Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kimberly Demeyer"'
Autor:
Kimberly Demeyer, Alberto Elosegui-Artola, Kristine Hole, Rafael Aldabe, Kris Gevaert, Elena M. De Juan-Pardo, Thomas Arnesen, Duk Soo Kim, Evy Timmerman, Jesús Prieto, Bogdan Polevoda, Esther Larrea, Fred Sherman, Petra Van Damme, Cristina Gazquez, Marta Lasa
Protein N-terminal acetylation (Nt-acetylation) is an important mediator of protein function, stability, sorting, and localization. Although the responsible enzymes are thought to be fairly well characterized, the lack of identified in vivo substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f7ca0df2a91204183b0d421b2d3a1aa
https://europepmc.org/articles/PMC3412031/
https://europepmc.org/articles/PMC3412031/
Autor:
Roel Broekhuizen, Daniel R. Hostetter, Stefanie A. H. de Poot, Kris Gevaert, Charles S. Craik, Marijn Westgeest, Kimberly Demeyer, Kim Plasman, Niels Bovenschen, Petra Van Damme
Publikováno v:
The Biochemical journal. 437(3)
Cytotoxic lymphocyte protease GrM (granzyme M) is a potent inducer of tumour cell death and a key regulator of inflammation. Although hGrM (human GrM) and mGrM (mouse GrM) display extensive sequence homology, the substrate specificity of mGrM remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4691b7fdf937a25a95077d2e2a410e65
https://pubmed.ncbi.nlm.nih.gov/21564021
https://pubmed.ncbi.nlm.nih.gov/21564021
Autor:
Pieter-Jan De Bock, Kimberly Demeyer, Petra Van Damme, Johan R. Lillehaug, Kris Gevaert, Joël Vandekerckhove, Håvard Foyn, Thomas Arnesen, Rune Evjenth
Publikováno v:
Molecularcellular proteomics : MCP. 10(5)
The impact of N(α)-terminal acetylation on protein stability and protein function in general recently acquired renewed and increasing attention. Although the substrate specificity profile of the conserved enzymes responsible for N(α)-terminal acety
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::320ca6de8bbb210b30e7aee13dc5da02
https://pubmed.ncbi.nlm.nih.gov/21383206
https://pubmed.ncbi.nlm.nih.gov/21383206
Autor:
Kris Gevaert, Marc Goethals, Francis Impens, Dion Kaiserman, Phillip I. Bird, Petra Van Damme, Joël Vandekerckhove, Kim Plasman, Kimberly Demeyer, Kenny Helsens
Several mass spectrometry-driven techniques allow to map the substrate repertoires and specificities of proteases. These techniques typically yield long lists of protease substrates and processed sites with (potential) physiological relevance, but in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8c957baa704fd35dd69f518d19527e8
https://europepmc.org/articles/PMC3033678/
https://europepmc.org/articles/PMC3033678/