Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Christiane Spillner"'
Autor:
Edith Bonnin, Pauline Cabochette, Alessandro Filosa, Ramona Jühlen, Shoko Komatsuzaki, Mohammed Hezwani, Achim Dickmanns, Valérie Martinelli, Marjorie Vermeersch, Lynn Supply, Nuno Martins, Laurence Pirenne, Gianina Ravenscroft, Marcus Lombard, Sarah Port, Christiane Spillner, Sandra Janssens, Ellen Roets, Jo Van Dorpe, Martin Lammens, Ralph H Kehlenbach, Ralf Ficner, Nigel G Laing, Katrin Hoffmann, Benoit Vanhollebeke, Birthe Fahrenkrog
Publikováno v:
PLoS Genetics, Vol 14, Iss 12, p e1007845 (2018)
Nucleoporins build the nuclear pore complex (NPC), which, as sole gate for nuclear-cytoplasmic exchange, is of outmost importance for normal cell function. Defects in the process of nucleocytoplasmic transport or in its machinery have been frequently
Externí odkaz:
https://doaj.org/article/88c96d3ae2aa45ddb907f5a735313301
Autor:
Sarah A. Port, Thomas Monecke, Achim Dickmanns, Christiane Spillner, Romina Hofele, Henning Urlaub, Ralf Ficner, Ralph H. Kehlenbach
Publikováno v:
Cell Reports, Vol 13, Iss 4, Pp 690-702 (2015)
CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tig
Externí odkaz:
https://doaj.org/article/b9e3ebdaa4eb4fa9bd017adef6b43a68
Autor:
Ralf Ficner, Birthe Fahrenkrog, Gianina Ravenscroft, Laurence Pirenne, Shoko Komatsuzaki, Marcus Lombard, Sandra Janssens, Ralph H. Kehlenbach, Ellen Roets, Ramona Jühlen, Benoit Vanhollebeke, Katrin Hoffmann, Lynn Supply, Jo Van Dorpe, Pauline Cabochette, Achim Dickmanns, Sarah A. Port, Nuno Martins, Marjorie Vermeersch, Edith Bonnin, Christiane Spillner, Nigel G. Laing, Alessandro Filosa, Valérie Martinelli, Mohammed Hezwani, Martin Lammens
Publikováno v:
PLoS Genetics
PLoS Genetics, Vol 14, Iss 12, p e1007845 (2018)
PLOS GENETICS
PLoS genetics
PLOS genetics, 14 (12
PLoS Genetics, Vol 14, Iss 12, p e1007845 (2018)
PLOS GENETICS
PLoS genetics
PLOS genetics, 14 (12
Nucleoporins build the nuclear pore complex (NPC), which, as sole gate for nuclear-cytoplasmic exchange, is of outmost importance for normal cell function. Defects in the process of nucleocytoplasmic transport or in its machinery have been frequently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2d48614b9458b3e4b28965ec49db3d8
http://edoc.mdc-berlin.de/17934/1/17934oa.pdf
http://edoc.mdc-berlin.de/17934/1/17934oa.pdf
Autor:
Ellen Roets, Ralf Ficner, Marcus Lombard, Alessandro Filosa, Pauline Cabochette, Martin Lammens, Nuno Martins, Christiane Spillner, Birthe Fahrenkrog, Achim Dickmanns, Nigel G. Laing, Marjorie Vermeersch, Sarah A. Port, Shoko Komatsuzaki, Lynn Supply, Ralph H. Kehlenbach, Valérie Martinelli, Benoit Vanhollebeke, Mohammed Hezwani, Katrin Hoffmann, Gianina Ravenscroft, Sandra Janssens, Jo Van Dorpe, Edith Bonnin, Ramona Juehlen, Laurence Pirenne
Nucleoporins build the nuclear pore complex (NPC), which, as sole gate for nuclear-cytoplasmic exchange, are of outmost importance for normal cell function. Defects in the process of nucleocytoplasmic transport or in its machinery have been frequentl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::586e7deecb389bd780e0af35818f2925
Publikováno v:
Molecularcellular proteomics : MCP. 17(7)
Importin 13 is a member of the importin β family of transport receptors. Unlike most family members, importin 13 mediates both, nuclear protein import and export. To search for novel importin 13 cargoes, we used stable isotope labeling of amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6625e3a5c4a8095ec0a2ead437d315c9
https://pubmed.ncbi.nlm.nih.gov/29666159
https://pubmed.ncbi.nlm.nih.gov/29666159
Publikováno v:
Journal of Biological Chemistry. 288:3952-3963
Nucleoporins containing phenylalanine glycine (FG) repeats play an important role in nucleocytoplasmic transport as they bind to transport receptors and mediate translocation of transport complexes across the nuclear pore complex (NPC). Nup214/CAN, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f03f261b168d686bb250c4adbb0af5
https://doi.org/10.1074/jbc.m112.433243
https://doi.org/10.1074/jbc.m112.433243
Autor:
Sarah Wälde, Ralph H. Kehlenbach, Ulrich Rothbauer, Annegret Nath, Ketan Thakar, Saskia Hutten, Christiane Spillner, Stefan Wiemann
Publikováno v:
Traffic. 13:218-233
In vertebrates, the nuclear pore complex (NPC), the gate for transport of macromolecules between the nucleus and the cytoplasm, consists of approximately 30 different nucleoporins (Nups). The Nup and SUMO E3-ligase Nup358/RanBP2 are the major compone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef960428f2201ccd4cdab624b352ac92
https://doi.org/10.1111/j.1600-0854.2011.01302.x
https://doi.org/10.1111/j.1600-0854.2011.01302.x
Publikováno v:
Journal of Cell Science. 122:1100-1110
Nup358 (also known as RanBP2), a component of the cytoplasmic filaments of the nuclear pore complex, has been implicated in various nucleocytoplasmic transport pathways. Here, we identify Nup358 as an important factor for transportin-mediated nuclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::622bcd687c0da0361188b9dd5d036f65
https://doi.org/10.1242/jcs.040154
https://doi.org/10.1242/jcs.040154
Publikováno v:
Journal of cell science. 125(Pt 1)
Translocation of transport complexes across the nuclear envelope is mediated by nucleoporins, proteins of the nuclear pore complex that contain phenylalanine-glycine (FG) repeats as a characteristic binding motif for transport receptors. CRM1 (export
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7510f3aef895d63266e0c8e261d0179a
https://pubmed.ncbi.nlm.nih.gov/22250199
https://pubmed.ncbi.nlm.nih.gov/22250199
Autor:
Desmond J. Fitzgerald, Simone Marcone, Tina Lampe, Annegret Nath, Christiane Spillner, Ralph H. Kehlenbach, Cornelia Frohnert, Mark Hilliard
The signaling molecule 15-deoxy-Delta(12,14)-prostaglandin J(2) (15d-PGJ(2)) has been described as the "anti-inflammatory prostaglandin." Here we show that substrates of the nuclear export receptor CRM1 accumulate in the nucleus in the presence of 15
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20757d60601e19ebd389bdbbfbf5455c
https://europepmc.org/articles/PMC2903415/
https://europepmc.org/articles/PMC2903415/