The advancements in next-generation sequencing technologies have given rise to large-scale, open-source protein databases consisting of hundreds of millions of sequences. However, to make these sequences useful in biomedical applications, they need to be painstakingly annotated by curating them from literature. To counteract this problem, many automated annotation algorithms have been developed over the years including deep learning models, especially in recent times. In this work, we propose a transformer-based deep-learning model that can predict the Enzyme Commission numbers of an enzyme from full-scale sequences with state-of-the-art accuracy compared to other recent machine learning annotation algorithms. The system does especially well on clustered split dataset which consists of training and testing samples derived from different distributions that are structurally dissimilar from each other. This proves that the model is able to understand deep patterns within the sequences and can accurately identify the motifs responsible for the different enzyme commission numbers. Moreover, the algorithm is able to retain similar accuracy even when the training size is significantly reduced, and also, the model accuracy is independent of the sequence length making it suitable for a wide range of applications consisting of varying sequence structures.
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http://dx.doi.org/10.1109/TCBB.2023.3311427 | DOI Listing |
Sci Rep
January 2025
1Nantong University, Nantong, 226007, People's Republic of China.
Estrogen sulfotransferase (SULT1E1), a member of the sulfotransferase family (SULTs), is the enzyme with the strongest affinity for estrogen. Despite significant associations between SULT1E1 and the progression and prognosis of a range of diseases, its functional role and potential mechanisms in lung adenocarcinoma (LUAD) remain unclear. The objective of this study was to examine the potential of SULT1E1 as a biomarker for LUAD.
View Article and Find Full Text PDFNat Chem Biol
January 2025
State Key Laboratory of Membrane Biology, School of Pharmaceutical Sciences, Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorous Chemistry and Chemical Biology (Ministry of Education), Tsinghua University, Beijing, China.
The E2 ubiquitin (Ub)-conjugating enzyme primarily determines Ub conjugation as Ub-isopeptide (lysine), Ub-oxyester (serine/threonine) or Ub-thioester (cysteine). However, E2-specific Ub conjugation profiles within cells remain elusive. Here we developed the fusion E2-Ub-R74G profiling (FUSEP) strategy to access E2-specific Ub conjugation profiles in cells with amino acid resolution.
View Article and Find Full Text PDFHepatol Commun
November 2024
Guangxi Key Laboratory of Molecular Medicine in Liver Injury and Repair, Affiliated Hospital of Guilin Medical University, Guilin, Guangxi, China.
Background: Overdose of acetaminophen (APAP), a commonly used antipyretic analgesic, can lead to severe liver injury and failure. Current treatments are only effective in the early stages of APAP-induced acute liver injury (ALI). Therefore, a detailed examination of the mechanisms involved in liver repair following APAP-induced ALI could provide valuable insights for clinical interventions.
View Article and Find Full Text PDFJ Med Virol
January 2025
Institute of Virology, Technical University of Munich/Helmholtz Munich, Munich, Germany.
SARS-CoV-2 infection is accompanied by elevated liver enzymes, and patients with pre-existing liver conditions experience more severe disease. While it was known that SARS-CoV-2 infects human hepatocytes, our study determines the mechanism of infection, demonstrates viral replication and spread, and highlights direct hepatocyte damage. Viral replication was readily detectable upon infection of primary human hepatocytes and hepatoma cells with the ancestral SARS-CoV-2, Delta, and Omicron variants.
View Article and Find Full Text PDFBMC Pregnancy Childbirth
January 2025
Department of Clinical Genetics, Rennes University Hospital, Rennes, France.
Background: Mucopolysaccharidosis type I (MPS I - IDUA gene) is a rare autosomal recessive lysosomal storage disorder. Clinical symptoms, including visceral overload, are progressive and typically begin postnatally. Descriptions of hepatosplenomegaly associated with lysosomal pathology are uncommon during the prenatal period.
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