Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Jia-Shu Yang"'
Autor:
Shao-Ling Chu, Jia-Rong Huang, Yu-Tzu Chang, Shu-Yun Yao, Jia-Shu Yang, Victor W. Hsu, Jia-Wei Hsu
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract The epidermal growth factor receptor (EGFR) plays important roles in multiple cellular events, including growth, differentiation, and motility. A major mechanism of downregulating EGFR function involves its endocytic transport to the lysosom
Externí odkaz:
https://doaj.org/article/18a86c233883442994380bf095186c8f
Autor:
Jia-Shu Yang, Jia-Wei Hsu, Seung-Yeol Park, Stella Y. Lee, Jian Li, Ming Bai, Claudia Alves, William Tseng, Xavier Michelet, I-Cheng Ho, Victor W. Hsu
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
Intracellular vesicle transport can be regulated by Brefeldin‐A ADP‐Ribosylated Substrate (BARS) during vesicle fission. Here, the authors show that NADH generated by aldehyde dehydrogenase 7A1 (ALDH7A1) inhibits intracellular transport by target
Externí odkaz:
https://doaj.org/article/1c893257dab047c3a63455ff031c0ff7
Autor:
Seung-Yeol Park, Jia-Shu Yang, Zhen Li, Pan Deng, Xiaohong Zhu, David Young, Maria Ericsson, Ruben L. H. Andringa, Adriaan J. Minnaard, Chunmei Zhu, Fei Sun, D. Branch Moody, Andrew J. Morris, Jun Fan, Victor W. Hsu
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Phosphatidic acid and diacylglycerol are required for COPI vesicle fission. Here, the authors find that shorter forms of these lipids promote the late stage of COPI vesicle fission, further suggesting how lipid geometry contributes to membrane deform
Externí odkaz:
https://doaj.org/article/b2379516ce72461c865a7a7a024c6752
Autor:
Nam Chu, Jian Li, Jia-Shu Yang, Jia-Wei Hsu, Philip A. Cole, Michael J. Eck, Ming Bai, Kunhua Li, Victor W. Hsu
Publikováno v:
Nature cell biology
Coat proteins have a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins1–3. We previously showed that Ar
Autor:
Petra Henklein, Victor W. Hsu, Alberto Luini, Giovanni D'Angelo, Julian Nüchel, Domenico Russo, Marinella Pirozzi, Takahiro Nitta, Charlotte Gehin, Mukund Thattai, Seetharaman Parashuraman, Ansuman Biswas, María José Hernández-Corbacho, Gabriele Turacchio, Markus Plomann, Nina A. Dathan, Prathyush Pothukuchi, Giovanna Vanacore, Ilenia Agliarulo, Jin-ichi Inokuchi, Lina M. Obeid, Laura Capolupo, Jia-Shu Yang, Yusuf A. Hannun, Riccardo Rizzo
Publikováno v:
EMBO journal
40 (2021). doi:10.15252/embj.2021107766
info:cnr-pdr/source/autori:Pothukuchi, Prathyush; Agliarulo, Ilenia; Pirozzi, Marinella; Rizzo, Riccardo; Russo, Domenico; Turacchio, Gabriele; Nüchel, Julian; Yang, Jia Shu; Gehin, Charlotte; Capolupo, Laura; Hernandez-Corbacho, Maria Jose; Biswas, Ansuman; Vanacore, Giovanna; Dathan, Nina; Nitta, Takahiro; Henklein, Petra; Thattai, Mukund; Inokuchi, Jin Ichi; Hsu, Victor W.; Plomann, Markus; Obeid, Lina M.; Hannun, Yusuf A.; Luini, Alberto; D'Angelo, Giovanni; Parashuraman, Seetharaman/titolo:GRASP55 regulates intra-Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis/doi:10.15252%2Fembj.2021107766/rivista:EMBO journal (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:40
The EMBO Journal
40 (2021). doi:10.15252/embj.2021107766
