Pub Date : 2012-12-05DOI: 10.3724/SP.J.1206.2011.00368
Yu-Zhen Li, Xiuhua Liu
{"title":"Advance in PUMA and Cardiomyocyte Apoptosis*: Advance in PUMA and Cardiomyocyte Apoptosis*","authors":"Yu-Zhen Li, Xiuhua Liu","doi":"10.3724/SP.J.1206.2011.00368","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2011.00368","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"49 1","pages":"1045-1049"},"PeriodicalIF":0.3,"publicationDate":"2012-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78851277","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-12-05DOI: 10.3724/SP.J.1206.2011.00430
Wei Li, Ying Lin
{"title":"Identification of Human Methyl-CpG Binding Domain Protein (MBD) 4 as a Substrate of Protein Kinase X*: Identification of Human Methyl-CpG Binding Domain Protein (MBD) 4 as a Substrate of Protein Kinase X*","authors":"Wei Li, Ying Lin","doi":"10.3724/SP.J.1206.2011.00430","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2011.00430","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"30 1","pages":"1109-1117"},"PeriodicalIF":0.3,"publicationDate":"2012-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85790669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-12-05DOI: 10.3724/SP.J.1206.2011.00558
Dafei Xie, Peng Li, Fei Li, X. Bo, Shengqi Wang
{"title":"Computational Approaches to Analyze the Strategies of Drug Repositioning*: Computational Approaches to Analyze the Strategies of Drug Repositioning*","authors":"Dafei Xie, Peng Li, Fei Li, X. Bo, Shengqi Wang","doi":"10.3724/SP.J.1206.2011.00558","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2011.00558","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"145 1","pages":"1029-1036"},"PeriodicalIF":0.3,"publicationDate":"2012-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86214678","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-12-05DOI: 10.3724/SP.J.1206.2012.00007
Kun He, Ya-Kun Zhang, Xian-long Ye, Wen-Fei Wang, Rui Chen, Ming-yao Liu, Mingxiao Feng, Jialei Xu, Deshan Li
{"title":"Stability and Glucose Regulation of FGF21 After Modified With Arginines*: Stability and Glucose Regulation of FGF21 After Modified With Arginines*","authors":"Kun He, Ya-Kun Zhang, Xian-long Ye, Wen-Fei Wang, Rui Chen, Ming-yao Liu, Mingxiao Feng, Jialei Xu, Deshan Li","doi":"10.3724/SP.J.1206.2012.00007","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2012.00007","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"11 1","pages":"1089-1098"},"PeriodicalIF":0.3,"publicationDate":"2012-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89697123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-12-05DOI: 10.3724/SP.J.1206.2012.00084
Qinghua Wu, Ji-yong Liu, Yixu Chen, R. Jiao
{"title":"dCAF-1-p55 is Essential for Drosophila Development and Involved in The Maintenance of Chromosomal Stability*: dCAF-1-p55 is Essential for Drosophila Development and Involved in The Maintenance of Chromosomal Stability*","authors":"Qinghua Wu, Ji-yong Liu, Yixu Chen, R. Jiao","doi":"10.3724/SP.J.1206.2012.00084","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2012.00084","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"8 1","pages":"1073-1081"},"PeriodicalIF":0.3,"publicationDate":"2012-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78555202","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-11-23DOI: 10.3724/SP.J.1206.2012.00048
Can Yuan, Xiaoroang Li, Dan Gu, Yue-hua Gu, Ying-Jie Gao, Sujuan Cui
{"title":"The Effect of Arabidopsis LFR Protein Domain on Its Co-transactivation and Subcellular Localization in Nucleus*: The Effect of Arabidopsis LFR Protein Domain on Its Co-transactivation and Subcellular Localization in Nucleus*","authors":"Can Yuan, Xiaoroang Li, Dan Gu, Yue-hua Gu, Ying-Jie Gao, Sujuan Cui","doi":"10.3724/SP.J.1206.2012.00048","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2012.00048","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"18 1","pages":"1003-1011"},"PeriodicalIF":0.3,"publicationDate":"2012-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80799302","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-11-23DOI: 10.3724/SP.J.1206.2012.00298
Liang-kuan Bi, Tianxin Lin, Kewei Xu, Jinli Han, Hai Huang, Cai-xia Zhang, W. Dong*, Hao Liu, Jian Huang
{"title":"IL-8 Regulates The Epithelial-mesenchymal Transition (EMT) of Renal Cancer Through PKC/ERK Signaling Pathway*: IL-8 Regulates The Epithelial-mesenchymal Transition (EMT) of Renal Cancer Through PKC/ERK Signaling Pathway*","authors":"Liang-kuan Bi, Tianxin Lin, Kewei Xu, Jinli Han, Hai Huang, Cai-xia Zhang, W. Dong*, Hao Liu, Jian Huang","doi":"10.3724/SP.J.1206.2012.00298","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2012.00298","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"37 1","pages":"981-986"},"PeriodicalIF":0.3,"publicationDate":"2012-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90447639","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-11-23DOI: 10.3724/SP.J.1206.2011.00228
