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1. News organisational culture and crisis of journalism in the Internet environment : the development of newspaper specialism in Korean journalism

Author

Kim, Sa-Seong

Subjects
079.519
Abstract

This study intends to explore how news organisational culture in Korean journalism deals with new policies introduced in an effort to resolve current problems. It aims to identify how the established news organisational culture of Korean newspaper journalism relates to the specialist journalism that news organisations are introducing in order to deal with such problems as journalists' job prospects and Internet challenges.;This study posits three research questions: "Why do news organisations intend to introduce specialism?"; "What does specialism have to do with news organisational culture?" and "Is specialism effective in providing 'better journalism'?" This study conducts four pieces of field research: 26 in-depth interviews, two focus group discussions, a survey, and a brief content analysis. This study finds that specialism is a strategic choice which is arbitrarily adapted for problem-solving rather than an established culture. Secondly, specialism reveals some significant conflicts between specialists and generalist reporters regarding personnel management policies and the routines of news production. Accordingly, specialism is considerably restricted by the news organisational culture. Lastly, specialism does not necessarily provide better journalism, especially in terms of supplying mobilising information to guide audiences out of their grievances caused by government's mishandling of public policies.;The current news organisational routines of Korean newspapers is related more closely to resisting changes rather than bridging the individuals of news organisations with newly emerging environments, and these routines do not provide effective systems for the newsgathering activities of specialist reporters.

Published
2003

2. NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods.

Author

De Leoz, Maria Lorna A, De Leoz, Maria Lorna A, Duewer, David L, Fung, Adam, Liu, Lily, Yau, Hoi Kei, Potter, Oscar, Staples, Gregory O, Furuki, Kenichiro, Frenkel, Ruth, Hu, Yunli, Sosic, Zoran, Zhang, Peiqing, Altmann, Friedrich, Grunwald-Grube, Clemens, Shao, Chun, Zaia, Joseph, Evers, Waltraud, Pengelley, Stuart, Suckau, Detlev, Wiechmann, Anja, Resemann, Anja, Jabs, Wolfgang, Beck, Alain, Froehlich, John W, Huang, Chuncui, Li, Yan, Liu, Yaming, Sun, Shiwei, Wang, Yaojun, Seo, Youngsuk, An, Hyun Joo, Reichardt, Niels-Christian, Ruiz, Juan Echevarria, Archer-Hartmann, Stephanie, Azadi, Parastoo, Bell, Len, Lakos, Zsuzsanna, An, Yanming, Cipollo, John F, Pucic-Bakovic, Maja, Štambuk, Jerko, Lauc, Gordan, Li, Xu, Wang, Peng George, Bock, Andreas, Hennig, René, Rapp, Erdmann, Creskey, Marybeth, Cyr, Terry D, Nakano, Miyako, Sugiyama, Taiki, Leung, Pui-King Amy, Link-Lenczowski, Paweł, Jaworek, Jolanta, Yang, Shuang, Zhang, Hui, Kelly, Tim, Klapoetke, Song, Cao, Rui, Kim, Jin Young, Lee, Hyun Kyoung, Lee, Ju Yeon, Yoo, Jong Shin, Kim, Sa-Rang, Suh, Soo-Kyung, de Haan, Noortje, Falck, David, Lageveen-Kammeijer, Guinevere SM, Wuhrer, Manfred, Emery, Robert J, Kozak, Radoslaw P, Liew, Li Phing, Royle, Louise, Urbanowicz, Paulina A, Packer, Nicolle H, Song, Xiaomin, Everest-Dass, Arun, Lattová, Erika, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Kasali, Toyin, Lindo, Viv, Chen, Yuetian, Goswami, Kudrat, Gau, Brian, Amunugama, Ravi, Jones, Richard, Stroop, Corné JM, Kato, Koichi, Yagi, Hirokazu, Kondo, Sachiko, Yuen, CT, Harazono, Akira, Shi, Xiaofeng, Magnelli, Paula E, Kasper, Brian T, Mahal, Lara, Harvey, David J, O'Flaherty, Roisin, De Leoz, Maria Lorna A, De Leoz, Maria Lorna A, Duewer, David L, Fung, Adam, Liu, Lily, Yau, Hoi Kei, Potter, Oscar, Staples, Gregory O, Furuki, Kenichiro, Frenkel, Ruth, Hu, Yunli, Sosic, Zoran, Zhang, Peiqing, Altmann, Friedrich, Grunwald-Grube, Clemens, Shao, Chun, Zaia, Joseph, Evers, Waltraud, Pengelley, Stuart, Suckau, Detlev, Wiechmann, Anja, Resemann, Anja, Jabs, Wolfgang, Beck, Alain, Froehlich, John W, Huang, Chuncui, Li, Yan, Liu, Yaming, Sun, Shiwei, Wang, Yaojun, Seo, Youngsuk, An, Hyun Joo, Reichardt, Niels-Christian, Ruiz, Juan Echevarria, Archer-Hartmann, Stephanie, Azadi, Parastoo, Bell, Len, Lakos, Zsuzsanna, An, Yanming, Cipollo, John F, Pucic-Bakovic, Maja, Štambuk, Jerko, Lauc, Gordan, Li, Xu, Wang, Peng George, Bock, Andreas, Hennig, René, Rapp, Erdmann, Creskey, Marybeth, Cyr, Terry D, Nakano, Miyako, Sugiyama, Taiki, Leung, Pui-King Amy, Link-Lenczowski, Paweł, Jaworek, Jolanta, Yang, Shuang, Zhang, Hui, Kelly, Tim, Klapoetke, Song, Cao, Rui, Kim, Jin Young, Lee, Hyun Kyoung, Lee, Ju Yeon, Yoo, Jong Shin, Kim, Sa-Rang, Suh, Soo-Kyung, de Haan, Noortje, Falck, David, Lageveen-Kammeijer, Guinevere SM, Wuhrer, Manfred, Emery, Robert J, Kozak, Radoslaw P, Liew, Li Phing, Royle, Louise, Urbanowicz, Paulina A, Packer, Nicolle H, Song, Xiaomin, Everest-Dass, Arun, Lattová, Erika, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Kasali, Toyin, Lindo, Viv, Chen, Yuetian, Goswami, Kudrat, Gau, Brian, Amunugama, Ravi, Jones, Richard, Stroop, Corné JM, Kato, Koichi, Yagi, Hirokazu, Kondo, Sachiko, Yuen, CT, Harazono, Akira, Shi, Xiaofeng, Magnelli, Paula E, Kasper, Brian T, Mahal, Lara, Harvey, David J, and O'Flaherty, Roisin

