The cryo-EM resolution revolution and transcription complexes

Autor: Hanske, Jonas, Sadian, Yashar, Müller, Christoph W

Publikováno v: In Current Opinion in Structural Biology October 2018 52:8-15

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The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Autor: Bhattacharya, Kaushik, Weidenauer, Lorenz, Luengo, Tania Morán, Pieters, Ellis C., Echeverría, Pablo C., Bernasconi, Lilia, Wider, Diana, Sadian, Yashar, Koopman, Margreet B., Villemin, Matthieu, Bauer, Christoph, Rüdiger, Stefan G. D., Quadroni, Manfredo, Picard, Didier

Publikováno v: Nature communications, vol. 11, no. 1, pp. 5975
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-21 (2020)
Nature Communications, Vol. 11, No 5975 (2020)

Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86f0303de9d74f104f895a228e479a13
https://serval.unil.ch/notice/serval:BIB_A3C58F977248

Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction.

Autor: Tüting, Christian, Kyrilis, Fotis L., Müller, Johannes, Sorokina, Marija, Skalidis, Ioannis, Hamdi, Farzad, Sadian, Yashar, Kastritis, Panagiotis L.

Publikováno v: Nature Communications; 11/26/2021, Vol. 12 Issue 1, p1-13, 13p