| Year |
Citation |
Score |
| 2019 |
Lange J, Baakman C, Pistorius A, Krieger E, Hooft R, Joosten R, Vriend G. Facilities that make the PDB data collection more powerful. Protein Science : a Publication of the Protein Society. PMID 31724231 DOI: 10.1002/Pro.3788 |
0.371 |
|
| 2019 |
Shalaeva DN, Cherepanov DA, Galperin MY, Vriend G, Mulkidjanian AY. G protein-coupled receptors of class A harness the energy of membrane potential to increase their sensitivity and selectivity. Biochimica Et Biophysica Acta. Biomembranes. 183051. PMID 31449800 DOI: 10.1016/J.Bbamem.2019.183051 |
0.32 |
|
| 2018 |
Shirvanizadeh N, Vriend G, Arab SS. Loop modelling 1.0. Journal of Molecular Graphics & Modelling. 84: 64-68. PMID 29920424 DOI: 10.1016/J.Jmgm.2018.06.001 |
0.302 |
|
| 2018 |
Wozniak PP, Pelc J, Skrzypecki M, Vriend G, Kotulska M. Bio-knowledge-based filters improve residue-residue contact prediction accuracy. Bioinformatics (Oxford, England). 34: 3675-3683. PMID 29850768 DOI: 10.1093/Bioinformatics/Bty416 |
0.313 |
|
| 2018 |
Kooistra AJ, Vass M, McGuire R, Leurs R, de Esch IJ, Vriend G, Verhoeven S, de Graaf C. 3D-e-Chem: Structural Cheminformatics Workflows for Computer-Aided Drug Discovery. Chemmedchem. PMID 29337438 DOI: 10.1002/Cmdc.201700754 |
0.342 |
|
| 2018 |
Singh D, Berntsen KRM, Baakman C, Vriend G, Lahiri T. A Critical Note on Symmetry Contact Artifacts and the Evaluation of the Quality of Homology Models Symmetry. 10: 25. DOI: 10.3390/Sym10010025 |
0.366 |
|
| 2017 |
Wozniak PP, Konopka BM, Xu J, Vriend G, Kotulska M. Forecasting residue-residue contact prediction accuracy. Bioinformatics (Oxford, England). PMID 29036497 DOI: 10.1093/Bioinformatics/Btx416 |
0.317 |
|
| 2017 |
van den Bergh T, Tamo G, Nobili A, Tao Y, Tan T, Bornscheuer UT, Kuipers RKP, Vroling B, de Jong RM, Subramanian K, Schaap PJ, Desmet T, Nidetzky B, Vriend G, Joosten HJ. CorNet: Assigning function to networks of co-evolving residues by automated literature mining. Plos One. 12: e0176427. PMID 28545124 DOI: 10.1371/Journal.Pone.0176427 |
0.357 |
|
| 2017 |
Schwarte A, Genz M, Skalden L, Nobili A, Vickers C, Melse O, Kuipers R, Joosten HJ, Stourac J, Bendl J, Black J, Haase P, Baakman C, Damborsky J, Bornscheuer U, ... Vriend G, et al. NewProt - a protein engineering portal. Protein Engineering, Design & Selection : Peds. 1-7. PMID 28475759 DOI: 10.1093/Protein/Gzx024 |
0.34 |
|
| 2017 |
Wozniak PP, Vriend G, Kotulska M. Correlated mutations select misfolded from properly folded proteins. Bioinformatics (Oxford, England). 33: 1497-1504. PMID 28203707 DOI: 10.1093/Bioinformatics/Btx013 |
0.368 |
|
| 2016 |
Munk C, Isberg V, Mordalski S, Harpsøe K, Rataj K, Hauser AS, Kolb P, Bojarski AJ, Vriend G, Gloriam DE. GPCRdb: the G protein-coupled receptor database - an introduction. British Journal of Pharmacology. 173: 2195-207. PMID 27155948 DOI: 10.1111/Bph.13509 |
0.34 |
|
| 2016 |
Vollan HS, Tannæs T, Vriend G, Bukholm G. In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality. International Journal of Molecular Sciences. 17. PMID 27110766 DOI: 10.3390/Ijms17040599 |
0.327 |
|
| 2016 |
Touw WG, Joosten RP, Vriend G. New biological insights from better structure models. Journal of Molecular Biology. PMID 26869101 DOI: 10.1016/J.Jmb.2016.02.002 |
0.347 |
|
| 2015 |
Lange J, Wyrwicz LS, Vriend G. KMAD: Knowledge based multiple sequence alignment for intrinsically disordered proteins. Bioinformatics (Oxford, England). PMID 26568635 DOI: 10.1093/Bioinformatics/Btv663 |
0.336 |
|
| 2015 |
