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International Lawyer Interview with Professor Jerome A. Cohen
Jerome A. Cohen (사) 이준국제법연구원 2022 Journal of East Asia and International Law Vol.15 No.1
Dr. Jerome Cohen (孔傑榮/柯恩) is Professor Emeritus at New York University School of Law, Founder and Faculty Director Emeritus of its US-Asia Law Institute, and Adjunct Senior Fellow for Asia at the Council on Foreign Relations. Professor Cohen was born in Elizabeth, New Jersey as the son of a local government attorney. After graduating from Linden High School, he received his B.A. and J.D. degree from prestigious Yale University and its Law School in 1951 and 1955, respectively. As a law student, he served as the Editor-in-Chief of the Yale Law Journal. From 1955–56 he clerked at the Supreme Court under Chief Justice Earl Warren and then under Justice Felix Frankfurter. Professor Cohen joined the faculty of University of California- Berkeley School of Law in 1959. Then, Professor Cohen was asked to recommend a candidate for a four-year grant to study China offered by the Rockefeller Foundation. When there was no clear candidate, however, he decided to pursue the opportunity himself.
Cohen, J. G.,Goo, J. M.,Yoo, R. E.,Park, C. M.,Lee, C. H.,Ginneken, B.,Chung, D. H.,Kim, Y. T. Springer Science + Business Media 2016 EUROPEAN RADIOLOGY Vol.26 No.12
<P>To evaluate the performance of software in segmenting ground-glass and solid components of subsolid nodules in pulmonary adenocarcinomas. Seventy-three pulmonary adenocarcinomas manifesting as subsolid nodules were included. Two radiologists measured the maximal axial diameter of the ground-glass components on lung windows and that of the solid components on lung and mediastinal windows. Nodules were segmented using software by applying five (-850 HU to -650 HU) and nine (-130 HU to -500 HU) attenuation thresholds. We compared the manual and software measurements of ground-glass and solid components with pathology measurements of tumour and invasive components. Segmentation of ground-glass components at a threshold of -750 HU yielded mean differences of +0.06 mm (p = 0.83, 95 % limits of agreement, 4.51 to 4.67) and -2.32 mm (p < 0.001, -8.27 to 3.63) when compared with pathology and manual measurements, respectively. For solid components, mean differences between the software (at -350 HU) and pathology measurements and between the manual (lung and mediastinal windows) and pathology measurements were -0.12 mm (p = 0.74, -5.73 to 5.55]), 0.15 mm (p = 0.73, -6.92 to 7.22), and -1.14 mm (p < 0.001, -7.93 to 5.64), respectively. Software segmentation of ground-glass and solid components in subsolid nodules showed no significant difference with pathology. aEuro cent Software can effectively segment ground-glass and solid components in subsolid nodules. aEuro cent Software measurements show no significant difference with pathology measurements. aEuro cent Manual measurements are more accurate on lung windows than on mediastinal windows.</P>
p62- and ubiquitin-dependent stress-induced autophagy of the mammalian 26S proteasome
Cohen-Kaplan, Victoria,Livneh, Ido,Avni, Noa,Fabre, Bertrand,Ziv, Tamar,Kwon, Yong Tae,Ciechanover, Aaron National Academy of Sciences 2016 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.113 No.47
<P>The ubiquitin-proteasome system and autophagy are the two main proteolytic systems involved in, among other functions, the maintenance of cell integrity by eliminating misfolded and damaged proteins and organelles. Both systems remove their targets after their conjugation with ubiquitin. An interesting, yet incompletely understood problem relates to the fate of the components of the two systems. Here we provide evidence that amino acid starvation enhances polyubiquitination on specific sites of the proteasome, a modification essential for its targeting to the autophagic machinery. The uptake of the ubiquitinated proteasome is mediated by its interaction with the ubiquitin-associated domain of p62/SQSTM1, a process that also requires interaction with LC3. Importantly, deletion of the PB1 domain of p62, which is important for the targeting of ubiquitinated substrates to the proteasome, has no effect on stress-induced autophagy of this proteolytic machinery, suggesting that the domain of p62 that binds to the proteasome determines the function of p62 in either targeting substrates to the proteasome or targeting the proteasome to autophagy.</P>
HDAC4 Regulates Muscle Fiber Type-Specific Gene Expression Programs
Cohen, Todd J.,Choi, Moon-Chang,Kapur, Meghan,Lira, Vitor A.,Yan, Zhen,Yao, Tso-Pang Korean Society for Molecular and Cellular Biology 2015 Molecules and cells Vol.38 No.4
Fiber type-specific programs controlled by the transcription factor MEF2 dictate muscle functionality. Here, we show that HDAC4, a potent MEF2 inhibitor, is predominantly localized to the nuclei in fast/glycolytic fibers in contrast to the sarcoplasm in slow/oxidative fibers. The cytoplasmic localization is associated with HDAC4 hyper-phosphorylation in slow/oxidative-fibers. Genetic reprogramming of fast/glycolytic fibers to oxidative fibers by active CaMKII or calcineurin leads to increased HDAC4 phosphorylation, HDAC4 nuclear export, and an increase in markers associated with oxidative fibers. Indeed, HDAC4 represses the MEF2-dependent, PGC-$1{\alpha}$-mediated oxidative metabolic gene program. Thus differential phosphorylation and localization of HDAC4 contributes to establishing fiber type-specific transcriptional programs.