Cell Stress and Chaperones

Aims & Scope

Cell Stress and Chaperones is an integrative journal that bridges the gap between laboratory model systems and natural populations.

The journal captures the eclectic spirit of the cellular stress response field in a single, concentrated source of current information.

Major emphasis is placed on the effects of climate change on individual species in the natural environment and their capacity to adapt.

This emphasis expands our focus on stress biology and medicine by linking climate change effects to research on cellular stress responses of animals, micro-organisms and plants.

Metrics & Ranking

Abstracting & Indexing

Journal is indexed in leading academic databases, ensuring global visibility and accessibility of our peer-reviewed research.

• Scopus
• Google Scholar
• Directory of Open Access Journals (DOAJ)
• Web of Science
• Embase

Subjects & Keywords

Journal’s research areas, covering key disciplines and specialized sub-topics in Biochemistry, Genetics and Molecular Biology, designed to support cutting-edge academic discovery.

Licensing & Copyright

This journal operates under an Open Access model. Articles are freely accessible to the public immediately upon publication. The content is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0), allowing users to share and adapt the work with proper attribution.

Copyright remains with the author(s), and no permission is required for non-commercial use, provided the original source is cited.

Policy Links

This section provides access to essential policy documents, guidelines, and resources related to the journal’s publication and submission processes.

• Aims scope
• Homepage
• Oa statement
• Author instructions
• License terms
• Review url
• Board url
• Copyright url
• Plagiarism url
• Preservation url
• Apc url
• License

Plagiarism Policy

This journal follows a plagiarism policy. All submitted manuscripts are screened using reliable plagiarism detection software to ensure originality and academic integrity. Authors are responsible for proper citation and acknowledgment of all sources, and any form of plagiarism, including self-plagiarism, will not be tolerated.

For more details, please refer to our official: Plagiarism Policy.

APC Details

The journal’s Article Processing Charge (APC) policies support open access publishing in Biochemistry, Genetics and Molecular Biology, ensuring accessibility and quality in research dissemination.

This journal requires an Article Processing Charge (APC) to support open access publishing, covering peer review, editing, and distribution. The current APC is 2,850.00 USD. Learn more.

Explore journals without APCs for alternative publishing options.

Most Cited Articles

The Most Cited Articles section features the journal's most impactful research, based on citation counts. These articles have been referenced frequently by other researchers, indicating their significant contribution to their respective fields.

• Guidelines for the nomenclature of the human heat shock proteins

  Citation: 1131

  Authors: Harm H., Jurre, Michel J., Hiroshi, Robert M., Elspeth A., Michael E., Bin, Lawrence E.

• Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications

  Citation: 1112

  Authors: Daniel R., Stuart K.

• &cestflwr; Arabidopsis and the heat stress transcription factor world: how many heat stress transcription factors do we need?

  Citation: 617

  Authors: Lutz, Kapil, Pascal, Shravan Kumar, Arnab, Klaus-Dieter

• Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

  Citation: 499

  Authors: Michael E., Avrom J.

• The human HSP70 family of chaperones: where do we stand?

  Citation: 467

  Authors: Jürgen

• Influence of molecular and chemical chaperones on protein folding

  Citation: 400

  Authors: William J., C. Randell

• CHIP: a link between the chaperone and proteasome systems

  Citation: 377

  Authors: Holly, Cam

• The human genome encodes 10 α-crystallin–related small heat shock proteins: HspB1–10

  Citation: 367

  Authors: Guido, Erik, Pauline, Wilbert C., Jack A. M., Wilfried W.

• Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

  Citation: 333

  Authors: Theodor W., Shiro, Shiro, William, Bridget, David, Leonard M.

• Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein

  Citation: 328

  Authors: C. Randell, Ly Q., Joachim, A. S., William. J