Zarzycka B, Kuenemann MA, Miteva MA, Nicolaes GA, Vriend G, Sperandio O. Stabilization of protein-protein interaction complexes through small molecules. Drug Discovery Today. PMID 26434617 DOI: 10.1016/J.Drudis.2015.09.011 |
0.309 |
|
| 2015 |
Labbé CM, Kuenemann MA, Zarzycka B, Vriend G, Nicolaes GA, Lagorce D, Miteva MA, Villoutreix BO, Sperandio O. iPPI-DB: an online database of modulators of protein-protein interactions. Nucleic Acids Research. PMID 26432833 DOI: 10.1093/Nar/Gkv982 |
0.338 |
|
| 2015 |
Holliday GL, Bairoch A, Bagos PG, Chatonnet A, Craik DJ, Finn RD, Henrissat B, Landsman D, Manning G, Nagano N, O'Donovan C, Pruitt KD, Rawlings ND, Saier M, Sowdhamini R, ... ... Vriend G, et al. Key challenges for the creation and maintenance of specialist protein resources. Proteins. 83: 1005-13. PMID 25820941 DOI: 10.1002/Prot.24803 |
0.315 |
|
| 2014 |
Kwon TJ, Oh SK, Park HJ, Sato O, Venselaar H, Choi SY, Kim S, Lee KY, Bok J, Lee SH, Vriend G, Ikebe M, Kim UK, Choi JY. The effect of novel mutations on the structure and enzymatic activity of unconventional myosins associated with autosomal dominant non-syndromic hearing loss. Open Biology. 4. PMID 25080041 DOI: 10.1098/Rsob.140107 |
0.302 |
|
| 2014 |
van der Kant R, Vriend G. Alpha-bulges in G protein-coupled receptors. International Journal of Molecular Sciences. 15: 7841-64. PMID 24806342 DOI: 10.3390/Ijms15057841 |
0.303 |
|
| 2014 |
Berntsen KR, Vriend G. Anomalies in the refinement of isoleucine. Acta Crystallographica. Section D, Biological Crystallography. 70: 1037-49. PMID 24699648 DOI: 10.1107/S139900471400087X |
0.33 |
|
| 2013 |
Venselaar H, Camilli F, Gholizadeh S, Snelleman M, Brunner HG, Vriend G. Status quo of annotation of human disease variants. Bmc Bioinformatics. 14: 352. PMID 24305467 DOI: 10.1186/1471-2105-14-352 |
0.337 |
|
| 2012 |
Doreleijers JF, Sousa da Silva AW, Krieger E, Nabuurs SB, Spronk CA, Stevens TJ, Vranken WF, Vriend G, Vuister GW. CING: an integrated residue-based structure validation program suite. Journal of Biomolecular Nmr. 54: 267-83. PMID 22986687 DOI: 10.1007/S10858-012-9669-7 |
0.322 |
|
| 2012 |
Cho HJ, Park HJ, Trexler M, Venselaar H, Lee KY, Robertson NG, Baek JI, Kang BS, Morton CC, Vriend G, Patthy L, Kim UK. A novel COCH mutation associated with autosomal dominant nonsyndromic hearing loss disrupts the structural stability of the vWFA2 domain. Journal of Molecular Medicine (Berlin, Germany). 90: 1321-31. PMID 22610276 DOI: 10.1007/S00109-012-0911-2 |
0.32 |
|
| 2012 |
Hensen U, Meyer T, Haas J, Rex R, Vriend G, Grubmüller H. Exploring protein dynamics space: the dynasome as the missing link between protein structure and function. Plos One. 7: e33931. PMID 22606222 DOI: 10.1371/Journal.Pone.0033931 |
0.335 |
|
| 2012 |
Doreleijers JF, Vranken WF, Schulte C, Markley JL, Ulrich EL, Vriend G, Vuister GW. NRG-CING: integrated validation reports of remediated experimental biomolecular NMR data and coordinates in wwPDB. Nucleic Acids Research. 40: D519-24. PMID 22139937 DOI: 10.1093/Nar/Gkr1134 |
0.314 |
|
| 2012 |
Meyer T, Hensen U, Haas J, Rex R, Vriend G, Grubmüller H. The Dynasome as the Missing Link Between Protein Structure and Function Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.2465 |
0.348 |
|
| 2011 |
Joosten RP, Joosten K, Cohen SX, Vriend G, Perrakis A. Automatic rebuilding and optimization of crystallographic structures in the Protein Data Bank. Bioinformatics (Oxford, England). 27: 3392-8. PMID 22034521 DOI: 10.1093/Bioinformatics/Btr590 |
0.366 |
|
| 2011 |
