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Rule-Based Pruning and In Silico Identification of Essential Proteins in Yeast PPIN
Proteins are vital for the significant cellular activities of living organisms. However, not all of them are essential. Identifying essential proteins through different biological experiments is relatively more laborious and time-consuming than the computational approaches used in recent times. Howe...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9454873/ https://www.ncbi.nlm.nih.gov/pubmed/36078056 http://dx.doi.org/10.3390/cells11172648 |
Sumario: | Proteins are vital for the significant cellular activities of living organisms. However, not all of them are essential. Identifying essential proteins through different biological experiments is relatively more laborious and time-consuming than the computational approaches used in recent times. However, practical implementation of conventional scientific methods sometimes becomes challenging due to poor performance impact in specific scenarios. Thus, more developed and efficient computational prediction models are required for essential protein identification. An effective methodology is proposed in this research, capable of predicting essential proteins in a refined yeast protein–protein interaction network (PPIN). The rule-based refinement is done using protein complex and local interaction density information derived from the neighborhood properties of proteins in the network. Identification and pruning of non-essential proteins are equally crucial here. In the initial phase, careful assessment is performed by applying node and edge weights to identify and discard the non-essential proteins from the interaction network. Three cut-off levels are considered for each node and edge weight for pruning the non-essential proteins. Once the PPIN has been filtered out, the second phase starts with two centralities-based approaches: (1) local interaction density (LID) and (2) local interaction density with protein complex (LIDC), which are successively implemented to identify the essential proteins in the yeast PPIN. Our proposed methodology achieves better performance in comparison to the existing state-of-the-art techniques. |
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