| Year |
Citation |
Score |
| 2022 |
Zavarise A, Sridhar S, Kiema TR, Wierenga RK, Widersten M. Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics. The Febs Journal. PMID 36002154 DOI: 10.1111/febs.16603 |
0.403 |
|
| 2021 |
Kelpšas V, Caldararu O, Blakeley MP, Coquelle N, Wierenga RK, Ryde U, von Wachenfeldt C, Oksanen E. Neutron structures of triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. Iucrj. 8: 633-643. PMID 34258011 DOI: 10.1107/S2052252521004619 |
0.323 |
|
| 2020 |
Sridhar S, Schmitz W, Hiltunen JK, Venkatesan R, Bergmann U, Kiema TR, Wierenga RK. Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallographica. Section D, Structural Biology. 76: 1256-1269. PMID 33263331 DOI: 10.1107/S2059798320013819 |
0.37 |
|
| 2020 |
Orengo C, Velankar S, Wodak S, Zoete V, Bonvin AMJJ, Elofsson A, Feenstra KA, Gerloff DL, Hamelryck T, Hancock JM, Helmer-Citterich M, Hospital A, Orozco M, Perrakis A, Rarey M, ... ... Wierenga R, et al. A community proposal to integrate structural bioinformatics activities in ELIXIR (3D-Bioinfo Community). F1000research. 9. PMID 32566135 DOI: 10.12688/F1000Research.20559.1 |
0.308 |
|
| 2020 |
Sah-Teli SK, Hynönen MJ, Sulu R, Dalwani S, Schmitz W, Wierenga RK, Venkatesan R. Insights into the stability and substrate specificity of the E. coli aerobic β-oxidation trifunctional enzyme complex. Journal of Structural Biology. 210: 107494. PMID 32171906 DOI: 10.1016/j.jsb.2020.107494 |
0.309 |
|
| 2019 |
Abdelkreem E, Harijan RK, Yamaguchi S, Wierenga RK, Fukao T. Mutation update on ACAT1 variants associated with mitochondrial acetoacetyl-CoA thiolase (T2) deficiency. Human Mutation. PMID 31268215 DOI: 10.1002/Humu.23831 |
0.307 |
|
| 2019 |
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R. Complementary substrate specificity and distinct quaternary assembly of the aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. The Biochemical Journal. PMID 31235482 DOI: 10.1042/BCJ20190314 |
0.329 |
|
| 2019 |
Kiema TR, Thapa CJ, Laitaoja M, Schmitz W, Maksimainen MM, Fukao T, Rouvinen J, Jänis J, Wierenga RK. The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry. The Biochemical Journal. 476: 307-332. PMID 30573650 DOI: 10.1042/BCJ20180788 |
0.464 |
|
| 2018 |
Nguyen VD, Biterova E, Salin M, Wierenga RK, Ruddock LW. Crystal structure of human anterior gradient protein 3. Acta Crystallographica. Section F, Structural Biology Communications. 74: 425-430. PMID 29969106 DOI: 10.1107/S2053230X18009093 |
0.323 |
|
| 2017 |
Kasaragod P, Midekessa GB, Sridhar S, Schmitz W, Kiema TR, Hiltunen JK, Wierenga RK. Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part. Febs Open Bio. 7: 1830-1842. PMID 29226071 DOI: 10.1002/2211-5463.12337 |
0.395 |
|
| 2017 |
Harijan RK, Kiema TR, Syed SM, Qadir I, Mazet M, Bringaud F, Michels PAM, Wierenga RK. Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1. Protein Engineering, Design & Selection : Peds. 30: 225-233. PMID 28062645 DOI: 10.1093/protein/gzw080 |
0.373 |
|
| 2016 |
Ithayaraja M, Janardan N, Wierenga RK, Savithri HS, Murthy MR. Crystal structure of a thiolase from Escherichia coli at 1.8 Å resolution. Acta Crystallographica. Section F, Structural Biology Communications. 72: 534-44. PMID 27380370 DOI: 10.1107/S2053230X16008451 |
0.674 |
|
| 2016 |
Krause M, Kiema TR, Neubauer P, Wierenga RK. Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity. Acta Crystallographica. Section F, Structural Biology Communications. 72: 490-9. PMID 27303904 DOI: 10.1107/S2053230X16007548 |
0.377 |
|
| 2016 |
Richard JP, Amyes TL, Malabanan MM, Zhai X, Kim KJ, Reinhardt CJ, Wierenga RK, Drake EJ, Gulick AM. Structure-Function Studies on Hydrophobic Residues that Clamp a Basic Glutamate Side-Chain During Catalysis by Triosephosphate Isomerase. Biochemistry. PMID 27149328 DOI: 10.1021/Acs.Biochem.6B00311 |
0.303 |
|
| 2016 |
Harijan RK, Mazet M, Kiema TR, Bouyssou G, Alexson SE, Bergmann U, Moreau P, Michels PA, Bringaud F, Wierenga RK. The SCP2-thiolase-like protein (SLP) of Trypanosoma brucei is an enzyme involved in lipid metabolism. Proteins. PMID 27093562 DOI: 10.1002/prot.25054 |
