Xia Li

The gradability of know-how presents a persistent puzzle for theories of skill. While knowing that p is typically binary, knowing how to φ admits of degrees of excellence. Leading Intellectualist accounts (Pavese 2017; Zhang 2025) typically explicate this gradability in terms of representational resolution or default reliability in the actual world. This paper argues, however, that these "Actualist" metrics are insufficient because they fail to distinguish between the intrinsic competence of an "Unlucky Expert"(whose skill is masked by environmental deviation) and the structural luck of a "Lucky Novice"(whose skill is mimicked by environmental assistance). Mere reliability allows luck to masquerade as competence. Drawing on Modal Virtue Epistemology, we propose that gradability is best measured not by actual success frequencies, but by the agent's Weighted Modal Volume across counterfactual worlds. We conclude that propositional knowledge contributes to skill precisely by functioning as a "Modal Extender"that insulates the agent against modal fragility, resulting in a view I term Modal Intellectualism.

Molecular chaperones in cells constantly monitor and bind to exposed hydrophobicity in newly synthesized proteins and assist them in folding or targeting to cellular membranes for insertion. However, proteins can be misfolded or mistargeted, which often causes hydrophobic amino acids to be exposed to the aqueous cytosol. Again, chaperones recognize exposed hydrophobicity in these proteins to prevent nonspecific interactions and aggregation, which are harmful to cells. The chaperone‐bound misfolded proteins are then decorated with ubiquitin chains denoting them for proteasomal degradation. It remains enigmatic how molecular chaperones can mediate both maturation of nascent proteins and ubiquitination of misfolded proteins solely based on their exposed hydrophobic signals. In this review, we propose a dynamic ubiquitination and deubiquitination model in which ubiquitination of newly synthesized proteins serves as a “fix me” signal for either refolding of soluble proteins or retargeting of membrane proteins with the help of chaperones and deubiquitinases. Such a model would provide additional time for aberrant nascent proteins to fold or route for membrane insertion, thus avoiding excessive protein degradation and saving cellular energy spent on protein synthesis. Also see the video abstract here: https://youtu.be/gkElfmqaKG4.