Lingyun Qin

ORCID: 0009-0007-4009-4928
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About
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Research Areas
  • Cancer-related Molecular Pathways
  • Ubiquitin and proteasome pathways
  • Advanced biosensing and bioanalysis techniques
  • Cancer Research and Treatments
  • CRISPR and Genetic Engineering
  • Music and Audio Processing
  • bioluminescence and chemiluminescence research
  • Single-cell and spatial transcriptomics
  • Computational Drug Discovery Methods
  • RNA modifications and cancer
  • Video Analysis and Summarization
  • Sentiment Analysis and Opinion Mining
  • Protein Structure and Dynamics
  • Genetics, Bioinformatics, and Biomedical Research
  • Click Chemistry and Applications
  • Cancer-related gene regulation

The University of Sydney
2024

Nanjing Normal University
2021-2022

Hubei University of Technology
2014-2018

We introduce an ensemble model approach for multimodal sentiment analysis, focusing on the fusion of textual and video data to enhance accuracy depth emotion interpretation. By integrating three foundational models-IFFSA, BFSA, TBJE-using advanced techniques, we achieve a significant improvement in analysis performance across diverse datasets, including MOSI MOSEI. Specifically, propose two novel models-IFFSA which utilise large language models BERT GPT-2 extract features from text modality...

10.1145/3589335.3651971 article EN cc-by 2024-05-12

The aberrant interaction between p53 and Mdm2/MdmX is an attractive target for cancer drug discovery because the overexpression of Mdm2 and/or MdmX ultimately impairs function in approximately half all human cancers. Recent studies have shown that inhibition both more efficient than a single promoting cellular apoptosis In this study, we demonstrate dual small-molecule antagonist can efficiently reactivate pathway model cells overexpressing Mdm2. was rationally designed based on segmental...

10.1021/ja509223m article EN Journal of the American Chemical Society 2014-12-02

In nearly half of cancers, the anticancer activity p53 protein is often impaired by overexpressed oncoprotein Mdm2 and its homologue, MdmX, demanding efficient therapeutics to disrupt aberrant p53-MdmX/Mdm2 interactions restore activity. While many potent Mdm2-specific inhibitors have already undergone clinical investigations, searching for MdmX-specific has become very attractive, requiring a more screening strategy evaluating potential scaffolds or leads. this work, considering that...

10.1021/acs.biochem.7b00085 article EN Biochemistry 2017-06-05

The oncoprotein MdmX (mouse double minute X) is highly homologous to Mdm2 2) in terms of their amino acid sequences and three-dimensional conformations, but inhibitors exhibit very weak affinity for MdmX, providing an excellent model exploring how protein conformation distinguishes alters inhibitor binding. intrinsic flexibility proteins plays pivotal roles determining predicting the binding properties design inhibitors. Although molecular dynamics simulation approach enables us understand...

10.1021/acs.biochem.7b00903 article EN Biochemistry 2017-10-12

CRISPR/Cas machinery has revolutionized the analytical platform for precise detection of diverse analytes. Specific target recognition and robust signal transduction are crucial requirements a superior sensing platform. The generation is directly related to reporter traits in systems. This review illustrated engineering its significance improving CRISPR/Cas-based It first highlighting role elements, nucleic acid sequence transducer, multiplexing discriminate targets. We described reporters,...

10.2139/ssrn.3980666 article EN SSRN Electronic Journal 2021-01-01

The N-terminal domains of MdmX or Mdm2 are highly homologous and have similar conformation (Figure 1a & b). There three binding pockets for a p53 peptide (p53p), defined as F19, W23 L26 on their surfaces. Current inhibitors including nutlin-3a exhibit weak affinity to MdmX. Nutlin-3a 1c) mimics p53p with high (Kd ~ 20 nM) but very 29 M). pocket significantly differentiates the affinities between MdmX, detailed mechanism remains unclear.

10.17952/24aps.2015.232 article EN 2015-01-01
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