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2021/01/25

Recently, the Pingshan Biopharmaceutical R&D and Transformation Center of Shenzhen Bay Laboratory collaborated with the Shenzhen Graduate School of Peking University to publish a research paper titled "Molecular Design of Stacked Pentappeptides as Building Blocks of Self Assembled Coiled Coil Like Fibers" in the sub journal of Science Advances

2021/01/22

On the afternoon of January 22nd, the Pingshan Center held a "Annual Outstanding Employee" commendation meeting. Li Zigang, Executive Director of Pingshan Center, personally awarded the award certificates to the award-winning employees and took a photo with the winners as a souvenir.

2021/01/22

On the morning of January 22nd, Cheng Zhongyi, CEO of Hangzhou Jingjie Biotechnology Co., Ltd. (hereinafter referred to as "Jingjie Biotechnology"), and his delegation visited the Pingshan Biopharmaceutical R&D and Transformation Center of Shenzhen Bay Laboratory (hereinafter referred to as "Pingshan Center").

2021/01/21

In the afternoon of January 21, Shenzhen Zhongguang Industrial Technology Research Institute (hereinafter referred to as "Zhongguang Research Institute"), Shenzhen Angel Investment Guidance Fund (hereinafter referred to as "Angel Mother Fund"), Shenzhen Pingshan District Science and Technology Innovation Bureau (hereinafter referred to as "Science and Technology Innovation Bureau") came to Pingshan Biomedical Research and Transformation Center of Shenzhen Bay Laboratory (hereinafter referred to as "Pingshan Center"), which is located in the industry, university and research base of Shenzhen Pingshan High tech Zone, for a visit.

2021/01/11

On the morning of January 11, Li Zigang, Executive Director of Pingshan Center, had a discussion with Li Weixin, Deputy Chief physician of Neurosurgery, Director of Science and Education Department of Sami International Medical Center.

2021/01/08

On January 8, 2021, Pingshan Center held its first employee report meeting, and established a report evaluation leadership group to participate in the entire report meeting. The members of the leadership group include Chen Jie'an, Assistant Director and Minister of Chemistry of Pingshan Center, Yin Feng, Minister of Biology, Tang Hongmei, Minister of Comprehensive Department, and Fu Qingqing, Human Resources Supervisor. 30 employees from three departments, adhering to the principle of seeking truth from facts, reported on their work performance, experiences, difficulties encountered, existing problems, and work plans and goals for the next year in 2020.

2021/01/05

On the afternoon of January 5, 2021, the first board of directors of the Pingshan Biomedical R&D and Transformation Center (hereinafter referred to as the "Pingshan Center") of Shenzhen Bay Laboratory was established and held its first meeting. The meeting elected the first governing body of Pingshan Center. Chairman: Wu Yundong, academician of the CAS Member, executive deputy director of Shenzhen Bay Laboratory; Vice Chairman: Chen Huaping, deputy district chief of Pingshan District; Tu Huan, deputy director of Shenzhen Bay Laboratory; members of the board: Sun Yongkui, academician of the National Academy of Engineering; Huang Ming, director of Pingshan District Science and Technology Innovation Bureau; Li Zigang, executive director of Pingshan Center; Huang Yong, director of Shenzhen Bay Laboratory's Beipu Joint Research Center. The establishment of the council will further clarify the construction plan, organizational structure, institutional system, spatial platform and other matters of the Pingshan Center, and promote its better and faster development. In 2020, Pingshan Center actively promoted the integration of industry, academia, and research, promoting the transformation of achievements. Cooperated with Shenzhen Technology University, Shenzhen Third People's Hospital, IFlytek, Xinhe Biology, China Resources Sanjiu, Bangtai Hesheng, Jianyuan Medicine and other university research institutes, medical institutions, biomedical enterprises and institutions, and established a total of 7 projects; The Chemical biology platform and Medicinal chemistry platform were initially constructed, and the preliminary research on the public service platform was completed; Apply for 22 invention patents and 3 PCT patents. In 2021, Pingshan Center will be committed to accelerating the transformation and technological upgrading of Pingshan biopharmaceutical achievements. Develop 8-10 core technologies for building small molecule and peptide drugs; Establish a comprehensive scientific database and a scientific literature library; Promote the construction of academician workstations and cultivate scientific and technological innovation teams; Actively expanding cooperation and exchange with biopharmaceutical enterprises, medical institutions, and university research institutes in national, provincial, municipal, and Pingshan areas, or providing technical support and public services; Conduct research on regional biopharmaceutical related enterprises and actively promote the incubation of technology enterprises; Establish an asset management and service company, and build a technology transformation investment and financing platform. In addition, the Pingshan Biopharmaceutical R&D and Transformation Center of Shenzhen Bay Laboratory will establish a high-level project evaluation mechanism, further focus on the transformation field, and actively promote the construction of incubators. We will also actively strive to establish a public service platform for biopharmaceuticals in Shenzhen, providing systematic, convenient, efficient, and open services to higher education institutions, scientific research institutions, biopharmaceutical enterprises, government departments, and the public within the Pingshan District Biopharmaceutical Innovation Industrial Park, becoming an important supporting force for promoting the development of the national level biopharmaceutical industry base in Pingshan District. Related background: Shenzhen Bay Laboratory is a Guangdong Provincial Laboratory jointly established by the Municipal Science and Technology Innovation Commission and the Shenzhen Graduate School of Peking University, which was constructed by our city. As one of the research institutions directly under the Shenzhen Bay Laboratory, the Pingshan Biopharmaceutical R&D and Transformation Center of Shenzhen Bay Laboratory undertakes the industrial transformation function. It will build 2 new drug R&D platforms, 2 pharmaceutical transformation platforms, and 4 public service platforms, and carry out research cooperation with prestigious universities such as Princeton University to promote the industrial transformation of basic research achievements of Shenzhen Bay Laboratory. It will become an important achievement display base for Shenzhen Bay Laboratory, serving as the

