![]() Pluralism makes plausible why different senses of top-down causation can be coherent and not in conflict with reductionism, thereby illustrating a productive interface between philosophical analysis and scientific inquiry. ![]() Instead, a pluralist perspective is recommended-many different kinds of top-down causation (explanation) can exist alongside many different kinds of bottom-up causation (explanation). This locality suggests that no single metaphysical account of hierarchy for causal relations to obtain within emerges from the epistemology of scientific explanation. Representations used in top-down and bottom-up explanations are primarily 'local' and tied to distinct domains of science, illustrated here by protein structure and folding. A negative answer to this question undermines a commonplace view that the world is divided into stratified 'levels' of organization and suggests that attributions of causal responsibility in different hierarchical representations may not have a meaningful basis for comparison. Less attention has been given to the question of whether these representations of hierarchical relations pick out a single, common hierarchy. Much debate has been focused on whether top-down causation is coherent or in conflict with reductionism. The ubiquity of top-down causal explanations within and across the sciences is prima facie evidence for the existence of top-down causation. The aim of this article is to provide a brief summary of the origin and concepts used in the intracellular chaperone field, to provide a backdrop for discussion of their possible roles outside the cell. ![]() A cellular or extracellular event mediated by a chaperone protein is not necessarily a consequence of that protein's chaperone function. Chaperones may also have evolved to have additional roles. Chaperones have evolved to reduce, by a variety of mechanisms, the aggregation of proteins into non-functional, and sometimes cytotoxic, structures. We suggest that this function is a distinct and essential cellular function, mediated by many different proteins. We define the chaperone function as the prevention or reversal of incorrect interactions that may occur when reactive macromolecular surfaces are transiently exposed to the intracellular environment. ![]() The aim of this article is to provide a brief summary of the origin and concepts used in the intracellular chaperone field, to provide a backdrop for discussion of their possible roles outside the cell.What are molecular chaperones and how should we think about them? We propose that it is better to think in terms of a chaperone function rather than in terms of chaperone molecules. ![]() What are molecular chaperones and how should we think about them? We propose that it is better to think in terms of a chaperone function rather than in terms of chaperone molecules. ![]()
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