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Cited by 428

The DOI matches its Crossref record; 158 of the 158 references it cites were found in a registry or an index.

Protein Folding in the Cytoplasm and the Heat Shock Response

Open access
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M., Hartl, F. U.·2010·Cold Spring Harbor Perspectives in Biology

Abstract

Proteins generally must fold into precise three-dimensional conformations to fulfill their biological functions. In the cell, this fundamental process is aided by molecular chaperones, which act in preventing protein misfolding and aggregation. How this machinery assists newly synthesized polypeptide chains in navigating the complex folding energy landscape is now being understood in considerable detail. The mechanisms that ensure the maintenance of a functional proteome under normal and stress conditions are also of great medical relevance, as the aggregation of proteins that escape the cellular quality control underlies a range of debilitating diseases, including many age-of-onset neurodegenerative disorders.

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Crossref · 10.1101/cshperspect.a004390

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Metadata

Authors
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M., & Hartl, F. U.
Venue
Cold Spring Harbor Perspectives in Biology
Published
2010-12-01
Volume
2
Issue
12
Pages
a004390-a004390
ISSN
1943-0264 (ISSN-L)
OpenAlex
W2157013283
Cited by
428
References
158
Type
posted content
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Protein Folding in the Cytoplasm and the Heat Shock Response. https://app.cochat.ai/papers/10.1101/cshperspect.a004390
The paper
Vabulas, R. M., Raychaudhuri, S., Hayer-Hartl, M., & Hartl, F. U. (2010). Protein Folding in the Cytoplasm and the Heat Shock Response. Cold Spring Harbor Perspectives in Biology. https://doi.org/10.1101/cshperspect.a004390

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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