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  • Animals  (18)
  • ASTROPHYSICS  (9)
  • Aerospace Medicine  (8)
  • Nuclear Structure  (6)
  • 2010-2014  (20)
  • 2000-2004  (11)
  • 1980-1984  (10)
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  • 1
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    Surveying the N=40 island of inversion with new manganese masses (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-07-21
    Description: Author(s): S. Naimi, G. Audi, D. Beck, K. Blaum, Ch. Böhm, Ch. Borgmann, M. Breitenfeldt, S. George, F. Herfurth, A. Herlert, A. Kellerbauer, M. Kowalska, D. Lunney, E. Minaya Ramirez, D. Neidherr, M. Rosenbusch, L. Schweikhard, R. N. Wolf, and K. Zuber High-precision mass measurements of neutron-rich 57−66 Mn and 61−63 Fe isotopes are reported. The new mass surface shows no shell closure at N =40 . In contrast, there is an increase of the two-neutron separation energy at N =38 . This behavior is consistent with the onset of collectivity due to the occup... [Phys. Rev. C 86, 014325] Published Fri Jul 20, 2012
    Keywords: Nuclear Structure
    Print ISSN: 0556-2813
    Electronic ISSN: 1089-490X
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    ^{12}C(^{16}O,γ)^{28}Si radiative capture: Structural and statistical aspects of the γ decay (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-03-29
    Description: Author(s): D. Lebhertz, S. Courtin, F. Haas, D. G. Jenkins, C. Simenel, M.-D. Salsac, D. A. Hutcheon, C. Beck, J. Cseh, J. Darai, C. Davis, R. G. Glover, A. Goasduff, P. E. Kent, G. Levai, P. L. Marley, A. Michalon, J. E. Pearson, M. Rousseau, N. Rowley, and C. Ruiz The heavy-ion radiative capture reaction 12 C( 16 O, γ ) 28 Si has been studied at three energies E c.m. =8.5 , 8.8, and 9 MeV which are close to the Coulomb barrier. The weak radiative capture process has been identified by measuring the 28 Si recoils in the highly selective 0 ∘ spectrometer DRAGON at TRIUMF (... [Phys. Rev. C 85, 034333] Published Wed Mar 28, 2012
    Keywords: Nuclear Structure
    Print ISSN: 0556-2813
    Electronic ISSN: 1089-490X
    Topics: Physics
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  • 3
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    Evolution of nuclear ground-state properties of neutron-deficient isotopes around Z=82 from precision mass measurements (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-10-08
    Description: Author(s): Ch. Böhm, Ch. Borgmann, G. Audi, D. Beck, K. Blaum, M. Breitenfeldt, R. B. Cakirli, T. E. Cocolios, S. Eliseev, S. George, F. Herfurth, A. Herlert, M. Kowalska, S. Kreim, D. Lunney, V. Manea, E. Minaya Ramirez, S. Naimi, D. Neidherr, M. Rosenbusch, L. Schweikhard, J. Stanja, M. Wang, R. N. Wolf, and K. Zuber High-precision mass measurements of neutron-deficient Tl (A=184, 186, 190, 193–195, 198) isotopes as well as Pb (A=202,208), Fr (A=207,208), and Ra (A=224) are performed with the Penning-trap mass spectrometer ISOLTRAP at ISOLDE/CERN. The improved precision of the mass data now allows the study of s... [Phys. Rev. C 90, 044307] Published Tue Oct 07, 2014
    Keywords: Nuclear Structure
    Print ISSN: 0556-2813
    Electronic ISSN: 1089-490X
    Topics: Physics
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  • 4
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    Competition between pairing correlations and deformation from the odd-even mass staggering of francium and radium isotopes (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-08-05
    Description: Author(s): S. Kreim, D. Beck, K. Blaum, Ch. Borgmann, M. Breitenfeldt, T. E. Cocolios, A. Gottberg, F. Herfurth, M. Kowalska, Yu. A. Litvinov, D. Lunney, V. Manea, T. M. Mendonca, S. Naimi, D. Neidherr, M. Rosenbusch, L. Schweikhard, Th. Stora, F. Wienholtz, R. N. Wolf, and K. Zuber The masses of Fr222,224,226–233 and Ra233,234 have been determined with the Penning-trap mass spectrometer ISOLTRAP at the ISOLDE facility at CERN, including the previously unknown mass and half-life of Fr233. We study the evolution of the odd-even staggering of binding energies along the francium a... [Phys. Rev. C 90, 024301] Published Mon Aug 04, 2014
    Keywords: Nuclear Structure
    Print ISSN: 0556-2813
    Electronic ISSN: 1089-490X
    Topics: Physics
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  • 5
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    Sex-biased hatching order and adaptive population divergence in a passerine bird (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: Most species of birds can lay only one egg per day until a clutch is complete, and the order in which eggs are laid often has strong and sex-specific effects on offspring growth and survival. In two recently established populations of the house finch (Carpodacus mexicanus) in Montana and Alabama, breeding females simultaneously adjusted the sex and growth of offspring in relation to their position in the laying order, thereby reducing the mortality of sons and daughters by 10 to 20% in both environments. We show experimentally that the reduction in mortality is produced by persistent and sex-specific maternal effects on the growth and morphology of offspring. These strong parental effects may have facilitated the rapid adaptive divergence among populations of house finches.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Badyaev, Alexander V -- Hill, Geoffrey E -- Beck, Michelle L -- Dervan, Anne A -- Duckworth, Renee A -- McGraw, Kevin J -- Nolan, Paul M -- Whittingham, Linda A -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):316-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Sciences, University of Montana, Missoula, MT 59812, USA. abadyaev@selway.umt.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786641" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Alabama ; Animals ; Behavior, Animal ; *Biological Evolution ; Body Weight ; Ecosystem ; Environment ; Female ; Male ; Montana ; Oviposition ; *Reproduction ; Selection, Genetic ; *Sex Characteristics ; Sex Ratio ; Songbirds/anatomy & histology/growth & development/*physiology ; Tarsus, Animal/anatomy & histology/growth & development