Abstract

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

Published
2020

3. NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

Author

De Leoz, Maria Lorna A., Duewer, David L, Fung, Adam, Liu, Lily, Kei Yau, Hoi, Potter, Oscar, Staples, Gregory O, Furuki, Kenichiro, Frenkel, Ruth, Hu, Yunli, Socic, Zoran, Zhang, Peiqing, Altmann, Friedrich, Grunwald-Grube, Clemens, Shao, Chun, Zaia, Joseph, Evers, Waltraud, Pengelley, Stuart, Detlev, Suckau, Wiechmann, Anja, Resemann, Anja, Jabs, Wolfgang, Beck, Alain, Froehlich, John W, Huang, Chuncui, Yan, Li, Yaming, Liu, Sun, Shiwei, Wang, Yaojun, Seo, Youngsuk, An, Hyun Joo, Reichardt, Niels-Christian, Ruiz, Juan Echevarria, Archer-Hartmann, Stephanie, Azadi, Parastoo, Bell, Len, Lakos, Zsuzsanna, An, Yanming, Cipollo, John F, Pucic-Bakovic, Maja, Stambuk, Jerko, Lauc, Gordan, Li, Xu, Wang, Peng George, Bock, Andreas, Hennig, Rene, Rapp, Erdmann, Creskey, Marybeth, Cyr, Terry D, Nakano, Miyako, Sugiyama, Taiki, Leung, Pui-King Amy, Link-Lenczowski, Pawel, Jaworek, Jolanta, Yoo, Jong Shin, Kim, Sa-Rang, Suh, Soo-Kyung, de Haan, Noortje, Falck, David, Lageveen-Kammeijer, Guinevere S. M., Wuhrer, Manfred, Emery, Robert J, Liew, Li Phing, Royle, Louise, Urbanowicz, Paulina A, Packer, Nicolle H, Song, Xiaomin, Everest-Dass, Arun, Lattova, Erika, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Kasali, Toyin, Lindo, Viv, Chen, Yuetian, Goswami, Kudrat, Gau, Brian, Amunugama, Ravi, Jones, Richard, Stroop, Corné J M, Kato, Koichi, Yagi, Hirokazu, Kondo, Sachiko, Yuen, C T, Harazono, Akira, Shi, Xiafeng, Magnelli, Paula, Kasper, Brian T, Mahai, Lara, Harvey, David J, O'Flaherty, Roisin, Rudd, Pauline M., Saldova, Radka, Hecht, Elizabeth S, Muddiman, David C, Kang, Jichao, Bhoskar, Prachi, Menard, Daniele, Saati, Andrew, Merle, Christine, Mast, Steven, Tep, Sam, Truong, Jennie, Nishikaze, Takashi, Sekiya, Sadanori, Shafer, Aaron, Funaoka, Sohei, Toyoda, Masaaki, de Vreugd, Peter, Caron, Cassie, Pradhan, Pralima, Tan, Niclas Chiang, Mechref, Yehia, Patil, Sachin, Rohrer, Jeffrey S, Chakrabarti, Ranjan, Dadke, Disha, Lahori, Mohammedazam, Zou, Chunxia, Cairo, Christopher, Reiz, Béla, Whittal, Randy M, Lebrilla, Carlito B, Wu, Lauren, Guttman, Andras, Szigeti, Marton, Kremkow, Benjamin G, Lee, Kevin H, Sihlbom, Carina, Adamczyk, Barbara, Jin, Chunsheng, Karlsson, Niclas G, Omros, Jessica, Larson, Goran, Nilsson, Jonas, Meyer, Bernd, Alena, Wiegandt, Komatsu, Emy, Perreault, Helene, Bodnar, Edward D, Said, Nassur, Francois, Yannis-Nicolas, Leize-Wagner, Emmanuelle, Maier, Sandra, Zeck, Anne, Heck, Albert J R, Yang, Yang, Haselberg, Rob, Qing Yu, Ying, Alley, William, Leone, Joseph W, Yuan, Hua, Stein, Stephen E, De Leoz, Maria Lorna A., Duewer, David L, Fung, Adam, Liu, Lily, Kei Yau, Hoi, Potter, Oscar, Staples, Gregory O, Furuki, Kenichiro, Frenkel, Ruth, Hu, Yunli, Socic, Zoran, Zhang, Peiqing, Altmann, Friedrich, Grunwald-Grube, Clemens, Shao, Chun, Zaia, Joseph, Evers, Waltraud, Pengelley, Stuart, Detlev, Suckau, Wiechmann, Anja, Resemann, Anja, Jabs, Wolfgang, Beck, Alain, Froehlich, John W, Huang, Chuncui, Yan, Li, Yaming, Liu, Sun, Shiwei, Wang, Yaojun, Seo, Youngsuk, An, Hyun Joo, Reichardt, Niels-Christian, Ruiz, Juan Echevarria, Archer-Hartmann, Stephanie, Azadi, Parastoo, Bell, Len, Lakos, Zsuzsanna, An, Yanming, Cipollo, John F, Pucic-Bakovic, Maja, Stambuk, Jerko, Lauc, Gordan, Li, Xu, Wang, Peng George, Bock, Andreas, Hennig, Rene, Rapp, Erdmann, Creskey, Marybeth, Cyr, Terry D, Nakano, Miyako, Sugiyama, Taiki, Leung, Pui-King Amy, Link-Lenczowski, Pawel, Jaworek, Jolanta, Yoo, Jong Shin, Kim, Sa-Rang, Suh, Soo-Kyung, de Haan, Noortje, Falck, David, Lageveen-Kammeijer, Guinevere S. M., Wuhrer, Manfred, Emery, Robert J, Liew, Li Phing, Royle, Louise, Urbanowicz, Paulina A, Packer, Nicolle H, Song, Xiaomin, Everest-Dass, Arun, Lattova, Erika, Cajic, Samanta, Alagesan, Kathirvel, Kolarich, Daniel, Kasali, Toyin, Lindo, Viv, Chen, Yuetian, Goswami, Kudrat, Gau, Brian, Amunugama, Ravi, Jones, Richard, Stroop, Corné J M, Kato, Koichi, Yagi, Hirokazu, Kondo, Sachiko, Yuen, C T, Harazono, Akira, Shi, Xiafeng, Magnelli, Paula, Kasper, Brian T, Mahai, Lara, Harvey, David J, O'Flaherty, Roisin, Rudd, Pauline M., Saldova, Radka, Hecht, Elizabeth S, Muddiman, David C, Kang, Jichao, Bhoskar, Prachi, Menard, Daniele, Saati, Andrew, Merle, Christine, Mast, Steven, Tep, Sam, Truong, Jennie, Nishikaze, Takashi, Sekiya, Sadanori, Shafer, Aaron, Funaoka, Sohei, Toyoda, Masaaki, de Vreugd, Peter, Caron, Cassie, Pradhan, Pralima, Tan, Niclas Chiang, Mechref, Yehia, Patil, Sachin, Rohrer, Jeffrey S, Chakrabarti, Ranjan, Dadke, Disha, Lahori, Mohammedazam, Zou, Chunxia, Cairo, Christopher, Reiz, Béla, Whittal, Randy M, Lebrilla, Carlito B, Wu, Lauren, Guttman, Andras, Szigeti, Marton, Kremkow, Benjamin G, Lee, Kevin H, Sihlbom, Carina, Adamczyk, Barbara, Jin, Chunsheng, Karlsson, Niclas G, Omros, Jessica, Larson, Goran, Nilsson, Jonas, Meyer, Bernd, Alena, Wiegandt, Komatsu, Emy, Perreault, Helene, Bodnar, Edward D, Said, Nassur, Francois, Yannis-Nicolas, Leize-Wagner, Emmanuelle, Maier, Sandra, Zeck, Anne, Heck, Albert J R, Yang, Yang, Haselberg, Rob, Qing Yu, Ying, Alley, William, Leone, Joseph W, Yuan, Hua, and Stein, Stephen E

