An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control | Zendy

Frederik Eisele | Zendy; Anna Maria Eisele-Bürger | Zendy; Xinxin Hao | Zendy; Lisa Larsson Berglund | Zendy; Johanna L. Höög | Zendy; Beidong Liu | Zendy; Thomas Nyström | Zendy

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An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control

Author(s) -

Frederik Eisele,

Anna Maria Eisele-Bürger,

Xinxin Hao,

Lisa Larsson Berglund,

Johanna L. Höög,

Beidong Liu,

Thomas Nyström

Publication year - 2021

Publication title -

cell reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.264

H-Index - 154

eISSN - 2639-1856

pISSN - 2211-1247

DOI - 10.1016/j.celrep.2021.109328

Subject(s) - endoplasmic reticulum , ubiquitin ligase , chaperone (clinical) , protein folding , ubiquitin , aggresome , hsp90 , microbiology and biotechnology , proteasome , endoplasmic reticulum associated protein degradation , cytosol , protein degradation , ubiquitin protein ligases , organelle , protein quality , unfolded protein response , proteostasis , co chaperone , chemistry , biochemistry , biology , heat shock protein , enzyme , gene , medicine , pathology

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