E
Evert de Vries
Researcher at Netherlands Cancer Institute
Publications - 24
Citations - 2086
Evert de Vries is an academic researcher from Netherlands Cancer Institute. The author has contributed to research in topics: T cell & T-cell receptor. The author has an hindex of 20, co-authored 22 publications receiving 1807 citations. Previous affiliations of Evert de Vries include Leiden University & Leiden University Medical Center.
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Journal ArticleDOI
Identification of CMTM6 and CMTM4 as PD-L1 protein regulators
Riccardo Mezzadra,Chong Sun,Lucas T. Jae,Raquel Gomez-Eerland,Evert de Vries,Wei Wu,Meike Emma Willemijn Logtenberg,Maarten Slagter,Elisa A. Rozeman,Ingrid Hofland,Annegien Broeks,Hugo M. Horlings,Lodewyk F. A. Wessels,Christian U. Blank,Yanling Xiao,Albert J. R. Heck,Jannie Borst,Thijn R. Brummelkamp,Thijn R. Brummelkamp,Ton N. Schumacher +19 more
TL;DR: The data reveal that PD-L1 relies on CMTM6/4 to efficiently carry out its inhibitory function, and suggest potential new avenues to block this pathway.
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Bcl-2 family member Bfl-1/A1 sequesters truncated Bid to inhibit its collaboration with pro-apoptotic Bak or Bax
TL;DR: It is found that Bfl-1 associates with both full-length Bid and truncated (t)Bid, via the Bid BH3 domain, and remains tightly and selectively bound to tBid and blocks collaboration between tBID and Bax or Bak in the plane of the mitochondrial membrane, thereby preventing mitochondrial apoptotic activation.
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Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage–induced apoptosis
TL;DR: The data imply that Cer is not instrumental in the activation of inducer caspases or signaling to the mitochondria, Rather, Cer formation is associated with the execution phase of apoptosis.
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Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment
TL;DR: It is concluded that unconventional ubiquitination and proteasome-dependent degradation of tBid-N is required to unleash the proapoptotic activity of t Bcl-2 homology 3 (BH3) domain in the cleaved complex.
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CD95/Fas-induced ceramide formation proceeds with slow kinetics and is not blocked by caspase-3/CPP32 inhibition.
Annemiek D. Tepper,Jeanine G.R. Boesen-de Cock,Evert de Vries,Jannie Borst,Wim J. van Blitterswijk +4 more
TL;DR: The results support the idea that ceramide acts in conjunction with the caspase cascade in CD95-induced apoptosis, with kinetics closely paralleling apoptosis induction.