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Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase

Refolding aggregated proteins is essential in combating cellular proteotoxic stress. Together with Hsp70, Hsp100 chaperones, including Escherichia coli ClpB, form a powerful disaggregation machine that threads aggregated polypeptides through the central pore of tandem adenosine triphosphatase (ATPas...

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Dettagli Bibliografici
Pubblicato in:Sci Adv
Autori principali: Deville, Célia, Carroni, Marta, Franke, Kamila B., Topf, Maya, Bukau, Bernd, Mogk, Axel, Saibil, Helen R.
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Association for the Advancement of Science 2017
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC5544394/
https://ncbi.nlm.nih.gov/pubmed/28798962
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1126/sciadv.1701726
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