0.396 |
|
| 2016 |
Meriläinen G, Koski MK, Wierenga RK. The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis Protein Science. 25: 987-998. DOI: 10.1002/pro.2906 |
0.373 |
|
| 2015 |
Janardan N, Harijan RK, Kiema TR, Wierenga RK, Murthy MR. Structural characterization of a mitochondrial 3-ketoacyl-CoA (T1)-like thiolase from Mycobacterium smegmatis. Acta Crystallographica. Section D, Biological Crystallography. 71: 2479-93. PMID 26627655 DOI: 10.1107/S1399004715019331 |
0.686 |
|
| 2015 |
Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK. Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole. Acta Crystallographica. Section D, Biological Crystallography. 71: 2178-91. PMID 26527136 DOI: 10.1107/S139900471501559X |
0.332 |
|
| 2015 |
Onwukwe GU, Kursula P, Koski MK, Schmitz W, Wierenga RK. Human Δ³,Δ²-enoyl-CoA isomerase, type 2: a structural enzymology study on the catalytic role of its ACBP domain and helix-10. The Febs Journal. 282: 746-68. PMID 25515061 DOI: 10.1111/febs.13179 |
0.395 |
|
| 2014 |
Kiema TR, Harijan RK, Strozyk M, Fukao T, Alexson SE, Wierenga RK. The crystal structure of human mitochondrial 3-ketoacyl-CoA thiolase (T1): insight into the reaction mechanism of its thiolase and thioesterase activities. Acta Crystallographica. Section D, Biological Crystallography. 70: 3212-25. PMID 25478839 DOI: 10.1107/S1399004714023827 |
0.368 |
|
| 2014 |
Meriläinen G, Wierenga RK. Crystallization and preliminary X-ray diffraction studies of the C-terminal domain of Chlamydia trachomatis CdsD. Acta Crystallographica. Section F, Structural Biology Communications. 70: 1431-3. PMID 25286957 DOI: 10.1107/S2053230X14019712 |
0.31 |
|
| 2014 |
Anbazhagan P, Harijan RK, Kiema TR, Janardan N, Murthy MR, Michels PA, Juffer AH, Wierenga RK. Phylogenetic relationships and classification of thiolases and thiolase-like proteins of Mycobacterium tuberculosis and Mycobacterium smegmatis. Tuberculosis (Edinburgh, Scotland). 94: 405-12. PMID 24825023 DOI: 10.1016/J.Tube.2014.03.003 |
0.53 |
|
| 2014 |
Peterhoff D, Beer B, Rajendran C, Kumpula EP, Kapetaniou E, Guldan H, Wierenga RK, Sterner R, Babinger P. A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization. Molecular Microbiology. 92: 885-99. PMID 24684232 DOI: 10.1111/mmi.12596 |
0.358 |
|
| 2013 |
Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK. The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. Structure (London, England : 1993). 21: 2107-18. PMID 24207127 DOI: 10.1016/j.str.2013.09.005 |
0.307 |
|
| 2013 |
Harijan RK, Kiema TR, Karjalainen MP, Janardan N, Murthy MR, Weiss MS, Michels PA, Wierenga RK. Crystal structures of SCP2-thiolases of Trypanosomatidae, human pathogens causing widespread tropical diseases: the importance for catalysis of the cysteine of the unique HDCF loop. The Biochemical Journal. 455: 119-30. PMID 23909465 DOI: 10.1042/Bj20130669 |
0.675 |
|
| 2013 |
Venkatesan R, Wierenga RK. Structure of mycobacterial β-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathway. Acs Chemical Biology. 8: 1063-73. PMID 23496842 DOI: 10.1021/cb400007k |
0.362 |
|
| 2013 |
Kasaragod P, Schmitz W, Hiltunen JK, Wierenga RK. The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA. The Febs Journal. 280: 3160-75. PMID 23351063 DOI: 10.1111/febs.12150 |
0.418 |
|
| 2012 |
Janardan N, Harijan RK, Wierenga RK, Murthy MR. Crystal structure of a monomeric thiolase-like protein type 1 (TLP1) from Mycobacterium smegmatis. Plos One. 7: e41894. PMID 22844533 DOI: 10.1371/Journal.Pone.0041894 |
0.668 |
|
| 2012 |
Sharma S, Bhaumik P, Schmitz W, Venkatesan R, Hiltunen JK, Conzelmann E, Juffer AH, Wierenga RK. The enolization chemistry of a thioester-dependent racemase: the 1.4 Ã… crystal structure of a reaction intermediate complex characterized by detailed QM/MM calculations. The Journal of Physical Chemistry. B. 116: 3619-29. PMID 22360758 DOI: 10.1021/jp210185m |
