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  Agglomeration: when folded proteins clump together.

Romero-Romero, M. L., & Garcia-Seisdedos, H. (2023). Agglomeration: when folded proteins clump together. Biophysical reviews, 15(6), 1987-2003. doi:10.1007/s12551-023-01172-4.

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 Creators:
Romero-Romero, M. Luisa1, Author           
Garcia-Seisdedos, H, Author
Affiliations:
1Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 Abstract: Protein self-association is a widespread phenomenon that results in the formation of multimeric protein structures with critical roles in cellular processes. Protein self-association can lead to finite protein complexes or open-ended, and potentially, infinite structures. This review explores the concept of protein agglomeration, a process that results from the infinite self-assembly of folded proteins. We highlight its differences from other better-described processes with similar macroscopic features, such as aggregation and liquid-liquid phase separation. We review the sequence, structural, and biophysical factors influencing protein agglomeration. Lastly, we briefly discuss the implications of agglomeration in evolution, disease, and aging. Overall, this review highlights the need to study protein agglomeration for a better understanding of cellular processes.

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 Dates: 2023-12-01
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1007/s12551-023-01172-4
Other: cbg-8667
PMID: 38192350
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Title: Biophysical reviews
  Other : Biophys Rev
Source Genre: Journal
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Pages: - Volume / Issue: 15 (6) Sequence Number: - Start / End Page: 1987 - 2003 Identifier: -