Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Julien Béthune"'
Autor:
Lea Kubitz, Sebastian Bitsch, Xiyan Zhao, Kerstin Schmitt, Lukas Deweid, Amélie Roehrig, Elisa Cappio Barazzone, Oliver Valerius, Harald Kolmar, Julien Béthune
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-14 (2022)
A small-size engineered enzyme, ultraID, is presented for proximity-dependent biotinylation, that shows efficient labeling in mammalian cell culture, E. coli and S. cerevisiae.
Externí odkaz:
https://doaj.org/article/bda3a7b2012d4b0897455b223b4048a3
Autor:
Mahmoud‐Reza Rafiee, Gianluca Sigismondo, Mathias Kalxdorf, Laura Förster, Britta Brügger, Julien Béthune, Jeroen Krijgsveld
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 5, Pp 1-12 (2020)
Abstract Streptavidin‐mediated enrichment is a powerful strategy to identify biotinylated biomolecules and their interaction partners; however, intense streptavidin‐derived peptides impede protein identification by mass spectrometry. Here, we pre
Externí odkaz:
https://doaj.org/article/38d85c958ac1461aaa30bac0a429cf0c
Autor:
Isabel Myriam Schopp, Cinthia Claudia Amaya Ramirez, Jerneja Debeljak, Elisa Kreibich, Merle Skribbe, Klemens Wild, Julien Béthune
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
The BioID approaches takes advantage of the promiscuous biotinylation enzyme (BirA*) to identify proteins that closely interact. Here the authors improve the resolution of BioID using a protein fragment complementation approach that allows the assign
Externí odkaz:
https://doaj.org/article/5f14accf245a4ad4ab177b2e58e2b7ee
Autor:
Cappio Barazzone E, Kerstin Schmitt, Sebastian Bitsch, Lukas Deweid, Julien Béthune, Oliver Valerius, Zhao X, Harald Kolmar, Roehrig A, Kubitz L
Proximity-dependent biotinylation (PDB) combined with mass spectrometry analysis has established itself as a key technology to study protein-protein interactions in living cells. A widespread approach, BioID, uses an abortive variant of the E. coli B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82fc4a484bd841b28cad5cab0d3ec5a7
https://doi.org/10.1101/2021.06.16.448656
https://doi.org/10.1101/2021.06.16.448656
Autor:
Lea, Kubitz, Sebastian, Bitsch, Xiyan, Zhao, Kerstin, Schmitt, Lukas, Deweid, Amélie, Roehrig, Elisa Cappio, Barazzone, Oliver, Valerius, Harald, Kolmar, Julien, Béthune
Publikováno v:
Communications biology. 5(1)
Proximity-dependent biotinylation (PDB) combined with mass spectrometry analysis has established itself as a key technology to study protein-protein interactions in living cells. A widespread approach, BioID, uses an abortive variant of the E. coli B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8bd969fc323c9890bccb378a078bf034
https://pubmed.ncbi.nlm.nih.gov/35788163
https://pubmed.ncbi.nlm.nih.gov/35788163
Publikováno v:
Trends in Cell Biology. 29:178-188
Proteins are positioned and act at defined subcellular locations. This is particularly important in eukaryotic cells that deliver proteins to membrane-bound organelles such as the endoplasmic reticulum (ER), mitochondria, or endosomes. It is axiomati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14347847720437b90a5be1c5f28e5604
https://doi.org/10.1016/j.tcb.2018.10.005
https://doi.org/10.1016/j.tcb.2018.10.005
Autor:
Julien Béthune, Stefanie Egetemaier
Publikováno v:
BIOspektrum. 25:45-48
Analytical methods are required to characterize the protein-protein interactions that underlie all biological processes. Beside affinity purification/mass spectrometry approaches, proximity-dependent labeling techniques rely on the biotinylation of i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c59316daf08ba3d1bfab216b6c6c5ac
https://doi.org/10.1007/s12268-019-1004-3
https://doi.org/10.1007/s12268-019-1004-3
Publikováno v:
Methods in Molecular Biology ISBN: 9781071611258
Proximity-dependent labeling techniques such as BioID and APEX2 allow the biotinylation of proteins proximal to a protein of interest in living cells. Following streptavidin pulldown and mass spectrometry analysis, this enables the identification of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::718f9e25aa64bd3a19cb8402d7e393ca
https://doi.org/10.1007/978-1-0716-1126-5_17
https://doi.org/10.1007/978-1-0716-1126-5_17
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2247
Proximity-dependent labeling techniques such as BioID and APEX2 allow the biotinylation of proteins proximal to a protein of interest in living cells. Following streptavidin pulldown and mass spectrometry analysis, this enables the identification of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1226f07394f09a0eef824a9db2427306
https://pubmed.ncbi.nlm.nih.gov/33301125
https://pubmed.ncbi.nlm.nih.gov/33301125
Autor:
Manu Jain Goyal, Michaela Mueller-McNicoll, Cecilia de Heus, Julien Béthune, Mariya Bozhinova, Zhao X, Judith Klumperman, Karla Lisette Andrade-López, Sandra Schulze-Dramac
Coat protein complex I (COPI)-coated vesicles mediate membrane trafficking between Golgi cisternae as well as retrieval of proteins from the Golgi to the endoplasmic reticulum. There are several flavors of the COPI coat defined by paralogous subunits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e13632601383b432fd318519e58a571
https://doi.org/10.1101/2020.01.27.921924
https://doi.org/10.1101/2020.01.27.921924