Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Noortje Samyn"'
Autor:
Sven Eyckerman, Kevin Titeca, Emmy Van Quickelberghe, Eva Cloots, Annick Verhee, Noortje Samyn, Leentje De Ceuninck, Evy Timmerman, Delphine De Sutter, Sam Lievens, Serge Van Calenbergh, Kris Gevaert, Jan Tavernier
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
A large portion of the proteome carries out its cellular function as part of macromolecular complexes. Here the authors describe Virotrap, a novel lysis-free approach for the isolation and identification of biologically relevant protein-protein and s
Externí odkaz:
https://doaj.org/article/034899752e504bb59ee91df15e16d4af
Autor:
Emmy Van Quickelberghe, Sven Eyckerman, Kris Gevaert, Giel Vandemoortele, Delphine De Sutter, Noortje Samyn, Francis Impens, Jan Tavernier
Publikováno v:
Journal of Proteome Research. 15:3929-3937
Protein complexes are essential in all organizational and functional aspects of the cell. Different strategies currently exist for analyzing such protein complexes by mass spectrometry, including affinity purification (AP-MS) and proximal labeling-ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1acf2364e468525be5dec84a6dd7870
https://doi.org/10.1021/acs.jproteome.6b00517
https://doi.org/10.1021/acs.jproteome.6b00517
Autor:
Kris Gevaert, Emmy Van Quickelberghe, Noortje Samyn, Delphine De Sutter, Sven Eyckerman, Annick Verhee, Jan Tavernier, Kevin Titeca
Publikováno v:
Nature protocols. 12(5)
The analysis of protein interaction networks is one of the key challenges in the study of biology. It connects genotypes to phenotypes, and disruption of such networks is associated with many pathologies. Virtually all the approaches to the study of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95b12bf8fe900231ee3e2627723461b1
https://pubmed.ncbi.nlm.nih.gov/28358392
https://pubmed.ncbi.nlm.nih.gov/28358392
Autor:
Giulia Gonnelli, Sven Eyckerman, An Staes, Delphine De Sutter, Evy Timmerman, Lennart Martens, Kris Gevaert, Giel Vandemoortele, Elien Vandermarliere, Noortje Samyn
Publikováno v:
SCIENTIFIC REPORTS
Scientific Reports
Scientific Reports
The use of protein tagging to facilitate detailed characterization of target proteins has not only revolutionized cell biology, but also enabled biochemical analysis through efficient recovery of the protein complexes wherein the tagged proteins resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37b6da549f8ba81008cc6496f5d13c0c
https://doi.org/10.1038/srep27220
https://doi.org/10.1038/srep27220
Autor:
Serge Van Calenbergh, Annick Verhee, Leentje De Ceuninck, Kevin Titeca, Kris Gevaert, Eva Cloots, Jan Tavernier, Sam Lievens, Delphine De Sutter, Emmy Van Quickelberghe, Sven Eyckerman, Evy Timmerman, Noortje Samyn
Publikováno v:
Nature Communications
NATURE COMMUNICATIONS
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
NATURE COMMUNICATIONS
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
Cell lysis is an inevitable step in classical mass spectrometry–based strategies to analyse protein complexes. Complementary lysis conditions, in situ cross-linking strategies and proximal labelling techniques are currently used to reduce lysis eff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca244aadf1ceaebba8f51ee9368ebf10
http://europepmc.org/articles/PMC4853472
http://europepmc.org/articles/PMC4853472
Autor:
Elisabeth Stes, Mathias Laga, Evy Timmerman, Sofie Goormachtig, Kris Gevaert, Alan Walton, Noortje Samyn, Ive De Smet
Publikováno v:
Journal of Proteome Research
Here, we apply the COmbined FRActional DIagonal Chromatography (COFRADIC) technology to enrich for ubiquitinated peptides and to identify sites of ubiquitination by mass spectrometry. Our technology bypasses the need to overexpress tagged variants of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aef66d5948354b1f4848b9236701a9d
https://pubmed.ncbi.nlm.nih.gov/24816145
https://pubmed.ncbi.nlm.nih.gov/24816145