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| 1 | “生物化学与分子生物学”课程思政案例的整合与教学实施显示文摘为完成高等教育课程育人根本目标,重塑医学生的价值观、职业观,教师挖掘“生物化学与分子生物学”课程中蕴含的思政资源,整合思政案例,使专业知识与思政元素有机融合,培养学生对专业的认知、认同和自豪感,提升学生的思想道德素养和综合素质。 | 吴明彩 吕俊 叶彩宏 | 2022 | 黑龙江教育(理论与实践)2022，，3： | 7 |
| 2 | Structures of the human pre-catalytic spliceosome and its precursor spliceosome显示文摘The pre-catalytic spliceosome (B complex) is preceded by its precursor spliceosome (pre-B complex) and followed by the activated spliceosome (Bact complex). The pre-B-to-B and B-to-Bact transitions are driven by the ATPase/helicases Prp28 and Brr2,respectively. In this study,we report the cryo-electron microscopy structures of the human pre-B complex and the human B complex at an average resolution of 5.7 and 3.8 A,respectively. In the pre-B complex,U1 and U2 small nuclear ribonucleoproteins (snRNPs) associate with two edges of the tetrahedron-shaped U4/U6.U5 tri-snRNP. The pre-mRNA is yet to be recognized by U5 or U6 small nuclear RNA (snRNA),and loop I of U5 snRNA remains unengaged. In the B complex,U1 snRNP and Prp28 are dissociated,the 5’-exon is anchored to loop I of U5 snRNA,and the 5’-splice site is recognized by U6 snRNA through duplex formation. In sharp contrast to S. cerevisiae,most components of U2 snRNP and tri-snRNP,exemplified by Brr2,undergo pronounced rearrangements in the human pre-B-to-B transition. Structural analysis reveals mechanistic insights into the assembly and activation of the human spliceosome. | Xiechao Zhan Chuangye Yan Xiaofeng Zhang Jianlin Lei Yigong Shi | 2018 | Cell Research2018，28，12： | 4 |
| 3 | Significance of alternative splicing in cancer cells显示文摘Objective:Alternative splicing can generate various structural and functional protein isoforms.Recently,accumulating evidence shows a relationship between alternative splicing and cancer.Cancer is a complex and chronic disease that involves malignant transformation.In this review,we consider alternative splicing events in relation to the hallmarks of cancer cells,and discuss current therapies to treat cancer-related to alternative splicing.Data sources:Data cited in this article are from the PubMed and Embase database,primarily focusing on research published from 2000 to 2018.Study selection:Articles were selected with the search terms“alternative splicing,”“cancer cell,”“tumor microenvironment,”and“therapy.”Results:Alternative splicing plays an important role in tumorigenesis,development,and escape from cell death.Taking this trait of cancer cells into consideration will allow more definite diagnoses of cancer,and allow the development of more effective medicines to intervene in cancer that could focus on controlling alternative splicing or competitively binding to the final products.Conclusions:Alternative splicing is common in cancer cells.Consideration of alternative splicing may allow different strategies for cancer therapy or the identification of novel biomarkers for cancer diagnosis. | Fei Qi Yong Li Xue Yang Yan-Ping Wu Lian-Jun Lin Xin-Min Liu | 2020 | Chinese Medical Journal2020，，2： | 0 |
| 4 | Structures of the human spliceosomes before and after release of the ligated exon显示文摘Pre-mRNA splicing is executed by the spliceosome,which has eight major functional states each with distinct composition.Five of these eight human spliceosomal complexes,all preceding exon ligation,have been structurally characterized.In this study,we report the cryo-electron microscopy structures of the human post-catalytic spliceosome(P complex)and intron lariat spliceosome(ILS)at average resolutions of 3.0 and 2.9??,respectively.In the P complex,the ligated exon remains anchored to loop I of U5 small nuclear RNA,and the 3′-splice site is recognized by the junction between the 5′-splice site and the branch point sequence.The ATPase/helicase Prp22,along with the ligated exon and eight other proteins,are dissociated in the P-to-ILS transition.Intriguingly,the ILS complex exists in two distinct conformations,one with the ATPase/helicase Prp43 and one without.Comparison of these three late-stage human spliceosomes reveals mechanistic insights into exon release and spliceosome disassembly. | Xiaofeng Zhang Xiechao Zhan Chuangye Yan Wenyu Zhang Dongliang Liu Jianlin Lei Yigong Shi | 2019 | Cell Research2019，29，4： | 0 |
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