scispace - formally typeset
H

Hongyong Fu

Researcher at Southwest University of Political Science & Law

Publications -  25
Citations -  2120

Hongyong Fu is an academic researcher from Southwest University of Political Science & Law. The author has contributed to research in topics: Proteasome & Protein subunit. The author has an hindex of 14, co-authored 23 publications receiving 2035 citations. Previous affiliations of Hongyong Fu include University of Wisconsin-Madison & Texas A&M University.

Papers
More filters
Journal ArticleDOI

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

TL;DR: Recombinant Mcb1 protein bound multiubiquitin chains in vitro and, like its plant and animal counterparts, exhibited a binding preference for longer chains, suggesting that Mcb 1 is not the sole factor involved in ubiquitin recognition by the 26S proteasome and thatMcb1 may interact with only a subset of ubiquitinated substrates.
Journal ArticleDOI

Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome

TL;DR: Comprehensive subunit interaction maps for the 26S proteasome and CSN support the ancestral relationship of these two complexes.
Journal ArticleDOI

Sink- and vascular-associated sucrose synthase functions are encoded by different gene classes in potato.

TL;DR: Two differentially regulated classes of sucrose synthase genes, Sus3 and Sus4, were identified in potato and appear to have evolved after the divergence of the major families of dicotyledonous plants but before the divergenceOf tomato and potato.
Journal ArticleDOI

Multiubiquitin Chain Binding and Protein Degradation Are Mediated by Distinct Domains within the 26 S Proteasome Subunit Mcb1

TL;DR: The role of Mcb1 in substrate recognition by the 26 S proteasome is defined and it is indicated that residues near the N terminus, and not the multiubiquitin chain-binding site, are most critical for Mcb 1 function in vivo.
Journal ArticleDOI

Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms.

TL;DR: The incorporation of paralogous subunits into the Arabidopsis holoprotease raises the intriguing possibility that plants synthesize multiple 26 S proteasome types with unique properties and/or target specificities.