The DOI matches its Crossref record; 187 of the 187 references it cites were found in a registry or an index.
Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases
Open accessAbstract
SUMMARY: Increased synthesis of heat shock proteins (hsp) occurs in prokaryotic and eukaryotic cells when they are exposed to stress. By increasing their hsp content, cells protect themselves from lethal assaults, primarily because hsp interfere with the uncontrolled protein unfolding that occurs under stress. However, hsp are not produced only by stressed cells; some hsp are synthesized constitutively and perform important housekeeping functions. Accordingly, hsp are involved in the assembly of molecules which play important roles in the immune system. It is not surprising that due to their wide distribution and their homology among different species, hsp represent target antigens of the immune response. Frequent confrontation of the immune system with conserved regions of hsp which are shared by various microbial pathogens can potentiate antimicrobial immunity. However, long-term confrontation of the immune system with hsp antigens which are similar in the host and invaders may convert the immune response against these host antigens and promote autoimmune disease. This review provides an overview of the role of hsp in immunity with a focus on infectious and autoimmune diseases.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mosmann, T. R., & Coffman, R. L. (1989) · Annual Review of Immunology · doi:10.1146/annurev.iy.07.040189.001045 · Cited by 7,692
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,568
CD28/B7 SYSTEM OF T CELL COSTIMULATION
Lenschow, D. J., Walunas, T. L., & Bluestone, J. A. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.233 · Cited by 2,717
Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
Brown, J. H., Jardetzky, T. S., Gorga, J. C., Stern, L. J., Urban, R. G., Strominger, J. L., & Wiley, D. C. (1993) · Nature · doi:10.1038/364033a0 · Cited by 2,379
Speculations on the functions of the major heat shock and glucose-regulated proteins
Pelham, H. R. B. (1986) · Cell · doi:10.1016/0092-8674(86)90693-8 · Cited by 1,546
The Role of the CD28 Receptor During T Cell Responses to Antigen
Linsley, P. S., & Ledbetter, J. A. (1993) · Annual Review of Immunology · doi:10.1146/annurev.iy.11.040193.001203 · Cited by 1,298
The Biology of heat shock proteins and molecular chaperones.
Morimoto, R. I., Tissieres, A., & Georgopoulos, C. P. (1994) · Cold Spring Harbor Laboratory eBooks · Cited by 1,243
Recognition of Stress-Induced MHC Molecules by Intestinal Epithelial γδ T Cells
Groh, V., Steinle, A., Bauer, S., & Spies, T. (1998) · Science · doi:10.1126/science.279.5357.1737 · Cited by 1,142
Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent.
Fields, P. I., Swanson, R. V., Haidaris, C. G., & Heffron, F. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.14.5189 · Cited by 1,114
Role of the Major Heat Shock Proteins as Molecular Chaperones
Georgopoulos, C., & Welch, W. J. (1993) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.09.110193.003125 · Cited by 1,096
Cited by
Roles of Heat Shock Proteins in Apoptosis, Oxidative Stress, Human Inflammatory Diseases, and Cancer
Ikwegbue, P., Masamba, P., Oyinloye, B., & Kappo, A. (2017) · Pharmaceuticals · doi:10.3390/ph11010002 · Cited by 323
Johnson, J. D., & Fleshner, M. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0905523 · Cited by 251
GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.
Hennequin, C., Collignon, A., Bourlioux, P., Waligora-Dupriet, A.-J., Karjalainen, T., Barc, M.-C., & Porcheray, F. (2001) · Microbiology · doi:10.1099/00221287-147-1-87 · Cited by 226
Heat-shock proteins and the host-pathogen interaction during bacterial infection.
Stewart, G. R., & Young, D. B. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2004.05.007 · Cited by 79
Metadata
- Authors
- Zügel, U., & Kaufmann, S. H. E.
- Venue
- Clinical Microbiology Reviews
- Publisher
- American Society for Microbiology
- Published
- 1999-01
- Volume
- 12
- Issue
- 1
- Pages
- 19-39
- ISSN
- 0893-8512 (ISSN-L)
- 1098-6618
- OpenAlex
- W2137799085
- Cited by
- 559
- References
- 187
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases. https://app.cochat.ai/papers/10.1128/cmr.12.1.19
- The paper
- Zügel, U., & Kaufmann, S. H. E. (1999). Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases. Clinical Microbiology Reviews. https://doi.org/10.1128/cmr.12.1.19
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
