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【期刊论文】西洋参胚性的细胞和胚状体细胞中的核内含与细胞质内含体
郑晓峰, 黄百渠
植物学报,1994,36(1):73~74,-0001,():
-1年11月30日
The presence of intranuclear and cytoplasmic inclusions in cells of embryogenic callus and developing embryoids from tissue cultures of Panax quinque folius L. was described, These cellular structures were not found in non-embryogenic cells. The size of intranuclear and cytoplasmic inclusions seemed to be related to the developmental status of the cell.
西洋参, 核内含体, 细胞质内含体
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【期刊论文】The Crystal Structure of human AK6 An Adenylate Kinase Isoform Localized to the Cell Nucleus
郑晓峰
,-0001,():
-1年11月30日
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郑晓峰, Hui Ren*†‡, Liya Wang‡§, Matthew Bennett*‡, Yuhe Liang*, Xiaofeng Zheng†, Fei Lu, Lanfen Li*†, Jie Nan†, Ming Luo†, Staffan Eriksson§, Chuanmao Zhang, and Xiao-Dong Su*†**
PNAS January 11, 2005 vol. 102 no.2 303-308,-0001,():
-1年11月30日
Adenylate kinases (AKs) play important roles in nucleotide metabolism in all organisms and in cellular energetics by means of phosphotransfer networks in eukaryotes. The crystal structure of a human AK named AK6 was determined by in-house sulfur single-wavelength anomalous dispersion phasing methods and refined to 2.0-Å resolution with a free R factor of 21.8%. Sequence analyses revealed that human AK6 belongs to a distinct subfamily of AKs present in all eukaryotic organisms sequenced so far. Enzymatic assays show that human AK6 has properties similar with other AKs, particularly with AK5. Fluorescence microscopy showed that human AK6 is localized predominantly to the nucleus of HeLa cells. The identification of a nuclear-localized AK sheds light on nucleotide metabolism in the nucleus and the energetic communication between mitochondria and nucleus by means of phosphotransfer networks.
x-ray crystallographyㄧnuclear localizationㄧnucleotide metabolismㄧphosphotransfer networks
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【期刊论文】Systematic high-yield production of human secreted proteins in Escherichia coli
郑晓峰, Xueyu Dai a, b, Qiang Chen a, Min Lian a, Yanfeng Zhou b, Mo Zhou b, Shanyun Lu b, Yunjia Chen a, Jingchu Luo a, Xiaocheng Gu a, Ying Jiang a, Ming Luo b, c, Xiaofeng Zheng a, *
Biochemical and Biophysical Research Communications 332(2005)593-601,-0001,():
-1年11月30日
Human secreted proteins play a very important role in signal transduction. In order to study all potential secreted proteins identified from the human genome sequence, systematic production of large amounts of biologically active secreted proteins is a prerequisite. We selected 25 novel genes as a trial case for establishing a reliable expression system to produce active human secreted proteins in Escherichia coli. Expression of proteins with or without signal peptides was examined and compared in E. coli strains. The results indicated that deletion of signal peptides, to a certain extent, can improve the expression of these proteins and their solubilities. More importantly, under expression conditions such as induction temperature, N-terminus fusion peptides need to be optimized in order to express adequate amounts of soluble proteins. These recombinant proteins were characterized as well-folded proteins. This system enables us to rapidly obtain soluble and highly purified human secreted proteins for further functional studies.
Secreted protein, Signal peptide, Escherichia coli, Protein expression
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【期刊论文】Systematic high-yield production of human secreted proteins in Escherichia coli
郑晓峰
,-0001,():
-1年11月30日
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