Sigurskjold BW - Search Results

1

Specificity determinants in the interaction of apolipoprotein(a) kringles with tetranectin and LDL.

Caterer NR, Graversen JH, Jacobsen C, Moestrup SK, Sigurskjold BW, Etzerodt M, Thøgersen HC. Caterer NR, et al. Among authors: sigurskjold bw. Biol Chem. 2002 Nov;383(11):1743-50. doi: 10.1515/BC.2002.195. Biol Chem. 2002. PMID: 12530539

2

Tetranectin-binding site on plasminogen kringle 4 involves the lysine-binding pocket and at least one additional amino acid residue.

Graversen JH, Sigurskjold BW, Thøgersen HC, Etzerodt M. Graversen JH, et al. Among authors: sigurskjold bw. Biochemistry. 2000 Jun 27;39(25):7414-9. doi: 10.1021/bi000155j. Biochemistry. 2000. PMID: 10858289

3

Mutational analysis of affinity and selectivity of kringle-tetranectin interaction. Grafting novel kringle affinity ontp the trtranectin lectin scaffold.

Graversen JH, Jacobsen C, Sigurskjold BW, Lorentsen RH, Moestrup SK, Thogersen HC, Etzerodt M. Graversen JH, et al. Among authors: sigurskjold bw. J Biol Chem. 2000 Dec 1;275(48):37390-6. doi: 10.1074/jbc.M004873200. J Biol Chem. 2000. PMID: 10964919 Free article.

4

The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine.

Graversen JH, Lorentsen RH, Jacobsen C, Moestrup SK, Sigurskjold BW, Thogersen HC, Etzerodt M. Graversen JH, et al. Among authors: sigurskjold bw. J Biol Chem. 1998 Oct 30;273(44):29241-6. doi: 10.1074/jbc.273.44.29241. J Biol Chem. 1998. PMID: 9786936 Free article.

5

Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes.

Johansson E, Fanø M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoës M. Johansson E, et al. Among authors: sigurskjold bw. J Biol Chem. 2005 Jan 28;280(4):3051-9. doi: 10.1074/jbc.M409534200. Epub 2004 Nov 10. J Biol Chem. 2005. PMID: 15539408 Free article.

6

Small angle X-ray studies reveal that Aspergillus niger glucoamylase has a defined extended conformation and can form dimers in solution.

Jørgensen AD, Nøhr J, Kastrup JS, Gajhede M, Sigurskjold BW, Sauer J, Svergun DI, Svensson B, Vestergaard B. Jørgensen AD, et al. Among authors: sigurskjold bw. J Biol Chem. 2008 May 23;283(21):14772-80. doi: 10.1074/jbc.M801709200. Epub 2008 Mar 31. J Biol Chem. 2008. PMID: 18378674 Free article.

7

Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding.

Hansen MJ, Olsen JG, Bernichtein S, O'Shea C, Sigurskjold BW, Goffin V, Kragelund BB. Hansen MJ, et al. Among authors: sigurskjold bw. J Mol Recognit. 2011 Jul-Aug;24(4):533-47. doi: 10.1002/jmr.1064. Epub 2010 Sep 14. J Mol Recognit. 2011. PMID: 20842635

8

Bacterial expression and secretion of various single-chain Fv genes encoding proteins specific for a Salmonella serotype B O-antigen.

Anand NN, Mandal S, MacKenzie CR, Sadowska J, Sigurskjold B, Young NM, Bundle DR, Narang SA. Anand NN, et al. J Biol Chem. 1991 Nov 15;266(32):21874-9. J Biol Chem. 1991. PMID: 1939211 Free article.

9

Thermodynamics of inhibitor binding to mutant forms of glucoamylase from Aspergillus niger determined by isothermal titration calorimetry.

Berland CR, Sigurskjold BW, Stoffer B, Frandsen TP, Svensson B. Berland CR, et al. Among authors: sigurskjold bw. Biochemistry. 1995 Aug 15;34(32):10153-61. doi: 10.1021/bi00032a008. Biochemistry. 1995. PMID: 7640269

10

Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules.

Nielsen MM, Bozonnet S, Seo ES, Mótyán JA, Andersen JM, Dilokpimol A, Abou Hachem M, Gyémánt G, Naested H, Kandra L, Sigurskjold BW, Svensson B. Nielsen MM, et al. Among authors: sigurskjold bw. Biochemistry. 2009 Aug 18;48(32):7686-97. doi: 10.1021/bi900795a. Biochemistry. 2009. PMID: 19606835

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