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Jul 20, 2011 · We define a molecular chaperone as any protein that interacts with, ... (K agg > K on ≥ K fold), unless chaperone expression is induced via the stress-response pathway. Structures in this figure ...
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Apr 1, 2015 · Molecular chaperones are necessary for protein folding in cells. For most proteins to perform their functions in cells, they should form their native structures, which are coded in their amino acid sequences. Thus, the formation of protein structure (protein folding) is an essential process in all living organisms.
- Fumihiro Motojima
- 10.2142/biophysics.11.93
- 2015
- Biophysics (Nagoya-shi). 2015; 11: 93-102.
Dec 22, 2017 · A chaperone is defined by its ability to bind and help fold client proteins and prevent the aggregation of proteins in the cytoplasm [7,9,56]. Co-chaperones are non-client proteins that assist chaperones in protein folding and stimulate the ATP cycling of molecular chaperones [57,58]. As assembly factors, chaperones also aid in the building of ...
- Casey Carlisle, Kendal Prill, Dave Pilgrim
- 10.3390/ijms19010032
- 2017
- Int J Mol Sci. 2018 Jan; 19(1): 32.
Apr 12, 2021 · Moreover, human chaperone genes that were at least 2-fold differentially expressed in skeletal muscle by GTEx were also enriched for C. elegans muscle chaperones (Fig. 3e), and for chaperones ...
- Netta Shemesh, Juman Jubran, Shiran Dror, Eyal Simonovsky, Omer Basha, Chanan Argov, Idan Hekselman,...
- 2021
Jun 14, 2021 · A chaperone is shown in green. The chaperone features a chaotropic pocket to bind and stabilize the protein, protecting it from premature hydrophobic collapse into a misfolded state and allowing it to explore the conformational space. The protein may fold into its native structure on the chaperone surface or upon release.
- Jakub Macošek, Guillaume Mas, Sebastian Hiller
- 10.3389/fmolb.2021.683132
- 2021
- Front Mol Biosci. 2021; 8: 683132.
Sep 12, 2013 · Chaperones are heavy-duty molecular machines that assist nascent proteins to reach their native fold but also mediate unfolding and prevent the accumulation of toxic protein aggregates. There is ...
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What is a molecular chaperone?
For example, O-mannosylation can terminate folding attempts of difficult-to-fold substrates, thus liberating the chaperone from futile cycles and limiting ATP consumption. 229 It is, therefore, intriguing that budding yeast also contain enzymes to trim glucose from core glycans, but they lack UGGT. This feature similarly frees this rapidly ...
