Distributed Hash Tables (DHTs) are pivotal in numerous high-impact key-value applications built on distributed networked systems, offering a decentralized architecture that avoids single points of failure and improves data availability. Despite their widespread utility, DHTs face substantial challenges in handling range queries, which are crucial for applications such as LLM serving, distributed storage, databases, content delivery networks, and blockchains. To address this limitation, we present LEAD, a novel system incorporating learned models within DHT structures to significantly optimize range query performance. LEAD utilizes recursive machine learning models as the Learned Hash Function to map and retrieve data across a distributed system while preserving the inherent order of data. LEAD includes the designs to minimize range query latency and message cost while maintaining high scalability and resilience to network churn. Our comprehensive evaluations, conducted in both testbed implementation and simulations, demonstrate that LEAD achieves tremendous advantages in system efficiency compared to existing range query methods in large-scale distributed systems, reducing query latency and message cost by 80% to 90%+. Furthermore, LEAD exhibits scalability and robustness against system churn, providing a robust, scalable structure for efficient data retrieval in distributed key-value systems.

Microbial community proteomics, also termed metaproteomics, investigates all proteins expressed by a microbiota. Tandem mass spectrometry (MS/MS) is the typical method for identifying proteins in metaproteomics, which involves searching the mass spectra against a protein sequence database. A major post-analysis step is controlling the false discovery rate (FDR), i.e., the ratio of false positives to the total number of annotations. The current popular target-decoy FDR estimation method treats all the peptides and proteins equally and overlooks that they could have varied probabilities of being identified. In this study, we report FineFDR, a framework for FDR assessment at fine-grained levels with taxonomy information considered. FineFDR groups the identified peptide-spectrum matches, peptides, and proteins from different taxonomic units and estimates the FDR in each group separately. Empirical experiments on the simulated and real-world data sets demonstrate that our FineFDR achieved higher precision and more peptide and protein identifications when compared to the state-of-the-art methods, such as Comet, Percolator, TIDD, and Tailor. FineFDR is freely available under the GNU GPL license at https://github.com/Biocomputing-Research-Group/FDR.