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Jang, Yunseon,Choo, Hyosun,Lee, Min Joung,Han, Jeongsu,Kim, Soo Jeong,Ju, Xianshu,Cui, Jianchen,Lee, Yu Lim,Ryu, Min Jeong,Oh, Eung Seok,Choi, Song-Yi,Chung, Woosuk,Kweon, Gi Ryang,Heo, Jun Young MDPI AG 2019 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.20 No.14
<P>Current therapeutics for Parkinson’s disease (PD) are only effective in providing relief of symptoms such as rigidity, tremors and bradykinesia, and do not exert disease-modifying effects by directly modulating mitochondrial function. Here, we investigated auraptene (AUR) as a potent therapeutic reagent that specifically protects neurotoxin-induced reduction of mitochondrial respiration and inhibits reactive oxygen species (ROS) generation. Further, we explored the mechanism and potency of AUR in protecting dopaminergic neurons. Treatment with AUR significantly increased the viability of substantia nigra (SN)-derived SN4741 embryonic dopaminergic neuronal cells and reduced rotenone-induced mitochondrial ROS production. By inducing antioxidant enzymes AUR treatment also increased oxygen consumption rate. These results indicate that AUR exerts a protective effect against rotenone-induced mitochondrial oxidative damage. We further assessed AUR effects in vivo, investigating tyrosine hydroxylase (TH) expression in the striatum and substantia nigra of MPTP-induced PD model mice and behavioral changes after injection of AUR. AUR treatment improved movement, consistent with the observed increase in the number of dopaminergic neurons in the substantia nigra. These results demonstrate that AUR targets dual pathogenic mechanisms, enhancing mitochondrial respiration and attenuating ROS production, suggesting that the preventative potential of this natural compound could lead to improvement in PD-related neurobiological changes.</P>
Jang, Sung Kyu,Kim, Sookyung,Salman, Muhammad Saad,Jang, Ji-ryang,Um, Yu Mi,Tan, Lihan,Park, Jin-Hong,Choe, Woo-Seok,Lee, Sungjoo American Chemical Society 2018 Chemistry of materials Vol.30 No.3
<P>A high-performance biomaterial-based resistive switching (RS) device is fabricated by harnessing a thermally denatured protein (hexa-His-tagged recombinant molecular chaperone DnaJ (rDnaJ)) as a switching layer in a Cu/rDnaJ/Pt configuration on SiO<SUB>2</SUB>/Si substrate. The conductivity of the heat-denatured rDnaJ protein layer between the metal electrodes can be reversibly controlled to enable the formation/rupture of conductive Cu filaments by tailoring the metal chelating properties of the amino acid residues in the insulating protein matrix in a pH- and/or redox potential-dependent manner, giving rise to high-performance nonvolatile RS behavior. The rDnaJ-based RS device exhibits extremely low set voltage (∼0.12 V) and reset voltage (∼−0.08 V) with excellent uniformity, along with large memory window (<I>R</I><SUB>HRS</SUB>/<I>R</I><SUB>LRS</SUB> > 10<SUP>6</SUP>) and long retention time (>10<SUP>6</SUP> s). In addition, the rDnaJ RS device, which is fabricated on a flexible poly(ethylene terephthalate) substrate, exhibits an uncompromised switching performance. The present study is the first attempt to explore the use of a recombinant protein as a functional switching layer in RS devices. This approach opens up a new method of harnessing recombinant proteins with engineered properties as powerful building blocks to suit the requirements of next-generation biocompatible, flexible, high-performance, and low power consumption electronics.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/cmatex/2018/cmatex.2018.30.issue-3/acs.chemmater.7b04261/production/images/medium/cm-2017-04261p_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/cm7b04261'>ACS Electronic Supporting Info</A></P>
SUC2 promoter를 갖는 재조합 Saccharomyces cerevisiae의 발효동력학적 연구
변유량,최동원,조형용,장재권,김인규 연세대학교 산업기술연구소 1990 논문집 Vol.22 No.1
In order to improve the productivity of invertase by recombinant Saccharomyces cerevisiae SUC2 promoter, growth kinetics was investigated in batch and continuous culture. In glucose limited chemostat culture under nonaerated condition, the biomass concentration decreased with an increase of dilution rate. However the invertase activity was found to have a peak at a dilution rate of 0.185??, where the concentration of glucose was 0.055g/ℓ. Beyond this rate, the invertase biosynthesis was repressed by residual glucose in the culture. Specific and total invertase activity increased about in 1.7 and 2.9 fold in a batch culture by the fed batch culture with continuous feeding of 0.096g/ℓ glucose supplemented with a small amount of organic nutrient. A kinetic model was developed to analyze the invertase production of recombinant cells and the model could successfully demonstrated the experimental results.
Kim, Dae-Jin,Jang, Hyeung-Jin,Pyun, Yu-Ryang,Kim, Yu-Sam 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.3
A gene, coined tay, for a thermostable DNA polymerase from the novel, extremely thermophilic bacterium Thermoanaerobacter yonseiensis was cloned and expressed in E. coli. Using a DNA polymerase homologous PCR product as a hybridization probe, tay was isolated and sequenced to consist of 2621 nucleotides that encode 872 amino acids. A database analysis showed that DNA polymerase, coined Tay, from T. yonseiensis shared a 39% to 47% identity in the amino acid sequence with those from other DNA polymerases. Tay was overexpressed in E. coli as a fusion protein with a poly-histidine tag at the C-terminus. It was purified by heat treatment, followed by a $Ni^{2+}$-chelate column. The molecular weight of purified Tay was approximately 97 kDa, as shown by SDS PAGE, and it showed high DNA polymerase activity and thermostability. However, it had no 3'$\rightarrow$5' exonuclease activity.
Kim, Kwang Su,Um, Yu Mi,Jang, Ji-ryang,Choe, Woo-Seok,Yoo, Pil J. American Chemical Society 2013 ACS APPLIED MATERIALS & INTERFACES Vol.5 No.9
<P>Graphene-based electrochemical impedance sensors have recently received much attention due to their outstanding sensing capability and economic viability. In this study, we present a novel means of constructing an impedance sensing platform via harnessing intrinsic π-stacking interactions between probe protein molecules and reduced graphene oxide (RGO) substrate, obviating the need for introducing external chemical groups often required for covalent anchoring of the probes. To achieve this goal, protein molecules used as a probe were denatured to render their hydrophobic residues exposed in order to facilitate their direct π-stacking interactions with the surface of RGO nanosheets. The protein molecules in denatured form, which would otherwise have difficulty in undergoing π-stacking interactions with the RGO surface, were found to uniformly cover the RGO nanosheets at high density, conducive to providing a graphene-based impedance sensing platform capable of detecting a probe-specific analyte at high sensitivity. The proof-of-concept performance of thus-constructed RGO-based impedance sensors was demonstrated via selective detection of biological binding events of antigen–antibody reaction at a femtomolar range. Notably, since the π-stacking interaction can occur on the entire RGO surface, it can desirably exclude a backfill process indispensable for the conventional biosensors to suppress background noise signals. Since the procedure of π-stacking mediated direct deposition of on-purpose denatured protein probes onto the RGO surface is facile and straightforward, the proposed strategy is anticipated to extend its applicability for fabrication of high performance graphene-based bio or chemical sensors.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/aamick/2013/aamick.2013.5.issue-9/am303238r/production/images/medium/am-2012-03238r_0011.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/am303238r'>ACS Electronic Supporting Info</A></P>