Author

B. F. Brian

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

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Organism:mouse· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

T. S. Freedman· 3 shared M. G. Nunez· 2 shared A. S. Jolicoeur· 1 shared B. A. Binstadt· 1 shared B. L. Ruis· 1 shared B. S. Moriarity· 1 shared C. A. Lowell· 1 shared C. R. Guerrero· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

T. S. Freedman

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

SH3-domain mutations selectively disrupt Csk homodimerization or PTPN22 binding

B. F. Brian, F. V. Sjaastad, T. S. Freedman

This study identifies SH3-domain mutations in Csk that selectively disrupt homodimerization or PTPN22 binding, showing both impair Csk's negative regulatory function in cells.

bioRxiv · Jan 13, 2022Biochemistry

Splice-specific lyn knockout mice reveal a dominant function of LynB in preventing autoimmunity

B. F. Brian, M. L. Sauer, B. L. Ruis, J. L. Auger, S. E. Senevirathne, W. L. Swanson, M. G. Nunez, B. S. Moriarity, C. A. Lowell, B. A. Binstadt, T. S. Freedman

This study shows that LynB, a splice variant of Lyn, prevents autoimmunity, while its absence leads to TLR4 hyper-responsiveness and lupus-like disease.

bioRxiv · May 3, 2021 · PreprintImmunology

Unique-region phosphorylation targets LynA for rapid degradation, tuning its expression and signaling in myeloid cells

B. F. Brian, A. S. Jolicoeur, C. R. Guerrero, M. G. Nunez, Z. E. Sychev, S. A. Hegre, P. Satrom, N. Habib, J. M. Drake, K. L. Schwertfeger, T. S. Freedman

The paper identifies how LynA is selectively degraded in macrophages via c-Cbl targeting tyrosine 32, while mast cells, with low c-Cbl, maintain high LynA levels, affecting signaling.

bioRxiv · Jul 2, 2019Biochemistry