2023
DOI: 10.1039/d3tc02259e
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Application convenient and energy-saving mechano-optics of Er3+-doped X2O2S (X = Y/Lu/Gd) for thermometry

Yixiao Han,
Leipeng Li,
Chongyang Cai
et al.

Abstract: Herein, Han et al. introduced a strategy to extend mechanoluminescent materials for optical thermometry by using green mechanoluminescence in a X2O2S (X = Y/Lu/Gd) system.

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Cited by 4 publications
(2 citation statements)
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“…The COMPASS protein complex consists of four core members: RBBP5, WDR5, ASH2L, and one of the six methyltransferases 36 . The methyltransferases have the enzymatic SET1 domain to methylate H3K4, while RBBP5 functions to modulate the activity of the complex and mediate the interaction between the nucleosome and the complex 4,37 . Our structural analysis showed both the T232 and E296 residues are located at critical positions of the interface between RBBP5 and the histone H2B, which has been known to be essential for the recruitment of COMPASS to the nucleosome [38][39][40] .…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The COMPASS protein complex consists of four core members: RBBP5, WDR5, ASH2L, and one of the six methyltransferases 36 . The methyltransferases have the enzymatic SET1 domain to methylate H3K4, while RBBP5 functions to modulate the activity of the complex and mediate the interaction between the nucleosome and the complex 4,37 . Our structural analysis showed both the T232 and E296 residues are located at critical positions of the interface between RBBP5 and the histone H2B, which has been known to be essential for the recruitment of COMPASS to the nucleosome [38][39][40] .…”
Section: Discussionmentioning
confidence: 99%
“…The methylation of histone 3 lysine 4 (H3K4) is an evolutionarily conserved chromatin mark that is typically found in active transcription sites and is considered a marker for gene activation 3 . H3K4 methylation is predominantly mediated by the COMPASS (COMplex of Proteins Associated with Set1) protein complex, which includes one of the six SET1 domain-containing methyltransferases (KMT2A-F) and three other core members WDR5, ASH2L and RBBP5 to modulate the catalytic activity of methyltransferases 4 .…”
Section: Introductionmentioning
confidence: 99%