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  1. 1
    A. R. Forrest ; H. Kawaji ; M. Rehli ; J. K. Baillie ; M. J. de Hoon ; V. Haberle ; T. Lassmann ; I. V. Kulakovskiy ; M. Lizio ; M. Itoh ; R. Andersson ; C. J. Mungall ; T. F. Meehan ; S. Schmeier ; N. Bertin ; M. Jorgensen ; E. Dimont ; E. Arner ; C. Schmidl ; U. Schaefer ; Y. A. Medvedeva ; C. Plessy ; M. Vitezic ; J. Severin ; C. Semple ; Y. Ishizu ; R. S. Young ; M. Francescatto ; I. Alam ; D. Albanese ; G. M. Altschuler ; T. Arakawa ; J. A. Archer ; P. Arner ; M. Babina ; S. Rennie ; P. J. Balwierz ; A. G. Beckhouse ; S. Pradhan-Bhatt ; J. A. Blake ; A. Blumenthal ; B. Bodega ; A. Bonetti ; J. Briggs ; F. Brombacher ; A. M. Burroughs ; A. Califano ; C. V. Cannistraci ; D. Carbajo ; Y. Chen ; M. Chierici ; Y. Ciani ; H. C. Clevers ; E. Dalla ; C. A. Davis ; M. Detmar ; A. D. Diehl ; T. Dohi ; F. Drablos ; A. S. Edge ; M. Edinger ; K. Ekwall ; M. Endoh ; H. Enomoto ; M. Fagiolini ; L. Fairbairn ; H. Fang ; M. C. Farach-Carson ; G. J. Faulkner ; A. V. Favorov ; M. E. Fisher ; M. C. Frith ; R. Fujita ; S. Fukuda ; C. Furlanello ; M. Furino ; J. Furusawa ; T. B. Geijtenbeek ; A. P. Gibson ; T. Gingeras ; D. Goldowitz ; J. Gough ; S. Guhl ; R. Guler ; S. Gustincich ; T. J. Ha ; M. Hamaguchi ; M. Hara ; M. Harbers ; J. Harshbarger ; A. Hasegawa ; Y. Hasegawa ; T. Hashimoto ; M. Herlyn ; K. J. Hitchens ; S. J. Ho Sui ; O. M. Hofmann ; I. Hoof ; F. Hori ; L. Huminiecki ; K. Iida ; T. Ikawa ; B. R. Jankovic ; H. Jia ; A. Joshi ; G. Jurman ; B. Kaczkowski ; C. Kai ; K. Kaida ; A. Kaiho ; K. Kajiyama ; M. Kanamori-Katayama ; A. S. Kasianov ; T. Kasukawa ; S. Katayama ; S. Kato ; S. Kawaguchi ; H. Kawamoto ; Y. I. Kawamura ; T. Kawashima ; J. S. Kempfle ; T. J. Kenna ; J. Kere ; L. M. Khachigian ; T. Kitamura ; S. P. Klinken ; A. J. Knox ; M. Kojima ; S. Kojima ; N. Kondo ; H. Koseki ; S. Koyasu ; S. Krampitz ; A. Kubosaki ; A. T. Kwon ; J. F. Laros ; W. Lee ; A. Lennartsson ; K. Li ; B. Lilje ; L. Lipovich ; A. Mackay-Sim ; R. Manabe ; J. C. Mar ; B. Marchand ; A. Mathelier ; N. Mejhert ; A. Meynert ; Y. Mizuno ; D. A. de Lima Morais ; H. Morikawa ; M. Morimoto ; K. Moro ; E. Motakis ; H. Motohashi ; C. L. Mummery ; M. Murata ; S. Nagao-Sato ; Y. Nakachi ; F. Nakahara ; T. Nakamura ; Y. Nakamura ; K. Nakazato ; E. van Nimwegen ; N. Ninomiya ; H. Nishiyori ; S. Noma ; T. Noazaki ; S. Ogishima ; N. Ohkura ; H. Ohimiya ; H. Ohno ; M. Ohshima ; M. Okada-Hatakeyama ; Y. Okazaki ; V. Orlando ; D. A. Ovchinnikov ; A. Pain ; R. Passier ; M. Patrikakis ; H. Persson ; S. Piazza ; J. G. Prendergast ; O. J. Rackham ; J. A. Ramilowski ; M. Rashid ; T. Ravasi ; P. Rizzu ; M. Roncador ; S. Roy ; M. B. Rye ; E. Saijyo ; A. Sajantila ; A. Saka ; S. Sakaguchi ; M. Sakai ; H. Sato ; S. Savvi ; A. Saxena ; C. Schneider ; E. A. Schultes ; G. G. Schulze-Tanzil ; A. Schwegmann ; T. Sengstag ; G. Sheng ; H. Shimoji ; Y. Shimoni ; J. W. Shin ; C. Simon ; D. Sugiyama ; T. Sugiyama ; M. Suzuki ; N. Suzuki ; R. K. Swoboda ; P. A. t Hoen ; M. Tagami ; N. Takahashi ; J. Takai ; H. Tanaka ; H. Tatsukawa ; Z. Tatum ; M. Thompson ; H. Toyodo ; T. Toyoda ; E. Valen ; M. van de Wetering ; L. M. van den Berg ; R. Verado ; D. Vijayan ; I. E. Vorontsov ; W. W. Wasserman ; S. Watanabe ; C. A. Wells ; L. N. Winteringham ; E. Wolvetang ; E. J. Wood ; Y. Yamaguchi ; M. Yamamoto ; M. Yoneda ; Y. Yonekura ; S. Yoshida ; S. E. Zabierowski ; P. G. Zhang ; X. Zhao ; S. Zucchelli ; K. M. Summers ; H. Suzuki ; C. O. Daub ; J. Kawai ; P. Heutink ; W. Hide ; T. C. Freeman ; B. Lenhard ; V. B. Bajic ; M. S. Taylor ; V. J. Makeev ; A. Sandelin ; D. A. Hume ; P. Carninci ; Y. Hayashizaki
