Kathrine Tejlgård Jensen

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Ph.d.-studerende, Lønnet ph.d-stipendiat

Institut for Molekylærbiologi og Genetik - Proteinvidenskab
Universitetsbyen 81
bygning 1874, 235
8000 Aarhus C
Danmark
kat@mbg.au.dk
Institut for Molekylærbiologi og Genetik - Proteinvidenskab
Universitetsbyen 81
bygning 1874, 117
8000 Aarhus C
Danmark
kat@mbg.au.dk

Seneste publikationer

Udgivet
The conformational change of the protease inhibitor α₂-macroglobulin is triggered by the retraction of the cleaved bait region from a central channel
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
Udgivet
Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review
Udgivet
α₂-Macroglobulin-like protein 1 can conjugate and inhibit proteases through their hydroxyl groups, because of an enhanced reactivity of its thiol ester
Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

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Kathrine Tejlgård Jensen

Seneste publikationer

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

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

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

Find uddannelse

Studievejledning

Besøg AU

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Aktuel forskning

Talent

Virksomheder

Kommuner og regioner

Gymnasier

Myndigheder

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Om AU

Kathrine Tejlgård Jensen

Seneste publikationer

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

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

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