0.308 |
|
| 2011 |
Janardan N, Paul A, Harijan RK, Wierenga RK, Murthy MR. Cloning, expression, purification and preliminary X-ray diffraction studies of a putative Mycobacterium smegmatis thiolase. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 817-20. PMID 21795802 DOI: 10.1107/S1744309111019324 |
0.616 |
|
| 2011 |
Venkatesan R, Alahuhta M, Pihko PM, Wierenga RK. High resolution crystal structures of triosephosphate isomerase complexed with its suicide inhibitors: the conformational flexibility of the catalytic glutamate in its closed, liganded active site. Protein Science : a Publication of the Protein Society. 20: 1387-97. PMID 21633986 DOI: 10.1002/Pro.667 |
0.362 |
|
| 2010 |
Wierenga RK, Kapetaniou EG, Venkatesan R. Triosephosphate isomerase: a highly evolved biocatalyst. Cellular and Molecular Life Sciences : Cmls. 67: 3961-82. PMID 20694739 DOI: 10.1007/s00018-010-0473-9 |
0.376 |
|
| 2010 |
Salin M, Kapetaniou EG, Vaismaa M, Lajunen M, Casteleijn MG, Neubauer P, Salmon L, Wierenga RK. Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase. Acta Crystallographica. Section D, Biological Crystallography. 66: 934-44. PMID 20693693 DOI: 10.1107/S0907444910025710 |
0.368 |
|
| 2010 |
Kasaragod P, Venkatesan R, Kiema TR, Hiltunen JK, Wierenga RK. Crystal structure of liganded rat peroxisomal multifunctional enzyme type 1: a flexible molecule with two interconnected active sites. The Journal of Biological Chemistry. 285: 24089-98. PMID 20463028 DOI: 10.1074/Jbc.M110.117606 |
0.529 |
|
| 2010 |
Alahuhta M, Wierenga RK. Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism. Proteins. 78: 1878-88. PMID 20235230 DOI: 10.1002/prot.22701 |
0.305 |
|
| 2009 |
Meriläinen G, Poikela V, Kursula P, Wierenga RK. The thiolase reaction mechanism: the importance of Asn316 and His348 for stabilizing the enolate intermediate of the Claisen condensation. Biochemistry. 48: 11011-25. PMID 19842716 DOI: 10.1021/bi901069h |
0.356 |
|
| 2009 |
Koski MK, Hieta R, Hirsilä M, Rönkä A, Myllyharju J, Wierenga RK. The crystal structure of an algal prolyl 4-hydroxylase complexed with a proline-rich peptide reveals a novel buried tripeptide binding motif. The Journal of Biological Chemistry. 284: 25290-301. PMID 19553701 DOI: 10.1074/jbc.M109.014050 |
0.399 |
|
| 2008 |
Meriläinen G, Schmitz W, Wierenga RK, Kursula P. The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme. The Febs Journal. 275: 6136-48. PMID 19016856 DOI: 10.1111/j.1742-4658.2008.06737.x |
0.362 |
|
| 2008 |
Nguyen VD, Wallis K, Howard MJ, Haapalainen AM, Salo KE, Saaranen MJ, Sidhu A, Wierenga RK, Freedman RB, Ruddock LW, Williamson RA. Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain. Journal of Molecular Biology. 383: 1144-55. PMID 18801374 DOI: 10.1016/j.jmb.2008.08.085 |
0.321 |
|
| 2008 |
Chen ZJ, Pudas R, Sharma S, Smart OS, Juffer AH, Hiltunen JK, Wierenga RK, Haapalainen AM. Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties. Journal of Molecular Biology. 379: 830-44. PMID 18479707 DOI: 10.1016/J.Jmb.2008.04.041 |
0.385 |
|
| 2007 |
Bhaumik P, Schmitz W, Hassinen A, Hiltunen JK, Conzelmann E, Wierenga RK. The catalysis of the 1,1-proton transfer by alpha-methyl-acyl-CoA racemase is coupled to a movement of the fatty acyl moiety over a hydrophobic, methionine-rich surface. Journal of Molecular Biology. 367: 1145-61. PMID 17320106 DOI: 10.1016/j.jmb.2007.01.062 |
0.326 |
|
| 2007 |
Taskinen JP, van Aalten DM, Knudsen J, Wierenga RK. High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand. Proteins. 66: 229-38. PMID 17044054 DOI: 10.1002/prot.21124 |
0.323 |
|
| 2006 |
Casteleijn MG, Alahuhta M, Groebel K, El-Sayed I, Augustyns K, Lambeir AM, Neubauer P, Wierenga RK. Functional role of the conserved active site proline of triosephosphate isomerase. Biochemistry. 45: 15483-94. PMID 17176070 DOI: 10.1021/Bi061683J |
0.374 |
|
| 2006 |
Donnini S, Groenhof G, Wierenga RK, Juffer AH. The planar conformation of a strained proline ring: a QM/MM study. Proteins. 64: 700-10. PMID 16741995 DOI: 10.1002/prot.21006 |
