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  • 1
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    Efficient and accurate linear algebraic methods for large-scale electronic structure calculations with nonorthogonal atomic orbitals (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-04-07
    Description: Author(s): H. Teng, T. Fujiwara, T. Hoshi, T. Sogabe, S.-L. Zhang, and S. Yamamoto The need for large-scale electronic structure calculations arises recently in the field of material physics, and efficient and accurate algebraic methods for large simultaneous linear equations become greatly important. We investigate the generalized shifted conjugate orthogonal conjugate gradient m... [Phys. Rev. B 83, 165103] Published Wed Apr 06, 2011
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    In situ visualization of a glycoform of transferrin: localization of {alpha}2,6-sialylated transferrin in the liver (2015)
    Oxford University Press
    Details
    Publication Date: 2015-03-28
    Description: We previously found that a lectin, Sambucus sieboldiana agglutinin (SSA), bound to α2,6-sialylated glycan epitopes on transferrin and inhibited anti-transferrin antibody binding to the antigen in ELISA (SSA inhibition). Here we report that SSA inhibition is applicable to immunohistochemistry, localizing α2,6-sialylated transferrin in the liver. Immunohistochemistry using anti-transferrin polyclonal antibody revealed that transferrin was detected in hepatocytes near interlobular veins. Addition of SSA lectin markedly attenuated the staining. Sialidase treatment of a liver section abolished SSA binding and concomitantly cancelled SSA inhibition, suggesting that SSA binding to glycan epitopes on the section was essential for the inhibition. To examine the importance of proximity between antigen epitopes and SSA-binding (glycosylation) sites, we prepared two anti-peptide antibodies against partial amino acid sequences of transferrin. One antibody (Tf-596Ab) is against a peptide sequence, Cys596-Ala614, which is proximal to N -glycosylation sites (Asn-432 and Asn-630). The other (Tf-120Ab) is against a peptide sequence, Val120-Cys137, distal to the sites. The staining signals of Tf-596Ab were reduced by the addition of SSA, whereas those of Tf-120Ab were reduced only a little. This result suggests that proximity of the antigen epitope to SSA binding sites is critical for SSA inhibition in immunohistochemistry.
    Print ISSN: 0021-924X
    Electronic ISSN: 1756-2651
    Topics: Biology , Chemistry and Pharmacology
    Published by Oxford University Press on behalf of The Japanese Biochemical Society (JBS).
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  • 3
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    Operation of the GaSb p-channel metal-oxide-semiconductor field-effect transistors fabricated on (111)A surfaces (2014)
    American Institute of Physics (AIP)
    Details
    Publication Date: 2014-12-10
    Description: We demonstrate the operation of GaSb p-channel metal-oxide-semiconductor field-effect transistors (p-MOSFETs) on (111)A surfaces with Al 2 O 3 gate dielectrics formed by atomic-layer deposition at 150 °C. The p-MOSFETs on (111)A surfaces exhibit higher drain current and lower subthreshold swing than those on (100) surfaces. We find that the interface-state density ( D it ) values at the Al 2 O 3 /GaSb MOS interfaces on the (111)A surfaces are lower than those on the (100) surfaces, which can lead to performance enhancement of the GaSb p-MOSFETs on (111)A surfaces. The mobility of the GaSb p-MOSFETs on (111)A surfaces is 80% higher than that on (100) surfaces.
    Print ISSN: 0003-6951
    Electronic ISSN: 1077-3118
    Topics: Physics
    Published by American Institute of Physics (AIP)
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  • 4
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    A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2 (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-07-07
    Description: The existence of a large number of receptors coupled to heterotrimeric guanine nucleotide binding proteins (G proteins) raises the question of how a particular receptor selectively regulates specific targets. We provide insight into this question by identifying a prototypical macromolecular signaling complex. The beta(2) adrenergic receptor was found to be directly associated with one of its ultimate effectors, the class C L-type calcium channel Ca(v)1.2. This complex also contained a G protein, an adenylyl cyclase, cyclic adenosine monophosphate-dependent protein kinase, and the counterbalancing phosphatase PP2A. Our electrophysiological recordings from hippocampal neurons demonstrate highly localized signal transduction from the receptor to the channel. The assembly of this signaling complex provides a mechanism that ensures specific and rapid signaling by a G protein-coupled receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davare, M A -- Avdonin, V -- Hall, D D -- Peden, E M -- Burette, A -- Weinberg, R J -- Horne, M C -- Hoshi, T -- Hell, J W -- AG00213/AG/NIA NIH HHS/ -- AG17502/AG/NIA NIH HHS/ -- GM08688/GM/NIGMS NIH HHS/ -- GM56900/GM/NIGMS NIH HHS/ -- HL61645/HL/NHLBI NIH HHS/ -- NS35563/NS/NINDS NIH HHS/ -- NS39444/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 6;293(5527):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11441182" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Adrenergic beta-2 Receptor Agonists ; Albuterol/pharmacology ; Animals ; Calcium Channels, L-Type/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Electric Conductivity ; Fluorescent Antibody Technique ; Heterotrimeric GTP-Binding Proteins/metabolism ; Humans ; Isoproterenol/pharmacology ; Kinetics ; Macromolecular Substances ; Neurons/cytology/drug effects/enzymology/metabolism ; Phosphoprotein Phosphatases/metabolism ; Precipitin Tests ; Prosencephalon/cytology/metabolism ; Protein Binding ; Pyramidal Cells/cytology/drug effects/enzymology/metabolism ; Rats ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; *Signal Transduction ; Substrate Specificity
    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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  • 5