Read RJ, Adams PD, Arendall WB, Brunger AT, Emsley P, Joosten RP, Kleywegt GJ, Krissinel EB, Lütteke T, Otwinowski Z, Perrakis A, Richardson JS, Sheffler WH, Smith JL, Tickle IJ, ... Vriend G, et al. A new generation of crystallographic validation tools for the protein data bank. Structure (London, England : 1993). 19: 1395-412. PMID 22000512 DOI: 10.1016/J.Str.2011.08.006 |
0.32 |
|
| 2011 |
Joosten RP, te Beek TA, Krieger E, Hekkelman ML, Hooft RW, Schneider R, Sander C, Vriend G. A series of PDB related databases for everyday needs. Nucleic Acids Research. 39: D411-9. PMID 21071423 DOI: 10.1093/Nar/Gkq1105 |
0.368 |
|
| 2010 |
Venselaar H, Te Beek TA, Kuipers RK, Hekkelman ML, Vriend G. Protein structure analysis of mutations causing inheritable diseases. An e-Science approach with life scientist friendly interfaces. Bmc Bioinformatics. 11: 548. PMID 21059217 DOI: 10.1186/1471-2105-11-548 |
0.345 |
|
| 2010 |
Hekkelman ML, Te Beek TA, Pettifer SR, Thorne D, Attwood TK, Vriend G. WIWS: a protein structure bioinformatics Web service collection. Nucleic Acids Research. 38: W719-23. PMID 20501602 DOI: 10.1093/Nar/Gkq453 |
0.313 |
|
| 2010 |
Kuipers RK, Joosten HJ, van Berkel WJ, Leferink NG, Rooijen E, Ittmann E, van Zimmeren F, Jochens H, Bornscheuer U, Vriend G, dos Santos VA, Schaap PJ. 3DM: systematic analysis of heterogeneous superfamily data to discover protein functionalities. Proteins. 78: 2101-13. PMID 20455266 DOI: 10.1002/Prot.22725 |
0.358 |
|
| 2010 |
Huberts DH, Venselaar H, Vriend G, Veenhuis M, van der Klei IJ. The moonlighting function of pyruvate carboxylase resides in the non-catalytic end of the TIM barrel. Biochimica Et Biophysica Acta. 1803: 1038-42. PMID 20359504 DOI: 10.1016/J.Bbamcr.2010.03.018 |
0.321 |
|
| 2010 |
Stary A, Wacker SJ, Boukharta L, Zachariae U, Karimi-Nejad Y, Aqvist J, Vriend G, de Groot BL. Toward a consensus model of the HERG potassium channel. Chemmedchem. 5: 455-67. PMID 20104563 DOI: 10.1002/Cmdc.200900461 |
0.323 |
|
| 2009 |
Joosten RP, Salzemann J, Bloch V, Stockinger H, Berglund AC, Blanchet C, Bongcam-Rudloff E, Combet C, Da Costa AL, Deleage G, Diarena M, Fabbretti R, Fettahi G, Flegel V, Gisel A, ... ... Vriend G, et al. PDB_REDO: automated re-refinement of X-ray structure models in the PDB. Journal of Applied Crystallography. 42: 376-384. PMID 22477769 DOI: 10.1107/S0021889809008784 |
0.329 |
|
| 2009 |
Doreleijers JF, Vranken WF, Schulte C, Lin J, Wedell JR, Penkett CJ, Vuister GW, Vriend G, Markley JL, Ulrich EL. The NMR restraints grid at BMRB for 5,266 protein and nucleic acid PDB entries. Journal of Biomolecular Nmr. 45: 389-96. PMID 19809795 DOI: 10.1007/S10858-009-9378-Z |
0.325 |
|
| 2009 |
Lee HK, Song MH, Kang M, Lee JT, Kong KA, Choi SJ, Lee KY, Venselaar H, Vriend G, Lee WS, Park HJ, Kwon TK, Bok J, Kim UK. Clinical and molecular characterizations of novel POU3F4 mutations reveal that DFN3 is due to null function of POU3F4 protein. Physiological Genomics. 39: 195-201. PMID 19671658 DOI: 10.1152/Physiolgenomics.00100.2009 |
0.339 |
|
| 2009 |
Kuipers RK, Joosten HJ, Verwiel E, Paans S, Akerboom J, van der Oost J, Leferink NG, van Berkel WJ, Vriend G, Schaap PJ. Correlated mutation analyses on super-family alignments reveal functionally important residues. Proteins. 76: 608-16. PMID 19274741 DOI: 10.1002/Prot.22374 |
0.322 |
|
| 2008 |
von Grotthuss M, Plewczynski D, Vriend G, Rychlewski L. 3D-Fun: predicting enzyme function from structure. Nucleic Acids Research. 36: W303-7. PMID 18515349 DOI: 10.1093/Nar/Gkn308 |
0.333 |
|
| 2008 |