2020/12/31

2020年12月31日，深圳湾实验室党委书记胡晓军率队对高科创新中心、坪山生物医药研发转化中心开展“元旦”节前安全巡查。 　　   　　胡晓军书记一行先后对高科创新实验区域、办公区域、坪山生物医药研发转化中心实验区域等进行实地安全巡查，了解“元旦”前各项安全措施落实情况，并与员工进行亲近的访谈。 　　   　　胡晓军书记强调，一是各研究所/中心、部门在“元旦”前要切实落实好各项安全措施，重点关注化学试剂、消防、用电等方面安全，在假期前要清理废弃纸箱等可燃物质，关闭非必要连续供电的电源;二是要加大安全检查力度，及时发现并消除安全隐患;三是要做好节假日期间人员值班安排，增加节假日期间巡查频次。他表示，过去的一年，在全体员工共同努力下，深圳湾实验室取得一定成绩，在来年发展也将会更加辉煌。走访过程中，他向员工致以节日问候和新春祝福。 　　   　　深圳湾实验室综合部、平台部等有关人员陪同巡查。 　　撰稿 | 平台部 吴帅 　　摄影 | 姬 二 　　编辑 | 鍮 鍮On December 31, 2020, Hu Xiaojun, Secretary of the Party Committee of Shenzhen Bay Laboratory, led a team to conduct a pre New Year's Day safety inspection of the High Tech Innovation Center and Pingshan Biomedical Research and Development Transformation Center. Secretary Hu Xiaojun and his delegation conducted on-site safety inspections on the high-tech innovation experimental area, office area, and Pingshan Biomedical Research and Transformation Center experimental area, to understand the implementation of various safety measures before the New Year's Day, and conducted close interviews with employees. Secretary Hu Xiaojun emphasized that firstly, all research institutes/centers and departments should effectively implement various safety measures before the "New Year's Day", focusing on the safety of chemical reagents, fire protection, electricity, and other aspects. Before the holiday, combustible materials such as discarded cardboard boxes should be cleaned up, and unnecessary continuous power supply should be turned off; Secondly, we need to increase the intensity of safety inspections, promptly identify and eliminate safety hazards; Thirdly, it is necessary to arrange personnel on duty during holidays and increase the frequency of inspections during holidays. He stated that in the past year, with the joint efforts of all employees, Shenzhen Bay Laboratory has achieved certain results, and its development will be even more brilliant in the coming year. During the visit, he extended holiday greetings and New Year greetings to the employees. Personnel from the Comprehensive Department and Platform Department of Shenzhen Bay Laboratory accompanied the inspection. Author | Wu Shuai from the Platform Department Photography | Ji Er Edit | B and B

2020/12/30

Introduction Recently, the Pingshan Biomedical R&D and Transformation Center of Shenzhen Bay Laboratory collaborated with the Shenzhen Graduate School of Peking University to publish a research paper titled "Substrate-binding stabilizes the hydrodynamic cluster to understand the inhibition of bacterial ubiquitin ligase IpaH9.8" in the sub journal "Communications Biology" of Nature, This article introduces the new progress made in the study of the activation mechanism of bacterial E3 enzymes. This study focuses on the Shigella E3 enzyme IpaH9.8, and elucidates the mechanism of IpaH9.8 self inhibition and substrate induced activation by analyzing the crystal structure of the full length protein of IpaH9.8 and its complex with substrate protein hGBP1. (Long press to recognize the QR code in the picture below to read the paper) Recently, the Pingshan Biomedical R&D and Transformation Center of Shenzhen Bay Laboratory collaborated with the Shenzhen Graduate School of Peking University to publish a research paper titled "Substrate-binding stabilizes the hydrodynamic cluster to understand the inhibition of bacterial ubiquitin ligase IpaH9.8" in the sub journal "Communications Biology" of Nature, This article introduces the new progress made in the study of the activation mechanism of bacterial E3 enzymes. This study focuses on the Shigella E3 enzyme IpaH9.8, and elucidates the mechanism of IpaH9.8 self inhibition and substrate induced activation by analyzing the crystal structure of the full length protein of IpaH9.8 and its complex with substrate protein hGBP1. IpaH family proteins are E3 Ubiquitin ligase from Gram-negative bacteria, which are composed of three parts: the N-terminal T3SS signal sequence, the LRR domain responsible for binding the substrate, and the C-terminal conserved NEL domain with E3 enzyme function. These E3 enzymes can inhibit host inflammation and endogenous immune response by hijacking the host's ubiquitin Proteasome signaling pathway, thus promoting the infection process. In host cells, in order to avoid self ubiquitination and degradation by the host's ubiquitin system, or to avoid the production of free Ub chains that activate the host immune response, IpaH proteins are usually in a self inhibitory state when there is no substrate. IpaH9.8 is an E3 enzyme secreted by Shigella, which can target ubiquitination to degrade NEMO (NF) in host cells- κ B regulator), GBP1 (Guanylate-binding protein 1) and other proteins, which in turn affect the immune response of the host. In this study,