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版本更新 · v3arXiv:2610.21375

Memorilla: Latent Semantic Memory for LLMs

Adibvafa Fallahpour, Parsa Idehpour, Vignesh Kothapalli, Nikita Mounier, Shirley Wu, Shayan Pardis, Jure Leskovec

原文摘要

Memory enables large language models (LLMs) to use information beyond their parameters, such as past user conversations, long documents, or an agent's earlier actions. For a frozen LLM, access to this accumulated knowledge is limited to what a memory system places in its context window. However, gathering and combining relevant information needed for each query while keeping the model's context short remains challenging for existing systems. Here we introduce Memorilla, a memory system that gathers information from an entire document collection into a fixed number of query-dependent 'memory tokens' for a frozen LLM. Memorilla encodes documents (such as user chats, book chapters) once into reusable embeddings, then learns to retrieve and place query-specific information in the LLM's input embedding space. Using only 16 memory tokens, Memorilla achieves the best performance against baselines including Mem0 and MemoRAG on five of eight benchmarks spanning personalization, long-document and knowledge-intensive question answering. Notably, on FactKG, it reaches 84.33% accuracy versus 80.43% with full-context inference, while using 108x fewer tokens to represent the source documents. Furthermore, Memorilla can facilitate continual learning in agentic systems where the document count (the agent's past turns) increases throughout the trajectory. In a TextWorld environment, we show that Memorilla reduces the agent's tendency to wander between rooms it has already explored, and improves its average success rate from 18.6% with full-history in-context learning to 24.2%. Overall, Memorilla aids frozen LLMs in accumulating and using knowledge effectively across long-context interactions and takes a step towards building continually learning AI systems.

cs.LG · cs.AI

新论文 · v1arXiv:2611.03963

ProteoCraft: Protein Design as Proposal-Verification Search

Fang Wu, Hongbin Lin, Bingchen Duan, Yuchen Wang, Li Erran Li, Yanjie Huang, Mingxuan Cao, Yijun Ma 等 27 位作者

原文摘要

Protein-protein interactions underpin nearly all biological processes. Yet, designing proteins with desired interactions remains challenging due to the structural complexity governing molecular recognition. This study views protein design as a search optimization problem over a combinatorial sequence space under expensive structural evaluation. Toward this goal, we introduce a novel tree-based search framework, ProteoCraft, that employs approximate structural gradients from diffusion-based structure predictors as effective proposal policies to specify where the search should explore. Complete no-gradient inference of folding models separately assigns values to the resulting sequences, determining what is good. ProteoCraft allocates this verification budget through a coarse-to-fine paradigm: multi-site edits first explore distinct sequence basins, then verified promising states undergo strict single-site refinement. Across fourteen de novo binder-design settings spanning eight target proteins, five immune-relevant TCR-facing targets, and four localized CDR redesign tasks, ProteoCraft improves design quality and high-confidence yield. These improvements persist under independent AF2-IG and Rosetta-based interface evaluation. Prospective experimental validation further yielded an 82.9% binding hit rate for PD-L1 miniproteins, with a best measured KD of 0.879 nM, and confirmed binding of designed IFNAR2 VHH. Our code is available at https://github.com/smiles724/ProteoCraft_v1.

cs.CE · cs.AI · q-bio.BM