Abstract
Human misfolding diseases result from the failure of proteins to reach their active state or from the accumulation of aberrantly folded proteins. The mechanisms by which molecular chaperones influence the development of these diseases is beginning to be understood. Mutations that compromise the activity of chaperones lead to several rare syndromes. In contrast, the more frequent amyloid-related neurodegenerative diseases are caused by a gain of toxic function of misfolded proteins. Toxicity in these disorders may result from an imbalance between normal chaperone capacity and production of dangerous protein species. Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 17-29 |
| Number of pages | 13 |
| Journal | Seminars in Cell and Developmental Biology |
| Volume | 15 |
| Issue number | 1 |
| DOIs | |
| State | Published - Feb 2004 |
| Externally published | Yes |
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Keywords
- Amyloid
- Misfolding diseases
- Molecular chaperones
- Polyglutamine diseases
- Ubiquitin-proteasome system
ASJC Scopus subject areas
- Developmental Biology
Cite this
Roles of molecular chaperones in protein misfolding diseases. / Barral, José M.; Broadley, Sarah A.; Schaffar, Gregor; Hartl, F. Ulrich.
In: Seminars in Cell and Developmental Biology, Vol. 15, No. 1, 02.2004, p. 17-29.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Roles of molecular chaperones in protein misfolding diseases
AU - Barral, José M.
AU - Broadley, Sarah A.
AU - Schaffar, Gregor
AU - Hartl, F. Ulrich
PY - 2004/2
Y1 - 2004/2
N2 - Human misfolding diseases result from the failure of proteins to reach their active state or from the accumulation of aberrantly folded proteins. The mechanisms by which molecular chaperones influence the development of these diseases is beginning to be understood. Mutations that compromise the activity of chaperones lead to several rare syndromes. In contrast, the more frequent amyloid-related neurodegenerative diseases are caused by a gain of toxic function of misfolded proteins. Toxicity in these disorders may result from an imbalance between normal chaperone capacity and production of dangerous protein species. Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies.
AB - Human misfolding diseases result from the failure of proteins to reach their active state or from the accumulation of aberrantly folded proteins. The mechanisms by which molecular chaperones influence the development of these diseases is beginning to be understood. Mutations that compromise the activity of chaperones lead to several rare syndromes. In contrast, the more frequent amyloid-related neurodegenerative diseases are caused by a gain of toxic function of misfolded proteins. Toxicity in these disorders may result from an imbalance between normal chaperone capacity and production of dangerous protein species. Increased chaperone expression can suppress the neurotoxicity of these molecules, suggesting possible therapeutic strategies.
KW - Amyloid
KW - Misfolding diseases
KW - Molecular chaperones
KW - Polyglutamine diseases
KW - Ubiquitin-proteasome system
UR - http://www.scopus.com/inward/record.url?scp=0842303213&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0842303213&partnerID=8YFLogxK
U2 - 10.1016/j.semcdb.2003.12.010
DO - 10.1016/j.semcdb.2003.12.010
M3 - Article
VL - 15
SP - 17
EP - 29
JO - Seminars in Cell and Developmental Biology
JF - Seminars in Cell and Developmental Biology
SN - 1084-9521
IS - 1
ER -