D. Ren, M. Cui, Yiqiu Xia, Zheng You
{"title":"Micropatterning and Its Applications in Biomedical Research*: Micropatterning and Its Applications in Biomedical Research*","authors":"D. Ren, M. Cui, Yiqiu Xia, Zheng You","doi":"10.3724/SP.J.1206.2011.00228","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2011.00228","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"37 1","pages":"931-944"},"PeriodicalIF":0.3,"publicationDate":"2012-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85749402","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-11-23DOI: 10.3724/SP.J.1206.2012.00469
Haitao Luo, Yi Zhao
{"title":"The Functional Roles of microRNA: The Functional Roles of microRNA","authors":"Haitao Luo, Yi Zhao","doi":"10.3724/SP.J.1206.2012.00469","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2012.00469","url":null,"abstract":"","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"27 1","pages":"979-980"},"PeriodicalIF":0.3,"publicationDate":"2012-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78997043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-11-23DOI: 10.3724/SP.J.1206.2011.00611
Jian Li, Lihua（孙丽华） Sun, Chunyan Xu, F. Yu, Huan Zhou, L. Tang, Jianhua He
Heat shock protein 90 (Hsp90) is essential for folding, maturation and stabilization of many important proteins, which are involved in cell cycle regulation, signal transduction, and cell growth regulation. The highly conserved N-terminal domain contains an ATP binding cleft and thus is responsible for the catalytic activity of Hsp90. In order to further study the function and structure of Hsp90, the N-terminal of the human Hsp90 was cocrystallized with AMPPNP and ATP gamma S. The cocrystallization experiments were carried out at 277K using the hanging drop vapor-diffusion method, X-ray diffraction data were collected on beamline 17U at the SSRF and the structures were solved by molecular replacement. The densities of the two nucleotides were captured and the interactions between Hsp90(N) and nucleotides were clearly described. We confirmed that the gamma-phosphate of ATP gamma S was not hydrolyzed by Hsp90(N). The position of S 1 and ATP lid in human Hsp90(N)-AMPPNP differs significantly from that of the structure of yeast Hsp90-AMPPNP. By analyzing the structure of human Hsp90(N)-AMPPNP, we found that the interactions of E18-K100 and N40-D127 block the moving of Si and ATP lid, and then prevent the dimerization of Hsp90(N). This reflects the complexity and coordination of Hsp90 on the regulation of the function.
{"title":"Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90*: Crystal Structures of N-terminal Domain of Human Hsp90 With ATP Analogues Reveal The Functional Regulation of Hsp90*","authors":"Jian Li, Lihua（孙丽华） Sun, Chunyan Xu, F. Yu, Huan Zhou, L. Tang, Jianhua He","doi":"10.3724/SP.J.1206.2011.00611","DOIUrl":"https://doi.org/10.3724/SP.J.1206.2011.00611","url":null,"abstract":"Heat shock protein 90 (Hsp90) is essential for folding, maturation and stabilization of many important proteins, which are involved in cell cycle regulation, signal transduction, and cell growth regulation. The highly conserved N-terminal domain contains an ATP binding cleft and thus is responsible for the catalytic activity of Hsp90. In order to further study the function and structure of Hsp90, the N-terminal of the human Hsp90 was cocrystallized with AMPPNP and ATP gamma S. The cocrystallization experiments were carried out at 277K using the hanging drop vapor-diffusion method, X-ray diffraction data were collected on beamline 17U at the SSRF and the structures were solved by molecular replacement. The densities of the two nucleotides were captured and the interactions between Hsp90(N) and nucleotides were clearly described. We confirmed that the gamma-phosphate of ATP gamma S was not hydrolyzed by Hsp90(N). The position of S 1 and ATP lid in human Hsp90(N)-AMPPNP differs significantly from that of the structure of yeast Hsp90-AMPPNP. By analyzing the structure of human Hsp90(N)-AMPPNP, we found that the interactions of E18-K100 and N40-D127 block the moving of Si and ATP lid, and then prevent the dimerization of Hsp90(N). This reflects the complexity and coordination of Hsp90 on the regulation of the function.","PeriodicalId":20655,"journal":{"name":"生物化学与生物物理进展","volume":"10 1","pages":"995-1002"},"PeriodicalIF":0.3,"publicationDate":"2012-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82093662","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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