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  • 1
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    Long-range two-dimensional superstructure in the superconducting electron-doped cuprate Pr_{0.88} LaCe_{0.12} CuO_{4} (2015)
    American Physical Society (APS)
    Details
    Publication Date: 2015-07-30
    Description: Author(s): B. J. Campbell, S. Rosenkranz, H. J. Kang, H. T. Stokes, P. J. Chupas, S. Komiya, Y. Ando, Shiliang Li, and Pengcheng Dai Utilizing single-crystal synchrotron x-ray scattering, we observe distorted CuO 2 planes in the electron-doped superconductor Pr 1 − x LaCe x CuO 4 + δ ,   x = 0.12. Resolution-limited rods of scattering are indicative of a long-range two-dimensional 2 2 × 2 2 superstructure in the a − b plane, adhering to planar spac… [Phys. Rev. B 92, 014118] Published Wed Jul 29, 2015
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    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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    Magnetic Field Splitting of the Spin Resonance in CeCoIn_{5} (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-10-18
    Description: Author(s): C. Stock, C. Broholm, Y. Zhao, F. Demmel, H. J. Kang, K. C. Rule, and C. Petrovic Neutron scattering in strong magnetic fields is used to show the spin resonance in superconducting CeCoIn 5 ( T c =2.3  K) is a doublet. The underdamped resonance ( ℏ Γ =0.069±0.019  meV) Zeeman splits into two modes at E ± = ℏ Ω 0 ± α μ B μ 0 H with α =0.96±0.05. A linear extrapolation of the lower peak reaches zero e... [Phys. Rev. Lett. 109, 167207] Published Wed Oct 17, 2012
    Keywords: Condensed Matter: Electronic Properties, etc.
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Stripe order in superconducting La_{2-x} Ba_{x} CuO_{4} (0.095⩽x⩽0.155) (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-03-18
    Description: Author(s): M. Hücker, M. v. Zimmermann, G. D. Gu, Z. J. Xu, J. S. Wen, Guangyong Xu, H. J. Kang, A. Zheludev, and J. M. Tranquada The correlations between stripe order, superconductivity, and crystal structure in La_{2-x} Ba_{x} CuO_{4} single crystals have been studied by means of x-ray and neutron diffraction as well as static magnetization measurements. The derived phase diagram shows that charge stripe order (CO) coexists ... [Phys. Rev. B 83, 104506] Published Thu Mar 17, 2011
    Keywords: Superfluidity and superconductivity
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 4
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    Structural basis of abscisic acid signalling (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-10-27
    Description: The phytohormone abscisic acid (ABA) mediates the adaptation of plants to environmental stresses such as drought and regulates developmental signals such as seed maturation. Within plants, the PYR/PYL/RCAR family of START proteins receives ABA to inhibit the phosphatase activity of the group-A protein phosphatases 2C (PP2Cs), which are major negative regulators in ABA signalling. Here we present the crystal structures of the ABA receptor PYL1 bound with (+)-ABA, and the complex formed by the further binding of (+)-ABA-bound PYL1 with the PP2C protein ABI1. PYL1 binds (+)-ABA using the START-protein-specific ligand-binding site, thereby forming a hydrophobic pocket on the surface of the closed lid. (+)-ABA-bound PYL1 tightly interacts with a PP2C domain of ABI1 by using the hydrophobic pocket to cover the active site of ABI1 like a plug. Our results reveal the structural basis of the mechanism of (+)-ABA-dependent inhibition of ABI1 by PYL1 in ABA signalling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyazono, Ken-Ichi -- Miyakawa, Takuya -- Sawano, Yoriko -- Kubota, Keiko -- Kang, Hee-Jin -- Asano, Atsuko -- Miyauchi, Yumiko -- Takahashi, Mihoko -- Zhi, Yuehua -- Fujita, Yasunari -- Yoshida, Takuya -- Kodaira, Ken-Suke -- Yamaguchi-Shinozaki, Kazuko -- Tanokura, Masaru -- England -- Nature. 2009 Dec 3;462(7273):609-14. doi: 10.1038/nature08583.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19855379" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/*physiology ; Arabidopsis/*physiology ; Arabidopsis Proteins/*chemistry/*metabolism ; Binding Sites ; *Models, Molecular ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; *Signal Transduction
    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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  • 5
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    Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-12-08
