1H, 15N, 13C resonance assignment of human osteopontin

被引：0
|
作者：
Gerald Platzer
Szymon Żerko
Saurabh Saxena
Wiktor Koźmiński
Robert Konrat
机构：
[1] University of Vienna,Max F. Perutz Laboratories, Department of Computational and Structural Biology
[2] University of Warsaw,Faculty of Chemistry, Biological and Chemical Research Centre
来源：
Biomolecular NMR Assignments | 2015年 / 9卷
关键词：
Osteopontin; Intrinsically disordered protein; Extracellular matrix; Biomineralization;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Osteopontin (OPN) is a 33.7 kDa intrinsically disordered protein and a member of the SIBLING family of proteins. OPN is bearing a signal peptide for secretion into the extracellular space, where it exerts its main physiological function, the control of calcium biomineralization. It is often involved in tumorigenic processes influencing proliferation, migration and survival, as well as the adhesive properties of cancer cells via CD44 and integrin signaling pathways. Here we report the nearly complete NMR chemical shift assignment of recombinant human osteopontin.
引用
收藏
页码：289 / 292
页数：3
相关论文
共 50 条
  • [21] 1H, 13C and 15N resonance assignments of human muscle acylphosphatase
    Giuliana Fusco
    Alfonso De Simone
    Shang-Te Danny Hsu
    Francesco Bemporad
    Michele Vendruscolo
    Fabrizio Chiti
    Christopher M. Dobson
    [J]. Biomolecular NMR Assignments, 2012, 6 : 27 - 29
  • [22] 1H, 13C and 15N resonance assignments of human parvulin 17
    Lin, Yi-Jan
    Schmidt, Andreas
    Burgardt, Noelia Ines
    Thiele, Alexandra
    Weiwad, Matthias
    Luecke, Christian
    [J]. BIOMOLECULAR NMR ASSIGNMENTS, 2013, 7 (02) : 325 - 329
  • [23] 1H, 13C and 15N resonance assignments of human muscle acylphosphatase
    Fusco, Giuliana
    De Simone, Alfonso
    Hsu, Shang-Te Danny
    Bemporad, Francesco
    Vendruscolo, Michele
    Chiti, Fabrizio
    Dobson, Christopher M.
    [J]. BIOMOLECULAR NMR ASSIGNMENTS, 2012, 6 (01) : 27 - 29
  • [24] 1H, 13C and 15N resonance assignments of human parvulin 17
    Yi-Jan Lin
    Andreas Schmidt
    Noelia Inés Burgardt
    Alexandra Thiele
    Matthias Weiwad
    Christian Lücke
    [J]. Biomolecular NMR Assignments, 2013, 7 : 325 - 329
  • [25] 1H, 13C and 15N resonance assignments of human BASP1
    Geist, Leonhard
    Zawadzka-Kazimierczuk, Anna
    Saxena, Saurabh
    Zerko, Szymon
    Kozminski, Wiktor
    Konrat, Robert
    [J]. BIOMOLECULAR NMR ASSIGNMENTS, 2013, 7 (02) : 315 - 319
  • [26] 1H, 13C and 15N resonance assignments of human BASP1
    Leonhard Geist
    Anna Zawadzka-Kazimierczuk
    Saurabh Saxena
    Szymon Żerko
    Wiktor Koźmiński
    Robert Konrat
    [J]. Biomolecular NMR Assignments, 2013, 7 : 315 - 319
  • [27] 1H, 13C and 15N resonance assignment of truncated SUMO from Trypanosoma brucei
    Shang, Qiang
    Lin, Lin
    Zhang, Jiahai
    Tu, Xiaoming
    [J]. BIOMOLECULAR NMR ASSIGNMENTS, 2007, 1 (01) : 103 - 104
  • [28] 1H, 13C and 15N resonance assignment of truncated SUMO from Trypanosoma brucei
    Qiang Shang
    Lin Lin
    Jiahai Zhang
    Xiaoming Tu
    [J]. Biomolecular NMR Assignments, 2007, 1 : 103 - 104
  • [29] 1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein
    Phelan, Marie M.
    McLean, Lynn
    Simpson, Deborah M.
    Hurst, Jane L.
    Beynon, Robert J.
    Lian, Lu-Yun
    [J]. BIOMOLECULAR NMR ASSIGNMENTS, 2010, 4 (02) : 239 - 241
  • [30] 1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein
    Marie M. Phelan
    Lynn McLean
    Deborah M Simpson
    Jane L Hurst
    Robert J Beynon
    Lu-Yun Lian
    [J]. Biomolecular NMR Assignments, 2010, 4 : 239 - 241
12345