Zachariae U, Schneider R, Velisetty P, Lange A, Seeliger D, Wacker SJ, Karimi-Nejad Y, Vriend G, Becker S, Pongs O, Baldus M, de Groot BL. The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation. Structure (London, England : 1993). 16: 747-54. PMID 18462679 DOI: 10.1016/J.Str.2008.01.018 |
0.313 |
|
| 2008 |
Collin RW, Chellappa R, Pauw RJ, Vriend G, Oostrik J, van Drunen W, Huygen PL, Admiraal R, Hoefsloot LH, Cremers FP, Xiang M, Cremers CW, Kremer H. Missense mutations in POU4F3 cause autosomal dominant hearing impairment DFNA15 and affect subcellular localization and DNA binding. Human Mutation. 29: 545-54. PMID 18228599 DOI: 10.1002/Humu.20693 |
0.324 |
|
| 2008 |
Collin RW, Kalay E, Tariq M, Peters T, van der Zwaag B, Venselaar H, Oostrik J, Lee K, Ahmed ZM, Caylan R, Li Y, Spierenburg HA, Eyupoglu E, Heister A, Riazuddin S, ... ... Vriend G, et al. Mutations of ESRRB encoding estrogen-related receptor beta cause autosomal-recessive nonsyndromic hearing impairment DFNB35. American Journal of Human Genetics. 82: 125-38. PMID 18179891 DOI: 10.1016/J.Ajhg.2007.09.008 |
0.311 |
|
| 2007 |
Joosten RP, Vriend G. PDB improvement starts with data deposition. Science (New York, N.Y.). 317: 195-6. PMID 17626865 DOI: 10.1126/Science.317.5835.195 |
0.333 |
|
| 2006 |
Krieger E, Nielsen JE, Spronk CA, Vriend G. Fast empirical pKa prediction by Ewald summation. Journal of Molecular Graphics & Modelling. 25: 481-6. PMID 16644253 DOI: 10.1016/J.Jmgm.2006.02.009 |
0.448 |
|
| 2006 |
Van Durme J, Horn F, Costagliola S, Vriend G, Vassart G. GRIS: glycoprotein-hormone receptor information system. Molecular Endocrinology (Baltimore, Md.). 20: 2247-55. PMID 16543405 DOI: 10.1210/Me.2006-0020 |
0.317 |
|
| 2006 |
van Driel MA, Bruggeman J, Vriend G, Brunner HG, Leunissen JA. A text-mining analysis of the human phenome. European Journal of Human Genetics : Ejhg. 14: 535-42. PMID 16493445 DOI: 10.1038/Sj.Ejhg.5201585 |
0.308 |
|
| 2006 |
Nabuurs SB, Spronk CA, Vuister GW, Vriend G. Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Plos Computational Biology. 2: e9. PMID 16462939 DOI: 10.1371/Journal.Pcbi.0020009 |
0.362 |
|
| 2005 |
Nabuurs SB, Krieger E, Spronk CA, Nederveen AJ, Vriend G, Vuister GW. Definition of a new information-based per-residue quality parameter. Journal of Biomolecular Nmr. 33: 123-34. PMID 16258830 DOI: 10.1007/S10858-005-2826-5 |
0.307 |
|
| 2004 |
Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G. Making optimal use of empirical energy functions: force-field parameterization in crystal space. Proteins. 57: 678-83. PMID 15390263 DOI: 10.1002/Prot.20251 |
0.327 |
|
| 2004 |
Eijsink VG, Bjørk A, Gåseidnes S, Sirevåg R, Synstad B, van den Burg B, Vriend G. Rational engineering of enzyme stability. Journal of Biotechnology. 113: 105-20. PMID 15380651 DOI: 10.1016/J.Jbiotec.2004.03.026 |
0.334 |
|
| 2004 |
Nabuurs SB, Nederveen AJ, Vranken W, Doreleijers JF, Bonvin AM, Vuister GW, Vriend G, Spronk CA. DRESS: a database of REfined solution NMR structures. Proteins. 55: 483-6. PMID 15103611 DOI: 10.1002/Prot.20118 |
0.333 |
|
| 2004 |
Synstad B, Gåseidnes S, Van Aalten DM, Vriend G, Nielsen JE, Eijsink VG. Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase. European Journal of Biochemistry / Febs. 271: 253-62. PMID 14717693 DOI: 10.1046/J.1432-1033.2003.03923.X |
0.471 |
|
| 2004 |
Spronk CAEM, Nabuurs SB, Krieger E, Vriend G, Vuister GW. Validation of protein structures derived by NMR spectroscopy Progress in Nuclear Magnetic Resonance Spectroscopy. 45: 315-337. DOI: 10.1016/J.Pnmrs.2004.08.003 |
0.333 |
|
| 2004 |
