Zhiyuan Wang

How should insecure leaders deal with labor rights in the face of an economic downturn? Economic theory suggests that suppressing labor rights boosts the economy and that economic growth also dampens violent political opposition. As a result, the suppression of labor rights should contribute to more job security for leaders. However, some other scholars maintain that more repression actually increases the probability of opposition. As a result, the policy implication of this argument is that leaders would be better off if they choose to improve the protection of labor rights. Our simple formal model demonstrates that the second argument is more likely to be the case. The probit analysis of 146 countries from 1984 to 2004 bears out this prediction. We also find that this relationship is stronger in non-democracies than in democracies. Our study appears to provide some support to Bueno de Mesquita et al.’s statement that policies that are good for political survival may not necessarily be good for the economy.

This study investigates the determinants of the ratification of International Covenant on Economic, Social, and Cultural Rights (ICESCR). To do so, it proposes an explanation that postulates that states employ treaty ratification as a device to signal their resolve to implement polices required by the treaty at issue in order to appease demanding domestic constituencies, predicting that states with lower compliance capacity tend to commit faster than states with higher compliance capacity. Applying this explanation to the ICESCR leads to two expectations. First, the larger government spending a proxy of high compliance capacity is hypothesized to delay the ratification process. Second, states with the unitary system are expected to ratify the ICESCR more promptly because the centralized power structure in unitary states significantly restricts the pursuit of the policy autonomy by minorities at local level that the right to self-determination entails. The Cox proportional hazard analysis lends support to both hypotheses.

© 2016, American Society for Biochemistry and Molecular Biology Inc. All rights reserved.Glycyl-tRNA synthetase is the enzyme that covalently links glycine to cognate tRNA for translation. It is of great research interest because of its nonconserved quaternary structures, unique species-specific aminoacylation properties, and noncanonical functions in neurological diseases, but none of these is fully understood. We report two crystal structures of human GlyRS variants, in the free form and in complex with tRNAGly respectively, and reveal new aspects of the glycylation mechanism. We discover that insertion 3 differs considerably in conformation in catalysis and that it acts like a "switch" and fully opens to allow tRNA to bind in a cross-subunit fashion. The flexibility of the protein is supported by molecular dynamics simulation, as well as enzymatic activity assays. The biophysical and biochemical studies suggest that human GlyRS may utilize its flexibility for both the traditional function and alternative functions.