0.315 |
|
| 2006 |
Haapalainen AM, Meriläinen G, Wierenga RK. The thiolase superfamily: condensing enzymes with diverse reaction specificities. Trends in Biochemical Sciences. 31: 64-71. PMID 16356722 DOI: 10.1016/j.tibs.2005.11.011 |
0.324 |
|
| 2006 |
Taskinen JP, Kiema TR, Hiltunen JK, Wierenga RK. Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1. Journal of Molecular Biology. 355: 734-46. PMID 16330050 DOI: 10.1016/j.jmb.2005.10.085 |
0.369 |
|
| 2005 |
Kursula P, Sikkilä H, Fukao T, Kondo N, Wierenga RK. High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I. Journal of Molecular Biology. 347: 189-201. PMID 15733928 DOI: 10.1016/j.jmb.2005.01.018 |
0.376 |
|
| 2005 |
Savolainen K, Bhaumik P, Schmitz W, Kotti TJ, Conzelmann E, Wierenga RK, Hiltunen JK. Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold. The Journal of Biological Chemistry. 280: 12611-20. PMID 15632186 DOI: 10.1074/Jbc.M409704200 |
0.507 |
|
| 2005 |
Noble ME, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont AC, Martial JA. Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution. Acta Crystallographica. Section D, Biological Crystallography. 49: 403-17. PMID 15299515 DOI: 10.1107/S0907444993002628 |
0.368 |
|
| 2004 |
Bhaumik P, Koski MK, Bergmann U, Wierenga RK. Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 60: 1964-70. PMID 15502303 DOI: 10.1107/S0907444904021912 |
0.522 |
|
| 2004 |
Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J. The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues. The Journal of Biological Chemistry. 279: 52255-61. PMID 15456751 DOI: 10.1074/jbc.M410007200 |
0.373 |
|
| 2004 |
Partanen ST, Novikov DK, Popov AN, Mursula AM, Hiltunen JK, Wierenga RK. The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group. Journal of Molecular Biology. 342: 1197-208. PMID 15351645 DOI: 10.1016/j.jmb.2004.07.039 |
0.381 |
|
| 2004 |
Kursula I, Salin M, Sun J, Norledge BV, Haapalainen AM, Sampson NS, Wierenga RK. Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase. Protein Engineering, Design & Selection : Peds. 17: 375-82. PMID 15166315 DOI: 10.1093/Protein/Gzh048 |
0.318 |
|
| 2004 |
Mursula AM, Hiltunen JK, Wierenga RK. Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily. Febs Letters. 557: 81-7. PMID 14741345 DOI: 10.1016/S0014-5793(03)01450-9 |
0.386 |
|
| 2003 |
Pekkala M, Hieta R, Kursula P, Kivirikko KI, Wierenga RK, Myllyharju J. Crystallization of the proline-rich-peptide binding domain of human type I collagen prolyl 4-hydroxylase. Acta Crystallographica. Section D, Biological Crystallography. 59: 940-2. PMID 12777818 DOI: 10.1107/S0907444903005420 |
0.33 |
|
| 2003 |
Bhaumik P, Kursula P, Ratas V, Conzelmann E, Hiltunen JK, Schmitz W, Wierenga RK. Crystallization and preliminary X-ray diffraction studies of an alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Acta Crystallographica. Section D, Biological Crystallography. 59: 353-5. PMID 12554951 DOI: 10.1107/S0907444902020735 |
0.338 |
|
| 2003 |
Kursula I, Wierenga RK. Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution. The Journal of Biological Chemistry. 278: 9544-51. PMID 12522213 DOI: 10.1074/jbc.M211389200 |
0.378 |
|
| 2002 |
Kursula P, Ojala J, Lambeir AM, Wierenga RK. The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Biochemistry. 41: 15543-56. PMID 12501183 DOI: 10.1021/bi0266232 |
0.359 |
|
| 2002 |
Taskinen JP, Kiema TR, Koivuranta KT, Wierenga RK, Hiltunen JK. Crystallization and characterization of the dehydrogenase domain from rat peroxisomal multifunctional enzyme type 1. Acta Crystallographica. Section D, Biological Crystallography. 58: 690-3. PMID 11914498 DOI: 10.1107/S0907444902001890 |
0.393 |
|
| 2001 |
Haapalainen AM, van Aalten DM, Meriläinen G, Jalonen JE, Pirilä P, Wierenga RK, Hiltunen JK, Glumoff T. Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. Journal of Molecular Biology. 313: 1127-38. PMID 11700068 DOI: 10.1006/Jmbi.2001.5084 |
