Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Sebastian M. Richter"'
SUMO's Intrinsically Disordered N-Terminus is an Intramolecular Inhibitor of SUMO - SIM Interactions
Publikováno v:
SSRN Electronic Journal.
Small Ubiquitin-related modifiers of the SUMO family are known to regulate thousands of proteins in eukaryotic cells. How specificity is achieved in target selection, in SUMO paralogue choice and in SUMO-dependent interactions is poorly understood. F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44df0caca4f2cd1c9617f4abf88cdb72
https://doi.org/10.2139/ssrn.3554087
https://doi.org/10.2139/ssrn.3554087
Publikováno v:
The EMBO Journal. 31:1518-1528
In eukaryotic cells, Hsp90 chaperones assist late folding steps of many regulatory protein clients by a complex ATPase cycle. Binding of clients to Hsp90 requires prior interaction with Hsp70 and a transfer reaction that is mediated by the co-chapero
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3072f29ceda6363d658849664394e711
https://doi.org/10.1038/emboj.2012.37
https://doi.org/10.1038/emboj.2012.37
Publikováno v:
Journal of Biological Chemistry
The SUMO E3 ligase complex RanBP2/RanGAP1*SUMO1/Ubc9 localizes at cytoplasmic nuclear pore complex (NPC) filaments and is a docking site in nucleocytoplasmic transport. RanBP2 has four Ran binding domains (RBDs), two of which flank RanBP2's E3 ligase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9ca9155cfa8e01fa9474ee6e176ce33
https://pubmed.ncbi.nlm.nih.gov/26251516
https://pubmed.ncbi.nlm.nih.gov/26251516