No structure, no problem: Protein stabilization by Hero proteins and other chaperone-like IDPs

• Published in: Biochimica et biophysica acta. General subjects Vol. 1869; no. 6; p. 130786
• Main Authors: Lam, Andy Y.W., Tomari, Yukihide, Tsuboyama, Kotaro
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2025
• Subjects: Animals; Chaperone-like IDPs; Heat-resistant obscure (Hero) proteins; Humans; Intrinsically disordered proteins (IDPs); Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Molecular Chaperones - chemistry; Molecular Chaperones - metabolism; Protein aggregation; Protein chaperones; Protein Folding; Protein Stability; Protein stabilization; Intrinsically disordered proteins (IDPs); Heat-resistant obscure (Hero) proteins; Protein aggregation; Chaperone-like IDPs; Protein chaperones; Protein stabilization

In order for a protein to function, it must fold into its proper three-dimensional structure. Otherwise, improperly folded proteins are typically prone to aggregate through a process that is detrimental to cellular health. It is widely known that a diverse group of proteins, called molecular chapero...