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EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers
Redirection of amyloid fibril formation through the action of a small molecule is demonstrated, resulting in off-pathway, highly stable oligomers, suggesting a generic effect on aggregation pathways in neurodegenerative diseases. Expand
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
It is proposed that frataxins are iron sensors that act as regulators of Fe-S cluster formation to fine-tune the quantity of Fe -S cluster formed to the concentration of the available acceptors. Expand
Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.
It is suggested that titin Ig domains in the I-band function as extensible components of muscle elasticity by stretching the hinge regions. Expand
The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.
The solution structure of Josephin is determined and it is shown that it belongs to the family of papain-like cysteine proteases, sharing the highest degree of structural similarity with bacterial staphopain. Expand
Three-Dimensional Structure and Stability of the KH Domain: Molecular Insights into the Fragile X Syndrome
This work presents the three-dimensional solution structure of the KH module, a sequence motif found in a number of proteins that are known to be in close association with RNA, and suggests a potential surface for RNA binding centered on the loop between the first two helices. Expand
Mutations in the mitochondrial protease gene AFG3L2 cause dominant hereditary ataxia SCA28
This work identifies AFG3L2 as a novel cause of dominant neurodegenerative disease and indicates a previously unknown role for this component of the mitochondrial protein quality control machinery in protecting the human cerebellum against neurodegenersation. Expand
A standardized and biocompatible preparation of aggregate-free amyloid beta peptide for biophysical and biological studies of Alzheimer's disease.
The main advantage of the proposed protocol over others is that it results in standardized aggregate-free Aβ peptide samples that are biocompatible for cell culture studies and yield reproducible aggregation kinetics and cytotoxicities. Expand
Structure of the dsRNA binding domain of E. coli RNase III.
The double‐stranded RNA binding domain (dsRBD) is a approximately 70 residue motif found in a variety of modular proteins exhibiting diverse functions, yet always in association with dsRNA. We reportExpand
Fragile X Mental Retardation Protein (FMRP) Binds Specifically to the Brain Cytoplasmic RNAs BC1/BC200 via a Novel RNA-binding Motif*
It is demonstrated that the N terminus of FMRP binds strongly and specifically to BC1 and to its potential human analog BC200, raising the possibility that FMRp plays a direct role in BC1/mRNA annealing. Expand
The C terminus of fragile X mental retardation protein interacts with the multi-domain Ran-binding protein in the microtubule-organising centre.
The results suggest that the functional role of RanBPM binding is modulation of the RNA-binding properties of FMRP. Expand