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  1. Muttlib NA, Azman AN, Seng YT, Alawi R, Ariffin Z
    Acta Stomatol Croat, 2016 12;50(4):329-336.
    PMID: 28275280 DOI: 10.15644/asc50/4/6
    BACKGROUND: The purpose of this study was to compare the adaptation of fiber reinforced composite post system and cast post-and-core.

    METHODS: 17 extracted human permanent maxillary central incisors were endodontically treated following the standard protocol. 17 fiber reinforced composite post had been fabricated and adapted to the prepared parallel root canals. A light body poly vinyl siloxane (EXAMIX NDS, Japan) impression material was inserted into the root canals followed by the post. A digital scale was used to measure the weight of the remaining material that filled the gap between the post and the canal wall. The adaptation was indicated by the weight difference before and after impression material insertion. The same procedures were repeated with 17 cast post-and-core in the same teeth specimens.

    RESULT: The mean difference for the weight of the material within the group was statistically significant (P-value <0.001) with the value of 6.1mg(± 2.7mg) for cast metal post and 6.4mg(± 2.7mg) for fiber reinforced composite post. However, the mean difference was not statistically significant when compared with both materials (P-value>0.05).

    CONCLUSIONS: Both cast post-and-core and fiber reinforced composite post systems showed similar adaptation to the canal.

  2. Md Yusuf N, Azman AN, Abdul Aziz AA, Ahmad Fuad FA, Nasarudin RN, Hisam S
    PLoS One, 2024;19(8):e0306975.
    PMID: 39146276 DOI: 10.1371/journal.pone.0306975
    Malaria, an ancient mosquito-borne illness caused by Plasmodium parasites, is mostly treated with Artemisinin Combination Therapy (ACT). However, Single Nucleotide Polymorphisms (SNPs) mutations in the P. falciparum Kelch 13 (PfK13) protein have been associated with artemisinin resistance (ART-R). Therefore, this study aims to generate PfK13 recombinant proteins incorporating of two specific SNPs mutations, PfK13-V494I and PfK13-N537I, and subsequently analyze their binding interactions with artemisinin (ART). The recombinant proteins of PfK13 mutations and the Wild Type (WT) variant were expressed utilizing a standard protein expression protocol with modifications and subsequently purified via IMAC and confirmed with SDS-PAGE analysis and Orbitrap tandem mass spectrometry. The binding interactions between PfK13-V494I and PfK13-N537I propeller domain proteins ART were assessed through Isothermal Titration Calorimetry (ITC) and subsequently validated using fluorescence spectrometry. The protein concentrations obtained were 0.3 mg/ml for PfK13-WT, 0.18 mg/ml for PfK13-V494I, and 0.28 mg/ml for PfK13-N537I. Results obtained for binding interaction revealed an increased fluorescence intensity in the mutants PfK13-N537I (83 a.u.) and PfK13-V494I (143 a.u.) compared to PfK13-WT (33 a.u.), indicating increased exposure of surface proteins because of the looser binding between PfK13 protein mutants with ART. This shows that the PfK13 mutations may induce alterations in the binding interaction with ART, potentially leading to reduced effectiveness of ART and ultimately contributing to ART-R. However, this study only elucidated one facet of the contributing factors that could serve as potential indicators for ART-R and further investigation should be pursued in the future to comprehensively explore this complex mechanism of ART-R.
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