ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (5)
  • Amino Acid Sequence  (2)
  • Jupiter  (2)
  • *Chromosomal Instability  (1)
  • 2020-2024
  • 2010-2014  (1)
  • 2005-2009  (4)
  • 1995-1999
  • 1990-1994
  • 1980-1984
  • 1965-1969
  • Computer Science  (5)
  • 1
    Publication Date: 2007-01-27
    Description: Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. We identified in bovine retinal pigment epithelium cells STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, Riki -- Yu, Jiamei -- Honda, Jane -- Hu, Jane -- Whitelegge, Julian -- Ping, Peipei -- Wiita, Patrick -- Bok, Dean -- Sun, Hui -- 5T32EY07026/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2007 Feb 9;315(5813):820-5. Epub 2007 Jan 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255476" target="_blank"〉PubMed〈/a〉
    Keywords: Acyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Blood-Retinal Barrier ; COS Cells ; Cattle ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Embryonic Development ; Endocytosis ; Humans ; Molecular Sequence Data ; Mutation, Missense ; Pigment Epithelium of Eye/*metabolism ; Placenta/metabolism ; Receptors, Cell Surface/*metabolism ; Retinal Vessels/metabolism ; Retinol-Binding Proteins/*metabolism ; Spleen/metabolism ; Transfection ; Vitamin A/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2005-09-10
    Description: On 4 July 2005, many observatories around the world and in space observed the collision of Deep Impact with comet 9P/Tempel 1 or its aftermath. This was an unprecedented coordinated observational campaign. These data show that (i) there was new material after impact that was compositionally different from that seen before impact; (ii) the ratio of dust mass to gas mass in the ejecta was much larger than before impact; (iii) the new activity did not last more than a few days, and by 9 July the comet's behavior was indistinguishable from its pre-impact behavior; and (iv) there were interesting transient phenomena that may be correlated with cratering physics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meech, K J -- Ageorges, N -- A'Hearn, M F -- Arpigny, C -- Ates, A -- Aycock, J -- Bagnulo, S -- Bailey, J -- Barber, R -- Barrera, L -- Barrena, R -- Bauer, J M -- Belton, M J S -- Bensch, F -- Bhattacharya, B -- Biver, N -- Blake, G -- Bockelee-Morvan, D -- Boehnhardt, H -- Bonev, B P -- Bonev, T -- Buie, M W -- Burton, M G -- Butner, H M -- Cabanac, R -- Campbell, R -- Campins, H -- Capria, M T -- Carroll, T -- Chaffee, F -- Charnley, S B -- Cleis, R -- Coates, A -- Cochran, A -- Colom, P -- Conrad, A -- Coulson, I M -- Crovisier, J -- deBuizer, J -- Dekany, R -- de Leon, J -- Dello Russo, N -- Delsanti, A -- DiSanti, M -- Drummond, J -- Dundon, L -- Etzel, P B -- Farnham, T L -- Feldman, P -- Fernandez, Y R -- Filipovic, M D -- Fisher, S -- Fitzsimmons, A -- Fong, D -- Fugate, R -- Fujiwara, H -- Fujiyoshi, T -- Furusho, R -- Fuse, T -- Gibb, E -- Groussin, O -- Gulkis, S -- Gurwell, M -- Hadamcik, E -- Hainaut, O -- Harker, D -- Harrington, D -- Harwit, M -- Hasegawa, S -- Hergenrother, C W -- Hirst, P -- Hodapp, K -- Honda, M -- Howell, E S -- Hutsemekers, D -- Iono, D -- Ip, W-H -- Jackson, W -- Jehin, E -- Jiang, Z J -- Jones, G H -- Jones, P A -- Kadono, T -- Kamath, U W -- Kaufl, H U -- Kasuga, T -- Kawakita, H -- Kelley, M S -- Kerber, F -- Kidger, M -- Kinoshita, D -- Knight, M -- Lara, L -- Larson, S M -- Lederer, S -- Lee, C-F -- Levasseur-Regourd, A C -- Li, J Y -- Li, Q-S -- Licandro, J -- Lin, Z-Y -- Lisse, C M -- LoCurto, G -- Lovell, A J -- Lowry, S C -- Lyke, J -- Lynch, D -- Ma, J -- Magee-Sauer, K -- Maheswar, G -- Manfroid, J -- Marco, O -- Martin, P -- Melnick, G -- Miller, S -- Miyata, T -- Moriarty-Schieven, G H -- Moskovitz, N -- Mueller, B E A -- Mumma, M J -- Muneer, S -- Neufeld, D A -- Ootsubo, T -- Osip, D -- Pandea, S K -- Pantin, E -- Paterno-Mahler, R -- Patten, B -- Penprase, B E -- Peck, A -- Petitas, G -- Pinilla-Alonso, N -- Pittichova, J -- Pompei, E -- Prabhu, T P -- Qi, C -- Rao, R -- Rauer, H -- Reitsema, H -- Rodgers, S D -- Rodriguez, P -- Ruane, R -- Ruch, G -- Rujopakarn, W -- Sahu, D K -- Sako, S -- Sakon, I -- Samarasinha, N -- Sarkissian, J M -- Saviane, I -- Schirmer, M -- Schultz, P -- Schulz, R -- Seitzer, P -- Sekiguchi, T -- Selman, F -- Serra-Ricart, M -- Sharp, R -- Snell, R L -- Snodgrass, C -- Stallard, T -- Stecklein, G -- Sterken, C -- Stuwe, J A -- Sugita, S -- Sumner, M -- Suntzeff, N -- Swaters, R -- Takakuwa, S -- Takato, N -- Thomas-Osip, J -- Thompson, E -- Tokunaga, A T -- Tozzi, G P -- Tran, H -- Troy, M -- Trujillo, C -- Van Cleve, J -- Vasundhara, R -- Vazquez, R -- Vilas, F -- Villanueva, G -- von Braun, K -- Vora, P -- Wainscoat, R J -- Walsh, K -- Watanabe, J -- Weaver, H A -- Weaver, W -- Weiler, M -- Weissman, P R -- Welsh, W F -- Wilner, D -- Wolk, S -- Womack, M -- Wooden, D -- Woodney, L M -- Woodward, C -- Wu, Z-Y -- Wu, J-H -- Yamashita, T -- Yang, B -- Yang, Y-B -- Yokogawa, S -- Zook, A C -- Zauderer, A -- Zhao, X -- Zhou, X -- Zucconi, J-M -- New York, N.Y. -- Science. 2005 Oct 14;310(5746):265-9. Epub 2005 Sep 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Astronomy, University of Hawaii at Manoa, 2680 Woodlawn Drive, Honolulu, HI 96822, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16150977" target="_blank"〉PubMed〈/a〉
    Keywords: Cosmic Dust ; Jupiter ; *Meteoroids ; Organic Chemicals ; Photometry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2005-09-17
    Description: The impact cratering process on a comet is controversial but holds the key for interpreting observations of the Deep Impact collision with comet 9P/Tempel 1. Mid-infrared data from the Cooled Mid-Infrared Camera and Spectrometer (COMICS) of the Subaru Telescope indicate that the large-scale dust plume ejected by the impact contained a large mass (approximately 10(6) kilograms) of dust and formed two wings approximately +/-45 degrees from the symmetric center, both consistent with gravity as the primary control on the impact and its immediate aftermath. The dust distribution in the inner part of the plume, however, is inconsistent with a pure gravity control and implies that evaporation and expansion of volatiles accelerated dust.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sugita, S -- Ootsubo, T -- Kadono, T -- Honda, M -- Sako, S -- Miyata, T -- Sakon, I -- Yamashita, T -- Kawakita, H -- Fujiwara, H -- Fujiyoshi, T -- Takato, N -- Fuse, T -- Watanabe, J -- Furusho, R -- Hasegawa, S -- Kasuga, T -- Sekiguchi, T -- Kinoshita, D -- Meech, K J -- Wooden, D H -- Ip, W H -- A'Hearn, M F -- New York, N.Y. -- Science. 2005 Oct 14;310(5746):274-8. Epub 2005 Sep 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Complexity Science and Engineering, University of Tokyo, Kashiwa, Chiba, Japan. sugita@k.u-tokyo.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166476" target="_blank"〉PubMed〈/a〉
    Keywords: Cosmic Dust ; Jupiter ; *Meteoroids ; Spectrophotometry, Infrared ; Volatilization
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2009-12-08
