Erratum: Experimental characterisation of diffuse multipath at 10.2 GHz using method of multiple windows

1991 ◽  
Vol 27 (14) ◽  
pp. 1311
Author(s):  
A. Drosopoulos ◽  
S. Haykin
Keyword(s):  
Experimental Characterisation

Experimental characterisation of irradiance and spectral non-uniformity and its impact on multi-junction solar cells: Refractive vs. reflective optics

2021 ◽  
Vol 225 ◽  
pp. 111061
Author(s):  
Jose M. Saura ◽  
Pedro M. Rodrigo ◽  
Florencia M. Almonacid ◽  
Daniel Chemisana ◽  
Eduardo F. Fernández
Keyword(s):  
Solar Cells ◽  
Reflective Optics ◽  
Experimental Characterisation

scholarly journals Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability

2021 ◽  
Vol 22 (5) ◽  
pp. 2240
Author(s):  
Yu Wai Chen ◽  
Shah Kamranur Rahman
Keyword(s):  
Intellectual Disability ◽  
Rna Splicing ◽  
Intrinsically Disordered Proteins ◽  
Cognitive Disorder ◽  
Disordered Proteins ◽  
Thermal Stabilities ◽  
Conformational Disease ◽  
Intrinsically Disordered ◽  
Fatal Attraction ◽  
Experimental Characterisation

The frameshift mutants K192Sfs*7 and R153Sfs*41, of the polyglutamine tract-binding protein 1 (PQBP-1), are stable intrinsically disordered proteins (IDPs). They are each associated with the severe cognitive disorder known as the Renpenning syndrome, a form of X-linked intellectual disability (XLID). Relative to the monomeric wild-type protein, these mutants are dimeric, contain more folded contents, and have higher thermal stabilities. Comparisons can be drawn to the toxic oligomerisation in the “conformational diseases”, which collectively describe medical conditions involving a substantial protein structural transition in the pathogenic mechanism. At the molecular level, the end state of these diseases is often cytotoxic protein aggregation. The conformational disease proteins contain varying extents of intrinsic disorder, and the consensus pathogenesis includes an early oligomer formation. We reviewed the experimental characterisation of the toxic oligomers in representative cases. PQBP-1 mutant dimerisation was then compared to the oligomerisation of the conformational disease proteins. The PQBP-1 mutants are unique in behaving as stable soluble dimers, which do not further develop into higher oligomers or aggregates. The toxicity of the PQBP-1 mutant dimers lies in the native functions (in transcription regulation and possibly, RNA splicing) being compromised, rather than proceeding to aggregation. Other examples of stable IDP dimers were discussed and we speculated on the roles of IDP dimerisation in protein evolution.

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