0.471 |
|
| 2001 |
Kursula I, Partanen S, Lambeir AM, Antonov DM, Augustyns K, Wierenga RK. Structural determinants for ligand binding and catalysis of triosephosphate isomerase. European Journal of Biochemistry / Febs. 268: 5189-96. PMID 11589711 DOI: 10.1046/J.0014-2956.2001.02452.X |
0.343 |
|
| 2001 |
Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK. The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase. Journal of Molecular Biology. 309: 845-53. PMID 11399063 DOI: 10.1006/Jmbi.2001.4671 |
0.58 |
|
| 2001 |
Wierenga RK. The TIM-barrel fold: a versatile framework for efficient enzymes. Febs Letters. 492: 193-8. PMID 11257493 DOI: 10.1016/S0014-5793(01)02236-0 |
0.376 |
|
| 2001 |
Norledge BV, Lambeir AM, Abagyan RA, Rottmann A, Fernandez AM, Filimonov VV, Peter MG, Wierenga RK. Modeling, mutagenesis, and structural studies on the fully conserved phosphate-binding loop (loop 8) of triosephosphate isomerase: toward a new substrate specificity. Proteins. 42: 383-9. PMID 11151009 DOI: 10.1002/1097-0134(20010215)42:3<383::AID-PROT80>3.0.CO;2-G |
0.41 |
|
| 2000 |
van Aalten DM, DiRusso CC, Knudsen J, Wierenga RK. Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold. The Embo Journal. 19: 5167-77. PMID 11013219 DOI: 10.1093/emboj/19.19.5167 |
0.398 |
|
| 2000 |
Mursula AM, van Aalten DM, Modis Y, Hiltunen JK, Wierenga RK. Crystallization and X-ray diffraction analysis of peroxisomal Delta3-Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae. Acta Crystallographica. Section D, Biological Crystallography. 56: 1020-3. PMID 10944342 DOI: 10.1107/S0907444900006533 |
0.479 |
|
| 2000 |
van Aalten DM, Synstad B, Brurberg MB, Hough E, Riise BW, Eijsink VG, Wierenga RK. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 97: 5842-7. PMID 10823940 DOI: 10.1073/Pnas.97.11.5842 |
0.484 |
|
| 2000 |
Lambeir AM, Backmann J, Ruiz-Sanz J, Filimonov V, Nielsen JE, Kursula I, Norledge BV, Wierenga RK. The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. European Journal of Biochemistry / Febs. 267: 2516-24. PMID 10785370 DOI: 10.1046/J.1432-1327.2000.01254.X |
0.335 |
|
| 2000 |
Modis Y, Wierenga RK. Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase. Journal of Molecular Biology. 297: 1171-82. PMID 10764581 DOI: 10.1006/Jmbi.2000.3638 |
0.686 |
|
| 2000 |
van Aalten DM, Knudsen J, DiRusso CC, Kokko T, Wierenga RK. Crystallization and X-ray diffraction studies of the fatty-acid responsive transcription factor FadR from Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography. 56: 469-71. PMID 10739923 DOI: 10.1107/S0907444900000937 |
0.363 |
|
| 1999 |
Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins. 37: 441-53. PMID 10591103 DOI: 10.1002/(Sici)1097-0134(19991115)37:3<441::Aid-Prot11>3.0.Co;2-7 |
0.4 |
|
| 1999 |
Modis Y, Wierenga RK. A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism. Structure (London, England : 1993). 7: 1279-90. PMID 10545327 DOI: 10.1016/S0969-2126(00)80061-1 |
0.717 |
|
| 1999 |
Williams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK. Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Engineering. 12: 243-50. PMID 10235625 DOI: 10.1093/Protein/12.3.243 |
0.579 |
|
| 1999 |
Kiema TR, Engel CK, Schmitz W, Filppula SA, Wierenga RK, Hiltunen JK. Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1. Biochemistry. 38: 2991-9. PMID 10074351 DOI: 10.1021/bi981646v |
0.333 |
|
| 1998 |
Modis Y, Wierenga R. Two crystal structures of N-acetyltransferases reveal a new fold for CoA-dependent enzymes Structure. 6: 1345-1350. PMID 9817851 DOI: 10.1016/S0969-2126(98)00134-8 |
0.671 |
|
| 1998 |
Modis Y, Filppula SA, Novikov DK, Norledge B, Hiltunen JK, Wierenga RK. The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure (London, England : 1993). 6: 957-70. PMID 9739087 DOI: 10.1016/S0969-2126(98)00098-7 |
0.689 |
|
| 1998 |
Williams JC, Wierenga RK, Saraste M. Insights into Src kinase functions: structural comparisons. Trends in Biochemical Sciences. 23: 179-84. PMID 9612082 DOI: 10.1016/S0968-0004(98)01202-X |
