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RISS 인기검색어
- 검색키워드
- 저자 : Hein, David W (검색결과 110 건)
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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.
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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.
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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 $0.5-50{\mu}g/ml$.
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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>
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BUILDING BRAND PERSONALITY IN THE HIGH-END CULTURAL AND CREATIVE INDUSTRIES
Klaus Heine,Marco Eisenberg,Vera Seidemann 글로벌지식마케팅경영학회 2017 Global Fashion Management Conference Vol.2017 No.07
In response to growing instability and a perceived over-commercialization also of luxury brands, there is a trend among consumers to search for meaning and for experiences that feel genuine. The “humanization” of brands may feed the consumers growing desire for authenticity. This paper combines the brand personality concept and brand anthropomorphization and introduces the notion of personality-driven brand management especially for luxury brands and high-end cultural and creative businesses. After an introduction into the concept of brand personality, and with reference to identitydriven brand management, we explain what personality-driven brand management actually means. When the focal point of brand management shifts to the enlivened brand, the brand personality becomes the main source of inspiration for brand-building and influences all branding decisions. With personality-driven branding, managers may leverage the full potential of brand anthropomorphization. For instance, it can help to turn the brand into a strong character, which can spark the employee’s enthusiasm and thus also the customer’s passion for the brand. As a prerequisite of (internal) brand anthropomorphization, managers need to decide what kind of person they would like their brand to represent. For this purpose, they can consult a framework of brand personality dimensions for some guidance. A central part of this paper is a study about the major dimensions of luxury brand personality. Results suggest that there exist five distinct luxury personality dimensions including tradition, modesty, elitism, eccentricity, and sensuality. They help brand managers to develop distinct brand personalities by encouraging them to decide between contrasting traits. After presenting the major strategies to bring a luxury brand personality alive, the paper discusses the benefits of personality-based brand management and concludes with some major lessons learned.
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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.
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