Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Sandy H.M. Litjens"'
Autor:
Sandy H.M. Litjens, Kevin Wilhelmsen, Jacco van Rheenen, Ingrid Kuikman, Coert Margadant, Arnoud Sonnenberg
Publikováno v:
Molecular Biology of the Cell. 18:3512-3522
Hemidesmosomes (HDs) are multiprotein adhesion complexes that promote attachment of epithelial cells to the basement membrane. The binding of alpha6beta4 to plectin plays a central role in their assembly. We have defined three regions on beta4 that t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ac0d6719837112fe2ad7abafea81d5
https://doi.org/10.1091/mbc.e07-04-0306
https://doi.org/10.1091/mbc.e07-04-0306
Publikováno v:
Molecular and Cellular Biology. 26:2877-2886
Since the discovery of the α6β4 integrin in the late 1980s, our understanding of its role in providing stable adhesion of epithelial cells to basement membranes (BM) has significantly increased. α6β4 plays a key role in the formation and stabiliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb920bf1000a0611b9c51bfcdc7a175
https://doi.org/10.1128/mcb.26.8.2877-2886.2006
https://doi.org/10.1128/mcb.26.8.2877-2886.2006
Autor:
Ingrid Kuikman, Marcel Raspe, Arnoud Sonnenberg, Sandy H.M. Litjens, Kevin Wilhelmsen, Michael O. Ports, Evelyne Frijns, Kees Jalink
Publikováno v:
Molecular Biology of the Cell
T1736 is a novel phosphorylation site on the integrin β4 subunit that is phosphorylated downstream of protein kinase C and EGF receptor activation and is a substrate for protein kinase D1 in vitro and in cells. It contributes to the regulation of HD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8245b7aa4d49200f807efb78302b5c76
https://pubmed.ncbi.nlm.nih.gov/22357621
https://pubmed.ncbi.nlm.nih.gov/22357621
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
et al.
Hemidesmosomes are multiprotein adhesion complexes that promote epithelial stromal attachment in stratified and complex epithelia. Modulation of their function is of crucial importance in a variety of biological processes, such as differe
Hemidesmosomes are multiprotein adhesion complexes that promote epithelial stromal attachment in stratified and complex epithelia. Modulation of their function is of crucial importance in a variety of biological processes, such as differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d4b7fe9a5a0c5e11aa6fb1face6deac
http://hdl.handle.net/10261/60007
http://hdl.handle.net/10261/60007
Autor:
Arnoud Sonnenberg, Ingrid Kuikman, Iman van den Bout, Hans Janssen, Karine Raymond, Sandy H.M. Litjens, Ntambua Tshimbalanga, Kevin Wilhelmsen
Publikováno v:
The Journal of Cell Biology
Despite their importance in cell biology, the mechanisms that maintain the nucleus in its proper position in the cell are not well understood. This is primarily the result of an incomplete knowledge of the proteins in the outer nuclear membrane (ONM)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::108966debf22a2f25c586ed9b95bcf98
https://pubmed.ncbi.nlm.nih.gov/16330710
https://pubmed.ncbi.nlm.nih.gov/16330710
Autor:
Anastassis Perrakis, Sandy H.M. Litjens, Kevin Wilhelmsen, Arnoud Sonnenberg, José M. de Pereda
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The binding of plectin to the β4 subunit of the α6β4 integrin is a critical step in the formation of hemidesmosomes. An important interaction between these two proteins occurs between the actin-binding domain (ABD) of plectin and the first pair of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f90c9e9ce96d38908acea453b60d9ccb
http://hdl.handle.net/10261/61425
http://hdl.handle.net/10261/61425
Publikováno v:
Molecular biology of the cell, 15(3), 1211-1223. American Society for Cell Biology
We have previously shown that plectin is recruited into hemidesmosomes through association of its actin-binding domain (ABD) with the first pair of fibronectin type III (FNIII) repeats and a small part of the connecting segment (residues 1328-1355) o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4651573454026c44fec6de68be3af156
https://pubmed.ncbi.nlm.nih.gov/14668477
https://pubmed.ncbi.nlm.nih.gov/14668477
Autor:
Sandra van Wilpe, Ingrid Kuikman, Arnoud Sonnenberg, Jan Koster, José M. de Pereda, Sandy H.M. Litjens
Publikováno v:
Molecular biology of the cell, 14(10), 4039-4050. American Society for Cell Biology
Plectin is a major component of the cytoskeleton and links the intermediate filament system to hemidesmosomes by binding to the integrin beta4 subunit. Previously, a binding site for beta4 was mapped on the actin-binding domain (ABD) of plectin and b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::782a40643d03a97ee4b3752e8420871d
https://pubmed.ncbi.nlm.nih.gov/14517317
https://pubmed.ncbi.nlm.nih.gov/14517317