Shuliang Chen, Ph.D.
Affiliations: | 2008 | Wayne State University, Detroit, MI, United States |
Area:
Molecular Biology, Cell BiologyGoogle:
"Shuliang Chen"Parents
Sign in to add mentorMiriam L Greenberg | grad student | 2008 | Wayne State | |
(Essential cellular functions of cardiolipin in Saccharomyces cerevisiae.) |
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Publications
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Chen S, Mari M, Parashar S, et al. (2020) Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy. Proceedings of the National Academy of Sciences of the United States of America |
Cui Y, Parashar S, Zahoor M, et al. (2019) A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation. Science (New York, N.Y.). 365: 53-60 |
Chen S, Cui Y, Parashar S, et al. (2018) ER-phagy requires Lnp1, a protein that stabilizes rearrangements of the ER network. Proceedings of the National Academy of Sciences of the United States of America |
Ding J, Segarra VA, Chen S, et al. (2015) Auxilin facilitates membrane traffic in the early secretory pathway. Molecular Biology of the Cell |
Casey AK, Chen S, Novick P, et al. (2015) Nuclear pore complex integrity requires Lnp1, a regulator of cortical ER. Molecular Biology of the Cell |
Chen S, Desai T, McNew JA, et al. (2015) Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America. 112: 418-23 |
Ye C, Lou W, Li Y, et al. (2014) Deletion of the cardiolipin-specific phospholipase Cld1 rescues growth and life span defects in the tafazzin mutant: implications for Barth syndrome. The Journal of Biological Chemistry. 289: 3114-25 |
Bhandari D, Zhang J, Menon S, et al. (2013) Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits. Molecular Biology of the Cell. 24: 2727-38 |
Chen S, Novick P, Ferro-Novick S. (2013) ER structure and function. Current Opinion in Cell Biology. 25: 428-33 |
Chen S, Novick P, Ferro-Novick S. (2012) ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p. Nature Cell Biology. 14: 707-16 |