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of 4
pro vyhledávání: '"Isabel Myriam Schopp"'
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:
Merle Skribbe, Elisa Kreibich, Klemens Wild, Cinthia Claudia Amaya Ramirez, Julien Béthune, Jerneja Debeljak, Isabel Myriam Schopp
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
Nature Communications
Nature Communications
Understanding the function of the thousands of cellular proteins is a central question in molecular cell biology. As proteins are typically part of multiple dynamic and often overlapping macromolecular complexes exerting distinct functions, the ident
Autor:
Julien Béthune, Isabel Myriam Schopp
Publikováno v:
Journal of Visualized Experiments.
To complement existing affinity purification (AP) approaches for the identification of protein-protein interactions (PPI), enzymes have been introduced that allow the proximity-dependent labeling of proteins in living cells. One such enzyme, BirA* (u
Publikováno v:
Molecular Cell
Summary ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known. Here we identify a number of endogenous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f3131a364e0c651a23a58f1d460add6
https://eprints.gla.ac.uk/82455/1/82455.pdf
https://eprints.gla.ac.uk/82455/1/82455.pdf