[번역논문] 유대인의 역사: 알렉산드로스에서 하드리아누스까지

Chris Seeman,Adam Kolman Marshak,박정수(Jeongsoo Park) 한국복음주의신약학회 2020 신약연구 Vol.19 No.4

이 글은 John J. Collins와 Daniel C. Harlow에 의해 편집된 Early Judaism: A Comprehensive Overview (Grand Rapids, MI: Eerdmans, 2012)에 수록된 글이다. 이 논문은 제2성전기 유대교와 신구약 중간사 역사가 Chris Seeman과 Adam Kolman Marshak의 종합적인 연구결과물이다. Seeman은 첫 파트인 헬레니즘 시대 중에서 알렉산드로스에서 폼페이우스까지, 그리고 Marshak은 두 번째 파트인 폼페이우스에서 하드리아누스까지가 기술했다. 이들은 각 시대별로 유대교와 유대인에 관한 세부적인 역사와 문화에 대한 객관적인 진술은 물론, 이에 대한 매우 통찰력 있는 평가를 내리고 있다. 번역자는 한국의 신약학분야에서 제2성전기유대교 연구와 신구약 중간사에서 사용되는 인명과 지명 및 학술자료 및 용어의 우리말 표기를 통일적으로 사용하여 학술연구와 교육에 진보가 있기를 기대하며 이 번역논문을 기고한다. 이를 위하여 이 분야의 인명과 지명 및 관련용어들을 현대어가 아닌 헬라어와 라틴어에 근거하여 우리말로 음역하여 제공하였다. 특히 그간 사용된 영어식 음역을 교정하기 위하여 특히 인명과 지명을 그리스어로 음역하고 괄호 안에 영어식 표기법을 병기(倂記)하였다. 또한 번역자는 대중적인 독자들의 이해를 돕기 위하여 간단하게나마 많은 역주를 넣었는데, 이를 통해서 신구약중간사에 대한 지평이 확대되어 신약성경 연구와 이해의 폭이 넓어지기를 기대한다. This article is included in Early Jadaism: A Compressive Overview (Grand Rapids, MI: Eirdmans, 2012), edited by John J. Collins and Daniel C. Harlow. It is a comprehensive study result of Chris Seman and Adam Kolman Marshak, historians in the Second Temple Judaism and the History between the Old and New Testament. Seeman described the first part, from Alexandros to Pompey, and Marshak from Pompey to Hadrian, the second part. They make very insightful assessments of the detailed history and culture of Judaism and Jews, as well as objective statements of each period. The translator writes this translation paper in hopes of progress in academic research and education in the field of New Testament in Korea, by using the names of people and places, academic materials, and Korean expressions of terms used in the History of Between the Testaments. For this purpose, the names of peolpe and places, and related terms of this field are provided in Korean transliteration based on Koine and Latin, not modern languages. In particular, in order to correct the orthography of English loanword used hitherto, these names are transliterated based in Greek and the English notation was written in parentheses. In addition, translators simply put in a lot of translator’s annotations to help the public understand, which is expected to expand the horizons of the Histoy of Between the Testaments, thereby expanding the scope of research and understanding of the New Testament.

Cellular Changes During Aging in Neural and Mesenchymal Tissues

Marshak, Daniel R. 한림대학교 한림과학원 부설 환경ㆍ생명과학연구소 1995 국제학술회의 Vol.1995 No.-

Among the afflictions of the elderly, many of the cruelest are degenerative neurological diseases that rob the individual of selected functions, leaving others intact. Tardive dyskinesia and other motor disorders resulting from Parkinsonism, amyotrophic lateral sclerosis, and Huntington's disease leave the patient mentally sound, but physically debilitated. In contrast to this, Alzheimer disease and related degenerative, neurological disorders find patients, particularly in the early stages of the ailment, physically able but suffering from increasing loss of memory, language, and emotional stability.

Pharmaco-& Toxico-genomics Symposium : Human somatic stem cell and progenitor cell systems for research in cell therapy, toxicity screening, and target validation

( Daniel R. Marshak ) 한국생화학분자생물학회 (구 한국생화학회) 2004 생화학분자생물학회 춘계학술발표논문집 Vol.2004 No.-

강원도 지역에 서식하는 무당개구리에서 생물학적 활성을 지닌 Bombesin 유사 Peptide 에 관한 연구

박형진,이윤렬,권혁일,김일,유일재,D . R . Marshak ( Hyoung Jin Park,Yun Lyul Lee,Hyeok Yil Kwon,Yil Kim,Il Je Yu,Daniel r . Marshak ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.3

The present study was performed to purify a BLI from the skin of frogs, B. orientalis inhabiting Kangwon-Do, Korea, and then determine its physiological activities and amino acid sequence. A substance that shows bombesin-like immunoreactivity (BLI) was partially purified from crude methanol extract of the frog skin by using a column of alkaline alumina and Sephadex G-10. BLI was further purified by using RP C18 preparative HPLC in which BLI was separated into 5 peaks. The major peak (BLI-K1) containing 65% of total BLI was subjected to purify as a single component by using sequential HPLC of SP-ion exchange and RP C18. Content of BLI in each fraction was monitored by RIA for which bombesin antiserum with a high titer and affinity to BBS was raised in a guinea pig. Eventually, 890 ㎍ of BLI-K1 was homogeneously purified from 420g of the skin of B. orientalis and it was not differentiated from synthetic BBS in RP C18, gel permeation and SP-ion exchange HPLC. In the physiological activities, BLI-K1 was identical to synthetic BBS in stimulation of gastrin release and exocrine pancreatic secretion including volume, protein, bicarbonate, amylase and chymotrypsin output in anesthetized rats. Furthermore, molecular weight and partial amino acid sequence of BLI-K1 was revealed to be identical to synthetic BBS. Therefore, it is concluded from the above results that the skin of B. orientalis contains the same BBS that has been isolated from the skin of European Bombina.