    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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  • 6
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    Miniature genome in the marine chordate Oikopleura dioica (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seo, H C -- Kube, M -- Edvardsen, R B -- Jensen, M F -- Beck, A -- Spriet, E -- Gorsky, G -- Thompson, E M -- Lehrach, H -- Reinhardt, R -- Chourrout, D -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2506.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sars [corrected] Centre for Marine Molecular Biology, Thormo- hlensgt. 55, 5020 Bergen, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752568" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Artificial, Bacterial ; Ciona intestinalis/genetics ; Cloning, Molecular ; DNA, Complementary ; DNA, Intergenic ; Expressed Sequence Tags ; Genes ; *Genome ; Introns ; Male ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Spermatozoa/chemistry ; Urochordata/anatomy & histology/*genetics/growth & development
    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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    Intravascular danger signals guide neutrophils to sites of sterile inflammation (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-16
    Description: Neutrophils are recruited from the blood to sites of sterile inflammation, where they contribute to wound healing but may also cause tissue damage. By using spinning disk confocal intravital microscopy, we examined the kinetics and molecular mechanisms of neutrophil recruitment to sites of focal hepatic necrosis in vivo. Adenosine triphosphate released from necrotic cells activated the Nlrp3 inflammasome to generate an inflammatory microenvironment that alerted circulating neutrophils to adhere within liver sinusoids. Subsequently, generation of an intravascular chemokine gradient directed neutrophil migration through healthy tissue toward foci of damage. Lastly, formyl-peptide signals released from necrotic cells guided neutrophils through nonperfused sinusoids into the injury. Thus, dynamic in vivo imaging revealed a multistep hierarchy of directional cues that guide neutrophil localization to sites of sterile inflammation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McDonald, Braedon -- Pittman, Keir -- Menezes, Gustavo B -- Hirota, Simon A -- Slaba, Ingrid -- Waterhouse, Christopher C M -- Beck, Paul L -- Muruve, Daniel A -- Kubes, Paul -- Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2010 Oct 15;330(6002):362-6. doi: 10.1126/science.1195491.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunology Research Group, University of Calgary, Alberta T2N 4N1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20947763" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Carrier Proteins/metabolism ; Cell Adhesion ; Chemokine CXCL2/metabolism ; Chemokines/metabolism ; Chemotaxis, Leukocyte ; Cues ; Endothelium, Vascular/physiology ; Inflammation/*immunology/metabolism/*pathology ; Kinetics ; Liver/blood supply/*immunology/metabolism/*pathology ; Liver Diseases/*immunology/metabolism/*pathology ; Macrophage-1 Antigen/physiology ; Mice ; Microscopy/methods ; Microscopy, Confocal ; Microvessels/physiology ; Necrosis ; *Neutrophil Infiltration ; Neutrophils/physiology ; Peptides/metabolism ; Receptors, Formyl Peptide/metabolism ; Receptors, Interleukin-8B/metabolism ; Receptors, Purinergic P2/metabolism ; Receptors, Purinergic P2X7 ; Signal Transduction
    Print ISSN: 0036-8075
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  • 8
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    The C-terminal domain of RNA polymerase II is modified by site-specific methylation (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-04-02
    Description: The carboxy-terminal domain (CTD) of RNA polymerase II (RNAPII) in mammals undergoes extensive posttranslational modification, which is essential for transcriptional initiation and elongation. Here, we show that the CTD of RNAPII is methylated at a single arginine (R1810) by the coactivator-associated arginine methyltransferase 1 (CARM1). Although methylation at R1810 is present on the hyperphosphorylated form of RNAPII in vivo, Ser2 or Ser5 phosphorylation inhibits CARM1 activity toward this site in vitro, suggesting that methylation occurs before transcription initiation. Mutation of R1810 results in the misexpression of a variety of small nuclear RNAs and small nucleolar RNAs, an effect that is also observed in Carm1(-/-) mouse embryo fibroblasts. These results demonstrate that CTD methylation facilitates the expression of select RNAs, perhaps serving to discriminate the RNAPII-associated machinery recruited to distinct gene types.