A survey of protein interactions and posttranslational modifications that influence the polyglutamine diseases
The presence and aggregation of misfolded proteins has deleterious effects in the nervous
system. Among the various diseases caused by misfolded proteins is the family of the …
system. Among the various diseases caused by misfolded proteins is the family of the …
Neurotoxic protein oligomerisation associated with polyglutamine diseases
SL Hands, A Wyttenbach - Acta neuropathologica, 2010 - Springer
Polyglutamine (polyQ) diseases are associated with a CAG/polyQ expansion mutation in
unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate …
unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate …
Polyglutamine disorders: Pathogenesis and potential drug interventions
S Tandon, P Aggarwal, S Sarkar - Life Sciences, 2024 - Elsevier
Polyglutamine/poly (Q) diseases are a group nine hereditary neurodegenerative disorders
caused due to abnormally expanded stretches of CAG trinucleotide in functionally distinct …
caused due to abnormally expanded stretches of CAG trinucleotide in functionally distinct …
Therapeutic approaches to polyglutamine diseases: combating protein misfolding and aggregation
M Herbst, EE Wanker - Current pharmaceutical design, 2006 - ingentaconnect.com
Polyglutamine diseases are autosomal dominant, late-onset neurodegenerative disorders.
Expansion of a polyglutamine (polyQ) tract above a threshold size leads to misfolding and …
Expansion of a polyglutamine (polyQ) tract above a threshold size leads to misfolding and …
Towards the treatment of polyglutamine diseases: the modulatory role of protein context
AL Robertson, SP Bottomley - Current medicinal chemistry, 2010 - ingentaconnect.com
Protein aggregation is a key mechanism involved in neurodegeneration associated with
Alzheimer's, Parkinson's and Huntington's diseases. Nine diseases (including Huntington's) …
Alzheimer's, Parkinson's and Huntington's diseases. Nine diseases (including Huntington's) …
Flanking sequences profoundly alter polyglutamine toxicity in yeast
ML Duennwald, S Jagadish… - Proceedings of the …, 2006 - National Acad Sciences
Protein misfolding is the molecular basis for several human diseases. How the primary
amino acid sequence triggers misfolding and determines the benign or toxic character of the …
amino acid sequence triggers misfolding and determines the benign or toxic character of the …
Protein misfolding and aggregation as a therapeutic target for polyglutamine diseases
T Takeuchi, Y Nagai - Brain sciences, 2017 - mdpi.com
The polyglutamine (polyQ) diseases, such as Huntington's disease and several types of
spinocerebellar ataxias, are a group of inherited neurodegenerative diseases that are …
spinocerebellar ataxias, are a group of inherited neurodegenerative diseases that are …
Therapeutic opportunities in polyglutamine disease
Polyglutamine diseases comprise a class of familial neurodegenerative disorders caused by
expression of proteins containing expanded polyglutamine tracts. Great progress has been …
expression of proteins containing expanded polyglutamine tracts. Great progress has been …
Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity
The polyglutamine (polyQ) diseases are a class of inherited neurodegenerative diseases
including Huntington's disease, caused by the expansion of a polyQ stretch within each …
including Huntington's disease, caused by the expansion of a polyQ stretch within each …
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
H Sakahira, P Breuer… - Proceedings of the …, 2002 - National Acad Sciences
The formation of insoluble protein aggregates in neurons is a hallmark of neurodegenerative
diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the …
diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the …
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