Author

M. Pilsl

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· 6 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:chromatin & epigenetic regulation· 3 Assay:cryo-EM· 3 Organism:human· 3 Organism:yeast· 3 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2

Frequent Co-Authors

C. Engel· 5 shared H. Tschochner· 3 shared J. Griesenbeck· 3 shared P. Milkereit· 3 shared A. Vannini· 2 shared G. Abascal-Palacios· 2 shared G. Längst· 2 shared J. L. Daiss· 2 shared

Activity by Year

2018-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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5 shared papersBiochemistry

C. Engel

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Author profile →

7 papers

Recent·Most cited

Structural basis of archaeal RNA polymerase transcription elongation and Spt4/5 recruitment

D. Tarau, F. Grunberger, M. Pilsl, R. Reichelt, F. Heiss, S. Konig, H. Urlaub, W. Hausner, C. Engel, D. Grohmann

This study determines the structure of archaeal RNA polymerase and its interaction with Spt4/5, revealing conformational changes and a DNA-binding role for Spt5.

Nucleic Acids Research · Jun 10, 2024Peer-reviewedBiochemistry

The human RNA polymerase I structure reveals an HMG-like transcription factor docking domain specific to metazoans

J. L. Daiss, M. Pilsl, K. Straub, A. Bleckmann, M. Höcherl, F. B. Heiss, G. Abascal-Palacios, E. Ramsay, K. Tluckova, J.-C. Mars, A. Bruckmann, C. Bernecky, V. Lamour, K. Panov, A. Vannini, , C. Engel

The paper determines the structure of human RNA polymerase I, identifies a novel HMG-like domain in RPA1, and shows its role in recruiting Topoisomerase 2a and UBF for transcription regulation.

bioRxiv · Dec 22, 2021 · PreprintBiochemistry

Cryo-EM structure of the NLRP3 decamer bound to the cytokine release inhibitory drug CRID3

I. V. Hochheiser, M. Pilsl, G. Hagelueken, J. Moecking, M. Marleaux, R. Brinkschulte, E. Latz, C. Engel, M. Geyer

The paper determines the cryo-EM structure of NLRP3 bound to CRID3, revealing how the inhibitor stabilizes the protein and provides insights for drug development.

bioRxiv · Jul 22, 2021Immunology

Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.

P. Milkereit, G. Pöll, M. Pilsl, J. Griesenbeck, H. Tschochner

The paper examines the role of three yeast large ribosomal subunit proteins in the folding and stability of intermediate nuclear rRNA precursors using structural and biochemical data.

bioRxiv · May 18, 2021Biochemistry

Structure of human RNA Polymerase III

E. P. Ramsay, G. Abascal-Palacios, J. L. Daiss, H. King, J. Gouge, M. Pilsl, F. Beuron, E. Morris, P. Gunkel, C. Engel, A. Vannini

The paper determines the structure of human RNA Polymerase III using cryo-EM and maps mutations linked to neurodevelopmental disorders and viral hypersensitivity.

bioRxiv · Jun 29, 2020 · PreprintBiochemistry

RNA polymerase I passage through nucleosomes depends on its lobe binding subunits

H. Tschochner, P. E. Merkl, M. Pilsl, T. Fremter, K. Schwank, C. Engel, G. Längst, P. Milkereit, J. Griesenbeck

This study shows that RNA polymerase I can transcribe through nucleosomes, and its subunits Rpa34.5/Rpa49 and Rpa12.2 are critical for this process.

bioRxiv · Oct 31, 2019 · PreprintBiochemistry

RNA polymerase I transcription fidelity, speed and processivity depend on the interplay of its lobe binding subunits

H. Tschochner, P. E. Merkl, M. Pilsl, T. Fremter, G. Längst, P. Milkereit, J. Griesenbeck

The paper investigates how the lobe-binding module of RNA polymerase I affects transcription fidelity, speed, and processivity in vitro, showing its unique ability to transcribe nucleosomal templates compared to Pol II.

bioRxiv · Oct 2, 2018 · PreprintBiochemistry