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오형근 한국사진학회 2002 AURA Vol.0 No.9
As adults, we see sometimes what the youths may not see. We even decide what seemed true and necessary in a particular world, which we provide them, yet we have little control over how they perceive it. Every girls in my photographs look at the camera straight-on, willing to appear in their finery. It is as if we are looking at them, but they are seeing us. School uniform became increasingly strange as I sensed that it functioned as protective tools for these high school girls' youths. If it protects them, which is doubtful to begin with, I might have forgotten how my desire was repressed and how claustrophobic I felt just being inside of it. Again, as adults, we are the ones who force them into this particular world called as uniform. Pictorially, the circles around them in my photographs are implying another kind of uniform symbolizing repressed environment surrounding the high school girls. I did not anticipate these girls' particular emotion. However, I had always sensed both vulnerability and formidableness through their expressions and postures at the moment of photograph. I did not intend to glamorize their looks, however, there was always fascination about their star's quality of straight forward involvement mixed with self-containment. I hope these photographs make us pause to look at guesses and desires emerged deeply in their expressions and postures.
Quantitation and Validation of Atorvastatin using HPLC-UV
Heine, Daniel,Yong, Chul-Soon,Kim, Jung-Sun The Korean Society of Pharmaceutical Sciences and 2007 Journal of Pharmaceutical Investigation Vol.37 No.3
A reversed phase HPLC analysis of atorvastatin (AS) standard solution was performed using diclofenac (DF) as internal standard. Column oven temperature, flow rate and the composition of the mobile phase were varied in order to determine a practical system setup using a C18 column and UV detector. Two C18 columns of different length were compared regarding their influence on the AS peak shape. Based on these preliminary experiments a validation study was performed utilizing a C18 column at $62^{\circ}C$ with a mobile phase consisting of sodium phosphate buffer (0.05 M, pH 4.0), methanol and acetonitrile (40:50:10, v/v/v). The detection limit for AS was $0.1{\mu}g/ml$ and inter- and intra-day calibration curves were linear over a concentration range of $0.2-50{\mu}g/ml$. Accuracy and precision were satisfactory in the AS concentration range of $0.5-50{\mu}g/ml$.
The brain’s functional network architecture reveals human motives
Hein, Grit,Morishima, Yosuke,Leiberg, Susanne,Sul, Sunhae,Fehr, Ernst American Association for the Advancement of Scienc 2016 Science Vol.351 No.6277
<P>Goal-directed human behaviors are driven by motives. Motives are, however, purely mental constructs that are not directly observable. Here, we show that the brain's functional network architecture captures information that predicts different motives behind the same altruistic act with high accuracy. In contrast, mere activity in these regions contains no information about motives. Empathy-based altruism is primarily characterized by a positive connectivity from the anterior cingulate cortex (ACC) to the anterior insula (AI), whereas reciprocity-based altruism additionally invokes strong positive connectivity from the AI to the ACC and even stronger positive connectivity from the AI to the ventral striatum. Moreover, predominantly selfish individuals show distinct functional architectures compared to altruists, and they only increase altruistic behavior in response to empathy inductions, but not reciprocity inductions.</P>
Bioinformatics Analysis of Hsp20 Sequences in Proteobacteria
Heine, Michelle,Chandra, Sathees B.C. Korea Genome Organization 2009 Genomics & informatics Vol.7 No.1
Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell's danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.
Christoph Hein,김낙수,홍석무,Joungsik Suh,Hartmut Hoffmann 한국자동차공학회 2008 International journal of automotive technology Vol.9 No.2
It is essential to develop efficient and cost-effective production methods to achieve or maintain international competitiveness. An innovative production method, such as rotary blanking, enables manufacturers to both reduce expenses and economize production time. However, there are not enough numerical analyses for this process. In this paper, numerical simulations of rotary blanking were performed. After comparing the cutting planes generated by conventional and rotary blanking experimental tests, the cutting areas of two punch geometries were analyzed. The influence of punch geometry on part quality was then investigated through simulations. The procedure for die stress analysis was established and stress distributions of the worksheet and the tools were analyzed. It is essential to develop efficient and cost-effective production methods to achieve or maintain international competitiveness. An innovative production method, such as rotary blanking, enables manufacturers to both reduce expenses and economize production time. However, there are not enough numerical analyses for this process. In this paper, numerical simulations of rotary blanking were performed. After comparing the cutting planes generated by conventional and rotary blanking experimental tests, the cutting areas of two punch geometries were analyzed. The influence of punch geometry on part quality was then investigated through simulations. The procedure for die stress analysis was established and stress distributions of the worksheet and the tools were analyzed.
Bioinformatics Analysis of Hsp20 Sequences in Proteobacteria
Michelle Heine,Sathees B.C.Chandra 한국유전체학회 2009 Genomics & informatics Vol.7 No.1
Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell’s danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species. Heat shock proteins are a class of molecular chaperones that can be found in nearly all organisms from Bacteria, Archaea and Eukarya domains. Heat shock proteins experience increased transcription during periods of heat induced osmotic stress and are involved in protein disaggregation and refolding as part of a cell’s danger signaling cascade. Heat shock protein, Hsp20 is a small molecular chaperone that is approximately 20kDa in weight and is hypothesized to prevent aggregation and denaturation. Hsp20 can be found in several strains of Proteobacteria, which comprises the largest phyla of the Bacteria domain and also contains several medically significant bacterial strains. Genomic analyses were performed to determine a common evolutionary pattern among Hsp20 sequences in Proteobacteria. It was found that Hsp20 shared a common ancestor within and among the five subclasses of Proteobacteria. This is readily apparent from the amount of sequence similarities within and between Hsp20 protein sequences as well as phylogenetic analysis of sequences from proteobacterial and non-proteobacterial species.