Kathrine Tejlgård Jensen

Emailkatmbg.audk

Universitetsbyen 81
8000 Aarhus C
Denmark
Universitetsbyen 81, 1874, 235
8000 Aarhus C
Denmark

Research activity per year

6 Journal article
1 Comment/debate/letter to the editor

7 results

2025
Three cryo-EM structures of CD109 reveal its mechanism of protease inhibition
Almeida, A. V., Jensen, K. T., Harwood, S. L., Jørgensen, M. H., Nielsen, N. S., Thøgersen, I. B., Enghild, J. J. & Andersen, G. R., 24 Jun 2025, In: Cell Reports. 44, 6, 115787.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
2024
Proteolytic cleavage of the TGFβ co-receptor CD109 changes its conformation, resulting in protease inhibition via activation of its thiol ester, and dissociation from the cell membrane
Jensen, K. T., Nielsen, N. S., Viana Almeida, A., Thøgersen, I. B., Enghild, J. J. & Harwood, S. L., Jul 2024, In: FEBS journal. 291, 14, p. 3169-3190 22 p.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
2 Citations (Scopus)
2022
Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family
Nielsen, N. S., Zarantonello, A., Harwood, S. L., Jensen, K. T., Kjøge, K., Thøgersen, I. B., Schauser, L., Karlsen, J. L., Andersen, G. R. & Enghild, J. J., Dec 2022, In: Nature Communications. 13, 1, 15 p., 3033.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
8 Citations (Scopus)
The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel
Harwood, S. L., Diep, K., Nielsen, N. S., Jensen, K. T. & Enghild, J. J., Aug 2022, In: Journal of Biological Chemistry. 298, 8, 11 p., 102230.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
1 Citation (Scopus)
2021

Correction: α2-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester (The Journal of biological chemistry (2020) 295 49 (16732-16742) PII: S0021-9258(20)00204-5)
Harwood, S. L., Nielsen, N. S., Jensen, K. T., Nielsen, P. K., Thøgersen, I. B. & Enghild, J. J., 1 Jan 2021, In: The Journal of Biological Chemistry. 296, p. 100208 1 p.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Comment/debate/letter to the editor › Research › peer-review

Open Access
Development of selective protease inhibitors via engineering of the bait region of human α2-macroglobulin
Harwood, S. L., Nielsen, N. S., Diep, K., Jensen, K. T., Nielsen, P. K., Yamamoto, K. & Enghild, J. J., Jul 2021, In: The Journal of Biological Chemistry. 297, 1, 12 p., 100879.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
11 Citations (Scopus)
2020
α₂-macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester
Harwood, S. L., Nielsen, N. S., Jensen, K. T., Nielsen, P. K., Thøgersen, I. B. & Enghild, J. J., 4 Dec 2020, In: Journal of Biological Chemistry. 295, 49, p. 16732-16742 11 p.
Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Open Access
7 Citations (Scopus)

Kathrine Tejlgård Jensen

Research output

Search results

Three cryo-EM structures of CD109 reveal its mechanism of protease inhibition

Proteolytic cleavage of the TGFβ co-receptor CD109 changes its conformation, resulting in protease inhibition via activation of its thiol ester, and dissociation from the cell membrane

Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family

The conformational change of the protease inhibitor α2-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel

Correction: α2-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester (The Journal of biological chemistry (2020) 295 49 (16732-16742) PII: S0021-9258(20)00204-5)

Development of selective protease inhibitors via engineering of the bait region of human α2-macroglobulin

α2-macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester

The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel

α₂-macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester