Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Yeon Gil Choi"'
UXT chaperone prevents proteotoxicity by acting as an autophagy adaptor for p62-dependent aggrephagy
Autor:
Min Ji Yoon, Boyoon Choi, Eun Jin Kim, Jiyeon Ohk, Chansik Yang, Yeon-Gil Choi, Jinyoung Lee, Chanhee Kang, Hyun Kyu Song, Yoon Ki Kim, Jae-Sung Woo, Yongcheol Cho, Eui-Ju Choi, Hosung Jung, Chungho Kim
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
p62/SQSTM1 acts as a key mediator in the selective autophagy of protein aggregates, or aggrephagy. Here the authors identify the prefoldin-like chaperone UXT as an autophagy adaptor of p62 dependent aggrephagy and show that ectopic UXT expression del
Externí odkaz:
https://doaj.org/article/f97d34af557c40b1a93c7c19606cff1c
Autor:
Byungju Kim, Joori Park, Yeon Gil Choi, Ban Seok Lee, Heedo Park, Jae Sung Woo, Man Seong Park, Min Ji Yoon, Hyun Jung Hwang, Yoon Ki Kim, Chungho Kim, Jong-Bong Lee, Yeonkyoung Park, Jeeyoon Chang
Publikováno v:
Autophagy
Selective recognition and elimination of misfolded polypeptides are crucial for protein homeostasis. When the ubiquitin-proteasome system is impaired, misfolded polypeptides tend to form small cytosolic aggregates and are transported to the aggresome
Autor:
Sung Rae Cho, Jihyeon Yu, Jae Sung Woo, Jong-Seo Kim, Sangsu Bae, Yeon Gil Choi, You Kyeong Jeong, Eunju Cho, Yongwoo Na
Publikováno v:
ACS Synthetic Biology. 9:1591-1598
The overproduction and purification of human proteins is a requisite of both basic and medical research. Although many recombinant human proteins have been purified, current protein production methods have several limitations; recombinant proteins ar
UXT chaperone prevents proteotoxicity by acting as an autophagy adaptor for p62-dependent aggrephagy
Autor:
Hyun Kyu Song, Eun Jin Kim, Jinyoung Lee, Yoon Ki Kim, Min Ji Yoon, Chansik Yang, Jae Sung Woo, Chungho Kim, Yongcheol Cho, Eui Ju Choi, Chanhee Kang, Bo-Yoon Choi, Yeon Gil Choi, Hosung Jung, Jiyeon Ohk
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications
Nature Communications
p62/SQSTM1 is known to act as a key mediator in the selective autophagy of protein aggregates, or aggrephagy, by steering ubiquitinated protein aggregates towards the autophagy pathway. Here, we use a yeast two-hybrid screen to identify the prefoldin
Autor:
Jihyeon, Yu, Eunju, Cho, Yeon-Gil, Choi, You Kyeong, Jeong, Yongwoo, Na, Jong-Seo, Kim, Sung-Rae, Cho, Jae-Sung, Woo, Sangsu, Bae
Publikováno v:
ACS synthetic biology. 9(7)
The overproduction and purification of human proteins is a requisite of both basic and medical research. Although many recombinant human proteins have been purified, current protein production methods have several limitations; recombinant proteins ar
Publikováno v:
Nucleic Acids Research
Microprocessor, which consists of a ribonuclease III DROSHA and its cofactor DGCR8, initiates microRNA (miRNA) maturation by cleaving primary miRNA transcripts (pri-miRNAs). We recently demonstrated that the DGCR8 dimer recognizes the apical elements
Autor:
S. Chan Baek, Jae Sung Woo, Yeon Gil Choi, Jihye Yang, Young-suk Lee, V. Narry Kim, S. Chul Kwon
Publikováno v:
Molecular cell. 73(3)
Microprocessor, composed of DROSHA and its cofactor DGCR8, initiates microRNA (miRNA) biogenesis by processing the primary transcripts of miRNA (pri-miRNAs). Here we investigate the mechanism by which Microprocessor selects the cleavage site with sin
Autor:
Sungchul Hohng, Jae Sung Woo, Yeon Gil Choi, Joha Park, Tuan Anh Nguyen, Myung Hyun Jo, S. Chul Kwon, V. Narry Kim
Publikováno v:
Cell. 161:1374-1387
Summary MicroRNA (miRNA) maturation is initiated by Microprocessor composed of RNase III DROSHA and its cofactor DGCR8, whose fidelity is critical for generation of functional miRNAs. To understand how Microprocessor recognizes pri-miRNAs, we here re
Autor:
Jae Sung Woo, Sungchul Hohng, Tuan Anh Nguyen, Yeon Gil Choi, Myung Hyun Jo, S. Chul Kwon, V. Narry Kim
Publikováno v:
Cell. 164(1-2)
MicroRNA maturation is initiated by RNase III DROSHA that cleaves the stem loop of primary microRNA. DROSHA functions together with its cofactor DGCR8 in a heterotrimeric complex known as Microprocessor. Here, we report the X-ray structure of DROSHA
Autor:
Jong Hoon Park, Yeon-Gil Choi, Hye-Won Hong, Kyungeun Cha, Gyuha Ryu, Heejoon Myung, Hee-Kwon Chae, Min Joo Lee
Publikováno v:
Biotechnology letters. 30(11)
Mice were fed either 13 nm silver nanoparticles or 2-3.5 mum silver microparticles. The livers were then obtained after 3 days and subjected to a histopathological analysis. The nanoparticle-fed and microparticle-fed livers both exhibited lymphocyte