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    Biophysical and molecular mechanisms of Shaker potassium channel inactivation (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: The potassium channels encoded by the Drosophila Shaker gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in Shaker potassium channels expressed in Xenopus oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Zagotta, W N -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):533-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2122519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; DNA/genetics ; Drosophila melanogaster/*genetics ; Electric Conductivity ; Ion Channel Gating/drug effects/*physiology ; Kinetics ; Membrane Potentials/physiology ; Molecular Sequence Data ; Mutagenesis ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Potassium Channels/genetics/*physiology ; RNA Splicing ; Structure-Activity Relationship ; Trypsin/pharmacology ; Xenopus
    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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  • 6
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    Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-10-26
    Description: Site-directed mutagenesis experiments have suggested a model for the inactivation mechanism of Shaker potassium channels from Drosophila melanogaster. In this model, the first 20 amino acids form a cytoplasmic domain that interacts with the open channel to cause inactivation. The model was tested by the internal application of a synthetic peptide, with the sequence of the first 20 residues of the ShB alternatively spliced variant, to noninactivating mutant channels expressed in Xenopus oocytes. The peptide restored inactivation in a concentration-dependent manner. Like normal inactivation, peptide-induced inactivation was not noticeably voltage-dependent. Trypsin-treated peptide and peptides with sequences derived from the first 20 residues of noninactivating mutants did not restore inactivation. These results support the proposal that inactivation occurs by a cytoplasmic domain that occludes the ion-conducting pore of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zagotta, W N -- Hoshi, T -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Oct 26;250(4980):568-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2122520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Drosophila melanogaster/*genetics ; Electric Conductivity ; Hot Temperature ; Ion Channel Gating/drug effects/*physiology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Peptide Fragments/chemistry/*pharmacology ; Potassium Channels/chemistry/genetics/*physiology ; Structure-Activity Relationship ; Trypsin/pharmacology ; Xenopus
    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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  • 7
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    Cell biology. Oxygen sensing: it's a gas! (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, Toshinori -- Lahiri, Sukhamay -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2050-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. hoshi@hoshi.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604396" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbon Monoxide/*metabolism ; Carotid Body/*cytology/*physiology ; Cell Hypoxia ; Cell Membrane/physiology ; Cells, Cultured ; Heme/metabolism/pharmacology ; Heme Oxygenase (Decyclizing)/genetics/*metabolism ; Hemeproteins/metabolism ; Large-Conductance Calcium-Activated Potassium Channels ; Membrane Potentials ; Mitochondria/metabolism ; NADP/pharmacology ; NADPH Oxidase/metabolism ; Oxidation-Reduction ; Oxygen/*physiology ; Potassium Channels, Calcium-Activated ; Proteomics ; RNA, Small Interfering/pharmacology ; Signal Transduction
    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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  • 8
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    Effect of forskolin on voltage-gated K+ channels is independent of adenylate cyclase activation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Forskolin is commonly used to stimulate adenylate cyclase in the study of modulation of ion channels and other proteins by adenosine 3',5'-monophosphate (cAMP)-dependent second messenger systems. In addition to its action on adenylate cyclase, forskolin directly alters the gating of a single class of voltage-dependent potassium channels from a clonal pheochromocytoma (PC12) cell line. This alteration occurred in isolated cell-free patches independent of soluble cytoplasmic enzymes. The effect of forskolin was distinct from those of other agents that raise intracellular cAMP levels. The 1,9-dideoxy derivative of forskolin, which is unable to activate the cyclase, was also effective in altering the potassium channel activity. This direct action of forskolin can lead to misinterpretation of results in experiments in which forskolin is assumed to selectively activate adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Garber, S S -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454506" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adenylyl Cyclases/*metabolism ; Adrenal Gland Neoplasms/metabolism ; Colforsin/analogs & derivatives/*pharmacology ; Cyclic AMP/metabolism ; Electric Conductivity ; Enzyme Activation/drug effects ; Ion Channels/drug effects/*physiology ; Kinetics ; Pheochromocytoma/metabolism ; Potassium/*metabolism ; Theophylline/pharmacology ; Tumor Cells, Cultured
    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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  • 9
    Electronic Resource
    Electronic Resource
    Thin film growth of layered cobalt-oxide Bi2Sr3Co2O9+δ nearly isomorphic to Bi2Sr2CaCu2O8+δ superconductors (1994)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 76 (1994), S. 1317-1319 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Thin films of Bi2Sr3Co2O9+δ, which is nearly isomorphic to Bi2Sr2CaCu2O8+δ, are grown in situ by molecular beam epitaxy with pure ozone. For producing a molecular beam of Co by a Knudsen cell, we used MgO as a crucible material. The c-axis oriented films are successfully grown on Nd:YAlO3 (001) substrates, which are untwinned with their structural modulation along Nd:YAlO3[100]. With cooling the films from room temperature, it was found that they show a metallic behavior first (dρ/dT(approximately-greater-than)0), and then a semiconducting one at lower temperatures (dρ/dT〈0). One of the films, which shows the lowest resistivity, exhibits dρ/dT(approximately-greater-than)0 down to 86 K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.357793
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  • 10
    Electronic Resource
    Electronic Resource
    Relationship between the haemoglobin concentration of Daphnia magna and the ambient oxygen concentration
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part A: Physiology 72 (1982), S. 247-249 
    Details
    ISSN: 0300-9629
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0300-9629(82)90040-8
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