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Protein Misfolding Disorders

Known as: Protein Folding Disease, Misfolding Diseases, Protein, Protein Misfolding Disease 
Disorders caused by dysfunctions in PROTEIN FOLDING and degradation or clearance of misfolded proteins.
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

Proteostasis Deficiencies

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2015
2015
Amyloidogenicity of p53: A Hidden Link Between Protein Misfolding and Cancer.
Pathogenic aggregation is closely associated with various protein misfolding diseases such as type 2 diabetes mellitusand… 
Review
2013
Review
2013
Recent developments in targeting protein misfolding diseases.
Highly Cited
2012
Highly Cited
2012
Phase networks of cross-β peptide assemblies.
Recent evidence suggests that simple peptides can access diverse amphiphilic phases, and that these structures underlie the… 
2011
2011
Bortezomib for AL amyloidosis: moving forward.
Reece et al report that single-agent bortezomib resulted in hematologic responses in two-thirds of patients with relapsed Light… 
Highly Cited
2010
Highly Cited
2010
Direct observation of nucleation and growth in amyloid self-assembly.
Access to native protein structure depends on precise polypeptide folding and assembly pathways. Identifying folding missteps… 
Highly Cited
2009
Highly Cited
2009
Biochemical and Mechanical Dysfunction in a Mouse Model of Desmin-Related Myopathy
An R120G mutation in &agr;B-crystallin (CryABR120G) causes desmin-related myopathy (DRM). In mice with cardiomyocyte-specific… 
Highly Cited
2009
Highly Cited
2009
Novel Transthyretin Amyloid Fibril Formation Inhibitors: Synthesis, Biological Evaluation, and X-Ray Structural Analysis
Transthyretin (TTR) is one of thirty non-homologous proteins whose misfolding, dissociation, aggregation, and deposition is… 
2009
2009
Characterizing antibody specificity to different protein morphologies by AFM.
Protein misfolding and aggregation can lead to several neurodegenerative diseases including Alzheimer's Disease (AD), Parkinson's… 
Highly Cited
2003
Highly Cited
2003
Identification of an N-domain Histidine Essential for Chaperone Function in Calreticulin*
Calreticulin is an endoplasmic reticulum (ER) luminal Ca2+-binding chaperone involved in folding of newly synthesized… 
Review
2002
Review
2002
Amyloid fibril proteins
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