Database search identification algorithms, such as Sequest and Mascot, constitute powerful enablers for proteomic tandem mass spectrometry. We introduce DBDigger, an algorithm that reorganizes the database identification process to remove a problematic bottleneck. Typically such algorithms determine which candidate sequences can be compared to each spectrum. Instead, DBDigger determines which spectra can be compared to each candidate sequence, enabling the software to generate candidate sequences only once for each HPLC separation rather than for each spectrum. This reorganization also reduces the number of times a spectrum must be predicted for a particular candidate sequence and charge state. As a result, DBDigger can accelerate some database searches by more than an order of magnitude. In addition, the software offers features to reduce the performance degradation introduced by posttranslational modification (PTM) searching. DBDigger allows researchers to specify the sequence context in which each PTM is possible. In the case of CNBr digests, for example, modified methionine residues can be limited to occur only at the C-termini of peptides. Use of "context-dependent" PTM searching reduces the performance penalty relative to traditional PTM searching. We characterize the performance possible with DBDigger, showcasing MASPIC, a new statistical scorer. We describe the implementation of these innovations in the hope that other researchers will employ them for rapid and highly flexible proteomic database search.
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Commun Biol
January 2025
Department of Genetics, Genomics and Informatics, University of Tennessee Health Science Center, Memphis, TN, USA.
Enzymes play a pivotal role in orchestrating complex cellular responses to external stimuli and environmental changes through signal transduction pathways. Despite their crucial roles, measuring enzyme activities is typically indirect and performed on a smaller scale, unlike protein abundance measured by high-throughput proteomics. Moreover, it is challenging to derive the activity of enzymes from proteome-wide post-translational modification (PTM) profiling data.
View Article and Find Full Text PDFJ Proteome Res
January 2025
Institute for Bioinformatics and Medical Informatics (IBMI), University of Tuebingen, Sand 14, 72076 Tubingen, Germany.
Recent improvements in methods and instruments used in mass spectrometry have greatly enhanced the detection of protein post-translational modifications (PTMs). On the computational side, the adoption of open modification search strategies now allows for the identification of a wide variety of PTMs, potentially revealing hundreds to thousands of distinct modifications in biological samples. While the observable part of the proteome is continuously growing, the visualization and interpretation of this vast amount of data in a comprehensive fashion is not yet possible.
View Article and Find Full Text PDFPharmacol Res
December 2024
Department of General Medicine, the Fourth Affiliated Hospital of China Medical University, Shenyang, Liaoning, China. Electronic address:
Protein post translational modification (PTM) is the main regulatory mechanism for eukaryotic cell function, among which ubiquitination is based on the reversible degradation of proteins by the ubiquitin proteasome system to regulate cell homeostasis. The neural precursor cell expressed developmental downregulated gene 8 (NEDD8) is a kind of ubiquitin like protein that shares 80 % homology and 60 % identity with ubiquitin. The PTM process by covalently binding NEDD8 to lysine residues in proteins is called neddylation.
View Article and Find Full Text PDFWorld J Urol
December 2024
Department of Urology, Beijing Chaoyang Hospital, Capital Medical University, No.8 Gongti South Road, Beijing, 100020, China.
Purpose: Kidney transplantation is the optimal therapy for end-stage renal disease, but pre-transplant malignancy (PTM) is a concern due to the increased risk of cancer recurrence with immunosuppression. While advancements in immunosuppression and cancer treatments have improved kidney recipient and graft survival, the impact of PTM on survival remains unclear and warrants comprehensive assessment.
Methods: This systematic review and meta-analysis followed PRISMA guidelines.
Nucleic Acids Res
January 2025
Institute of Bioinformatics and Systems Biology, College of Engineering Bioscience, National Yang Ming Chiao Tung University, No. 1001, Daxue Rd. East Dist., Hsinchu City 300093, Taiwan.
Post-translational modifications (PTMs) are essential for modulating protein function and influencing stability, activity and signaling processes. The dbPTM 2025 update significantly expands the database to include over 2.79 million PTM sites, of which 2.
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