Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Li Ting Jang"'
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e74715 (2013)
Vps74p is a member of the PtdIns(4)P-binding protein family. Vps74p interacts with Golgi-resident glycosyltransferases and the coat protein COPI complex to modulate Golgi retention of glycosyltransferases and with the PtdIns(4)P phosphatase Sac1p to
Externí odkaz:
https://doaj.org/article/b5084b5e73f84a2caa5a0f2cf1b401e7
Autor:
Chih Hui Lin, Han Chieh Kao, Tung Ching Ho, Shiou-Hwei Yeh, Sui-Yuan Chang, Wen Hau Lee, Mi-Hua Tao, Yu Hao Pang, Chiao Ling Li, Ya-Wen Cheng, Sheng-Han Wang, Li Ting Jang, Tai Ling Chao, Ping-Yi Wu, Pei-Jer Chen, Mu Fan Chiu, Ya Min Tsai
Publikováno v:
Cell Reports
Development of specific antivirals is an urgent unmet need for SARS-coronavirus 2 (SARS-CoV-2) infections. This study focuses on host proteases that proteolytically activate the SARS-CoV-2 spike protein, critical for its fusion after binding to angio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5af037fc7686ccc103eb110b799f631a
http://europepmc.org/articles/PMC7510585
http://europepmc.org/articles/PMC7510585
Autor:
Chun-Chun Li, Tsung-Sheng Wu, Chun-Fang Huang, Li-Ting Jang, Yu-Tsan Liu, Shu-Ting You, Gunn-Guang Liou, Fang-Jen S Lee
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43552 (2012)
ARL4D, ARL4A, and ARL4C are closely related members of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of GTPases. All three ARL4 proteins contain nuclear localization signals (NLSs) at their C-termini and are primarily found at the pla
Externí odkaz:
https://doaj.org/article/3fd353239abe4a689f782c42d6af63f0
Autor:
Chieh-Hsin Chen, Ming-Chieh Lin, Meng-Chen Tsai, Tsai-Shin Chiang, Fang-Jen S. Lee, Li-Ting Jang
Publikováno v:
Molecular Biology of the Cell
Cell migration is a highly regulated event that is initiated by cell membrane protrusion and actin reorganization. Robo1, a single-pass transmembrane receptor, is crucial for neuronal guidance and cell migration. ADP-ribosylation factor (Arf)–like
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d4fc4d8c34189fce5e43244be06dbc7
https://pubmed.ncbi.nlm.nih.gov/30427759
https://pubmed.ncbi.nlm.nih.gov/30427759
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 9, p e74715 (2013)
PLoS ONE, Vol 8, Iss 9, p e74715 (2013)
Vps74p is a member of the PtdIns(4)P-binding protein family. Vps74p interacts with Golgi-resident glycosyltransferases and the coat protein COPI complex to modulate Golgi retention of glycosyltransferases and with the PtdIns(4)P phosphatase Sac1p to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::515953eb2769c6c7c6a3f54ffaa28811
https://pubmed.ncbi.nlm.nih.gov/24019977
https://pubmed.ncbi.nlm.nih.gov/24019977
Autor:
Li Ting Jang, Chun Fang Huang, Tsung Sheng Wu, Chun Chun Li, Fang-Jen S. Lee, Shu Ting You, Gunn-Guang Liou, Yu Tsan Liu
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43552 (2012)
PLoS ONE
PLoS ONE
ARL4D, ARL4A, and ARL4C are closely related members of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of GTPases. All three ARL4 proteins contain nuclear localization signals (NLSs) at their C-termini and are primarily found at the pla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32d38b6af03648062d929d9cdee7d5c2
http://europepmc.org/articles/PMC3424131?pdf=render
http://europepmc.org/articles/PMC3424131?pdf=render
Publikováno v:
Journal of cell science. 124(Pt 23)
ADP-ribosylation factor-like protein 4A (ARL4A) is a developmentally regulated member of the ARF/ARL GTPase family. The primary structure of ARL4A is very similar to that of other ARF/ARL molecules, but its function remains unclear. The trans-Golgi n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e684701c6e9a4e83f8d16fafa8bec98
https://pubmed.ncbi.nlm.nih.gov/22159419
https://pubmed.ncbi.nlm.nih.gov/22159419
Publikováno v:
The Journal of biological chemistry. 281(39)
Rbp1p, a yeast RNA-binding protein, decreases the level of mitochondrial porin mRNA by enhancing its degradation, but the intracellular location of the Rbp1p-mediated degradation complex remains unknown. We show here that Rbp1p in xrn1Delta mutant ye
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d06d398e676de1d706b7ac8041bb6e20
https://pubmed.ncbi.nlm.nih.gov/16885161
https://pubmed.ncbi.nlm.nih.gov/16885161
Autor:
Li-Ting Jang, 詹琍婷
94
Section I. Functional Characterization of RNA binding protein Rbp1p in Saccharomyces cerevisiae The Saccharomyces cerevisiae RNA-binding protein Rbp1p was initially identified as a negative growth regulator. Overexpression of Rbp1p can decrea
Section I. Functional Characterization of RNA binding protein Rbp1p in Saccharomyces cerevisiae The Saccharomyces cerevisiae RNA-binding protein Rbp1p was initially identified as a negative growth regulator. Overexpression of Rbp1p can decrea
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/58466877214892707958
Autor:
Li-Ting, Jang
Thesis (Ph.D.)--National Taiwan University Graduate Institute of Molecular Medicine
Includes bibliographical references
Includes bibliographical references