0.442 |
|
| 1998 |
Engel CK, Kiema TR, Hiltunen JK, Wierenga RK. The Crystal Structure of Enoyl-CoA Hydratase Complexed with Octanoyl-CoA Reveals the Structural Adaptations Required for Binding of a Long Chain Fatty Acid-CoA Molecule Journal of Molecular Biology. 275: 859-47. PMID 9514714 |
0.412 |
|
| 1998 |
Engel CK, Kiema TR, Hiltunen JK, Wierenga RK. The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. Journal of Molecular Biology. 275: 847-59. PMID 9480773 DOI: 10.1006/Jmbi.1997.1491 |
0.501 |
|
| 1998 |
Alvarez M, Zeelen JP, Mainfroid V, Rentier-Delrue F, Martial JA, Wyns L, Wierenga RK, Maes D. Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties. The Journal of Biological Chemistry. 273: 2199-206. PMID 9442062 DOI: 10.1074/Jbc.273.4.2199 |
0.327 |
|
| 1997 |
Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK. The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. Journal of Molecular Biology. 273: 714-28. PMID 9402066 DOI: 10.1006/Jmbi.1997.1331 |
0.695 |
|
| 1997 |
Weijland A, Williams JC, Neubauer G, Courtneidge SA, Wierenga RK, Superti-Furga G. Src regulated by C-terminal phosphorylation is monomeric. Proceedings of the National Academy of Sciences of the United States of America. 94: 3590-5. PMID 9108021 DOI: 10.1073/Pnas.94.8.3590 |
0.3 |
|
| 1997 |
Thanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W. Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop. Protein Engineering. 10: 159-67. PMID 9089815 DOI: 10.1093/Protein/10.2.159 |
0.373 |
|
| 1996 |
Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK. Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. The Embo Journal. 15: 5135-45. PMID 8895557 |
0.381 |
|
| 1996 |
Schliebs W, Thanki N, Eritja R, Wierenga R. Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies Protein Science. 5: 229-239. PMID 8745400 |
0.389 |
|
| 1996 |
Williams JC, Weijland A, Courtneidge SA, Superti-Furga G, Wierenga RK. Preliminary diffraction studies of the regulated form of chicken SRC protein tyrosine kinase Acta Crystallographica Section a Foundations of Crystallography. 52: C582-C582. DOI: 10.1107/S0108767396076350 |
0.388 |
|
| 1995 |
Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK. Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. Structure (London, England : 1993). 3: 669-79. PMID 8591044 DOI: 10.1016/S0969-2126(01)00202-7 |
0.395 |
|
| 1994 |
Kohl L, Callens M, Wierenga RK, Opperdoes FR, Michels PA. Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein. European Journal of Biochemistry / Febs. 220: 331-8. PMID 8125090 |
0.358 |
|
| 1994 |
Borchert TV, Abagyan R, Jaenicke R, Wierenga RK. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Proceedings of the National Academy of Sciences of the United States of America. 91: 1515-8. PMID 8108439 DOI: 10.1073/Pnas.91.4.1515 |
0.329 |
|
| 1994 |
Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK. Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms. Protein Science : a Publication of the Protein Society. 3: 779-87. PMID 8061607 DOI: 10.1002/pro.5560030507 |
0.413 |
|
| 1994 |
Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK. Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM. Protein Engineering. 7: 945-51. PMID 7809033 DOI: 10.1093/Protein/7.8.945 |
0.318 |
|
| 1994 |
Borchert TV, Mathieu M, Zeelen JP, Courtneidge SA, Wierenga RK. The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop. Febs Letters. 341: 79-85. PMID 7511113 DOI: 10.1016/0014-5793(94)80244-0 |
0.38 |
|
| 1993 |
Borchert TV, Abagyan R, Kishan KV, Zeelen JP, Wierenga RK. The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop. Structure (London, England : 1993). 1: 205-13. PMID 16100954 DOI: 10.1016/0969-2126(93)90021-8 |
0.374 |
|
| 1993 |
Borchert TV, Pratt K, Zeelen JP, Callens M, Noble MEM, Opperdoes FR, Michels PAM, Wierenga RK. Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant European Journal of Biochemistry. 211: 703-710. PMID 8436128 DOI: 10.1111/j.1432-1033.1993.tb17599.x |
