Author

B. Rius

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Cell Biology· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

J. W. Kelly· 2 shared L. Wiseman· 2 shared A. Galmozzi· 1 shared A. Madhavan· 1 shared A. Sukiasyan· 1 shared B. Nguyen· 1 shared B. P. Kok· 1 shared E. Powers· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

J. W. Kelly

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Pharmacologic IRE1/XBP1s Activation Promotes Systemic Adaptive Remodeling in Obesity

A. Madhavan, B. P. Kok, J. M. Grandjean, V. Albert, A. Sukiasyan, B. Rius, E. Powers, A. Galmozzi, E. Saez, L. Wiseman

This study shows that pharmacologic activation of IRE1/XBP1s signaling in obese mice improves glucose metabolism, insulin action, and reduces hepatic steatosis and inflammation.

bioRxiv · Dec 3, 2020Physiology

ER Proteostasis Regulators Reduce Amyloidogenic Light Chain Secretion Through an On-Target, ATF6-Independent Mechanism

B. Rius, J. S. Mesgarzadeh, I. C. Romine, R. J. Paxman, J. W. Kelly, L. Wiseman

This paper shows that compound 147 reduces amyloidogenic light chain secretion from AL patient plasma cells through PDI modification, independent of ATF6 activation.

bioRxiv · May 15, 2020 · PreprintBiochemistry

Quantitative Interactome Proteomics Reveals a Molecular Basis for ATF6-Dependent Regulation of a Destabilized Amyloidogenic Protein

L. Plate, B. Rius, B. Nguyen, J. Genereux, J. W. Kelly, R. L. Wiseman

The paper identifies how ATF6 activation reduces secretion of a destabilized amyloidogenic protein by enhancing its retention in the ER through specific proteostasis factors.

bioRxiv · Jul 31, 2018Cell Biology