Basic research and innovation management of frontier biotechnology / 中华医学科研管理杂志

Objective:To promote the development of basic research, clarify the development trend of frontier biotechnology, and strengthen scientific research management in project management, resource integration, risk supervision and other aspects.Methods:Through literature study and expert discussion, this paper analyzed the hot spots of frontier biotechnology research, and put forward suggestions for optimizing strategic tasks and innovation management from the perspective of innovation management.Results:The research of frontier biotechnology in our country showed a rapid development trend, but also faced with challenges such as insufficient technological innovation ability and relatively lagging management level. It is imperative to explore and establish a new scientific research management model and optimize the operation mechanism.Conclusions:The major research achievements of frontier biotechnology are emerging constantly, showing a trend of multi-disciplinary and multi-field integration. China should actively explore innovative management models, optimize and improve strategic tasks, improve the efficiency of scientific research management, and do a good job in supporting the realization of high-level scientific and technological self-reliance.

Crystal structure and functional implication of the RUN domain of human NESCA

NESCA, a newly discovered signaling adapter protein in the NGF-pathway, contains a RUN domain at its N-terminus. Here we report the crystal structure of the NESCA RUN domain determined at 2.0-Å resolution. The overall fold of the NESCA RUN domain comprises nine helices, resembling the RUN domain of RPIPx and the RUN1 domain of Rab6IP1. However, compared to the other RUN domains, the RUN domain of NESCA has significantly different surface electrostatic distributions at the putative GTPase-interacting interface. We demonstrate that the RUN domain of NESCA can bind H-Ras, a downstream signaling molecule of TrkA, with high affinity. Moreover, NESCA RUN can directly interact with TrkA. These results provide new insights into how NESCA participates in the NGF-TrkA signaling pathway.