Asymmetric feature interaction for interpreting model predictions

In natural language processing (NLP), deep neural networks (DNNs) could model complex interactions between context and have achieved impressive results on a range of NLP tasks. Prior works on feature interaction attribution mainly focus on studying symmetric interaction that only explains the additional influence of a set of words in combination, which fails to capture asymmetric influence that contributes to model prediction. In this work, we propose an asymmetric feature interaction attribution explanation model that aims to explore asymmetric higher-order feature interactions in the inference of deep neural NLP models. By representing our explanation with an directed interaction graph, we experimentally demonstrate interpretability of the graph to discover asymmetric feature interactions. Experimental results on two sentiment classification datasets show the superiority of our model against the state-of-the-art feature interaction attribution methods in identifying influential features for model predictions. Our code is available at https://github.com/StillLu/ASIV.Comment: Accepted by Findings of the Association for Computational Linguistics: ACL 2023 (long paper

Crystal structure of the signaling helix coiled-coil domain of the β1 subunit of the soluble guanylyl cyclase

<p>Abstract</p> <p>Background</p> <p>The soluble guanylyl cyclase (sGC) is a heterodimeric enzyme that, upon activation by nitric oxide, stimulates the production of the second messenger cGMP. Each sGC subunit harbor four domains three of which are used for heterodimerization: H-NOXA/H-NOBA domain, coiled-coil domain (CC), and catalytic guanylyl cyclase domain. The CC domain has previously been postulated to be part of a larger CC family termed the signaling helix (S-helix) family. Homodimers of sGC have also been observed but are not functionally active yet are likely transient awaiting their intended heterodimeric partner.</p> <p>Results</p> <p>To investigate the structure of the CC S-helix region, we crystallized and determined the structure of the CC domain of the sGCβ1 subunit comprising residues 348-409. The crystal structure was refined to 2.15 Å resolution.</p> <p>Conclusions</p> <p>The CC structure of sGCβ1 revealed a tetrameric arrangement comprised of a dimer of CC dimers. Each monomer is comprised of a long a-helix, a turn near residue P399, and a short second a-helix. The CC structure also offers insights as to how sGC homodimers are not as stable as (functionally) active heterodimers via a possible role for inter-helix salt-bridge formation. The structure also yielded insights into the residues involved in dimerization. In addition, the CC region is also known to harbor a number of congenital and man-made mutations in both membrane and soluble guanylyl cyclases and those function-affecting mutations have been mapped onto the CC structure. This mutant analysis indicated an importance for not only certain dimerization residue positions, but also an important role for other faces of the CC dimer which might perhaps interact with adjacent domains. Our results also extend beyond guanylyl cyclases as the CC structure is, to our knowledge, the first S-helix structure and serves as a model for all S-helix containing family members.</p