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Gwangju, South Korea

Chonnam National University is a South Korean university located in the metropolitan city of Gwangju which lies in the middle of South Jeolla or Jeonnam province, for which the school is named in the Southwest of the country. The university was formally established in January, 1952 through the union of Gwangju Medical College, Gwangju Agricultural College, Mokpo Commerce College, and Daeseong College. It currently consists of 59 academic departments in 19 colleges and 11 graduate programs. University attached facilities are the University Library, Museum, Health Service Center, Agro-Bioindustry Technical Support Center, Animal Hospital, Language Education Center, School of Lifelong Education, and University Computing Center. In March 2006, Yeosu National University merged with Chonnam National University to become a satellite campus.Chonnam National University used to be generally regarded as one of the five major national universities of South Korea together with Seoul National University, Pusan National University, Kyungpook National University, and Chungnam National University. Now the number of the key national universities has been expanded into ten. CNU is also recognized as one of the best performers in government supported HRD projects. Research expenses of CNU ranks 13th nationally. Moreover, the number of High-ranking public officials ranked 11th. In addition, 26 alumni passed the Second Round of the 51st national bar exam, which is the biggest since the CNU Law School was established. Wikipedia.


Provided are a peptide compound prepared by additional synthesis in a drug having an effect of inhibiting restenosis, a composition for inhibiting restenosis and promoting re-endothelialization including the peptide compound, and a stent having a surface coated by using the composition, in order to overcome a restenosis problem in the stent.


A method for preparing a catalyst having catalytically active materials selectively impregnated or supported only in the surface region of the catalyst particle using the mutual repulsive force of a hydrophobic solution and a hydrophilic solution and the solubility difference to a metal salt precursor between the hydrophobic and hydrophilic solutions. The hydrophobic solvent is a C2-C6 alcohol. The hydrophobic solvent is introduced into the catalyst support and then removed of a part of the pores connected to the outer part of the catalyst particle by drying under appropriate conditions. Then, a hydrophilic solution containing a metal salt is introduced to occupy the void spaces removed of the hydrophobic solvent, and the catalyst particle is dried at a low rate to selectively support or impregnate the catalytically active material or the precursor of the catalytically active material only in the outer part of the catalyst particle.


Patent
Chonnam National University | Date: 2014-01-13

Disclosed are a peptide for promoting osteogenesis and vascularization, and the use thereof. The peptide has a low molecular weight so that it can be economically produced. In addition, it promotes osteoblastic differentiation, thus inducing osteogenesis. Further, the peptide can promote the expression of VEGF, resulting in vascularization. Accordingly, the peptide is useful for the delay of the onset of ischemic diseases and the therapy of ischemic diseases.


Patent
Korea Basic Science Institute and Chonnam National University | Date: 2014-09-29

Disclosed is an economic method for concentrating virus and detecting virus, such that virus in a sample solution having low virus concentration can be concentrated with high efficiency within a short time. Particularly, the method comprising the steps of: (A) adding Concanavalin A (Con A) to a sample solution containing a virus, and reacting the added Concanavalin A with the virus in the sample solution to form a virus-Concanavalin A conjugate; and (B) separating the virus-Concanavalin A conjugate from the sample solution.


Provided is a ramp tag capable of solving instability in translation rate resulting from poor compatibility between codons in a foreign gene and a host when expressing a recombinant protein in

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