0.354 |
|
| 1993 |
Van Der Oost J, Musacchio A, Pauptit RA, Ceska TA, Wierenga RK, Saraste M. Crystallization and preliminary X-ray analysis of the periplasmic fragment of CyoA-a subunit of the Escherichia coli cytochrome o complex Journal of Molecular Biology. 229: 794-796. PMID 8433374 |
0.304 |
|
| 1993 |
Noble MEM, Zeelen JP, Wierenga RK. Structures of the 'open' and 'closed' state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism Proteins: Structure, Function and Genetics. 16: 311-326. PMID 8356028 |
0.419 |
|
| 1993 |
Noble MEM, Musacchio A, Saraste M, Courtneidge SA, Wierenga RK. Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin Embo Journal. 12: 2617-2624. PMID 7687536 DOI: 10.1002/J.1460-2075.1993.Tb05922.X |
0.34 |
|
| 1992 |
Wierenga RK, Borcher TV, Noble MEM. Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues Febs Letters. 307: 34-39. PMID 1639191 DOI: 10.1016/0014-5793(92)80897-P |
0.322 |
|
| 1992 |
Wierenga RK, Noble MEM, Davenport RC. Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase Journal of Molecular Biology. 224: 1115-1126. PMID 1569570 DOI: 10.1016/0022-2836(92)90473-W |
0.401 |
|
| 1992 |
Zeelen JP, Pauptit RA, Wierenga RK, Kunau WH, Hiltunen JK. Crystallization and preliminary X-ray diffraction studies of mitochondrial short-chain Δ3,Δ2-enoyl-CoA isomerase from rat liver Journal of Molecular Biology. 224: 273-275. PMID 1548706 DOI: 10.1016/0022-2836(92)90591-7 |
0.319 |
|
| 1992 |
Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M. Crystal structure of a Src-homology 3 (SH3) domain Nature. 359: 851-855. PMID 1279434 DOI: 10.1038/359851A0 |
0.314 |
|
| 1991 |
Noble MEM, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AMWH, Kalk KH, Groendijk H, Hol WGJ. The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes Proteins: Structure, Function and Genetics. 10: 50-69. PMID 2062828 DOI: 10.1002/Prot.340100106 |
0.427 |
|
| 1991 |
Wierenga RK, Noble MEM, Postma JPM, Groendijk H, Kalk KH, Hol WGJ, Opperdoes FR. The crystal structure of the 'open' and the 'closed' conformation of the flexible loop of trypanosomal triosephosphate isomerase Proteins: Structure, Function and Genetics. 10: 33-49. PMID 2062827 DOI: 10.1002/prot.340100105 |
0.395 |
|
| 1991 |
Michels PAM, Marchand M, Kohl L, Allert S, Wierenga RK, Opperdoes FR. The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Trypanosoma brucei have a distant evolutionary relationship European Journal of Biochemistry. 198: 421-428. PMID 2040303 |
0.31 |
|
| 1991 |
Verlinde CL, Noble ME, Kalk KH, Groendijk H, Wierenga RK, Hol WG. Anion binding at the active site of trypanosomal triosephosphate isomerase. Monohydrogen phosphate does not mimic sulphate. European Journal of Biochemistry / Febs. 198: 53-7. PMID 2040290 DOI: 10.1111/J.1432-1033.1991.Tb15985.X |
0.601 |
|
| 1991 |
Noble ME, Verlinde CL, Groendijk H, Kalk KH, Wierenga RK, Hol WG. Crystallographic and molecular modeling studies on trypanosomal triosephosphate isomerase: a critical assessment of the predicted and observed structures of the complex with 2-phosphoglycerate. Journal of Medicinal Chemistry. 34: 2709-18. PMID 1895291 DOI: 10.1021/Jm00113A007 |
0.531 |
|
| 1991 |
Wierenga RK, Noble MEM, Vriend G, Nauche S, Hol WGJ. Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 m-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex Journal of Molecular Biology. 220: 995-1015. PMID 1880808 DOI: 10.1016/0022-2836(91)90368-G |
0.609 |
|
| 1989 |
van der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J. The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation. Biochemistry. 28: 7199-205. PMID 2819062 DOI: 10.1021/Bi00444A011 |
0.699 |
|
| 1989 |
Marchand M, Kooystra U, Wierenga RK, Lambeir AM, Van Beeumen J, Opperdoes FR, Michels PA. Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of the enzyme European Journal of Biochemistry. 184: 455-464. PMID 2792108 DOI: 10.1111/J.1432-1033.1989.Tb15038.X |
0.33 |
|
| 1989 |
Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes. Journal of Molecular Biology. 208: 679-96. PMID 2553983 DOI: 10.1016/0022-2836(89)90158-7 |
0.722 |
|
| 1988 |
van Berkel WJ, Müller F, Jekel PA, Weijer WJ, Schreuder HA, Wierenga RK. Chemical modification of tyrosine-38 in p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-p-fluorosulfonylbenzoyladenosine: a probe for the elucidation of the NADPH binding site? Involvement in catalysis, assignment in sequence and fitting to the tertiary structure European Journal of Biochemistry. 176: 449-459. PMID 3138119 |
0.406 |
|
| 1987 |
Read RJ, Wierenga RK, Groendijk H, Hol WGJ, Lambeir A, Opperdoes FR. Preliminary crystallographic studies of glycosomal glyceraldehyde phosphate dehydrogenase from Trypanosoma brucei brucei Journal of Molecular Biology. 194: 573-575. PMID 3625777 DOI: 10.1016/0022-2836(87)90684-X |
0.302 |
|
| 1987 |
Wierenga RK, Swinkels B, Michels PA, Osinga K, Misset O, Van Beeumen J, Gibson WC, Postma JP, Borst P, Opperdoes FR. Common elements on the surface of glycolytic enzymes from Trypanosoma brucei may serve as topogenic signals for import into glycosomes. The Embo Journal. 6: 215-21. PMID 3582360 DOI: 10.1002/J.1460-2075.1987.Tb04741.X |
0.363 |
|
| 1987 |
Wierenga RK, Kalk KH, Hol WGJ. Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 Å resolution Journal of Molecular Biology. 198: 109-121. PMID 3430602 DOI: 10.1016/0022-2836(87)90461-X |
0.412 |
|
| 1986 |
Michels PA, Poliszczak A, Osinga KA, Misset O, Van Beeumen J, Wierenga RK, Borst P, Opperdoes FR. Two tandemly linked identical genes code for the glycosomal glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei The Embo Journal. 5: 1049-1056. PMID 3013612 DOI: 10.1002/J.1460-2075.1986.Tb04321.X |
0.325 |
|
| 1984 |
Wierenga RK, Misset O, Opperdoes FR, Hol WGJ. Structural investigations of the glycolytic enzymes ofTrypanosoma brucei Acta Crystallographica Section a Foundations of Crystallography. 40: C37-C37. DOI: 10.1107/S0108767384098676 |
0.359 |
|
| 1983 |
Wierenga RK, Drenth J, Schulz GE. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase. Journal of Molecular Biology. 167: 725-39. PMID 6876163 DOI: 10.1016/S0022-2836(83)80106-5 |
0.551 |
|
| 1983 |
Schierbeek AJ, van der Laan JM, Groendijk H, Wierenga RK, Drenth J. Crystallization and preliminary X-ray investigation of lipoamide dehydrogenase from Azotobacter vinelandii. Journal of Molecular Biology. 165: 563-4. PMID 6687741 DOI: 10.1016/S0022-2836(83)80221-6 |
0.552 |
|
| 1983 |
Dijkstra BW, Weijer WJ, Wierenga RK. Polypeptide chains with similar amino acid sequences but a distinctly different conformation. Bovine and porcine phospholipase A2 Febs Letters. 164: 25-27. PMID 6653783 DOI: 10.1016/0014-5793(83)80011-8 |
0.527 |
|
| 1983 |
Weijer WJ, Hofsteenge J, Beintema JJ, Wierenga RK, Drenth J. p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure. European Journal of Biochemistry / Febs. 133: 109-18. PMID 6406227 DOI: 10.1111/J.1432-1033.1983.Tb07435.X |
0.594 |
|
| 1981 |
Wierenga RK, Lewis DG, Rossmann MG, Ray WJ. The structure determination of rabbit phosphoglucomutase Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 293: 205-208. PMID 6115419 DOI: 10.1098/Rstb.1981.0073 |
0.551 |
|
| 1980 |
Hofsteenge J, Vereijken JM, Weijer WJ, Beintema JJ, Wierenga RK, Drenth J. Primary and tertiary structure studies of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Isolation and alignment of the CNBr peptides; interactions of the protein with flavin adenine dinucleotide. European Journal of Biochemistry / Febs. 113: 141-50. PMID 6780352 |
0.555 |
|
| 1979 |
Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J. Crystal structure of p-hydroxybenzoate hydroxylase. Journal of Molecular Biology. 131: 55-73. PMID 40036 DOI: 10.1016/0022-2836(79)90301-2 |
0.638 |
|
| 1975 |
Drenth J, Hol WG, Wierenga RK. Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. The Journal of Biological Chemistry. 250: 5268-9. PMID 807574 |
0.615 |
|
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