Nabuurs SB, Spronk CAEM, Vriend G, Vuister GW. Concepts and tools for NMR restraint analysis and validation Concepts in Magnetic Resonance Part a: Bridging Education and Research. 22: 90-105. DOI: 10.1002/Cmr.A.20016 |
0.324 |
|
| 2003 |
Campagne F, Bettler E, Vriend G, Weinstein H. Batch mode generation of residue-based diagrams of proteins. Bioinformatics (Oxford, England). 19: 1854-5. PMID 14512361 DOI: 10.1093/Bioinformatics/Btg236 |
0.324 |
|
| 2003 |
Nabuurs SB, Spronk CA, Krieger E, Maassen H, Vriend G, Vuister GW. Quantitative evaluation of experimental NMR restraints. Journal of the American Chemical Society. 125: 12026-34. PMID 14505424 DOI: 10.1021/Ja035440F |
0.311 |
|
| 2003 |
Bettler E, Krause R, Horn F, Vriend G. NRSAS: Nuclear Receptor Structure Analysis Servers. Nucleic Acids Research. 31: 3400-3. PMID 12824335 DOI: 10.1093/Nar/Gkg505 |
0.326 |
|
| 2003 |
Spronk CA, Nabuurs SB, Bonvin AM, Krieger E, Vuister GW, Vriend G. The precision of NMR structure ensembles revisited. Journal of Biomolecular Nmr. 25: 225-34. PMID 12652134 DOI: 10.1023/A:1022819716110 |
0.325 |
|
| 2002 |
Singer MS, Vriend G, Bywater RP. Prediction of protein residue contacts with a PDB-derived likelihood matrix. Protein Engineering. 15: 721-5. PMID 12456870 DOI: 10.1093/Protein/15.9.721 |
0.375 |
|
| 2002 |
Flohil JA, Vriend G, Berendsen HJ. Completion and refinement of 3-D homology models with restricted molecular dynamics: application to targets 47, 58, and 111 in the CASP modeling competition and posterior analysis. Proteins. 48: 593-604. PMID 12211026 DOI: 10.1002/prot.10105 |
0.581 |
|
| 2002 |
de Kreij A, van den Burg B, Venema G, Vriend G, Eijsink VG, Nielsen JE. The effects of modifying the surface charge on the catalytic activity of a thermolysin-like protease. The Journal of Biological Chemistry. 277: 15432-8. PMID 11859085 DOI: 10.1074/Jbc.M200807200 |
0.447 |
|
| 2001 |
Nielsen JE, Borchert TV, Vriend G. The determinants of alpha-amylase pH-activity profiles. Protein Engineering. 14: 505-12. PMID 11522925 DOI: 10.1093/Protein/14.7.505 |
0.342 |
|
| 2001 |
Nielsen JE, Vriend G. Optimizing the hydrogen-bond network in Poisson-Boltzmann equation-based pK(a) calculations. Proteins. 43: 403-12. PMID 11340657 DOI: 10.1002/Prot.1053 |
0.346 |
|
| 2001 |
Levashina EA, Moita LF, Blandin S, Vriend G, Lagueux M, Kafatos FC. Conserved role of a complement-like protein in phagocytosis revealed by dsRNA knockout in cultured cells of the mosquito, Anopheles gambiae. Cell. 104: 709-18. PMID 11257225 DOI: 10.1016/S0092-8674(01)00267-7 |
0.311 |
|
| 2001 |
Eijsink VGH, Vriend G, Van Den Burg B. Engineering a hyperstable enzyme by manipulation of early steps in the unfolding process Biocatalysis and Biotransformation. 19: 443-458. DOI: 10.3109/10242420108992029 |
0.314 |
|
| 1999 |
Nielsen JE, Andersen KV, Honig B, Hooft RW, Klebe G, Vriend G, Wade RC. Improving macromolecular electrostatics calculations. Protein Engineering. 12: 657-62. PMID 10469826 DOI: 10.1093/Protein/12.8.657 |
0.362 |
|
| 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 |
0.575 |
|
| 1999 |
Boteva R, Visser AJWG, Filippi B, Vriend G, Veenhuis M, Van Der Klei IJ. Conformational transitions accompanying oligomerization of yeast alcohol oxidase, a peroxisomal flavoenzyme Biochemistry. 38: 5034-5044. PMID 10213606 DOI: 10.1021/Bi982266C |
0.304 |
|
| 1999 |
de Groot BL, Vriend G, Berendsen HJ. Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism. Journal of Molecular Biology. 286: 1241-9. PMID 10047494 DOI: 10.1006/Jmbi.1998.2568 |
0.556 |
|
| 1998 |
Vriend G, Berendsen HJ, van den Burg B, Venema G, Eijsink VG. Early steps in the unfolding of thermolysin-like proteases. The Journal of Biological Chemistry. 273: 35074-7. PMID 9857041 DOI: 10.1074/Jbc.273.52.35074 |
0.585 |
|
| 1998 |
Veltman OR, Vriend G, Berendsen HJ, Van den Burg B, Venema G, Eijsink VG. A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases. Biochemistry. 37: 5312-9. PMID 9548763 DOI: 10.1021/Bi9725879 |
0.516 |
|
| 1998 |
Steinberger D, Vriend G, Mulliken JB, Müller U. The mutations in FGFR2-associated craniosynostoses are clustered in five structural elements of immunoglobulin-like domain III of the receptor Human Genetics. 102: 145-150. PMID 9521581 DOI: 10.1007/S004390050668 |
0.302 |
|
| 1998 |
Van Den Burg B, Vriend G, Veltman OR, Venema G, Eijsink VGH. Engineering an enzyme to resist boiling Proceedings of the National Academy of Sciences of the United States of America. 95: 2056-2060. PMID 9482837 DOI: 10.1073/Pnas.95.5.2056 |
0.329 |
|
| 1997 |
Sobolev V, Moallem TM, Wade RC, Vriend G, Edelman M. CASP2 molecular docking predictions with the LIGIN software Proteins: Structure, Function and Genetics. 29: 210-214. PMID 9485514 DOI: 10.1002/(Sici)1097-0134(1997)1+<210::Aid-Prot28>3.0.Co;2-Q |
0.34 |
|
| 1997 |
Veltman OR, Vriend G, Hardy F, Mansfeld J, Van Den Burg B, Venema G, Eijsink VGH. Mutational analysis of a surface area that is critical for the thermal stability of thermolysin-like proteases European Journal of Biochemistry. 248: 433-440. PMID 9346299 DOI: 10.1111/J.1432-1033.1997.00433.X |
0.308 |
|
| 1997 |
de Groot BL, van Aalten DM, Scheek RM, Amadei A, Vriend G, Berendsen HJ. Prediction of protein conformational freedom from distance constraints. Proteins. 29: 240-51. PMID 9329088 DOI: 10.1002/(Sici)1097-0134(199710)29:2<240::Aid-Prot11>3.0.Co;2-O |
0.6 |
|
| 1997 |
Mansfeld J, Vriend G, Dijkstra BW, Veltman OR, Van Den Burg B, Venema G, Ulbrich-Hofmann R, Eijsink VGH. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond Journal of Biological Chemistry. 272: 11152-11156. PMID 9111013 DOI: 10.1074/Jbc.272.17.11152 |
0.321 |
|
| 1996 |
Hooft RWW, Sander C, Scharf M, Vriend G. The PDBFINDER database: A summary of PDB, DSSP and HSSP information with added value Computer Applications in the Biosciences. 12: 525-529. PMID 9021272 DOI: 10.1093/Bioinformatics/12.6.525 |
0.336 |
|
| 1996 |
Veltman OR, Vriend G, Middelhoven PJ, Van den Burg B, Venema G, Eijsink VGH. Analysis of structural determinants of the stability of thermolysin-like proteases by molecular modelling and site-directed mutagenesis Protein Engineering. 9: 1181-1189. PMID 9010931 DOI: 10.1093/Protein/9.12.1181 |
0.347 |
|
| 1996 |
Aalten DMFv, Bywater R, Findlay JBC, Hendlich M, Hooft RWW, Vriend G. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. Journal of Computer-Aided Molecular Design. 10: 255-262. PMID 8808741 DOI: 10.1007/Bf00355047 |
0.305 |
|
| 1996 |
Sobolev V, Wade RC, Vriend G, Edelman M. Molecular docking using surface complementarity Proteins: Structure, Function and Genetics. 25: 120-129. PMID 8727324 DOI: 10.1002/(Sici)1097-0134(199605)25:1<120::Aid-Prot10>3.0.Co;2-M |
0.327 |
|
| 1995 |
Dunkel R, Vriend G, Beato M, Suske G. Progesterone binding to uteroglobin: two alternative orientations of the ligand. Protein Engineering. 8: 71-9. PMID 7770456 DOI: 10.1093/Protein/8.1.71 |
0.31 |
|
| 1995 |
van Aalten DM, Amadei A, Linssen AB, Eijsink VG, Vriend G, Berendsen HJ. The essential dynamics of thermolysin: confirmation of the hinge-bending motion and comparison of simulations in vacuum and water. Proteins. 22: 45-54. PMID 7675786 DOI: 10.1002/Prot.340220107 |