    Description: Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-beta domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Hae Joo -- Coulibaly, Fasseli -- Clow, Fiona -- Proft, Thomas -- Baker, Edward N -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1625-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland 1010, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063798" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Asparagine/chemistry ; Chemistry, Physical ; Crystallography, X-Ray ; Fimbriae Proteins/*chemistry ; Fimbriae, Bacterial/*chemistry/ultrastructure ; Hydrogen Bonding ; Lysine/chemistry ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Streptococcus pyogenes/*chemistry/metabolism/*ultrastructure
    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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    Spatio-temporal transcriptome of the human brain (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-10-28
    Description: Brain development and function depend on the precise regulation of gene expression. However, our understanding of the complexity and dynamics of the transcriptome of the human brain is incomplete. Here we report the generation and analysis of exon-level transcriptome and associated genotyping data, representing males and females of different ethnicities, from multiple brain regions and neocortical areas of developing and adult post-mortem human brains. We found that 86 per cent of the genes analysed were expressed, and that 90 per cent of these were differentially regulated at the whole-transcript or exon level across brain regions and/or time. The majority of these spatio-temporal differences were detected before birth, with subsequent increases in the similarity among regional transcriptomes. The transcriptome is organized into distinct co-expression networks, and shows sex-biased gene expression and exon usage. We also profiled trajectories of genes associated with neurobiological categories and diseases, and identified associations between single nucleotide polymorphisms and gene expression. This study provides a comprehensive data set on the human brain transcriptome and insights into the transcriptional foundations of human neurodevelopment.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3566780/" 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/PMC3566780/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Hyo Jung -- Kawasawa, Yuka Imamura -- Cheng, Feng -- Zhu, Ying -- Xu, Xuming -- Li, Mingfeng -- Sousa, Andre M M -- Pletikos, Mihovil -- Meyer, Kyle A -- Sedmak, Goran -- Guennel, Tobias -- Shin, Yurae -- Johnson, Matthew B -- Krsnik, Zeljka -- Mayer, Simone -- Fertuzinhos, Sofia -- Umlauf, Sheila -- Lisgo, Steven N -- Vortmeyer, Alexander -- Weinberger, Daniel R -- Mane, Shrikant -- Hyde, Thomas M -- Huttner, Anita -- Reimers, Mark -- Kleinman, Joel E -- Sestan, Nenad -- DA026119/DA/NIDA NIH HHS/ -- G0700089/Medical Research Council/United Kingdom -- G9900837/Medical Research Council/United Kingdom -- GR082557/Wellcome Trust/United Kingdom -- HD000836/HD/NICHD NIH HHS/ -- MH081896/MH/NIMH NIH HHS/ -- MH089929/MH/NIMH NIH HHS/ -- NS054273/NS/NINDS NIH HHS/ -- R01 NS054273/NS/NINDS NIH HHS/ -- R01 NS054273-07/NS/NINDS NIH HHS/ -- RC2 MH089929/MH/NIMH NIH HHS/ -- RC2 MH089929-02/MH/NIMH NIH HHS/ -- U01 MH081896/MH/NIMH NIH HHS/ -- U01 MH081896-03/MH/NIMH NIH HHS/ -- England -- Nature. 2011 Oct 26;478(7370):483-9. doi: 10.1038/nature10523.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, Connecticut 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22031440" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Aged, 80 and over ; Aging/*genetics ; Brain/embryology/*growth & development/*metabolism ; Child ; Child, Preschool ; Exons/genetics ; Female ; Fetus/metabolism ; *Gene Expression Profiling ; Gene Expression Regulation, Developmental/*genetics ; Gene Regulatory Networks/genetics ; Humans ; Infant ; Male ; Middle Aged ; Quality Control ; Quantitative Trait Loci/genetics ; Sex Characteristics ; Time Factors ; Transcriptome/*genetics ; Young Adult
    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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  • 7
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    A two-domain elevator mechanism for sodium/proton antiport (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-09-03
    Description: Sodium/proton (Na(+)/H(+)) antiporters, located at the plasma membrane in every cell, are vital for cell homeostasis. In humans, their dysfunction has been linked to diseases, such as hypertension, heart failure and epilepsy, and they are well-established drug targets. The best understood model system for Na(+)/H(+) antiport is NhaA from Escherichia coli, for which both electron microscopy and crystal structures are available. NhaA is made up of two distinct domains: a core domain and a dimerization domain. In the NhaA crystal structure a cavity is located between the two domains, providing access to the ion-binding site from the inward-facing surface of the protein. Like many Na(+)/H(+) antiporters, the activity of NhaA is regulated by pH, only becoming