埃德蒙德·亨利·费舍尔(Edmond Henri Fischer)是西雅图华盛顿大学的生化学家,1920年出生于中国上海,由于其在可逆磷酸化方面的发现:一种在绝大部分活体细胞中存在的活化和减活化酶的调节机制,1992年与他人共同获得诺贝尔生理...埃德蒙德·亨利·费舍尔(Edmond Henri Fischer)是西雅图华盛顿大学的生化学家,1920年出生于中国上海,由于其在可逆磷酸化方面的发现:一种在绝大部分活体细胞中存在的活化和减活化酶的调节机制,1992年与他人共同获得诺贝尔生理学或医学奖。展开更多
Using degenerate PCR and TAIL-PCR,a protein kinase gene OPK1(Genebank accession No.:EU417815) was cloned from mycoparasite fungi Olpitrichum tenellum.OPK1 has an open reading frame of 2 031 bp interrupted by two intro...Using degenerate PCR and TAIL-PCR,a protein kinase gene OPK1(Genebank accession No.:EU417815) was cloned from mycoparasite fungi Olpitrichum tenellum.OPK1 has an open reading frame of 2 031 bp interrupted by two introns(108 bp,84 bp) and putatively encodes a protein of 676 aa.Phylogenetic analysis indicated that OPK1 was most similar to other serine-threonine protein kinase in fungi.Southern blot analysis indicated that OPK1 is present as a single copy in the genome.RT-PCR showed it could be transcribed both in the phase of spore germination and hyphal growth.展开更多
DNA damage response (DDR) is among the most important of the mechanisms that maintain genome stability which, when destabilized, predisposes organs to cancer. Reversible phosphorylation mediated by protein kinases and...DNA damage response (DDR) is among the most important of the mechanisms that maintain genome stability which, when destabilized, predisposes organs to cancer. Reversible phosphorylation mediated by protein kinases and protein phosphatases regulates most, if not all, cellular activities, including DDR. Protein kinase inhibitors have become the main focus of targeted therapy and anticancer drug development. However, our limited knowledge of protein phosphatase function is compromising our capacity to develop therapeutic agents against phosphatases. In this review, we summarize the roles of serine/threonine protein phosphatases involved in DDR and propose that in situ dephosphorylation of phosphoproteins by protein phosphatases, instead of proteasome-mediated degradation of phosphoproteins, is mainly employed by cells.展开更多
文摘Using degenerate PCR and TAIL-PCR,a protein kinase gene OPK1(Genebank accession No.:EU417815) was cloned from mycoparasite fungi Olpitrichum tenellum.OPK1 has an open reading frame of 2 031 bp interrupted by two introns(108 bp,84 bp) and putatively encodes a protein of 676 aa.Phylogenetic analysis indicated that OPK1 was most similar to other serine-threonine protein kinase in fungi.Southern blot analysis indicated that OPK1 is present as a single copy in the genome.RT-PCR showed it could be transcribed both in the phase of spore germination and hyphal growth.
基金supported by the startup fund from Capital Normal Universitythe National Natural Science Foundation of China (30570371, 90608014, 30711120570 and 31071190)+3 种基金the Program for New Century Excellent Talents in University (NCET-06-0187)Beijing Natural Science Foundation Program and Scientific Research Key Program of Beijing Municipal Commission of Education (KZ200810028014)the National Basic Research Program of China (2010CB911904)Funding Project for Academic Human Resources Development in Institutions of Higher Learning under the Jurisdiction of Beijing Municipality (PHR20110508) to XU XingZhi
文摘DNA damage response (DDR) is among the most important of the mechanisms that maintain genome stability which, when destabilized, predisposes organs to cancer. Reversible phosphorylation mediated by protein kinases and protein phosphatases regulates most, if not all, cellular activities, including DDR. Protein kinase inhibitors have become the main focus of targeted therapy and anticancer drug development. However, our limited knowledge of protein phosphatase function is compromising our capacity to develop therapeutic agents against phosphatases. In this review, we summarize the roles of serine/threonine protein phosphatases involved in DDR and propose that in situ dephosphorylation of phosphoproteins by protein phosphatases, instead of proteasome-mediated degradation of phosphoproteins, is mainly employed by cells.
