Schreuder HA - Search Results

1

The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions.

Schreuder HA, de Boer B, Dijkema R, Mulders J, Theunissen HJ, Grootenhuis PD, Hol WG. Schreuder HA, et al. Nat Struct Biol. 1994 Jan;1(1):48-54. doi: 10.1038/nsb0194-48. Nat Struct Biol. 1994. PMID: 7656006

2

Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.

Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J. Schreuder HA, et al. Proteins. 1992 Oct;14(2):178-90. doi: 10.1002/prot.340140205. Proteins. 1992. PMID: 1409567

3

Analysis of the active site of the flavoprotein p-hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism.

Schreuder HA, Hol WG, Drenth J. Schreuder HA, et al. Biochemistry. 1990 Mar 27;29(12):3101-8. doi: 10.1021/bi00464a029. Biochemistry. 1990. PMID: 2337581

4

Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.

Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J. Schreuder HA, et al. J Mol Biol. 1989 Aug 20;208(4):679-96. doi: 10.1016/0022-2836(89)90158-7. J Mol Biol. 1989. PMID: 2553983

5

The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation.

van der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J. van der Laan JM, et al. Among authors: schreuder ha. Biochemistry. 1989 Sep 5;28(18):7199-205. doi: 10.1021/bi00444a011. Biochemistry. 1989. PMID: 2819062

6

Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase.

Schreuder HA, Hol WG, Drenth J. Schreuder HA, et al. J Biol Chem. 1988 Mar 5;263(7):3131-6. J Biol Chem. 1988. PMID: 3343242 Free article.

7

Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.

Schreuder HA, van der Laan JM, Hol WG, Drenth J. Schreuder HA, et al. J Mol Biol. 1988 Feb 20;199(4):637-48. doi: 10.1016/0022-2836(88)90307-5. J Mol Biol. 1988. PMID: 3351945

8

Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring.

Schreuder HA, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, van Berkel WJ. Schreuder HA, et al. Biochemistry. 1994 Aug 23;33(33):10161-70. doi: 10.1021/bi00199a044. Biochemistry. 1994. PMID: 7520279

9

Crystallization and preliminary X-ray analysis of human antithrombin III.

Schreuder H, de Boer B, Pronk S, Hol W, Dijkema R, Mulders J, Theunissen H. Schreuder H, et al. J Mol Biol. 1993 Jan 5;229(1):249-50. doi: 10.1006/jmbi.1993.1024. J Mol Biol. 1993. PMID: 8421307

10

Crystallization and preliminary crystallographic analysis of antistasin, a leech-derived inhibitor of blood coagulation factor Xa.

Schreuder H, Arkema A, de Boer B, Kalk K, Dijkema R, Mulders J, Theunissen H, Hol W. Schreuder H, et al. J Mol Biol. 1993 Jun 20;231(4):1137-8. doi: 10.1006/jmbi.1993.1360. J Mol Biol. 1993. PMID: 8515472

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