active above pH 6.5, at which point a conformational change is thought to occur. The only reported NhaA crystal structure so far is of the low pH inactivated form. Here we describe the active-state structure of a Na(+)/H(+) antiporter, NapA from Thermus thermophilus, at 3 A resolution, solved from crystals grown at pH 7.8. In the NapA structure, the core and dimerization domains are in different positions to those seen in NhaA, and a negatively charged cavity has now opened to the outside. The extracellular cavity allows access to a strictly conserved aspartate residue thought to coordinate ion binding directly, a role supported here by molecular dynamics simulations. To alternate access to this ion-binding site, however, requires a surprisingly large rotation of the core domain, some 20 degrees against the dimerization interface. We conclude that despite their fast transport rates of up to 1,500 ions per second, Na(+)/H(+) antiporters operate by a two-domain rocking bundle model, revealing themes relevant to secondary-active transporters in general.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3914025/" 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/PMC3914025/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Chiara -- Kang, Hae Joo -- von Ballmoos, Christoph -- Newstead, Simon -- Uzdavinys, Povilas -- Dotson, David L -- Iwata, So -- Beckstein, Oliver -- Cameron, Alexander D -- Drew, David -- 062164/Z/00/Z/Wellcome Trust/United Kingdom -- 099165/Wellcome Trust/United Kingdom -- BB/G02325/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/G023425/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0900399/Medical Research Council/United Kingdom -- G0900990/Medical Research Council/United Kingdom -- England -- Nature. 2013 Sep 26;501(7468):573-7. doi: 10.1038/nature12484. Epub 2013 Sep 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23995679" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Escherichia coli Proteins/chemistry ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Dynamics Simulation ; Protein Multimerization ; Protein Structure, Tertiary ; Protons ; Sodium/metabolism ; Sodium-Hydrogen Antiporter/*chemistry/genetics/metabolism ; Static Electricity ; Thermus thermophilus/*chemistry/genetics
    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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  • 8
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    Neural stem cell specific fluorescent probe [Cell Biology] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-06-27
    Description: Fluorescent small molecules have become indispensable tools for biomedical research along with the rapidly developing optical imaging technology. We report here a neural stem cell specific boron-dipyrromethane (BODIPY) derivative compound of designation red 3 (CDr3), developed through a high throughput/content screening of in-house generated diversity oriented fluorescence library in stem cells at different developmental stages. This novel compound specifically detects living neural stem cells of both human and mouse origin. Furthermore, we identified its binding target by proteomic analysis as fatty acid binding protein 7 (FABP7), also known as brain lipid binding protein) which is highly expressed in neural stem cells and localized in the cytoplasm. CDr3 will be a valuable chemical tool in the study and applications of neural stem cells.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    BRCA1 negatively regulates IGF-1 expression through an estrogen-responsive element-like site (2012)
    Springer Nature
    Details
    Publication Date: 2012-06-29
    Description: BRCA1 negatively regulates IGF-1 expression through an estrogen-responsive element-like site Cell Death and Disease 3, e336 (June 2012). doi:10.1038/cddis.2012.78 Authors: H J Kang, Y W Yi, H J Kim, Y B Hong, Y S Seong & I Bae
    Keywords: BRCA1IGF-1negative regulationERαpositive-feedback activation
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 10
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    From Incommensurate Correlations to Mesoscopic Spin Resonance in YbRh_{2}Si_{2} (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-09-18
    Description: Author(s): C. Stock, C. Broholm, F. Demmel, J. Van Duijn, J. W. Taylor, H. J. Kang, R. Hu, and C. Petrovic Spin fluctuations are reported near the magnetic field—driven quantum critical point in YbRh 2 Si 2 . On cooling, ferromagnetic fluctuations evolve into incommensurate correlations located at q 0 =± ( δ , δ ) , with δ =0.14±0.04  r.l.u. At low temperatures, an in-plane magnetic field induces a sharp intradoublet... [Phys. Rev. Lett. 109, 127201] Published Mon Sep 17, 2012
    Keywords: Condensed Matter: Electronic Properties, etc.
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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