With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintain protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triag...
Saved in:
Main Authors: | Selin Altinok, Rebekah Sanchez-Hodge, Mariah Stewart, Kaitlan Smith, Jonathan C. Schisler |
---|---|
Format: | article |
Language: | EN |
Published: |
MDPI AG
2021
|
Subjects: | |
Online Access: | https://doaj.org/article/a45b39cdebdc4eadbbfe89c4641cfb01 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Interplay between the Hsp90 Chaperone and the HslVU Protease To Regulate the Level of an Essential Protein in <named-content content-type="genus-species">Shewanella oneidensis</named-content>
by: Flora Ambre Honoré, et al.
Published: (2019) -
The Chaperone and Redox Properties of CnoX Chaperedoxins Are Tailored to the Proteostatic Needs of Bacterial Species
by: Camille V. Goemans, et al.
Published: (2018) -
Ins and Outs of Heat Shock Proteins in Colorectal Carcinoma: Its Role in Carcinogenesis and Therapeutic Perspectives
by: Batoul Abi Zamer, et al.
Published: (2021) -
A Heat Shock Protein 48 (HSP48) Biomolecular Condensate Is Induced during <named-content content-type="genus-species">Dictyostelium discoideum</named-content> Development
by: Stephanie Santarriaga, et al.
Published: (2019) -
Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding
by: Motonori Matsusaki, et al.
Published: (2021)