Characterization of DNA Topoisomerase II Using an Anti-Peptide Antibody

Lee, Kyung-Hee,Marshak, Daniel R.,Bae, Young-Seuk 생화학분자생물학회 1993 한국생화학회지 Vol.26 No.7

DNA topoisomerase II has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and $Mg^{2+}$, and is free of any nucleolytic, proteolytic, topoisomerase I, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase II has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomcrase II. The antibody BL1 does not affect topoisomerase II activity and the immunoprecipitates of topoisomerase II with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase II activity in crude extracts.

Characterization of DNA topoisomerase 2 Using an Anti - Peptide Antibody

Kyung Hee Lee,Daniel R . Marshak,Young Seuk Bae 생화학분자생물학회 1993 BMB Reports Vol.26 No.7

DNA topoisomerase Ⅱ has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and Mg^(2+), and is free of any nucleolytic, proteolytic, topoisomerase Ⅰ, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase Ⅱ has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomerase Ⅱ. The antibody BL1 does not affect topoisomerase Ⅱ activity and the immunoprecipitates of topoisomerase Ⅱ with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase Ⅱ activity in crude extracts.

POSTERS / PW-132 : PHOSPHORYLATION OF RIBOSOMAL PROTEIN L5 BY CASEIN KINASE 2 DECREASES ITS 5S rRNA BINDING ACTIVITY

(Jang Woon Park),(Daniel R . Marshak),(Young Seuk Bae) 한국생화학분자생물학회 (구 한국생화학회) 1999 6th IUBMB SEOUL CONFERENCE Vol.- No.-

Unconventional Slow Virus에 감염된 마우스 뇌조직에서 S100β 단백 mRNA 발현

최은경,김용선,양형모,김진,유일재,Marshak,R . I . Carp 대한바이러스학회 1993 Journal of Bacteriology and Virology Vol.23 No.2

Unconventional slow virus induced amyloid plaques formation in mouse brain is very useful animal model for research of Alzheimers disease(AD). The presense of abnormal levels of neurotrophic factors in AD is one possible explanation for the increased concentration of aggregates of over-grown neurites in neuritic plaques of AD. The data presented here demonstrate that the levels of S100p protein and mRNA were greatly elevated in extracts of brain samples of unconventional slow virus infected mice compared to those of control mice. The cells containing the increased S100 p were reactive astrocytes; the amyloid plaques were surrounded by S100p containing astrocytes. A generalization of our finding is that when elevated S100p expression accompanies the gliosis observed in chronic neurodegenerative disease and unconventional slow viurs infection, these will be on associated increase in neurotrophic activity result in abnormal neuritic morphology.

Characterization of DNA Topoisomerase II Using an Anti-Peptide Antibody

Lee, Kyung Hee,Bae, Young Seuk,Marshak, Daniel R . 경북대학교 유전공학연구소 1995 遺傳工學硏究所報 Vol.10 No.1

DNA topoisomerase II has been purified from bovine calf thymus nuclei using P4 phage knotted DNA as a substrate. The purified enzyme consists of two bands of molecular mass 170 and 160 kDa, as determined by sodium-dodecyl sulfate-polyacrylamide gel electrophoresis. The final product is dependent on ATP and Mg^(2+), and is free of any nucleolytic, proteolytic, topoisomerase I, or protein kinase activity. A specific antibody against the amino terminal region (residues 34 to 51) of topoisomerase II has been developed. The specific antibody, designated BL1, reacts with both the 170 and 160 kDa bands of topoisomerase II. The antibody BL1 does not affect topoisomerase II activity and the immunoprecipitates of topoisomerase II with BL1 have enzyme activity, suggesting that the 34 to 51 residues are not directly involved in the DNA binding, ATP-hydrolyzing, and DNA breaking-rejoining reactions of the enzyme. The immunoprecipitates can be used to assay topoisomerase II activity in crude extracts.

Interaction of the β Subunit of Casein Kinase 2 with the Ribosomal Protein L5

Bae, Young Seuk,Kim, Jeong Min,Cha, Ji Young,Marshak, Daniel R . 경북대학교 유전공학연구소 1996 遺傳工學硏究所報 Vol.11 No.1

Casein kinase II (CKII) usually exists as a heterotetramer with α₂β₂, αα'β₂, or α'₂β₂. The α or α' subunits catalyze protein phosphorylation, whereas the function of the β subunit remains unclear. One of the possible functions of the β subunit may be to mediate the interaction of the catalytic subunit with target proteins. To identify proteins capable of associating with the β subunit in vivo, we have used a two-hybrid system. One protein identified is human ribosomal protein L5. The protein L5 does not interact with the α or α' subunits of CKII, supporting the idea that the β subunit can determine a substrate specificity of CKII. These results furthermore suggest a novel role for CKII in ribosomal L5 phosphorylation, in ribosomal assembly, or ribosomal transport in the intact cells. The protein L5 may act as a regulator of the activity or subcellular localization of CKII.