0.538 |
|
| 1994 |
Van den Burg B, Dijkstra BW, Vriend G, Van der Vinne B, Venema G, Eijsink VGH. Protein stabilization by hydrophobic interactions at the surface European Journal of Biochemistry. 220: 981-985. PMID 8143751 DOI: 10.1111/J.1432-1033.1994.Tb18702.X |
0.33 |
|
| 1994 |
Rodenburg KW, Scheeren-Groot E, Vriend G, Hooykaas PJ. The N-terminal domain of VirG of Agrobacterium tumefaciens: modelling and analysis of mutant phenotypes. Protein Engineering. 7: 905-9. PMID 7971952 DOI: 10.1093/Protein/7.7.905 |
0.304 |
|
| 1993 |
Vriend G, Eijsink V. Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases Journal of Computer-Aided Molecular Design. 7: 367-396. PMID 8229092 DOI: 10.1007/Bf02337558 |
0.361 |
|
| 1993 |
Oliveira L, Paiva ACM, Vriend G. A common motif in G-protein-coupled seven transmembrane helix receptors Journal of Computer-Aided Molecular Design. 7: 649-658. DOI: 10.1007/Bf00125323 |
0.307 |
|
| 1992 |
Peter W, Dunkel R, Stouten PF, Vriend G, Beato M, Suske G. Interchain cysteine bridges control entry of progesterone to the central cavity of the uteroglobin dimer. Protein Engineering. 5: 351-9. PMID 1409556 DOI: 10.1093/Protein/5.4.351 |
0.329 |
|
| 1992 |
Holm L, Ouzounis C, Sander C, Tuparev G, Vriend G. A database of protein structure families with common folding motifs Protein Science. 1: 1691-1698. PMID 1304898 DOI: 10.1002/Pro.5560011217 |
0.375 |
|
| 1991 |
Peter W, Brüller HJ, Vriend G, Beato M, Suske G. Identification of residues essential for progesterone binding to uteroglobin by site-directed mutagenesis. The Journal of Steroid Biochemistry and Molecular Biology. 38: 27-33. PMID 1997121 DOI: 10.1016/0960-0760(91)90397-N |
0.344 |
|
| 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 |
0.544 |
|
| 1991 |
Vriend G, Berendsen HJ, van der Zee JR, van den Burg B, Venema G, Eijsink VG. Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule. Protein Engineering. 4: 941-5. PMID 1817257 |
0.576 |
|
| 1989 |
Schierbeek AJ, Swarte MB, Dijkstra BW, Vriend G, Read RJ, Hol WG, Drenth J, Betzel C. X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. Journal of Molecular Biology. 206: 365-79. PMID 2716052 DOI: 10.1016/0022-2836(89)90486-5 |
0.618 |
|
| 1989 |
Luo M, Vriend G, Kamer G, Rossmann MG. Structure determination of Mengo virus. Acta Crystallographica. Section B, Structural Science. 45: 85-92. PMID 2559754 DOI: 10.1107/S0108768188010894 |
0.395 |
|
| 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 |
0.683 |
|
| 1989 |
Kowalski H, Maurer-Fogy I, Vriend G, Casari G, Beyer A, Blaas D. Trypsin sensitivity of several human rhinovirus serotypes in their low pH-induced conformation. Virology. 171: 611-614. PMID 2548332 DOI: 10.1016/0042-6822(89)90632-6 |
0.317 |
|
| 1989 |
Voorintholt R, Kosters MT, Vegter G, Vriend G, Hol WG. A very fast program for visualizing protein surfaces, channels and cavities. Journal of Molecular Graphics. 7: 243-5. PMID 2486827 DOI: 10.1016/0263-7855(89)80010-4 |
0.413 |
|
| 1987 |
Arnold E, Luo M, Vriend G, Rossmann MG, Palmenberg AC, Parks GD, Nicklin MJ, Wimmer E. Implications of the picornavirus capsid structure for polyprotein processing Proceedings of the National Academy of Sciences of the United States of America. 84: 21-25. PMID 3467351 DOI: 10.1073/Pnas.84.1.21 |
0.428 |
|
| 1987 |
Luo M, Vriend G, Kamer G, Minor I, Arnold E, Rossmann MG, Boege U, Scraba DG, Duke GM, Palmenberg AC. The atomic structure of Mengo virus at 3.0 A resolution. Science (New York, N.Y.). 235: 182-91. PMID 3026048 DOI: 10.1126/Science.3026048 |
