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Author Foged, C.; Franzyk, H.; Bahrami, S.; Frokjaer, S.; Jaroszewski, J.W.; Nielsen, H.M.; Olsen, C.A. openurl 
  Title Cellular uptake and membrane-destabilizing properties of alpha -peptide/beta -peptoid chimeras: lessons for the design of new cell-penetrating peptides Type Journal Article
  Year 2008 Publication Biochim. Biophys. Acta, Biomembr. Abbreviated Journal  
  Volume (down) 1778 Issue 11 Pages 2487-2495  
  Keywords Peptides Role: PRP (Properties), SPN (Synthetic preparation), THU (Therapeutic use), BIOL (Biological study), PREP (Preparation), USES (Uses) (cell-penetrating; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Biological transport (diffusion; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Peptides Role: PRP (Properties), SPN (Synthetic preparation), THU (Therapeutic use), BIOL (Biological study), PREP (Preparation), USES (Uses) (fusion peptides, cationic; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Membrane phase transition (gel-liq. cryst.; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Biological transport (internalization; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Biological transport (intracellular; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Biological transport (permeation; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Stability (proteolytical; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Biological transport (uptake; alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Cell membrane; Dissolution; Fibroblast; Human; Melting point; Particle size distribution; Peptidomimetics; Pharmaceutical liposomes; Polydispersity (alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties); Phosphatidylcholines Role: THU (Therapeutic use), BIOL (Biological study), USES (Uses) (alpha -peptide/beta -peptoid chimeras cellular uptake and membrane-destabilizing properties)  
  Abstract Novel peptidomimetic backbone designs with stability towards proteases are of interest for several pharmaceutical applications including intracellular delivery. The present study concerns the cellular uptake and membrane-destabilizing effects of various cationic chimeras comprised of alternating N-alkylated beta -alanine and alpha -amino acid residues. For comparison, homomeric peptides displaying octacationic functionalities as well as the Tat47-57 sequence were included as ref. compds. Cellular uptake studies with fluorescently labeled compds. showed that guanidinylated chimeras were taken up four times more efficiently than Tat47-57. After internalization, the chimeras were localized primarily in vesicular compartments and diffusively in the cytoplasm. In murine NIH3T3 fibroblasts, the chimeras showed immediate plasma membrane permeabilizing properties, which proved highly dependent on the chimera chain length, and were remarkably different from the effects induced by Tat47-57. Finally, biophys. studies on model membranes showed that the chimeras in general increase the permeability of fluid phase and gel phase phosphatidylcholine (PC) vesicles without affecting membrane acyl chain packing, which suggests that they restrict lateral diffusion of the membrane lipids by interaction with phospholipid head groups. The alpha -peptide/beta -peptoid chimeras described herein exhibit promising cellular uptake properties, and thus represent proteolytically stable alternatives to currently known cell-penetrating peptides.  
  Address Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Copenhagen, Den  
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  Series Volume Series Issue Edition  
  ISSN 0005-2736 ISBN Medium  
  Area Expedition Conference  
  Notes CAN:150:83542 Approved no  
  Call Number refbase @ admin @ Serial 7356  
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Author חיים נחמן ביאלי&#1511 openurl 
  Title התפסן בשדה השיפון Type Book Whole
  Year 0 Publication Abbreviated Journal שק  
  Volume (down) מהדורה ש Issue 21 Pages  
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  Call Number refbase @ user @ Serial 13881  
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Author Pettorino, V.; Busoni, G.; De Simone, A.; Morgante, E.; Riotto, A.; others, openurl 
  Title Can AMS-02 discriminate the origin of an anti-proton signal? Type Journal Article
  Year 2014 Publication Jcap Abbreviated Journal  
  Volume (down) 1410 Issue 10 Pages 078  
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  Notes Approved no  
  Call Number refbase @ user @ Pettorino:2014sua Serial 15312  
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Author Busoni, G.; De Simone, A.; Gramling, J.; Morgante, E.; Riotto, A. openurl 
  Title On the Validity of the Effective Field Theory for Dark Matter Searches at the LHC, Part II: Complete Analysis for the $s$-channel Type Journal Article
  Year 2014 Publication Jcap Abbreviated Journal  
  Volume (down) 1406 Issue Pages 060  
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  Notes Approved no  
  Call Number refbase @ user @ Busoni:2014sya Serial 15310  
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Author Okabe, Y.; Kusaga, A.; Takahashi, T.; Mitsumasu, C.; Murai, Y.; Tanaka, E.; Higashi, H.; Matsuishi, T.; Kosai, K.-ichiro url  doi
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  Title Neural development of methyl-CpG-binding protein 2 null embryonic stem cells: a system for studying Rett syndrome Type Journal Article
  Year 2010 Publication Brain Research Abbreviated Journal Brain Res  
  Volume (down) 1360 Issue Pages 17-27  
  Keywords Adenoviridae/genetics; Animals; Blotting, Western; Cell Differentiation/physiology; Cells, Cultured; Chromatography, High Pressure Liquid; Clone Cells; Dopamine/physiology; Electrophysiological Phenomena; Embryonic Stem Cells/*physiology; Genetic Vectors; Glial Fibrillary Acidic Protein/metabolism; Immunohistochemistry; Methyl-CpG-Binding Protein 2/*genetics/*physiology; Mice; Mice, Inbred C57BL; Mice, Knockout; Neural Stem Cells/*physiology; Neurogenesis/physiology; Neuroglia/physiology; Neurons/physiology; Rett Syndrome/*genetics/*pathology; Reverse Transcriptase Polymerase Chain Reaction  
  Abstract Mutations in methyl-CpG-binding protein 2 (MeCP2) gene cause the neurodevelopmental disorder Rett syndrome (RTT). Here, we describe a new experimental system that efficiently elucidates the role of MeCP2 in neural development. MeCP2-null and control ES cells were generated by adenoviral conditional targeting and examined for maintenance of the undifferentiated ES cell state, neurogenesis, and gliogenesis during in vitro differentiation. In addition, dopamine release and electrophysiological features of neurons differentiated from these ES cells were examined. Loss of MeCP2 did not affect undifferentiated ES cell colony morphology and growth, or the timing or efficiency of neural stem cell differentiation into Nestin-, TuJ- or TH-positive neurons. In contrast, gliogenesis was drastically accelerated by MeCP2 deficiency. Dopamine production and release in response to a depolarizing stimulus in MeCP2-null ES-derived dopaminergic neurons was intact. However, MeCP2-null differentiated neurons showed significantly smaller voltage-dependent Na(+) currents and A-type K(+) currents, suggesting incomplete maturation. Thus, MeCP2 is not essential for maintenance of the undifferentiated ES cell state, neurogenesis, or dopaminergic function; rather, it is principally involved in inhibiting gliogenesis. Altered neuronal maturity may indirectly result from abnormal glial development and may underlie the pathogenesis of RTT. These data contribute to a better understanding of the developmental roles of MeCP2 and the pathogenesis of RTT.  
  Address Division of Gene Therapy and Regenerative Medicine, Kurume University, Kurume, Japan  
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  Series Volume Series Issue Edition  
  ISSN 0006-8993 ISBN Medium  
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  Notes PMID:20816763 Approved no  
  Call Number refbase @ user @ Serial 17003  
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