Protein Folding and Misfolding Implications for Disease and Therapeutics

Authors

  • Akshita Jain Students, Dayalbagh Educational Institute
  • Pallavi Tyagi Students, Dayalbagh Educational Institute

Abstract

Protein folding is a highly orchestrated process crucial for maintaining cellular homeostasis. However, aberrant protein folding can lead to misfolding, resulting in the accumulation of misfolded proteins and contributing to the pathogenesis of various diseases. This review explores the intricate mechanisms of protein folding, the consequences of misfolding, and the therapeutic strategies aimed at addressing protein misfolding disorders.

How to cite this article:
Jain A, Tyagi P. Protein Folding and Misfolding
Implications for Disease and Therapeutics. J Durg
Dis Dev 2023; 7(2): 21-26.

References

Anfinsen, C. B. (1973). Principles that Govern the Folding of Protein Chains. Science, 181(4096), 223–230.

Dobson, C. M. (2003). Protein folding and misfolding. Nature, 426(6968), 884–890.

Hartl, F. U., & Hayer-Hartl, M. (2009). Converging concepts of protein folding in vitro and in vivo. Nature Structural & Molecular Biology, 16(6), 574–581.

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science, 319(5865), 916–919.

Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333–366.

Fink, A. L. (1999). Chaperone-mediated protein folding. Physiological Reviews, 79(2), 425–449.

Walter, S., & Buchner, J. (2002). Molecular chaperones— cellular machines for protein folding. Angewandte Chemie International Edition, 41(7), 1098–1113.

Selkoe, D. J. (2003). Folding proteins in fatal ways. Nature, 426(6968), 900–904.

Uversky, V. N. (2017). Intrinsically disordered proteins in overcrowded milieu: Membrane-less organelles, phase separation, and intrinsic disorder. Current Opinion in Structural Biology, 44, 18–30.

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., ... & Stefani, M. (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature, 416(6880), 507–511.

Wang, S. S., Liu, K. N., Yang, A. K., & Sun, Y. (2016). Protein misfolding and aggregation in Alzheimer’s disease. Cellular and Molecular Neurobiology, 36(2), 203–213.

Knowles, T. P., Vendruscolo, M., & Dobson, C. M. (2014). The amyloid state and its association with protein misfolding diseases. Nature Reviews Molecular Cell Biology, 15(6), 384–396.

Fontana, A., de Laureto, P. P., Spolaore, B., Frare, E., & Picotti, P. (2004). Protein folding and misfolding in the cell. The Quarterly Review of Biophysics, 37(4), 337–397.

Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006). Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science, 311(5766), 1471–1474.

Lindquist, S., & Kelly, J. W. (2011). Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases—progress and prognosis. Cold Spring Harbor Perspectives in Biology, 3(9), a004507.

Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002). Toxic proteins in neurodegenerative disease. Science, 296(5575), 1991–1995.

Ross, C. A., & Poirier, M. A. (2004). Protein aggregation and neurodegenerative disease. Nature Medicine, 10(S7), S10–S17.

Nussbaum-Krammer, C. I., & Morimoto, R. I. (2014). Caenorhabditis elegans as a model system for studying non-cell-autonomous mechanisms in proteinmisfolding diseases. Disease Models & Mechanisms, 7(1), 31–39.

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Published

2023-12-31

How to Cite

Jain, A., & Tyagi, P. . (2023). Protein Folding and Misfolding Implications for Disease and Therapeutics. Journal of Drug Discovery and Development ( ISSN:2581-6861), 7(2), 21-26. Retrieved from http://medicaljournalshouse.com/index.php/JDrug-Discovery-Development/article/view/1084