The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
Protein Misfolding and Human Disease
Abstract
Protein misfolding is a common event in living cells. In young and healthy cells, the misfolded protein load is disposed of by protein quality control (PQC) systems. In aging cells and in cells from certain individuals with genetic diseases, the load may overwhelm the PQC capacity, resulting in accumulation of misfolded proteins. Dependent on the properties of the protein and the efficiency of the PQC systems, the accumulated protein may be degraded or assembled into toxic oligomers and aggregates. To illustrate this concept, we discuss a number of very different protein misfolding diseases including phenylketonuria, Parkinson's disease, α-1-antitrypsin deficiency, familial neurohypophyseal diabetes insipidus, and short-chain acyl-CoA dehydrogenase deficiency. Despite the differences, an emerging paradigm suggests that the cellular effects of protein misfolding provide a common framework that may contribute to the elucidation of the cell pathology and guide intervention and treatment strategies of many genetic and age-dependent diseases.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
SIFT: predicting amino acid changes that affect protein function
Ng, P. C. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg509 · Cited by 6,577
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,237
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,678
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,026
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
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Olzmann, J. A., Li, L., Chudaev, M. V., Chen, J., Perez, F. A., Palmiter, R. D., & Chin, L.-S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611128 · Cited by 339
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Chung, Y. J., Kim, J., & Park, C. B. (2020) · ACS Nano · doi:10.1021/acsnano.0c02114 · Cited by 299
ABCA4 disease progression and a proposed strategy for gene therapy
Cideciyan, A. V., Swider, M., Aleman, T. S., Tsybovsky, Y., Schwartz, S. B., Windsor, E. A. M., Roman, A. J., Sumaroka, A., Steinberg, J. D., Jacobson, S. G., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn421 · Cited by 186
A novel small molecule chaperone of rod opsin and its potential therapy for retinal degeneration
Chen, Y., Chen, Y., Jastrzebska, B., Golczak, M., Gulati, S., Tang, H., Seibel, W., Li, X., Jin, H., Han, Y., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04261-1 · Cited by 64
Metadata
- Authors
- Gregersen, N., Bross, P., Vang, S., & Christensen, J. H.
- Venue
- Annual Review of Genomics and Human Genetics
- Publisher
- Annual Reviews
- Published
- 2006-09-01
- Volume
- 7
- Issue
- 1
- Pages
- 103-124
- ISSN
- 1527-8204 (ISSN-L)
- 1545-293X
- OpenAlex
- W2113635620
- Cited by
- 301
- References
- 105
- FWCI
- 0.82
- Type
- journal article
- Language
- en
- Open access
- closed
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- Gregersen, N., Bross, P., Vang, S., & Christensen, J. H. (2006). Protein Misfolding and Human Disease. Annual Review of Genomics and Human Genetics. https://doi.org/10.1146/annurev.genom.7.080505.115737
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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.
