| The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa. Anand K., Pallares I., Valnickova Z., Christensen T., Vendrell J., Wendt K.U., Schreuder H.A., Enghild J.J., Aviles F.X.
J. Biol. Chem. 283:29416-29423(2008) · UniProtKB (1) |
| Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase. Eppink M.H., Overkamp K.M., Schreuder H.A., Van Berkel W.J.
J. Mol. Biol. 292:87-96(1999) · Mapped (1) |
| Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. Eppink M.H., Bunthol C., Schreuder H.A., van Berkel W.J.
FEBS Lett. 443:251-255(1999) · UniProtKB (1) |
| Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants. Eppink M.H., Schreuder H.A., van Berkel W.J.
J. Biol. Chem. 273:21031-21039(1998) · Mapped (1) |
| Inhibition of human neutrophil elastase. 4. Design, synthesis, X-ray crystallographic analysis, and structure-activity relationships for a series of P2-modified, orally active peptidyl pentafluoroethyl ketones. Cregge R.J., Durham S.L., Farr R.A., Gallion S.L., Hare C.M., Hoffman R.V., Janusz M.J., Kim H.O., Koehl J.R., Mehdi S. et al.
J. Med. Chem. 41:2461-2480(1998) · Mapped (2) |
| Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. Eppink M.H., Schreuder H.A., van Berkel W.J.
Eur. J. Biochem. 253:194-201(1998) · UniProtKB (1) |
| X-ray structure of antistasin at 1.9-A resolution and its modelled complex with blood coagulation factor Xa. Lapatto R., Krengel U., Schreuder H.A., Arkema A., de Boer B., Kalk K.H., Hol W.G.J., Grootenhuis P.D.J., Mulders J.W.M., Dijkema R. et al.
EMBO J. 16:5151-5161(1997) · UniProtKB (1) |
| Molecular design and characterization of an alpha-thrombin inhibitor containing a novel P1 moiety. Malikayil J.A., Burkhart J.P., Schreuder H.A., Broersma R.J. Jr., Tardif C., Kutcher L.W., Mehdi S., Schatzman G.L., Neises B., Peet N.P.
Biochemistry 36:1034-1040(1997) · Mapped (2) |
| Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea latex. Subroto T., van Koningsveld G.A., Schreuder H.A., Soedjanaatmadja U.M.S., Beintema J.J.
Phytochemistry 43:29-37(1996) · UniProtKB (1) |
| Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants. Lah M.S., Palfey B.A., Schreuder H.A., Ludwig M.L.
Biochemistry 33:1555-1564(1994) · UniProtKB (1) |
| Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline. Schreuder H.A., Rondeau J.-M., Tardif C., Soffientini A., Sarubbi E., Akeson A., Bowlin T.L., Yanofsky S., Barrett R.W.
Eur. J. Biochem. 227:838-847(1995) · UniProtKB (1) |
| Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin. van Berkel W.J., Eppink M.H., Schreuder H.A.
Protein Sci. 3:2245-2253(1994) · Mapped (1) |
| The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M., Grootenhuis P.D.J., Hol W.G.J.
Nat. Struct. Biol. 1:48-54(1994) · UniProtKB (1) |
| Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding. Eppink M.H., Schreuder H.A., van Berkel W.J.
Eur. J. Biochem. 231:157-165(1995) · UniProtKB (1) |
| 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 H.A., Mattevi A., Obmolova G., Kalk K.H., Hol W.G., van der Bolt F.J., van Berkel W.J.
Biochemistry 33:10161-10170(1994) · Mapped (1) |
| Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate. Schreuder H.A., van der Laan J.M., Hol W.G.J., Drenth J.
J. Mol. Biol. 199:637-648(1988) · UniProtKB (1) |
| The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation. van der Laan J.M., Schreuder H.A., Swarte M.B., Wierenga R.K., Kalk K.H., Hol W.G., Drenth J.
Biochemistry 28:7199-7205(1989) · Mapped (1) |
| 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 H.A., Prick P.A., Wierenga R.K., Vriend G., Wilson K.S., Hol W.G., Drenth J.
J. Mol. Biol. 208:679-696(1989) · Mapped (1) |
| Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3-A resolution. Schreuder H.A., van der Laan J.M., Swarte M.B.A., Kalk K.H., Hol W.G.J., Drenth J.
Proteins 14:178-190(1992) · UniProtKB (1) |