    Nature Publishing Group (NPG)
    Published 2014
    Staff View
    Publication Date:
    2014-03-29
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; *Atlases as Topic ; Cell Line ; Cells, Cultured ; Cluster Analysis ; Conserved Sequence/genetics ; Gene Expression Regulation/genetics ; Gene Regulatory Networks/genetics ; Genes, Essential/genetics ; Genome/genetics ; Humans ; Mice ; *Molecular Sequence Annotation ; Open Reading Frames/genetics ; Organ Specificity ; Promoter Regions, Genetic/*genetics ; RNA, Messenger/analysis/genetics ; Transcription Factors/metabolism ; Transcription Initiation Site ; Transcription, Genetic/genetics ; Transcriptome/*genetics
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Edge, A. S. B. ; Spiro, R. G.
    Springer
    Published 2000
    Staff View
    ISSN:
    1432-0428
    Keywords:
    Keywords Glomerular basement membrane ; diabetic glomerular basement membrane alterations ; 3-O-sulphated glucosamine ; heparan sulphate binding ; heparan sulphate sulphation sites ; hydrazine/nitrous acid fragmentation ; iduronic acid ; glomerular anionic filter.
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Abstract Aims/hypothesis. Heparan sulphate proteoglycan is an important component of the glomerular anionic filtration barrier and its reduced amount in diabetes contributes to glomerular dysfunction. The objective of this study was to determine if there is also an alteration in the sulphation pattern of the diabetic heparan sulphate chains. Methods. The heparan sulphate in the glomerular basement membrane/mesangial matrix from human diabetic and nondiabetic kidneys obtained at autopsy was fragmented by a hydrazine/nitrous acid procedure and after radiolabelling with NaB[3H]4, the disaccharide products were chromatographically resolved and quantified. Results. Six sulphated disaccharides were identified in both the diabetic and nondiabetic samples and the molar distribution of these was similar, with the notable exception of the iduronic acid-2-O-sulphateα1 → 4glucosamine-3-O-sulphate species which occurred in the diabetic glomeruli in less than half the amount as in the nondiabetic samples (9.0 % compared to 18.7 % of total sulphated disaccharides, p 〈 0.005). Conclusion/interpretation. 3-O-sulphated glucosamine is a rare constituent of heparan sulphate occurring usually in a glucuronic acidβ1 → 4glucosamine-3-O-sulphate( ± 6-O-sulphate) sequence within the antithrombin-binding domain. In the glomerular basement membrane where the 3-O-sulphated glucosamine is present in substantial amounts, however, it occurs exclusively in an iduronic acid-containing sequence. It is likely that the recently discovered 3-O-sulphotransferase variant which specifically acts on the iduronic acidα1 → 4glucosamine sequence is decreased in human diabetes and moreover that this unusual disaccharide could be a component of a specific heparan sulphate domain which interacts with bioactive proteins. [Diabetologia (2000) 43: 1056–1059]
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s001250051489

    Articles: DFG German National Licenses