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Effect of Proactive and Reactive Outside Directors’ Behavior on Banks’ Financial Performance
( Eunsuh Lee ),( Kwanghee Cho ),( Hyunjeong Baek ),( Wooseok Choi ) 한국생산성학회 2017 生産性論集 Vol.31 No.4
The board of directors plays a significant role in monitoring and advising managers. Board of directors are usually consisted of inside directors and outside directors. Inside directors are defined to be all employee directors, whereas outside directors are defined to be all non-employee directors (Beasley, 1996). Fama and Jensen (1983) argue that outside directors have strong incentive to monitor managers effectively in agency settings and not to collude with top managers to expropriate stockholder wealth. In addition, Weisbach (1988) argues that outside directors pay great attention to firm’s financial performance by replacing poor performing chief executive officers. In this study, we examine the influence of proactive and reactive outside directors’ behavior on banks’ financial performance in the Korean banking industry. We define proactive outside directors’ behavior as the board meeting attendance ratio by outside directors and reactive outside directors’ behavior as the board meeting frequency. We use non-performing loans (so-called bad loans) to measure banks’ financial performance (Barseghyan, 2010) because non-performing loans are the most common proxy to measure banks’ financial performance and the most common reason why banks fail (Beattie et al., 1995). We hypothesize that not all outside directors’ behavior would play a major role in improving banks’ financial performance. Results of this study indicate that only proactive outside directors’ behavior significantly improves banks’ financial performance, whereas reactive outside directors’ behavior does not play a significant role in improving banks’ financial performance. Overall, results of this study suggest that proactive outside directors’ behavior is an important dimension of improving banks’ financial performance, but not reactive board behavior. In addition, this study contributes to bank literature by examining the effect of outside directors’ behavior on non-performing loans.
RBP 신호배열 돌연변이 rbsB103에 대한 RBP 아미노산 50번 위치의 복귀 돌연변이 분리
강문석,백광희 경희대학교 유전공학연구소 1993 遺傳工學論文集 Vol.5 No.-
Ribose-binding protein(RBP) of E. coli function in the periplasm as a component of a high affinity transport system for ribose and as a primary receptor for chemotaxis toward ribose. A mutant(rbsB103) in the signal sequence of RBP has a defect in the export of the protein to the periplasm. The intragenic suppressors for rbsB103 were isolated genetically. One of them had a change at 50th amino acid of RBP. In order to assess the role of the 50th amino acid in the transport of RbsB103, we substituted the valine of 50th position with various amino acids by site-directed mutagenesis. The assay of the mutants by chemotaxis indicates that the replacement of the Val by Cys, Glu, Gln, Gly, His, Ile, Leu, Gln, Ser, Thr, or Tyr can suppress the defect of protein transport.
Agarwal, Kan,Baek, KwangHee,Jeon, ChoonJu,Miyamoto, Kenichi,Ueno, Akemichi,Yoon, HoSup 경희대학교 유전공학연구소 1991 遺傳工學論文集 Vol.3 No.-
The eukaryotic transcriptional factor TFIIS enhances transcript elongation by RNA polymerase Ⅱ. Here we describe two functional domains in the 280 amino acid human TFIIS protein: residues within positions 100-230 are required for binding to polymerase, and residues 230-280, which form a zinc finger, are required in conjunction with the polymerase binding region for transcriptional stimulation. Interestingly, a mutant TFIIS with only the polymerase binding domain actually inhibits transcription, whereas a mutant in which the polymerase binding and zinc finger domains are separated by an octapeptide is only weakly active. The zinc finger itself has no effect on transcription, but in contrast to the wild-type protein, it binds to oligonucleotides. These finding suggest that TFⅡS may interact with RNA polymerase Ⅱ such that the normally masked zinc finger can specifically contact nucleotides in the transcription elongation zone at a position juxtaposed to the polymerization site.