0.505 |
|
| 1987 |
Blaas D, Kuechler E, Vriend G, Arnold E, Luo M, Rossmann MG. Comparison of the three-dimensional structure of two human rhinoviruses (HRV2 and HRV14). Proteins. 2: 263-72. PMID 2834716 DOI: 10.1002/Prot.340020402 |
0.428 |
|
| 1987 |
Arnold E, Vriend G, Luo M, Griffith JP, Kamer G, Erickson JW, Johnson JE, Rossmann MG. The structure determination of a common cold virus, human rhinovirus 14 Acta Crystallographica Section a Foundations of Crystallography. 43: 346-361. DOI: 10.1107/S0108767387099306 |
0.541 |
|
| 1987 |
Vriend G, Rossmann MG. Determination of the orientation of a randomly placed crystal from a single oscillation photograph Journal of Applied Crystallography. 20: 338-343. DOI: 10.1107/S0021889887086515 |
0.354 |
|
| 1986 |
Vriend G, Verduin BJM, Hemminga MA. Role of the N-terminal part of the coat protein in the assembly of cowpea chlorotic mottle virus. A 500 MHz proton nuclear magnetic resonance study and structural calculations Journal of Molecular Biology. 191: 453-460. PMID 3820293 DOI: 10.1016/0022-2836(86)90140-3 |
0.525 |
|
| 1986 |
Smith TJ, Kremer MJ, Luo M, Vriend G, Arnold E, Kamer G, Rossmann MG, McKinlay MA, Diana GD, Otto MJ. The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating. Science (New York, N.Y.). 233: 1286-93. PMID 3018924 DOI: 10.1126/Science.3018924 |
0.375 |
|
| 1986 |
Rossmann MG, Arnold E, Vriend G. Comparison of vector search and feedback methods for finding heavy-atom sites in isomorphous derivatives Acta Crystallographica Section a Foundations of Crystallography. 42: 325-334. DOI: 10.1107/S0108767386099178 |
0.382 |
|
| 1986 |
Vriend G, Rossmann MG, Arnold E, Luo M, Griffith JP, Moffat K. Post-refinement of oscillation diffraction data collected at a synchrotron radiation source Journal of Applied Crystallography. 19: 134-139. DOI: 10.1107/S0021889886089793 |
0.353 |
|
| 1985 |
Vriend G, Hemminga MA, Haasnoot CAG, Hilbers CW. A two-dimensional nuclear overhauser enhancement NMR spectroscopy study at 500 MHz on cowpea chlorotic mottle virus protein assembled in spherical capsids Journal of Magnetic Resonance (1969). 64: 501-505. DOI: 10.1016/0022-2364(85)90113-1 |
0.499 |
|
| 1984 |
Arnold E, Ericksson JW, Frankenberger EA, Hecht H, Luo M, Rossmann MG, Vriend G. Progress in the structure determination of a common cold virus Acta Crystallographica Section a Foundations of Crystallography. 40: C48-C48. DOI: 10.1107/S0108767384098317 |
0.402 |
|
| 1984 |
Vriend G, Schilthuis JG, Verduin BJM, Hemminga MA. Saturation-transfer ESR spectroscopy on maleimide spin-labeled cowpea chlorotic mottle virus Journal of Magnetic Resonance (1969). 58: 421-427. DOI: 10.1016/0022-2364(84)90146-X |
0.433 |
|
| 1982 |
Vriend G, Verduin BJM, Hemminga MA, Schaafsma TJ. Mobility involved in protein-RNA interaction in spherical plant viruses, studied by nuclear magnetic resonance spectroscopy Febs Letters. 145: 49-52. DOI: 10.1016/0014-5793(82)81204-0 |
0.646 |
|
| 1982 |
Vriend G, Hemminga MA, Verduin BJM, Schaafsma TJ. Swelling of cowpea chlorotic mottle virus studied by proton nuclear magnetic resonance Febs Letters. 146: 319-321. DOI: 10.1016/0014-5793(82)80943-5 |
0.631 |
|
| 1981 |
Vriend G, Hemminga MA, Verduin BJM, Wit JLD, Schaafsma TJ. Segmental mobility involved in protein-RNA interaction in cowpea chlorotic mottle virus Febs Letters. 134: 167-171. DOI: 10.1016/0014-5793(81)80593-5 |
0.648 |
|
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