H
Hongxing Wang
Researcher at Icahn School of Medicine at Mount Sinai
Publications - 14
Citations - 823
Hongxing Wang is an academic researcher from Icahn School of Medicine at Mount Sinai. The author has contributed to research in topics: Endoplasmic reticulum & Medicine. The author has an hindex of 8, co-authored 8 publications receiving 799 citations. Previous affiliations of Hongxing Wang include Drexel University.
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Journal ArticleDOI
The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70.
Edward A. Fisher,Mingyue Zhou,Deborah M. Mitchell,Xujun Wu,Satoshi Omura,Hongxing Wang,Alfred L. Goldberg,Henry N. Ginsberg +7 more
TL;DR: It is shown that increasing the expression of Hsp70 in HepG2 cells promotes apoB degradation and is the first example of a wild-type mammalian protein whose secretion is regulated by degradation in the cytosol via the ubiquitin-proteasome pathway.
Journal ArticleDOI
The triple threat to nascent apolipoprotein B. Evidence for multiple, distinct degradative pathways.
Edward A. Fisher,Meihui Pan,Xiaoli Chen,Xinye Wu,Hongxing Wang,Jamil Haris,Janet D. Sparks,Kevin Jon Williams +7 more
TL;DR: F nascent apoB is subject to ER-associated degradation, re-uptake, and a third distinct degradative pathway that appears to target lipoproteins after considerable assembly and involves a post-ER compartment and PI3K signaling.
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Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence
Deborah M. Mitchell,Mingyue Zhou,Rajalakshmi Pariyarath,Hongxing Wang,John D. Aitchison,Henry N. Ginsberg,Edward A. Fisher +6 more
TL;DR: The data imply that during most of its association with the endoplasmic reticulum, apoB100 is close to or within the translocon and is accessible to both the ubiquitin-proteasome and lipoprotein-assembly pathways.
Journal ArticleDOI
Co-translational Interactions of Apoprotein B with the Ribosome and Translocon during Lipoprotein Assembly or Targeting to the Proteasome
Rajalakshmi Pariyarath,Hongxing Wang,John D. Aitchison,Henry N. Ginsberg,William J. Welch,Arthur E. Johnson,Edward A. Fisher +6 more
TL;DR: It is shown that independent of lipid synthesis, apoB chains that appear full-length are, in fact, incompletely translated polypeptides still engaged by the ribosome and associated with the ER translocon, and unlike other ER substrates of the proteasome, apiB does not fully retrotranslocate to the cytosol before entering the ubiquitin-proteasome pathway.
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The effects of n-3 fatty acids on the secretion of carboxyl-terminally truncated forms of human apoprotein B.
TL;DR: The ability of the n-3 fatty acids to promote apoB degradation correlated with the degree of lipidation of the secreted ApoB, consistent with specialized intracellular pathways for the degradation of apoBs and the assembly of buoyant, apo B-containing lipoproteins.