Automated Author Profile

Lu, Jie

Current S-Index

29.2

Sum of Dataset Indices for all datasets

Average Dataset Index per Dataset

0.6

Average Dataset Index per dataset

Total Datasets

48

Total datasets for this author

Average FAIR Score

14.3%

Average FAIR Score per dataset

Total Citations

41

Total citations to the author's datasets

Total Mentions

0

Total mentions of the author's datasets

S-Index Interpretation

S-Index Over Time

Cumulative Citations Over Time

Cumulative Mentions Over Time

Datasets

Heterogeneity in the seroprevalence of hepatitis E virus among hospital attendees: a retrospective study in Shanghai, China

Hepatitis E virus (HEV) infection is endemic in China. However, there are scarce data of HEV infection among hospital attendees seeking medical treatment or examination for various reasons. We aim to investigate the prevalence and incidence of HEV infection by time, age, sex, and across departments in a tertiary hospital. Paired results of anti-HEV immunoglobulin G (IgG) and IgM of 31,181 unique subjects during 2021–2022 were analysed. Overall seropositivity (95% confidence interval) of anti-HEV IgG and IgM was 41.25% (40.71%–41.80%) and 2.35% (2.19%–2.53%), respectively. Acute hepatitis E was more prevalent during winter–early spring and among adults aged 31–70. Anti-HEV IgG seroprevalence increased with age, levelling off at > 60 years of age. Not only the seropositivity, but also the levels of anti-HEV IgG were significantly lower in women than men of middle and old age. Young patients from the Department of Neurology had a significantly higher ratio of past HEV infection, while patients with manifestations of hepatitis, gastrointestinal symptoms or hematological diseases had higher seropositivity of anti-HEVIgM and should have high priority to HEV screening. Heterogeneity of HEV seroprevalence was noted at different times of the year, between sexes, among age groups and across departments in general hospital. The concentration of HEV-infected patients in a few departments supports a more focused screening strategy in health-care settings.

Authors

  • Lu, Jie ;
  • Li, Qing ;
  • Zhang, Chenxi ;
  • Li, Ziqiang ;
  • Guo, Qing ;
  • Cao, Zhujun ;
  • Yao, Yu-Feng ;
  • Xie, Qing
1 Citation0 Mentions13% FAIR0.7 Dataset Index
10.6084/m9.figshare.28512084January 2025

The composite influence data of energy-temperature-water source factors on vegetation in the source area of the Yangtze River and the Yellow River

Based on the multi-source remote sensing data set, the relationship between vegetation and energy, temperature and water source factors was identified, and the key influencing signals were quantitatively identified. Then, the causal chain analysis technology of regional energy distribution-temperature change-water source composition-vegetation growth was constructed to reveal the driving mechanism of vegetation change in the source area of the Yangtze River and the Yellow River, and further identify its sensitive water source.

Authors

  • Lu, Jie
0 Citations0 Mentions13% FAIR0.3 Dataset Index
10.6084/m9.figshare.29380277.v1January 2025

The composite influence data of energy-temperature-water source factors on vegetation in the source area of the Yangtze River and the Yellow River

Based on the multi-source remote sensing data set, the relationship between vegetation and energy, temperature and water source factors was identified, and the key influencing signals were quantitatively identified. Then, the causal chain analysis technology of regional energy distribution-temperature change-water source composition-vegetation growth was constructed to reveal the driving mechanism of vegetation change in the source area of the Yangtze River and the Yellow River, and further identify its sensitive water source.

Authors

  • Lu, Jie
0 Citations0 Mentions13% FAIR0.3 Dataset Index
10.6084/m9.figshare.29380277January 2025

CCDC 2380517: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

Authors

  • Cheng, Yan ;
  • Akramov, Davlat ;
  • Yakhshilikova, Lola ;
  • Zhu, Chengwei ;
  • Lu, Jie ;
  • Suo, Jin ;
  • Pugazh, Santhosh ;
  • Qin, Hongjian ;
  • Abduahadi, Safomuddin ;
  • Qin, Jishan ;
  • Hu, Tianwen ;
  • Shen, Jingshan ;
  • Yang, Feipu ;
  • Aisa, Haji A.
1 Citation0 Mentions15% FAIR0.7 Dataset Index
10.5517/ccdc.csd.cc2kx3whJanuary 2025

CCDC 2380525: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

Authors

  • Cheng, Yan ;
  • Akramov, Davlat ;
  • Yakhshilikova, Lola ;
  • Zhu, Chengwei ;
  • Lu, Jie ;
  • Suo, Jin ;
  • Pugazh, Santhosh ;
  • Qin, Hongjian ;
  • Abduahadi, Safomuddin ;
  • Qin, Jishan ;
  • Hu, Tianwen ;
  • Shen, Jingshan ;
  • Yang, Feipu ;
  • Aisa, Haji A.
1 Citation0 Mentions44% FAIR1.4 Dataset Index
10.5517/ccdc.csd.cc2kx44sJanuary 2025

