| Year |
Citation |
Score |
| 2023 |
Romanuka J, Folkers GE, Gnida M, Kovačič L, Wienk H, Kaptein R, Boelens R. Genetic switching by the Lac repressor is based on two-state Monod-Wyman-Changeux allostery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2311240120. PMID 38019859 DOI: 10.1073/pnas.2311240120 |
0.673 |
|
| 2018 |
Faridounnia M, Folkers GE, Boelens R. Function and Interactions of ERCC1-XPF in DNA Damage Response. Molecules (Basel, Switzerland). 23. PMID 30563071 DOI: 10.3390/Molecules23123205 |
0.536 |
|
| 2016 |
Das D, Faridounnia M, Kovacic L, Kaptein R, Boelens R, Folkers GE. Single-strand DNA Binding by the Helix-Hairpin-Helix Domain of XPF Contributes to Substrate Specificity of ERCC1-XPF. The Journal of Biological Chemistry. PMID 28028171 DOI: 10.1074/Jbc.M116.747857 |
0.753 |
|
| 2016 |
Dongre R, Folkers GE, Gualerzi CO, Boelens R, Wienk H. A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit. Protein Science : a Publication of the Protein Society. PMID 27364543 DOI: 10.1002/Pro.2977 |
0.524 |
|
| 2016 |
Dongre R, Folkers G, Gualerzi C, Boelens R, Wienk H. Structure and Dynamics of the Geobacillus stearothermophilus IF2 G3-subdomain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25975 |
0.474 |
|
| 2015 |
Faridounnia M, Wienk H, Kovačič L, Folkers GE, Jaspers NG, Kaptein R, Hoeijmakers JH, Boelens R. The Cerebro-oculo-facio-skeletal Syndrome Point Mutation F231L in the ERCC1 DNA Repair Protein Causes Dissociation of the ERCC1-XPF Complex. The Journal of Biological Chemistry. 290: 20541-55. PMID 26085086 DOI: 10.1074/Jbc.M114.635169 |
0.629 |
|
| 2014 |
Khan F, Daniëls MA, Folkers GE, Boelens R, Saqlan Naqvi SM, van Ingen H. Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function. Nucleic Acids Research. 42: 8705-18. PMID 24957607 DOI: 10.1093/Nar/Gku468 |
0.577 |
|
| 2014 |
Kastritis PL, Rodrigues JP, Folkers GE, Boelens R, Bonvin AM. Proteins feel more than they see: fine-tuning of binding affinity by properties of the non-interacting surface. Journal of Molecular Biology. 426: 2632-52. PMID 24768922 DOI: 10.1016/J.Jmb.2014.04.017 |
0.543 |
|
| 2013 |
Wienk H, Slootweg JC, Speerstra S, Kaptein R, Boelens R, Folkers GE. The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition. Nucleic Acids Research. 41: 6739-49. PMID 23661679 DOI: 10.1093/Nar/Gkt354 |
0.728 |
|
| 2012 |
Das D, Folkers GE, van Dijk M, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R. The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition. Structure (London, England : 1993). 20: 667-75. PMID 22483113 DOI: 10.1016/J.Str.2012.02.009 |
0.766 |
|
| 2012 |
Wienk H, Tishchenko E, Belardinelli R, Tomaselli S, Dongre R, Spurio R, Folkers GE, Gualerzi CO, Boelens R. Structural dynamics of bacterial translation initiation factor IF2. The Journal of Biological Chemistry. 287: 10922-32. PMID 22308033 DOI: 10.1074/Jbc.M111.333393 |
0.55 |
|
| 2011 |
Berger I, Blanco AG, Boelens R, Cavarelli J, Coll M, Folkers GE, Nie Y, Pogenberg V, Schultz P, Wilmanns M, Moras D, Poterszman A. Structural insights into transcription complexes. Journal of Structural Biology. 175: 135-46. PMID 21571073 DOI: 10.1016/J.Jsb.2011.04.015 |
0.516 |
|
| 2010 |
Huang A, de Jong RN, Folkers GE, Boelens R. NMR characterization of foldedness for the production of E3 RING domains. Journal of Structural Biology. 172: 120-7. PMID 20682345 DOI: 10.1016/J.Jsb.2010.07.014 |
0.539 |
|
| 2010 |
Bird LE, Ren J, Nettleship JE, Folkers GE, Owens RJ, Stammers DK. Novel structural features in two ZHX homeodomains derived from a systematic study of single and multiple domains. Bmc Structural Biology. 10: 13. PMID 20509910 DOI: 10.1186/1472-6807-10-13 |
0.353 |
|
| 2009 |
