Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Monique, Beullens"'
Autor:
Ranjit Ganguly, Ahmed Mohyeldin, Jordyn Thiel, Harley I Kornblum, Monique Beullens, Ichiro Nakano
Publikováno v:
Clinical and Translational Medicine, Vol 4, Iss 1, Pp n/a-n/a (2015)
Abstract Maternal embryonic leucine zipper kinase (MELK) is a highly conserved serine/threonine kinase initially found to be expressed in a wide range of early embryonic cellular stages, and as a result has been implicated in embryogenesis and cell c
Externí odkaz:
https://doaj.org/article/7bc97bbe9e104afbb892d228cf0fb485
Publikováno v:
Biochimica et Biophysica Acta. Molecular Cell Research
Protein phosphatase 1 (PP1) catalyzes more than half of all phosphoserine/threonine dephosphorylation reactions in mammalian cells. In vivo PP1 does not exist as a free catalytic subunit but is always associated with at least one regulatory PP1-inter
Autor:
Bernhard Hoermann, Javier del Pino Garcia, Maja Köhn, Francesca Salvi, Orsolya Barabas, Miriam Fontanillo, Mathieu Bollen, Rita Derua, Monique Beullens
Publikováno v:
'ChemBioChem ', vol: 22, pages: 834-838 (2021)
Chembiochem
ChemBioChem
Chembiochem
ChemBioChem
Phosphoprotein phosphatase‐1 (PP1) is a key player in the regulation of phospho‐serine (pSer) and phospho‐threonine (pThr) dephosphorylation and is involved in a large fraction of cellular signaling pathways. Aberrant activity of PP1 has been l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::745697fdb2291cc2548fd075fc1e3a31
https://lirias.kuleuven.be/handle/123456789/671428
https://lirias.kuleuven.be/handle/123456789/671428
Autor:
Cristina Martin-Granados, Alan R Prescott, Nele Van Dessel, Aleyde Van Eynde, Miguel Arocena, Izabela P Klaska, Janina Görnemann, Monique Beullens, Mathieu Bollen, John V Forrester, Colin D McCaig
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e40769 (2012)
Electrical gradients are present in many developing and regenerating tissues and around tumours. Mimicking endogenous electric fields in vitro has profound effects on the behaviour of many cell types. Intriguingly, specific cell types migrate cathoda
Externí odkaz:
https://doaj.org/article/53b1d6947e134e6aafbff575c15b6ec8
Autor:
Tatiana Ammosova, Yuri Obukhov, Alexander Kotelkin, Denitra Breuer, Monique Beullens, Victor R Gordeuk, Mathieu Bollen, Sergei Nekhai
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18985 (2011)
The cyclin-dependent kinase CDK9/cyclin T1 induces HIV-1 transcription by phosphorylating the carboxyterminal domain (CTD) of RNA polymerase II (RNAPII). CDK9 activity is regulated by protein phosphatase-1 (PP1) which was previously shown to dephosph
Externí odkaz:
https://doaj.org/article/2edfb43687bb43d09555f553a9698b3d
Autor:
Lijs Beke, Cenk Kig, Joannes T. M. Linders, Shannah Boens, An Boeckx, Erika van Heerde, Marc Parade, An De Bondt, Ilse Van den Wyngaert, Tarig Bashir, Souichi Ogata, Lieven Meerpoel, Aleyde Van Eynde, Christopher N. Johnson, Monique Beullens, Dirk Brehmer, Mathieu Bollen
Publikováno v:
Bioscience Reports
Protein kinase MELK has oncogenic properties and is highly overexpressed in some tumors. In the present study, we show that a novel MELK inhibitor causes both the inhibition and degradation of MELK, culminating in replication stress and a senescence
Autor:
Dan Wu, Veerle De Wever, Rita Derua, Aleyde Van Eynde, Mathieu Bollen, Monique Beullens, Claudia Winkler
Publikováno v:
The Journal of biological chemistry. 293(39)
The protein Ser/Thr phosphatase PP1 catalyzes an important fraction of protein dephosphorylation events and forms highly specific holoenzymes through an association with regulatory interactors of protein phosphatase one (RIPPOs). The functional chara
Autor:
Claudia, Winkler, Raphael, Rouget, Dan, Wu, Monique, Beullens, Aleyde, Van Eynde, Mathieu, Bollen
Publikováno v:
Journal of cell science. 131(13)
The ubiquitously expressed nuclear protein NIPP1 (also known as PPP1R8) recruits phosphoproteins for regulated dephosphorylation by the associated protein phosphatase PP1. To bypass the PP1 titration artifacts seen upon NIPP1 overexpression, we have
Publikováno v:
Journal of Cell Science.
The ubiquitously expressed nuclear protein NIPP1 (also known as PPP1R8) recruits phosphoproteins for regulated dephosphorylation by the associated protein phosphatase PP1. To bypass the PP1 titration artifacts seen upon NIPP1 overexpression, we have
Autor:
Dirk Brehmer, Cenk Kig, Lijs Beke, Mathieu Bollen, Johannes T. Linders, Aleyde Van Eynde, Monique Beullens
Maternal embryonic leucine zipper kinase (MELK) belongs to the subfamily of AMP-activated Ser/Thr protein kinases. The expression of MELK is very high in glioblastoma-type brain tumors, but it is not clear how this contributes to tumor growth. Here w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::408e934652a4539350049c1aaf310f29
https://europepmc.org/articles/PMC5546021/
https://europepmc.org/articles/PMC5546021/