Abstract

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.

Published
2020

4. Comparative proteomics: assessment of biological variability and dataset comparability.

Author

Kim, Sa Rang, Kim, Sa Rang, Nguyen, Tuong Vi, Seo, Na Ri, Jung, Seunghup, An, Hyun Joo, Mills, David A, Kim, Jae Han, Kim, Sa Rang, Kim, Sa Rang, Nguyen, Tuong Vi, Seo, Na Ri, Jung, Seunghup, An, Hyun Joo, Mills, David A, and Kim, Jae Han

Abstract

BackgroundComparative proteomics in bacteria are often hampered by the differential nature of dataset quality and/or inherent biological deviations. Although common practice compensates by reproducing and normalizing datasets from a single sample, the degree of certainty is limited in comparison of multiple dataset. To surmount these limitations, we introduce a two-step assessment criterion using: (1) the relative number of total spectra (R TS ) to determine if two LC-MS/MS datasets are comparable and (2) nine glycolytic enzymes as internal standards for a more accurate calculation of relative amount of proteins. Lactococcus lactis HR279 and JHK24 strains expressing high or low levels (respectively) of green fluorescent protein (GFP) were used for the model system. GFP abundance was determined by spectral counting and direct fluorescence measurements. Statistical analysis determined relative GFP quantity obtained from our approach matched values obtained from fluorescence measurements.ResultsL. lactis HR279 and JHK24 demonstrates two datasets with an R TS value less than 1.4 accurately reflects relative differences in GFP levels between high and low expression strains. Without prior consideration of R TS and the use of internal standards, the relative increase in GFP calculated by spectral counting method was 3.92 ± 1.14 fold, which is not correlated with the value determined by the direct fluorescence measurement (2.86 ± 0.42 fold) with the p = 0.024. In contrast, 2.88 ± 0.92 fold was obtained by our approach showing a statistically insignificant difference (p = 0.95).ConclusionsOur two-step assessment demonstrates a useful approach to: (1) validate the comparability of two mass spectrometric datasets and (2) accurately calculate the relative amount of proteins between proteomic datasets.

Published
2015

5. A case of traumatic corneal stromal edema with decreased endothelial cell density

Author

Kim,Jung-Hoon, Kim,Sa Kang, Han,Sang Beom, Lee,Seung-Jun, Kim,Moosang, Kim,Jung-Hoon, Kim,Sa Kang, Han,Sang Beom, Lee,Seung-Jun, and Kim,Moosang

Abstract

Jung-Hoon Kim, Sa Kang Kim, Sang Beom Han, Seung-Jun Lee, Moosang KimDepartment of Ophthalmology, School of Medicine, Kangwon National University, Chuncheon, KoreaAbstract: A 31-year-old man presented to our clinic for an ocular trauma to his left eye. His best-corrected visual acuity was 20/200 OS (left eye). Anterior segment examination showed an epithelial defect, which implies a direct injury to the cornea. A marked focal stromal edema accompanied by Descemet’s membrane folds were located at 10 o’clock in the paraxial area, about 4 mm apart from the corneal center. Anterior segment optical coherence tomography (AS-OCT) revealed marked corneal swelling of the lesion. Five days later, the patient’s best-corrected visual acuity improved to 20/50 OS. The stromal edema resolved showing no signs of epithelial defect, although small opacity remained. AS-OCT revealed complete resolution of corneal swelling. Despite the resolution of corneal edema, however, specular microscopy showed substantially decreased endothelial cell density in the lesion compared to the fellow eye. Here we report a case of traumatic corneal stromal edema discovered by AS-OCT.Keywords: AS-OCT, stromal edema, trauma

Published
2015

7. Angel by Kin, Shiryo_

Author

Mehnert, Klaus, 1906-1984, Kin, Shiryo [Kim, Sa-ryang, 1914-1950 ?], Mehnert, Klaus, 1906-1984, and Kin, Shiryo [Kim, Sa-ryang, 1914-1950 ?]

Published
1943

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