Inclusion bodies (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Inclusion bodies" in English language version.

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  • Cruts M, Gijselinck I, van der Zee J, Engelborghs S, Wils H, Pirici D, Rademakers R, Vandenberghe R, Dermaut B, Martin JJ, van Duijn C, Peeters K, Sciot R, Santens P, De Pooter T, Mattheijssens M, Van den Broeck M, Cuijt I, Vennekens K, De Deyn PP, Kumar-Singh S, Van Broeckhoven C (24 August 2006). "Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21". Nature. 442 (7105): 920–4. Bibcode:2006Natur.442..920C. doi:10.1038/nature05017. PMID 16862115. S2CID 4423699.

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rarediseases.org

  • "Sporadic Inclusion Body Myositis". NORD (National Organization for Rare Disorders). Retrieved 12 March 2021.

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  • Cruts M, Gijselinck I, van der Zee J, Engelborghs S, Wils H, Pirici D, Rademakers R, Vandenberghe R, Dermaut B, Martin JJ, van Duijn C, Peeters K, Sciot R, Santens P, De Pooter T, Mattheijssens M, Van den Broeck M, Cuijt I, Vennekens K, De Deyn PP, Kumar-Singh S, Van Broeckhoven C (24 August 2006). "Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21". Nature. 442 (7105): 920–4. Bibcode:2006Natur.442..920C. doi:10.1038/nature05017. PMID 16862115. S2CID 4423699.
  • Hardiman O, Al-Chalabi A, Chio A (5 October 2017). "Amyotrophic lateral sclerosis" (PDF). Nature Reviews. Disease Primers. 3: 17071. doi:10.1038/nrdp.2017.71. PMID 28980624. S2CID 1002680. Cite error: The named reference "Hardiman" was defined multiple times with different content (see the help page).
  • Singh SM, Panda AK (1 April 2005). "Solubilization and refolding of bacterial inclusion body proteins". Journal of Bioscience and Bioengineering. 99 (4): 303–310. doi:10.1263/jbb.99.303. PMID 16233795. S2CID 24807019. Inclusion bodies are dense electron-refractile particles of aggregated protein found in both the cytoplasmic and periplasmic spaces of E. coli during high-level expression of heterologous protein. It is generally assumed that high level expression of non-native protein (higher than 2% of cellular protein) and highly hydrophobic protein is more prone to lead to accumulation as inclusion bodies in E. coli. In the case of proteins having disulfide bonds, formation of protein aggregates as inclusion bodies is anticipated since the reducing environment of bacterial cytosol inhibits the formation of disulfide bonds. The diameter of spherical bacterial inclusion bodies varies from 0.5–1.3 μm and the protein aggregates have either an amorphous or paracrystalline nature depending on the localization. Inclusion bodies have higher density (~1.3 mg ml−1) than many of the cellular components, and thus can be easily separated by high-speed centrifugation after cell disruption. Inclusion bodies, despite being dense particles, are highly hydrated and have a porous architecture.
  • Rosenzweig R, Nillegoda NB, Mayer MP, Bukau B (November 2019). "The Hsp70 chaperone network". Nature Reviews. Molecular Cell Biology. 20 (11): 665–680. doi:10.1038/s41580-019-0133-3. ISSN 1471-0080. PMID 31253954. S2CID 195739183.
  • Ross, Poirier (2004). "Protein aggregation and neurodegenerative disease". Nature Medicine. 10 Suppl: S10-7. doi:10.1038/nm1066. PMID 15272267. S2CID 205383483.
  • Waugh DS (2016). "The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein". Postepy Biochemii. 62 (3): 377–382. doi:10.18388/pb.2016_41. ISSN 0032-5422. PMID 28132493. S2CID 23539643.

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