Qian Shen

This paper reviews research on anxiety of learning Chinese as a second or foreign language in and outside mainland China. This review involves 52 Chinese language articles identified in leading journals from the Chinese National Knowledge Infrastructure database and 42 English language articles from the Web of Science and ERIC database published during the period of 1999 to 2020. By adopting bibliometric analysis and content analysis, this study compares the topical issues and methodological approaches of research on CSL/CFL learning anxiety published in leading Chinese and international journals. The review found that, compared with mainland Chinese scholars, international researchers examined a broader range of topical issues from multidimensional perspectives. While most Chinese empirical studies are dominated by the quantitative approach, qualitative methods such as classroom observations and in-depth interviews were also widely adopted by international researchers. The analysis also revealed that although Chinese scholars had drawn on well-established theories and concepts originating from foreign language anxiety research, their role in CSL/CFL anxiety research is limited and peripheral. Consequently, we conclude this review with recommendations that encourage mainland Chinese researchers to be well informed by the updated theoretical perspective and methodological approaches such as the utilization of social network analysis and the integration of Information Communications Technology in language education.

© 2015 Nature America, Inc. All rights reserved. The AAA+ ATPase Vps4 disassembles ESCRT-III and is essential for HIV-1 budding and other pathways. Vps4 is a paradigmatic member of a class of hexameric AAA+ ATPases that disassemble protein complexes without degradation. To distinguish between local displacement versus global unfolding mechanisms for complex disassembly, we carried out hydrogen/deuterium exchange during Saccharomyces cerevisiae Vps4 disassembly of a chimeric Vps24-2 ESCRT-III filament. EX1 exchange behavior shows that Vps4 completely unfolds ESCRT-III substrates on a time scale consistent with the disassembly reaction. The established unfoldase ClpX showed the same pattern, thus demonstrating a common unfolding mechanism. Vps4 hexamers containing a single cysteine residue in the pore loops were cross-linked to ESCRT-III subunits containing unique cysteines within the folded core domain. These data support a mechanism in which Vps4 disassembles its substrates by completely unfolding them and threading them through the central pore.