Lee, C Yu, MH 2024-01-21T05:02:50Z 2024-01-21T05:02:50Z 2021-09-03 2005-05-31 1225-8687 https://pubs.kist.re.kr/handle/201004/136451 For most of proteins to be active, they need well-defined three-dimensional structures alone or in complex. Folding is a process through which newly synthesized proteins get to the native state. Protein folding inside cells is assisted by various chaperones and folding factors, and misfolded proteins are eliminated by the ubiquitin-proteasome degradation system to ensure high fidelity of protein expression. Under certain circumstances, misfolded proteins escape the degradation process, yielding to deposit of protein aggregates such as loop-sheet polymer and amyloid fibril. Diseases characterized by insoluble deposits of proteins have been recognized for long time and are grouped as conformational diseases. Study of protein folding mechanism is required for better understanding of the molecular pathway of such conformational diseases. English SPRINGER SINGAPORE PTE LTD MOLECULAR CHAPERONES ENDOPLASMIC-RETICULUM IN-VIVO HSP70 CHAPERONES AMYLOID FIBRILS QUALITY-CONTROL PEPTIDE AGGREGATION MECHANISM DNAK Protein folding and diseases Article 1 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.38, no.3, pp.275 - 280 JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY 38 3 275 280 scie scopus kci ART001108143 000229491300003 2-s2.0-25444485718 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Review MOLECULAR CHAPERONES ENDOPLASMIC-RETICULUM IN-VIVO HSP70 CHAPERONES AMYLOID FIBRILS QUALITY-CONTROL PEPTIDE AGGREGATION MECHANISM DNAK amyloid fibril chaperone conformational disease protein folding protein misfolding