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Items: 6

1.

Indoleamine 2,3-dioxygenase inhibitors isolated from the sponge Xestospongia vansoesti: structure elucidation, analogue synthesis, and biological activity.

Centko RM, Steinø A, Rosell FI, Patrick BO, de Voogd N, Mauk AG, Andersen RJ.

Org Lett. 2014 Dec 19;16(24):6480-3. doi: 10.1021/ol503337f. Epub 2014 Dec 11.

PMID:
25495618
2.

Halicloic acids A and B isolated from the marine sponge Haliclona sp. collected in the Philippines inhibit indoleamine 2,3-dioxygenase.

Williams DE, Steinø A, de Voogd NJ, Mauk AG, Andersen RJ.

J Nat Prod. 2012 Aug 24;75(8):1451-8. doi: 10.1021/np300345j. Epub 2012 Aug 7.

PMID:
22873824
3.

Interaction of the chaperone calreticulin with proteins and peptides of different structural classes.

Duus K, Sandhu N, Jørgensen CS, Hansen PR, Steinø A, Thaysen-Andersen M, Højrup P, Houen G.

Protein Pept Lett. 2009;16(11):1414-23.

PMID:
19594432
4.

Plasma elimination kinetics for factor VII are independent of its activation to factor VIIa and complex formation with plasma inhibitors.

Petersen LC, Elm T, Ezban M, Krogh TN, Karpf DM, Steinø A, Olsen EH, Sørensen BB.

Thromb Haemost. 2009 May;101(5):818-26.

PMID:
19404533
5.

Interaction of C1q with the receptor calreticulin requires a conformational change in C1q.

Steinø A, Jørgensen CS, Laursen I, Houen G.

Scand J Immunol. 2004 May;59(5):485-95.

6.

Dimerization and oligomerization of the chaperone calreticulin.

Jørgensen CS, Ryder LR, Steinø A, Højrup P, Hansen J, Beyer NH, Heegaard NH, Houen G.

Eur J Biochem. 2003 Oct;270(20):4140-8.

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