Author

D. A. Bachovchin

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

Immunology· 9

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 9 Research Focus:host-pathogen & immune response· 6 Organism:human· 5 Research Focus:cell signaling & trafficking· 4 Research Focus:protein folding & dynamics· 3 Research Focus:cell type annotation· 2 Assay:cryo-EM· 2 Assay:proteomics· 2

Frequent Co-Authors

A. R. Griswold· 7 shared D. P. Ball· 6 shared Q. Wang· 5 shared E. L. Orth-He· 3 shared H. Sharif· 3 shared H. Wu· 3 shared H.-C. Huang· 3 shared J. C. Hsiao· 3 shared

Activity by Year

2019-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 32 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

7 shared papersImmunology

A. R. Griswold

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

The interaction between NLRP1 and oxidized TRX1 involves a transient disulfide bond

M. B. Geeson, J. C. Hsiao, L. P. Tsamouri, D. P. Ball, D. A. Bachovchin

This study identifies a transient disulfide bond between NLRP1 and oxidized TRX1, revealing how NLRP1 senses cellular redox state to regulate inflammasome formation.

bioRxiv · Sep 27, 2023Immunology

Oxidized thioredoxin-1 restrains the NLRP1 inflammasome

D. P. Ball, A. E. Wang, C. D. Warren, Q. Wang, A. R. Griswold, S. D. Rao, D. A. Bachovchin

This study identifies oxidized thioredoxin-1 as a repressor of NLRP1 inflammasome activation, showing that mutations impair this interaction and cause autoinflammatory disease.

Science Immunology · Nov 25, 2022Peer-reviewedImmunology

The NLRP1 and CARD8 inflammasomes detect reductive stress

Q. Wang, J. Hsiao, N. Yardeny, H.-C. Huang, C. M. O'Mara, E. L. Orth-He, D. P. Ball, D. A. Bachovchin

This study identifies chemical probes that induce reductive stress and shows that reductive stress and peptide accumulation together strongly activate NLRP1 and CARD8 inflammasomes.

bioRxiv · Mar 22, 2022Immunology

A ubiquitin-independent proteasome pathway controls the CARD8 inflammasome

J. C. Hsiao, A. R. Neugroschl, A. J. Chui, C. Y. Taabazuing, A. R. Griswold, Q. Wang, H.-C. Huang, E. L. Orth-He, D. P. Ball, G. Hiotis, D. A. Bachovchin

This study identifies a ubiquitin-independent proteasome pathway that degrades the CARD8 N-terminal fragment, releasing the inflammatory C-terminal fragment and activating the inflammasome.

bioRxiv · Mar 22, 2022 · PreprintImmunology

Cytosolic peptide accumulation activates the NLRP1 and CARD8 inflammasomes

E. L. Orth-He, H.-C. Huang, S. D. Rao, Q. Wang, Q. Chen, C. M. O'Mara, A. J. Chui, M. Saoi, A. R. Griswold, A. Bhattacharjee, D. P. Ball, J. R. Cross, D. A. Bachovchin

This study identifies cytosolic peptide accumulation as a danger signal that activates NLRP1 and CARD8 inflammasomes by promoting NT degradation and disrupting DPP9-mediated sequestration of CT fragments.

bioRxiv · Mar 22, 2022 · PreprintImmunology

Structural mechanism of CARD8 regulation by DPP9

H. Sharif, L. R. Hollingsworth, A. R. Griswold, J. C. Hsiao, Q. Wang, D. A. Bachovchin, H. Wu

This study reveals how DPP9 regulates CARD8 by forming a ternary complex and shows that DPP9 inhibitors activate CARD8 inflammasomes through two distinct mechanisms.

bioRxiv · Jan 13, 2021Immunology

DPP9 directly sequesters the NLRP1 C-terminus to repress inflammasome activation

L. R. Hollingsworth, H. Sharif, A. R. Griswold, P. Fontana, J. Mintseris, K. B. Dagbay, J. A. Paulo, S. P. Gygi, D. A. Bachovchin, H. Wu

This study identifies DPP9 as a repressor of NLRP1 inflammasome activation by sequestering the NLRP1 C-terminus, preventing inflammation during protein turnover.

bioRxiv · Aug 14, 2020Immunology

Novel mode of filament formation in UPA-promoted CARD8 and NLRP1 Inflammasomes

L. R. Hollingsworth, L. David, Y. Li, A. R. Griswold, H. Sharif, P. Fontana, T.-M. Fu, J. Ruan, D. A. Bachovchin, H. Wu

This study reports cryo-EM structures of NLRP1-CT and CARD8-CT inflammasome assemblies, revealing unique filament formation mechanisms and ASC recruitment specificity.

bioRxiv · Jun 27, 2020Immunology

Human caspase-1 autoproteolysis is required for ASC-dependent and -independent inflammasome activation

D. P. Ball, C. Y. Taabazuing, A. R. Griswold, E. L. Orth, S. D. Rao, I. B. Kotliar, D. C. Johnson, D. A. Bachovchin

This study shows that pro-caspase-1 autoproteolysis is required for both ASC-dependent and -independent inflammasome activation in human cells.

bioRxiv · Jun 24, 2019 · PreprintImmunology