Author

B. Reljic

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· 4 Cell Biology· 3

Signature Assays, Organisms & Methods

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Organism:human· 6 Approach:experimental assay· 5 Research Focus:cell type annotation· 4 Assay:proteomics· 3 Assay:bulk RNA-seq· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:metabolism & bioenergetics· 2

Frequent Co-Authors

D. A. Stroud· 6 shared A. J. Sharpe· 3 shared L. Muellner-Wong· 3 shared M. T. Ryan· 3 shared D. R. Thorburn· 2 shared L. E. Formosa· 2 shared A. E. Frazier· 1 shared A. G. Compton· 1 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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6 shared papersBiochemistry

D. A. Stroud

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Author profile →

7 papers

Recent·Most cited

E3 ubiquitin ligase MARCHF5 controls BAK apoptotic activity independently of BH3-only proteins

G. Dewson, A. S. Huang, H. S. Chin, B. Reljic, T. M. Djajawi, I. K. Tan, D. A. Stroud, D. C. S. Huang, M. F. van Delft

This study identifies MARCHF5 as a regulator of BAK apoptotic activity through ubiquitin ligase activity, independent of BH3-only proteins, and shows its role in drug resistance.

bioRxiv · Jan 4, 2022 · PreprintCell Biology

Mitochondrial COA7 is a heme-binding protein involved in the early stages of complex IV assembly.

L. E. Formosa, S. Maghool, A. J. Sharpe, B. Reljic, L. Muellner-Wong, D. A. Stroud, M. Ryan, M. J. Maher

This study identifies COA7 as a heme-binding protein essential for complex IV assembly, revealing its structure and heme-binding mechanism in mitochondrial biogenesis.

bioRxiv · Jun 10, 2021 · PreprintBiochemistry

Training-induced bioenergetic improvement in human skeletal muscle is associated with non-stoichiometric changes in the mitochondrial proteome without reorganization of respiratory chain content

C. Granata, N. J. Caruana, J. Botella, N. A. Jamnick, K. Huynh, J. Kuang, H. A. Janssen, B. Reljic, N. A. Mellett, A. Laskowski, T. L. Stait, A. E. Frazier, M. T. Coughlan, P. J. Meikle, D. R. Thorburn, , D. J. Bishop

The paper investigates training-induced mitochondrial adaptations in human skeletal muscle, finding non-stoichiometric changes in the proteome and challenging previous assumptions about bioenergetic improvements.

bioRxiv · Feb 19, 2021Cell Biology

Optic Atrophy-associated TMEM126A is an assembly factor for the ND4-module of Mitochondrial Complex I

L. Formosa, B. Reljic, A. J. Sharpe, L. Muellner-Wong, D. A. Stroud, M. T. Ryan

This study identifies TMEM126A as a critical assembly factor for the ND4-module of mitochondrial complex I, distinct from its paralogue TMEM126B, which assembles the ND2-module.

bioRxiv · Sep 18, 2020Biochemistry

HIGD2A is required for assembly of the COX3 module of human mitochondrial complex IV

D. H. Hock, B. Reljic, C.-S. Ang, H. S. Mountford, A. G. Compton, M. T. Ryan, D. R. Thorburn, D. A. Stroud

This study shows HIGD2A is essential for assembling the COX3 module of human mitochondrial complex IV, leading to defects in complex IV activity and intermediate accumulation.

bioRxiv · Dec 19, 2019Biochemistry

Dissecting the Roles of Mitochondrial Complex I Intermediate Assembly (MCIA) Complex Factors in the Biogenesis of Complex I

L. E. Formosa, L. Muellner-Wong, B. Reljic, A. J. Sharpe, T. H. Beilharz, M. Lazarou, D. A. Stroud, M. T. Ryan

The paper identifies TMEM186 and COA1 as new components of the MCIA complex and elucidates their roles in complex I assembly.

bioRxiv · Oct 17, 2019Biochemistry

In the absence of apoptosis, myeloid cells arrest when deprived of growth factor, but remain viable by consuming extracellular glucose

L. Dong, B. Reljic, J. G. Cheung, E. S. Ng, L. M. Lindqvist, A. G. Elefanty, D. L. Vaux, H. Tran

The paper shows that Bax-/-Bak1-/- myeloid cells deprived of IL3 survive by consuming extracellular glucose, without needing Atg5-dependent autophagy.

bioRxiv · Nov 15, 2018Cell Biology