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3773223/" 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/PMC3773223/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sims, Robert J 3rd -- Rojas, Luis Alejandro -- Beck, David -- Bonasio, Roberto -- Schuller, Roland -- Drury, William J 3rd -- Eick, Dirk -- Reinberg, Danny -- F32 GM071166/GM/NIGMS NIH HHS/ -- GM-37120/GM/NIGMS NIH HHS/ -- GM-71166/GM/NIGMS NIH HHS/ -- R01 GM037120/GM/NIGMS NIH HHS/ -- R37 GM037120/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2011 Apr 1;332(6025):99-103. doi: 10.1126/science.1202663.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute (HHMI), Department of Biochemistry, New York University School of Medicine, 522 First Avenue, Smilow 211, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21454787" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/metabolism ; Cell Line ; HeLa Cells ; Humans ; Methylation ; Mice ; Mutation ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/metabolism ; RNA Polymerase II/genetics/*metabolism ; RNA, Small Nuclear/metabolism ; RNA, Small Nucleolar/metabolism ; Recombinant Proteins
    Print ISSN: 0036-8075
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  • 9
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    The structures of COPI-coated vesicles reveal alternate coatomer conformations and interactions (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-26
    Description: Transport between compartments of eukaryotic cells is mediated by coated vesicles. The archetypal protein coats COPI, COPII, and clathrin are conserved from yeast to human. Structural studies of COPII and clathrin coats assembled in vitro without membranes suggest that coat components assemble regular cages with the same set of interactions between components. Detailed three-dimensional structures of coated membrane vesicles have not been obtained. Here, we solved the structures of individual COPI-coated membrane vesicles by cryoelectron tomography and subtomogram averaging of in vitro reconstituted budding reactions. The coat protein complex, coatomer, was observed to adopt alternative conformations to change the number of other coatomers with which it interacts and to form vesicles with variable sizes and shapes. This represents a fundamentally different basis for vesicle coat assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Faini, Marco -- Prinz, Simone -- Beck, Rainer -- Schorb, Martin -- Riches, James D -- Bacia, Kirsten -- Brugger, Britta -- Wieland, Felix T -- Briggs, John A G -- New York, N.Y. -- Science. 2012 Jun 15;336(6087):1451-4. doi: 10.1126/science.1221443. Epub 2012 May 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22628556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COP-Coated Vesicles/*chemistry/*ultrastructure ; Coat Protein Complex I/*chemistry ; Coatomer Protein/*chemistry ; Cryoelectron Microscopy ; Electron Microscope Tomography ; Image Processing, Computer-Assisted ; Mice ; Models, Molecular ; Protein Conformation
    Print ISSN: 0036-8075
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  • 10
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    Molecular mechanics of cardiac myosin-binding protein C in native thick filaments (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-08-28
    Description: The heart's pumping capacity results from highly regulated interactions of actomyosin molecular motors. Mutations in the gene for a potential regulator of these motors, cardiac myosin-binding protein C (cMyBP-C), cause hypertrophic cardiomyopathy. However, cMyBP-C's ability to modulate cardiac contractility is not well understood. Using single-particle fluorescence imaging techniques, transgenic protein expression, proteomics, and modeling, we found that cMyBP-C slowed actomyosin motion generation in native cardiac thick filaments. This mechanical effect was localized to where cMyBP-C resides within the thick filament (i.e., the C-zones) and was modulated by phosphorylation and site-specific proteolytic degradation. These results provide molecular insight into why cMyBP-C should be considered a member of a tripartite complex with actin and myosin that allows fine tuning of cardiac muscle contraction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3561468/" 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/PMC3561468/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Previs, M J -- Beck Previs, S -- Gulick, J -- Robbins, J -- Warshaw, D M -- 8P20GM103449/GM/NIGMS NIH HHS/ -- HL007647/HL/NHLBI NIH HHS/ -- HL059408/HL/NHLBI NIH HHS/ -- P01 HL059408/HL/NHLBI NIH HHS/ -- P20 GM103449/GM/NIGMS NIH HHS/ -- R01 HL086728/HL/NHLBI NIH HHS/ -- T32 HL007647/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2012 Sep 7;337(6099):1215-8. doi: 10.1126/science.1223602. Epub 2012 Aug 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22923435" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology ; Actomyosin/metabolism ; Amino Acid Motifs ; Animals ; Carrier Proteins/chemistry/*metabolism ; Mice ; Mice, Transgenic ; *Myocardial Contraction ; Myocardium/*metabolism/ultrastructure ; Myofibrils/*metabolism ; Myosins/*metabolism ; Phosphorylation ; Proteolysis ; Sarcomeres/metabolism
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