{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:36:53Z","timestamp":1791329813392,"version":"4.3.1"},"reference-count":72,"publisher":"The Company of Biologists","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,1,1]]},"abstract":"<jats:p>For a protein to function appropriately, it must first achieve its proper conformation and location within the crowded environment inside the cell. Multiple chaperone systems are required to fold proteins correctly. In addition, degradation pathways participate by destroying improperly folded proteins. The intricacy of this multisystem process provides many opportunities for error. Furthermore, mutations cause misfolded, nonfunctional forms of proteins to accumulate. As a result, many pathological conditions are fundamentally rooted in the protein-folding problem that all cells must solve to maintain their function and integrity. Here, to illustrate the breadth of this phenomenon, we describe five examples of protein-misfolding events that can lead to disease: improper degradation, mislocalization, dominant-negative mutations, structural alterations that establish novel toxic functions, and amyloid accumulation. In each case, we will highlight current therapeutic options for battling such diseases.<\/jats:p>","DOI":"10.1242\/dmm.013474","type":"journal-article","created":{"date-parts":[[2014,1,6]],"date-time":"2014-01-06T16:29:28Z","timestamp":1389025768000},"page":"9-14","source":"Crossref","is-referenced-by-count":283,"title":["Mechanisms of protein-folding diseases at a glance"],"prefix":"10.1242","volume":"7","author":[{"given":"Julie S.","family":"Valastyan","sequence":"first","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA."},{"name":"Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan","family":"Lindquist","sequence":"additional","affiliation":[{"name":"Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA."},{"name":"Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA."},{"name":"Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042513042590700_b1-0070009","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1016\/S0140-6736(02)08273-9","article-title":"Protective effects of the sickle cell gene against malaria morbidity and mortality","volume":"359","author":"Aidoo","year":"2002","journal-title":"Lancet"},{"key":"2021042513042590700_b2-0070009","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1091\/mbc.11.5.1585","article-title":"Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck)","volume":"11","author":"Bijlmakers","year":"2000","journal-title":"Mol. 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