Author

Yuka Machida

National Cancer Institute

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· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

Yuichi MachidaiD· 3 shared Christian RenziD· 2 shared Helle D. UlrichiD· 2 shared Hyun-Seo KangiD· 2 shared Julian StingeleiD· 2 shared Michael SattleriD· 2 shared Sophie Dürauer· 2 shared Abigail C Major· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 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

Yuichi MachidaORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

SV40 Large T antigen inhibits the host serine protease FAM111A through a zinc-dependent, cleavage-avoiding mechanism

Allison L Welter, Sudhaker Dharavath, Yuka Machida, Julia R Alvey, Sowmiya Palani, Morgan E. Crewe, Anh T. Q. Cong, Connor P. Jewell, Kosei Iwata, Lisa M. Miller Jenkins, Matthew J. Schellenberg, Yuichi Machida

This paper identifies a zinc-dependent mechanism by which SV40 Large T antigen inhibits the host protease FAM111A to facilitate viral replication.

bioRxiv · Aug 10, 2026 · PreprintBiochemistry

Molecular basis of SPRTN activation by DNA and ubiquitin

Hyun-Seo Kang, Sophie Dürauer, Christian Renz, Yuka Machida, Helle D. Ulrich, Yuichi Machida, Michael Sattler, Julian Stingele

This study identifies how DNA and ubiquitin relieve autoinhibition in SPRTN, enabling its protease activity through conformational changes.

bioRxiv · Jun 16, 2026 · PreprintBiochemistry

Allosteric activation of the SPRTN protease by ubiquitin maintains genome stability

Sophie Dürauer, Hyun-Seo Kang, Christian Wiebeler, Yuka Machida, Dina S Schnapka, Denitsa Yaneva, Christian Renz, Maximilian J. Götz, Pedro Weickert, Abigail C Major, Aldwin Suryo Rahmanto, Sophie M. Gutenthaler, Lena Josefine Daumann, Petra Beli, Helle D. Ulrich, , Julian Stingele

This study shows that ubiquitin activates SPRTN protease to degrade DNA-protein crosslinks, maintaining genome stability and preventing disease.

Nature Communications · Jul 21, 2025Peer-reviewedBiochemistry