Kang, Dong Min Lukianenko, Nataliia Baik, Ja-Hyun Kim, Yun Kyung Lim, Sungsu 2025-07-18T06:30:59Z 2025-07-18T06:30:59Z 2025-07-18 2025-09 1439-4227 https://pubs.kist.re.kr/handle/201004/152783 Amyloidogenesis is a complex process in which normally soluble proteins misfold and assemble into beta-sheet-rich aggregates known as amyloid fibrils. This pathological process is implicated in a broad range of diseases, including neurodegenerative disorders and systemic amyloidosis. Recent studies indicate that disulfide-crosslinking plays a central role in promoting protein aggregation by stabilizing misfolded intermediates. This review highlights the cellular pathways leading to abnormal disulfide bond formation and examines their impact on disease progression. Additionally, a discussion is made on how disulfide-crosslinked oligomeric species resist degradation, overwhelm proteostasis systems, and serve as precursors for amyloid fibrils. By understanding the role of disulfide crosslinks in protein aggregation, insights into amyloid pathogenesis are gained and potential therapeutic targets for intervention are identified. English John Wiley & Sons Ltd. Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression Article 10.1002/cbic.202500316 1 ChemBioChem, v.26, no.18 ChemBioChem 26 18 Y scie scopus 001518142500001 Biochemistry & Molecular Biology Chemistry, Medicinal Biochemistry & Molecular Biology Pharmacology & Pharmacy Review AMYOTROPHIC-LATERAL-SCLEROSIS ENDOPLASMIC-RETICULUM STRESS ISOMERASE-IMMUNOPOSITIVE INCLUSIONS ANTISENSE OLIGONUCLEOTIDE TOFERSEN SUPEROXIDE-DISMUTASE DOUBLE-BLIND TAU-PROTEIN ALZHEIMERS-DISEASE AMYLOID FORMATION MOUSE MODEL aggregation amyloidogenic protein disulfide-crosslinking oxidation protein folding