Decentralised Routing in P2P-Systems with Incomplete Knowledge

THE SOURCE OF ERRORS IN INDONESIAN-ENGLISH TRANSLATION

Jurnal KATA ◽

10.22216/jk.v1i2.2351 ◽

2017 ◽

Vol 1 (2) ◽

pp. 192 ◽

Cited By ~ 1

Author(s):

Silvia Utami

Keyword(s):

Error Analysis ◽

English Translation ◽

Target Language ◽

Incomplete Knowledge ◽

Descriptive Research ◽

Grammatical Errors ◽

Translation Errors

<p>This research aimed to identify types of translation errors and to find out the sources of errors (interlingual and intralingual errors) in Indonesian-English translation written by the students. The type of this research was descriptive research which used Error Analysis procedures to identify and analyze the students’ error. The findings showed that the types of grammatical errors made by the students in their translation were three types, namely global errors, local errors, and other errors. The most frequent error made by the students was local errors and the fewest error made by the students was other errors. Then, this research revealed that mostly errors occurred in students’ translation were caused by intralingual error. Meanwhile, only few errors were caused by interlingual error. The errors occured due students’ incomplete knowledge of the target language.</p>

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Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

Nature Communications ◽

10.1038/s41467-020-20782-0 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Francesco Simone Ruggeri ◽

Johnny Habchi ◽

Sean Chia ◽

Robert I. Horne ◽

Michele Vendruscolo ◽

...

Keyword(s):

Small Molecules ◽

Single Molecule ◽

Protein Misfolding ◽

Molecular Mechanisms ◽

Chemical Sensitivity ◽

Incomplete Knowledge ◽

Parkinson’S Diseases ◽

Aggregation Inhibitor ◽

Misfolding Diseases

AbstractSignificant efforts have been devoted in the last twenty years to developing compounds that can interfere with the aggregation pathways of proteins related to misfolding disorders, including Alzheimer’s and Parkinson’s diseases. However, no disease-modifying drug has become available for clinical use to date for these conditions. One of the main reasons for this failure is the incomplete knowledge of the molecular mechanisms underlying the process by which small molecules interact with protein aggregates and interfere with their aggregation pathways. Here, we leverage the single molecule morphological and chemical sensitivity of infrared nanospectroscopy to provide the first direct measurement of the structure and interaction between single Aβ42 oligomeric and fibrillar species and an aggregation inhibitor, bexarotene, which is able to prevent Aβ42 aggregation in vitro and reverses its neurotoxicity in cell and animal models of Alzheimer’s disease. Our results demonstrate that the carboxyl group of this compound interacts with Aβ42 aggregates through a single hydrogen bond. These results establish infrared nanospectroscopy as a powerful tool in structure-based drug discovery for protein misfolding diseases.

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