Author

T. H. Jensen

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· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:chromatin & epigenetic regulation· 2 Approach:experimental assay· 2 Approach:biophysical modeling· 1 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Assay:proteomics· 1

Frequent Co-Authors

A.-E. Foucher· 1 shared B. Schwalb· 1 shared B. T. Chait· 1 shared C. Demel· 1 shared D. Fenyo· 1 shared E. Dubiez· 1 shared E. Pellegrini· 1 shared E. S. Molska· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

A.-E. Foucher

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Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivJul 25, 2023

Structural basis for competitive binding of productive and degradative co-transcriptional effectors to the nuclear cap-binding complex

E. Dubiez, E. Pellegrini, M. Finderup Brask…·J. Kadlec

The paper reveals how different effectors compete for binding to the CBC-ARS2 complex, influencing RNA fate through structural and biochemical analysis.

DOI 10.1016/j.celrep.2023.113639

structural biologybiophysical modeling

𝕏 PostBluesky

Cell BiologybioRxivJul 17, 2020

Integrator is a genome-wide attenuator of non-productive transcription

S. Lykke-Andersen, K. Zumer, E. S. Molska…·T. H. Jensen

The paper identifies genome-wide roles of the Integrator complex in attenuating non-productive transcription by dampening weak promoters and quality-controlling RNAPII complexes.

DOI 10.1016/j.molcel.2020.12.014

bulk RNA-seqstatistical model

𝕏 PostBluesky

BiochemistrybioRxivApr 20, 2020

Affinity proteomic dissection of the human nuclear cap-binding-complex interactome

Y. Dou, S. Kalmykova, M. Pashkova…·J. LaCava

This study maps the human nuclear cap-binding complex interactome using affinity proteomics to clarify the composition and interactions of NCBP1, NCBP2, and NCBP3-related macromolecular assemblies.

DOI 10.1093/nar/gkaa743

humanproteomics

𝕏 PostBluesky