Site-directed Mutagenesis에 의한 rbsB103의 복기 돌연변이 분리
이덕연,백광희 경희대학교 유전공학연구소 1992 遺傳工學論文集 Vol.4 No.-
Ribose-binding protein (RBP) of E. coli function in the periplasm as a component of a high affinity transport system for ribose and as a primary receptor for chemotaxis toward ribose. A mutational change(rbsB103) in the signel sequence of RBP block the export of the protein to the periplasm. One of the intragenic suppressors for rbsB103 isolated genetically carries mutation at 27th position of RBP. In order to assess the role of the 27th amino acid in protein transport, we substituted the Ala of 27th position with various amino acids by site-directed mutagenesis method. The assay of the mutants by chemotaxis indicates that the replacement of the Ala by Cys, Gly, Ser, Thr, or Val can suppress the defect of protein transport, but the replacement by Glu, Pro, or Leu cannot.
Cloning, expression and characterization of the human transcription elongation factor, TFIIS
Yoo, OokJoon,Yoon, HoSup,Baek, KwangHee,Jeon, ChoonJu,Miyamoto, Kenichi,Ueno, Akemichi,Agarwal, Kan 경희대학교 유전공학연구소 1991 遺傳工學論文集 Vol.3 No.-
The cDNA for the human elongation factor, TFIIS, has been cloned and expressed in E. coli with the T7 expression system. This 280-amino acid TFIIS protein is shorter by 21 residues than that of the mouse. The missing 21 residues are located in the amino-terminal region, which is not thought to be required for transcriptional stimulation. Apart from this gap, human and mouse proteins reveal 96% overall identity and 98.5% sequence similarity if conservative substitutions are taken into account. The bacterially expressed human protein and the purified calf thymus proteins are indistinguishable in their ability to stimulate transcript elongation by purified RNA polymerase Ⅱ. Estimation of the native molecular size of the human protein in solution indicates that it exists as a dimer.
Structure of the Human Gene Encoding the MAp19 and MASP-2 Proteins
Park, Dongkyu,Kim, Bongy,Baek, Kwanghee,Yoon, Jaeseung 한국유전학회 2002 Genes & Genomics Vol.24 No.3
We have characterized the complete structure of the human gene encoding the MAp19 and MASP-2 proteins which are involved in one of the important innate immune defense mechanisms of the hosts. The mRNA species encoding MASP-2 and MAp19 are encoded by the alternative splicing and polyadenylation from a single structural gene. The gene consists of 12 exons. The four exons are common to both MAp19 and MASP-2 transcripts, one exon is specific for MAp19 transcript, and seven exons are specific for MASP-2 transcript. The transcription start point was determined by 5'-RACE analysis.
Byun, Jaegoo,Yoon, Jaeseung,Baek, Kwanghee Springer-Verlag 2009 Molecules and cells Vol.27 No.5
<P>GTP cyclohydrolase I (GTPCH) is a key enzyme in the de novo synthesis of tetrahydrobiopterin. Previously, the Drosophila melanogaster GTPCH gene has been shown to be expressed from two different promoters (P1 and P2). In our study, the 5'-flanking DNA regions required for P1 and P2 promoter activities were characterized using transient expression assay. The DNA regions between -98 and +31, and between -73 and +35 are required for efficient P1 and P2 promoter activities, respectively. The regions between -98 and -56 and between -73 and -41 may contain critical elements required for the expression of GTPCH in Drosophila. By aligning the nucleotide sequences in the P1 and P2 promoter regions of the Drosophila melanogaster and Drosophila virilis GTPCH genes, several conserved elements including palindromic sequences in the regions critical for P1 and P2 promoter activities were identified. Western blot analysis of transgenic flies transformed using P1 or P2 promoter-lacZ fusion plasmids further revealed that P1 promoter expression is restricted to the late pupae and adult developmental stages but that the P2 promoter driven expression of GTPCH is constitutive throughout fly development. In addition, X-gal staining of the embryos and imaginal discs of transgenic flies suggests that the P2 promoter is active from stage 13 of embryo and is generally active in most regions of the imaginal discs at the larval stages.</P>