CCDC 2380523: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

Authors

  • Cheng, Yan ;
  • Akramov, Davlat ;
  • Yakhshilikova, Lola ;
  • Zhu, Chengwei ;
  • Lu, Jie ;
  • Suo, Jin ;
  • Pugazh, Santhosh ;
  • Qin, Hongjian ;
  • Abduahadi, Safomuddin ;
  • Qin, Jishan ;
  • Hu, Tianwen ;
  • Shen, Jingshan ;
  • Yang, Feipu ;
  • Aisa, Haji A.
1 Citation0 Mentions13% FAIR0.7 Dataset Index
10.5517/ccdc.csd.cc2kx42qJanuary 2025

CCDC 2380519: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

Authors

  • Cheng, Yan ;
  • Akramov, Davlat ;
  • Yakhshilikova, Lola ;
  • Zhu, Chengwei ;
  • Lu, Jie ;
  • Suo, Jin ;
  • Pugazh, Santhosh ;
  • Qin, Hongjian ;
  • Abduahadi, Safomuddin ;
  • Qin, Jishan ;
  • Hu, Tianwen ;
  • Shen, Jingshan ;
  • Yang, Feipu ;
  • Aisa, Haji A.
1 Citation0 Mentions15% FAIR0.7 Dataset Index
10.5517/ccdc.csd.cc2kx3ykJanuary 2025

Deciphering novel enzymatic and non-enzymatic lysine lactylation in <i>Salmonella</i>

Lysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins involved in metabolic processes, protein translation, and other biological functions are lactylated, with lactylation levels varying according to the growth phase or lactate supplementation. Lactylation is regulated by glycolysis, and inhibition of L-lactate utilization can enhance lactylation levels. In addition to the known lactylase in E. coli, the acetyltransferase YfiQ can also catalyse lactylation. More importantly, L-lactyl coenzyme A (L-La-CoA) and S,D-lactoylglutathione (LGSH) can directly donate lactyl groups to target proteins for chemical lactylation. Lactylation is involved in Salmonella invasion of eukaryotic cells, suggesting that lactylation is crucial for bacterial virulence. Collectively, we have comprehensively investigated protein lactylome and the regulatory mechanisms of lactylation in Salmonella, providing valuable insights into studying lactylation function across diverse bacterial species.

Authors

  • Zhang, Chuanzhen ;
  • Zhou, Tao ;
  • Li, Chengxi ;
  • Wang, Danni ;
  • Tao, Jing ;
  • Zhu, Xiaocen ;
  • Lu, Jie ;
  • Ni, Jinjing ;
  • Yao, Yu-Feng
1 Citation0 Mentions13% FAIR0.6 Dataset Index
10.6084/m9.figshare.28533246.v1January 2025

Deciphering novel enzymatic and non-enzymatic lysine lactylation in <i>Salmonella</i>

Lysine lactylation, a novel post-translational modification, is involved in multiple cellular processes. The role of lactylation remains largely unknown, especially in bacteria. Here, we identified 1090 lactylation sites on 469 proteins by mass spectrometry in Salmonella Typhimurium. Many proteins involved in metabolic processes, protein translation, and other biological functions are lactylated, with lactylation levels varying according to the growth phase or lactate supplementation. Lactylation is regulated by glycolysis, and inhibition of L-lactate utilization can enhance lactylation levels. In addition to the known lactylase in E. coli, the acetyltransferase YfiQ can also catalyse lactylation. More importantly, L-lactyl coenzyme A (L-La-CoA) and S,D-lactoylglutathione (LGSH) can directly donate lactyl groups to target proteins for chemical lactylation. Lactylation is involved in Salmonella invasion of eukaryotic cells, suggesting that lactylation is crucial for bacterial virulence. Collectively, we have comprehensively investigated protein lactylome and the regulatory mechanisms of lactylation in Salmonella, providing valuable insights into studying lactylation function across diverse bacterial species.

Authors

  • Zhang, Chuanzhen ;
  • Zhou, Tao ;
  • Li, Chengxi ;
  • Wang, Danni ;
  • Tao, Jing ;
  • Zhu, Xiaocen ;
  • Lu, Jie ;
  • Ni, Jinjing ;
  • Yao, Yu-Feng
1 Citation0 Mentions13% FAIR0.6 Dataset Index
10.6084/m9.figshare.28533246January 2025

CCDC 2383262: Experimental Crystal Structure Determination

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

Authors

  • Wu, Shengfu ;
  • Song, Xin ;
  • Lu, Jie ;
  • Hao, Wenchao ;
  • Liu, Minghua
1 Citation0 Mentions15% FAIR0.7 Dataset Index
10.5517/ccdc.csd.cc2kzzfzJanuary 2025