    Description: Bub1 is a multi-task protein kinase required for proper chromosome segregation in eukaryotes. Impairment of Bub1 in humans may lead to chromosomal instability (CIN) or tumorigenesis. Yet, the primary cellular substrate of Bub1 has remained elusive. Here, we show that Bub1 phosphorylates the conserved serine 121 of histone H2A in fission yeast Schizosaccharomyces pombe. The h2a-SA mutant, in which all cellular H2A-S121 is replaced by alanine, phenocopies the bub1 kinase-dead mutant (bub1-KD) in losing the centromeric localization of shugoshin proteins. Artificial tethering of shugoshin to centromeres largely restores the h2a-SA or bub1-KD-related CIN defects, a function that is evolutionally conserved. Thus, Bub1 kinase creates a mark for shugoshin localization and the correct partitioning of chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawashima, Shigehiro A -- Yamagishi, Yuya -- Honda, Takashi -- Ishiguro, Kei-ichiro -- Watanabe, Yoshinori -- New York, N.Y. -- Science. 2010 Jan 8;327(5962):172-7. doi: 10.1126/science.1180189. Epub 2009 Nov 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965387" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Centromere/*metabolism ; *Chromosomal Instability ; Chromosomal Proteins, Non-Histone/genetics/*metabolism ; *Chromosome Segregation ; Chromosomes, Fungal/metabolism ; Histones/*metabolism ; Humans ; Kinetochores/metabolism ; Meiosis ; Mice ; Mitosis ; Nucleosomes/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins/genetics/metabolism ; Schizosaccharomyces/cytology/genetics/*metabolism ; Schizosaccharomyces pombe Proteins/genetics/*metabolism ; Serine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    Publication Date: 2010-10-12
    Description: For proper partitioning of chromosomes in mitosis, the chromosomal passenger complex (CPC) including Aurora B and survivin must be localized at the center of paired kinetochores, at the site called the inner centromere. It is largely unknown what defines the inner centromere and how the CPC is targeted to this site. Here, we show that the phosphorylation of histone H3-threonine 3 (H3-pT3) mediated by Haspin cooperates with Bub1-mediated histone 2A-serine 121 (H2A-S121) phosphorylation in targeting the CPC to the inner centromere in fission yeast and human cells. H3-pT3 promotes nucleosome binding of survivin, whereas phosphorylated H2A-S121 facilitates the binding of shugoshin, the centromeric CPC adaptor. Haspin colocalizes with cohesin by associating with Pds5, whereas Bub1 localizes at kinetochores. Thus, the inner centromere is defined by intersection of two histone kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamagishi, Yuya -- Honda, Takashi -- Tanno, Yuji -- Watanabe, Yoshinori -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):239-43. doi: 10.1126/science.1194498.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aurora Kinase B ; Aurora Kinases ; Cell Cycle Proteins/metabolism ; Centromere/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation ; Chromosomes, Fungal/*physiology ; Chromosomes, Human/*physiology ; HeLa Cells ; Heterochromatin/metabolism ; Histones/*metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Intracellular Signaling Peptides and Proteins/chemistry/genetics/*metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Mitosis ; Molecular Sequence Data ; Mutation ; Nucleosomes/metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Schizosaccharomyces/*genetics/metabolism ; Schizosaccharomyces pombe Proteins/genetics/*metabolism ; Serine/metabolism ; Threonine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...