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Nathan L Clement

Publications and source records attributed to Nathan L Clement.

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Automatic Hard Example Synthesis with Multi-Level Agentic Data Curation

Multimodal Large Language Models (MLLMs) are increasingly deployed for nuanced content safety and moderation tasks, yet they remain vulnerable to adversarial attacks and out-of-distribution edge cases. Traditional active learning and manual annotation fail to scale against the complexity and volume of novel multimodal threats. In this paper, we propose an automated, agentic red-teaming framework that systematically synthesizes difficult examples using an iterative strategy that proposes novel hypotheses as well as mutating on past attempts. Leveraging a multi-agent architecture that consists of a high-reasoning Architect agent, an advanced image generator, and a multi-level verification committee of LLM raters, our system autonomously uncovers boundary-pushing violations and ambiguous policy edge cases without any human intervention. By employing these carefully synthesized adversarial examples as in-context demonstrations via test-time Retrieval, we substantially improve the target model's robustness, reducing the False Negative Rate (FNR) from 41.2% to 24.5% in a public image safety benchmark without relying on any human labeling.

cs.AI

Uncertainty Quantified Computational Analysis of the Energetics of Virus Capsid Assembly

Most of the existing research in assembly pathway prediction/analysis of virus cap- sids makes the simplifying assumption that the configuration of the intermediate states can be extracted directly from the final configuration of the entire capsid. This assump- tion does not take into account the conformational changes of the constituent proteins as well as minor changes to the binding interfaces that continues throughout the assembly process until stabilization. This paper presents a statistical-ensemble based approach which provides sufficient samples of the configurational space for each monomer and the relative local orientation between monomers, to capture the uncertainties in their binding and conformations. Furthermore, instead of using larger capsomers (trimers, pentamers) as building blocks, we allow all possible sub-assemblies to bind in all pos- sible combinations. We represent this assembly graph in two different ways. First, we use the Wilcoxon signed rank measure to compare the distributions of binding free energy computed on the sampled conformations to predict likely pathways. Second, we represent chemical equilibrium aspects of the transitions as a Bayesian Factor graph where both associations and dissociations are modeled based on concentrations and the binding free energies. Results from both of these experiments showed significant departure from those one would obtain if only the static configurations of the proteins were considered. Hence, we establish the importance of an uncertainty-aware protocol for pathway analysis, and provide a statistical framework as an important first step towards assembly pathway prediction with high statistical confidence.

q-bio.QM