info:cnr-pdr/source/autori:Pothukuchi, Prathyush; Agliarulo, Ilenia; Pirozzi, Marinella; Rizzo, Riccardo; Russo, Domenico; Turacchio, Gabriele; Nüchel, Julian; Yang, Jia Shu; Gehin, Charlotte; Capolupo, Laura; Hernandez-Corbacho, Maria Jose; Biswas, Ansuman; Vanacore, Giovanna; Dathan, Nina; Nitta, Takahiro; Henklein, Petra; Thattai, Mukund; Inokuchi, Jin Ichi; Hsu, Victor W.; Plomann, Markus; Obeid, Lina M.; Hannun, Yusuf A.; Luini, Alberto; D'Angelo, Giovanni; Parashuraman, Seetharaman/titolo:GRASP55 regulates intra-Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis/doi:10.15252%2Fembj.2021107766/rivista:EMBO journal (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:40
The EMBO Journal
The Golgi apparatus, the main glycosylation station of the cell, consists of a stack of discontinuous cisternae. Glycosylation enzymes are usually concentrated in one or two specific cisternae along the cis‐trans axis of the organelle. How such com
Publikováno v:
Advances in Engineering Software
Autor:
Hongsheng Liu, Maodu Chen, Luneng Zhao, Jijun Zhao, Shi-Qi Li, Lu Wang, Jia-Shu Yang, Junfeng Gao
Publikováno v:
Nanoscale. 13(10)
Two-dimensional MA2Z4 (M = Mo, W, V, Nb, Ta, Ti, Zr, Hf, or Cr; A = Si or Ge; Z = N, P, or As) is a new lead in the 2D family, because it exhibits versatile properties by tuning the components M, A and Z. However, theoretical studies on MA2Z4 are qui
Autor:
Victor W. Hsu, Seung-Yeol Park, Tobias C. Walther, Raif S. Geha, Maria Tsokos, Sarah Beaussant-Cohen, Seth Rakoff-Nahoum, Wayne Bainter, Shafiq Ur Rehman Naseem, Craig D. Platt, Janet Chou, Zachary Peters, Michel J. Massaad, Jennifer Jones, Chitong Rao, Michel Becuwe, Jordan S. Orange, Faris Jaber, Salem Al-Tamemi, Sandra Andrea Salinas, Jacqueline G. Wallace, Jia-Shu Yang, Kelsey Stafstrom
Publikováno v:
J Clin Invest
The coat protein I (COPI) complex mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER). Five siblings with persistent bacterial and viral infections and defective humoral and cellular immunity had a homozygous p.K652E muta
Autor:
Victor W. Hsu, Julian Nüchel, Gabriele Turacchio, Seetharaman Parashuraman, Ansuman Biswas, María José Hernández-Corbacho, Markus Plomann, Prathyush Pothukuchi, Alberto Luini, Jin-ichi Inokuchi, Vanacore G, Nina A. Dathan, Gehin Cjc, Yusuf A. Hannun, Ilenia Agliarulo, Laura Capolupo, Giovanni D'Angelo, Petra Henklein, Lina M. Obeid, Jia-Shu Yang, Mukund Thattai, Domenico Russo, Marinella Pirozzi, Takahiro Nitta, Renata Rizzo
Glycans are important regulators of cell and organismal physiology. This requires that the glycan biosynthesis be controlled to achieve specific cellular glycan profiles. Glycans are assembled in the Golgi apparatus on secretory cargoes that traverse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7454fcb69b8b50a99d787ac236f30f3
https://doi.org/10.1101/2020.05.03.074682
https://doi.org/10.1101/2020.05.03.074682
Autor:
Andrew J. Morris, Zhen Li, Maria Ericsson, David S. Young, Seung-Yeol Park, Victor W. Hsu, D. Branch Moody, Ruben L. H. Andringa, Chunmei Zhu, Xiaohong Zhu, Adriaan J. Minnaard, Pan Deng, Fei Sun, Jun Fan, Jia-Shu Yang
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Nature Communications, 10:3409. Nature Publishing Group
Nature Communications
Nature Communications, 10:3409. Nature Publishing Group
Nature Communications
Studies on vesicle formation by the Coat Protein I (COPI) complex have contributed to a basic understanding of how vesicular transport is initiated. Phosphatidic acid (PA) and diacylglycerol (DAG) have been found previously to be required for the fis