J A -- O'Tuama, L A -- Snyder, S H -- Kuhar, M J -- Gjedde, A -- 1RO1 53146/PHS HHS/ -- NS15080/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1558-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2878495" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antipsychotic Agents/*therapeutic use ; Caudate Nucleus/*metabolism ; Haloperidol/therapeutic use ; Humans ; Kinetics ; Receptors, Dopamine/*metabolism ; Receptors, Dopamine D2 ; Schizophrenia/drug therapy/*metabolism ; Spiperone/analogs & derivatives/metabolism ; Tomography, Emission-Computed
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  • 9
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    Actin polymerization and ATP hydrolysis (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-30
    Description: F-actin is the major component of muscle thin filaments and, more generally, of the microfilaments of the dynamic, multifunctional cytoskeletal systems of nonmuscle eukaryotic cells. Polymeric F-actin is formed by reversible noncovalent self-association of monomeric G-actin. To understand the dynamics of microfilament systems in cells, the dynamics of polymerization of pure actin must be understood. The following model has emerged from recent work. During the polymerization process, adenosine 5'-triphosphate (ATP) that is bound to G-actin is hydrolyzed to adenosine 5'-diphosphate (ADP) that is bound to F-actin. The hydrolysis reaction occurs on the F-actin subsequent to the polymerization reaction in two steps: cleavage of ATP followed by the slower release of inorganic phosphate (Pi). As a result, at high rates of filament growth a transient cap of ATP-actin subunits exists at the ends of elongating filaments, and at steady state a stabilizing cap of ADP.Pi-actin subunits exists at the barbed ends of filaments. Cleavage of ATP results in a highly stable filament with bound ADP.Pi, and release of Pi destabilizes the filament. Thus these two steps of the hydrolytic reaction provide potential mechanisms for regulating the monomer-polymer transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korn, E D -- Carlier, M F -- Pantaloni, D -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):638-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672117" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actins/*physiology ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Animals ; Cytoskeleton/*physiology ; Humans ; Hydrolysis ; Kinetics ; Polymers ; Protein Binding
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  • 10
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    Two classes of PDGF receptor recognize different isoforms of PDGF (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: Previous studies involving platelet-derived growth factor (PDGF) have been based on the premise that a single cell-surface receptor binds all three isoforms of PDGF (AA, BB, and AB). It is now shown that two populations of PDGF receptor exist and can be distinguished by their ligand binding specificity. The B receptor binds only the BB dimer, whereas the A/B receptor binds AA, BB, and AB dimers. Human dermal fibroblasts appear to express seven times as much B receptor as A/B receptor. The B receptor is responsible for most PDGF receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hart, C E -- Forstrom, J W -- Kelly, J D -- Seifert, R A -- Smith, R A -- Ross, R -- Murray, M J -- Bowen-Pope, D F -- DE07063-11/DE/NIDCR NIH HHS/ -- GM35501/GM/NIGMS NIH HHS/ -- HL18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1529-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836952" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Cell Membrane/metabolism ; Cells, Cultured ; Fibroblasts/metabolism ; Humans ; Kinetics ; Platelet-Derived Growth Factor/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Skin/*metabolism ; Structure-Activity Relationship
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