Automated Author ProfileHunyadi-Gulyas, Eva
Hunyadi-Gulyas, Eva
Current S-Index
Sum of Dataset Indices for all datasets
Average Dataset Index per Dataset
Average Dataset Index per dataset
Total Datasets
Total datasets for this author
Average FAIR Score
Average FAIR Score per dataset
Total Citations
Total citations to the author's datasets
Total Mentions
Total mentions of the author's datasets
S-Index Interpretation
The S-Index (Sharing Index) is a comprehensive metric that represents the cumulative impact of all your datasets. It is calculated as the sum of Dataset Index scores across all your claimed datasets.
What it means:
- A higher S-index indicates greater overall impact of your datasets relative to typical datasets in their fields of research
- The S-Index grows as you add more datasets or as existing datasets gain more citations and mentions
- It provides a single number to track your research data impact over time
Current S-Index: 1.8 (sum of 5 datasets Dataset Index scores)
More information here.
S-Index Over Time
Cumulative Citations Over Time
Cumulative Mentions Over Time
Datasets
The human proteome is more complex than genetic code have predicted it. Sub-protein level provides us a more complex point of view in proteomics and an opportunity to examine epitopes biomarkers values. Epitomics is a recently emerging omics technology that monitors dynamic changes of protein details, epitopes in health and disease. In this study we examined three different complement C9 epitopes via monoclonal antibodies (BSI0449, BSI0581, BSI0639) in control and lung cancerous plasma with ELISA and LC MS/MS methods. Our results suggest that the immunoprecipitated complement C9 is structurally same but we found differences in posttranslational modification ratio and coprecipitated protein composition in control and lung cancerous plasma. We demonstrated that C9 protein heterogeneity exists and shows cancer association at the sub-molecular epitope level.
Authors
- Pettkó-Szandtner, Aladár ;
- Lazar, Jozsef ;
- Ilona, Tornyi ;
- Ferenczi, Annamaria ;
- Takacs, Laszlo ;
- Hunyadi-Gulyas, Eva
The human proteome is more complex than genetic code have predicted it. Sub-protein level provides us a more complex point of view in proteomics and an opportunity to examine epitopes biomarkers values. Epitomics is a recently emerging omics technology that monitors dynamic changes of protein details, epitopes in health and disease. In this study we examined three different complement C9 epitopes via monoclonal antibodies (BSI0449, BSI0581, BSI0639) in control and lung cancerous plasma with ELISA and LC MS/MS methods. Our results suggest that the immunoprecipitated complement C9 is structurally same but we found differences in posttranslational modification ratio and coprecipitated protein composition in control and lung cancerous plasma. We demonstrated that C9 protein heterogeneity exists and shows cancer association at the sub-molecular epitope level.
Authors
- Pettkó-Szandtner, Aladár ;
- Lazar, Jozsef ;
- Ilona, Tornyi ;
- Ferenczi, Annamaria ;
- Takacs, Laszlo ;
- Hunyadi-Gulyas, Eva
The human proteome is more complex than genetic code have predicted it. Sub-protein level provides us a more complex point of view in proteomics and an opportunity to examine epitopes biomarkers values. Epitomics is a recently emerging omics technology that monitors dynamic changes of protein details, epitopes in health and disease. In this study we examined three different complement C9 epitopes via monoclonal antibodies (BSI0449, BSI0581, BSI0639) in control and lung cancerous plasma with ELISA and LC MS/MS methods. Our results suggest that the immunoprecipitated complement C9 is structurally same but we found differences in posttranslational modification ratio and coprecipitated protein composition in control and lung cancerous plasma. We demonstrated that C9 protein heterogeneity exists and shows cancer association at the sub-molecular epitope level.
Authors
- Pettkó-Szandtner, Aladár ;
- Lazar, Jozsef ;
- Tornyi, Ilona ;
- Ferenczi, Annamaria ;
- Takacs, Laszlo ;
- Hunyadi-Gulyas, Eva
The human proteome is more complex than genetic code have predicted it. Sub-protein level provides us a more complex point of view in proteomics and an opportunity to examine epitopes biomarkers values. Epitomics is a recently emerging omics technology that monitors dynamic changes of protein details, epitopes in health and disease. In this study we examined three different complement C9 epitopes via monoclonal antibodies (BSI0449, BSI0581, BSI0639) in control and lung cancerous plasma with ELISA and LC MS/MS methods. Our results suggest that the immunoprecipitated complement C9 is structurally same but we found differences in posttranslational modification ratio and coprecipitated protein composition in control and lung cancerous plasma. We demonstrated that C9 protein heterogeneity exists and shows cancer association at the sub-molecular epitope level.
Authors
- Pettkó-Szandtner, Aladár ;
- Lazar, Jozsef ;
- Tornyi, Ilona ;
- Ferenczi, Annamaria ;
- Takacs, Laszlo ;
- Hunyadi-Gulyas, Eva
The human proteome is more complex than genetic code have predicted it. Sub-protein level provides us a more complex point of view in proteomics and an opportunity to examine epitopes biomarkers values. Epitomics is a recently emerging omics technology that monitors dynamic changes of protein details, epitopes in health and disease. In this study we examined three different complement C9 epitopes via monoclonal antibodies (BSI0449, BSI0581, BSI0639) in control and lung cancerous plasma with ELISA and LC MS/MS methods. Our results suggest that the immunoprecipitated complement C9 is structurally same but we found differences in posttranslational modification ratio and coprecipitated protein composition in control and lung cancerous plasma. We demonstrated that C9 protein heterogeneity exists and shows cancer association at the sub-molecular epitope level.
Authors
- Pettkó-Szandtner, Aladár ;
- Lazar, Jozsef ;
- Tornyi, Ilona ;
- Ferenczi, Annamaria ;
- Takacs, Laszlo ;
- Hunyadi-Gulyas, Eva