The therapeutic potential of chemical chaperones in protein folding diseases
Several neurodegenerative diseases are caused by defects in protein folding, including
Alzheimer, Parkinson, Huntington, and prion diseases. Once a disease-specific protein …
Alzheimer, Parkinson, Huntington, and prion diseases. Once a disease-specific protein …
Survey of the year 2007 commercial optical biosensor literature
RL Rich, DG Myszka - Journal of Molecular Recognition: An …, 2008 - Wiley Online Library
In 2007, 1179 papers were published that involved the application of optical biosensors.
Reported developments in instrument hardware, assay design, and immobilization …
Reported developments in instrument hardware, assay design, and immobilization …
Targeting biomolecular flexibility with metadynamics
Metadynamics calculations allow investigating structure, plasticity, and energetics in a
variety of biological processes spanning from molecular docking to protein folding. Recent …
variety of biological processes spanning from molecular docking to protein folding. Recent …
Theoretical study of the prion protein based on the fragment molecular orbital method
T Ishikawa, T Ishikura, K Kuwata - Journal of computational …, 2009 - Wiley Online Library
We performed fragment molecular orbital (FMO) calculations to examine the molecular
interactions between the prion protein (PrP) and GN8, which is a potential curative agent for …
interactions between the prion protein (PrP) and GN8, which is a potential curative agent for …
[HTML][HTML] Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43)
A Shodai, T Morimura, A Ido, T Uchida, T Ayaki… - Journal of Biological …, 2013 - ASBMB
Aggregation of TAR DNA-binding protein of 43 kDa (TDP-43) is a pathological signature of
amyotrophic lateral sclerosis (ALS). Although accumulating evidence suggests the …
amyotrophic lateral sclerosis (ALS). Although accumulating evidence suggests the …
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding
MW van der Kamp, V Daggett - Journal of molecular biology, 2010 - Elsevier
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
and aggregation of the prion protein PrP. These diseases can be hereditary in humans and …
Protein misfolding diseases and therapeutic approaches
Protein folding is the process by which a polypeptide chain acquires its functional, native 3D
structure. Protein misfolding, on the other hand, is a process in which protein fails to fold into …
structure. Protein misfolding, on the other hand, is a process in which protein fails to fold into …
FK506 reduces abnormal prion protein through the activation of autolysosomal degradation and prolongs survival in prion-infected mice
T Nakagaki, K Satoh, D Ishibashi, T Fuse, K Sano… - Autophagy, 2013 - Taylor & Francis
Prion diseases are fatal neurodegenerative disorders and no effective treatment has been
established to date. In this study, we evaluated the effect of FK506 (tacrolimus), a macrolide …
established to date. In this study, we evaluated the effect of FK506 (tacrolimus), a macrolide …
Prions: beyond a single protein
AS Das, WQ Zou - Clinical microbiology reviews, 2016 - Am Soc Microbiol
Since the term protein was first coined in 1838 and protein was discovered to be the
essential component of fibrin and albumin, all cellular proteins were presumed to play …
essential component of fibrin and albumin, all cellular proteins were presumed to play …