Quantification of the anti-neoplastic polyacetylene falcarinol from carrots in human serum by LC-MS/MS

Autor: Jakobsen, Ulla, Kobæk-Larsen, Morten, Kjøller, Karoline D., Antonsen, Steen, Baatrup, Gunnar, Trelle, Morten B.

Publikováno v: In Journal of Chromatography B 1 November 2022 1210

Dynamic Histone H3 Epigenome Marking during the Intraerythrocytic Cycle of Plasmodium falciparum

Autor: Salcedo-Amaya, Adriana M., van Driel, Marc A., Alako, Blaise T., Trelle, Morten B., van den Elzen, Antonia M. G., Cohen, Adrian M., Janssen-Megens, Eva M., van de Vegte-Bolmer, Marga, Selzer, Rebecca R., Lniguez, A. Leonardo, Green, Roland D., Sauerwein, Robert W., Jensen, Ole N., Stunnenberg, Hendrik G., Hoffmann, Jules A.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 2009 Jun . 106(24), 9655-9660.

Externí odkaz: https://www.jstor.org/stable/40483123

Local Transient Unfolding of Native State PAI-1 Associated with Serpin Metastability.

Autor: Trelle, Morten B.¹, Madsen, Jeppe B.², Andreasen, Peter A.², Jørgensen, Thomas J. D.¹ tjdj@bmb.sdu.dk

Publikováno v: Angewandte Chemie. Sep2014, Vol. 126 Issue 37, p9909-9912. 4p.

Local Transient Unfolding of Native State PAI-1 Associated with Serpin Metastability

Autor: Trelle, Morten B, Madsen, Jeppe Buur, Andreasen, Peter A., Jørgensen, Thomas J D

Publikováno v: Trelle, M B, Madsen, J B, Andreasen, P A & Jørgensen, T J D 2014, ' Local Transient Unfolding of Native State PAI-1 Associated with Serpin Metastability ', Angewandte Chemie International Edition, vol. 53, no. 37, 201402796, pp. 9751-9754 . https://doi.org/10.1002/anie.201402796

The metastability of the native fold makes serpin (serine protease inhibitor) proteins prone to pathological conformational change, often by insertion of an extra β-strand into the central β-sheet A. How this insertion is made possible is a hithert

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::49e63c1f636977b062411692844f3cb9
https://pure.au.dk/portal/da/publications/local-transient-unfolding-of-native-state-pai1-associated-with-serpin-metastability(cab764f2-4446-49ef-89c2-e916dac7d499).html

Analysis of posttranslational modifications of proteins by tandem mass spectrometry

Autor: Larsen, Martin Røssel, Trelle, Morten B, Thingholm, Tine E, Jensen, Ole N

Publikováno v: Larsen, M R, Trelle, M B, Thingholm, T E & Jensen, O N 2006, ' Analysis of posttranslational modifications of proteins by tandem mass spectrometry ', BioTechniques, vol. 40, no. 6, pp. 790-8 . https://doi.org/10.2144/000112201

Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the three-dimensional protein structure is predominantly determined by the amino acid sequence, posttranslational modification (PTM) of proteins modulates the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3062::195fd97436220fbc57143604c9ab9715
https://portal.findresearcher.sdu.dk/da/publications/f57c40c2-cf00-4eb4-8757-924c68c74981