Romanuka J, van den Bulke H, Kaptein R, Boelens R, Folkers GE. Novel strategies to overcome expression problems encountered with toxic proteins: application to the production of Lac repressor proteins for NMR studies. Protein Expression and Purification. 67: 104-12. PMID 19460439 DOI: 10.1016/J.Pep.2009.05.008 |
0.619 |
|
| 2009 |
Romanuka J, Folkers GE, Biris N, Tishchenko E, Wienk H, Bonvin AM, Kaptein R, Boelens R. Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes. Journal of Molecular Biology. 390: 478-89. PMID 19450607 DOI: 10.1016/J.Jmb.2009.05.022 |
0.608 |
|
| 2009 |
Wienk H, Lammers I, Hotze A, Wu J, Wechselberger RW, Owens R, Stammers DK, Stuart D, Kaptein R, Folkers GE. The tandem zinc-finger region of human ZHX adopts a novel C2H2 zinc finger structure with a C-terminal extension. Biochemistry. 48: 4431-9. PMID 19348505 DOI: 10.1021/bi9001997 |
0.573 |
|
| 2008 |
Diercks T, AB E, Daniels MA, de Jong RN, Besseling R, Kaptein R, Folkers GE. Solution structure and characterization of the DNA-binding activity of the B3BP-Smr domain. Journal of Molecular Biology. 383: 1156-70. PMID 18804481 DOI: 10.1016/j.jmb.2008.09.005 |
0.676 |
|
| 2008 |
de Jong RN, Truffault V, Diercks T, Ab E, Daniels MA, Kaptein R, Folkers GE. Structure and DNA binding of the human Rtf1 Plus3 domain. Structure (London, England : 1993). 16: 149-59. PMID 18184592 DOI: 10.1016/j.str.2007.10.018 |
0.632 |
|
| 2008 |
Das D, Tripsianes K, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R, Folkers GE. The HhH domain of the human DNA repair protein XPF forms stable homodimers. Proteins. 70: 1551-63. PMID 17912758 DOI: 10.1002/Prot.21635 |
0.745 |
|
| 2007 |
Tripsianes K, Folkers GE, Zheng C, Das D, Grinstead JS, Kaptein R, Boelens R. Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization. Nucleic Acids Research. 35: 5789-98. PMID 17720715 DOI: 10.1093/Nar/Gkm503 |
0.758 |
|
| 2007 |
Kamphuis MB, Monti MC, van den Heuvel RH, Santos-Sierra S, Folkers GE, Lemonnier M, DÃaz-Orejas R, Heck AJ, Boelens R. Interactions between the toxin Kid of the bacterial parD system and the antitoxins Kis and MazE. Proteins. 67: 219-31. PMID 17206710 DOI: 10.1002/Prot.21254 |
0.53 |
|
| 2007 |
Tripsianes K, Folkers G, Zheng C, Das D, Grinstead J, Kaptein R, Boelens R. Solution structure of the ERCC1 central domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Jpd/Pdb |
0.691 |
|
| 2006 |
de Jong RN, Daniëls MA, Kaptein R, Folkers GE. Enzyme free cloning for high throughput gene cloning and expression. Journal of Structural and Functional Genomics. 7: 109-18. PMID 17295099 DOI: 10.1007/s10969-006-9014-z |
0.374 |
|
| 2006 |
Au K, Berrow NS, Blagova E, Boucher IW, Boyle MP, Brannigan JA, Carter LG, Dierks T, Folkers G, Grenha R, Harlos K, Kaptein R, Kalliomaa AK, Levdikov VM, Meier C, et al. Application of high-throughput technologies to a structural proteomics-type analysis of Bacillus anthracis. Acta Crystallographica. Section D, Biological Crystallography. 62: 1267-75. PMID 17001104 DOI: 10.1107/S0907444906033555 |
0.502 |
|
| 2006 |
Ab E, Atkinson AR, Banci L, Bertini I, Ciofi-Baffoni S, Brunner K, Diercks T, Dötsch V, Engelke F, Folkers GE, Griesinger C, Gronwald W, Günther U, Habeck M, de Jong RN, et al. NMR in the SPINE Structural Proteomics project. Acta Crystallographica. Section D, Biological Crystallography. 62: 1150-61. PMID 17001092 DOI: 10.1107/S0907444906032070 |
0.469 |
|
| 2006 |
Grenha R, Rzechorzek NJ, Brannigan JA, de Jong RN, Ab E, Diercks T, Truffault V, Ladds JC, Fogg MJ, Bongiorni C, Perego M, Kaptein R, Wilson KS, Folkers GE, Wilkinson AJ. Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli. The Journal of Biological Chemistry. 281: 37993-8003. PMID 17001075 DOI: 10.1074/jbc.M607617200 |
0.486 |
|
| 2006 |
Milon P, Tischenko E, Tomsic J, Caserta E, Folkers G, La Teana A, Rodnina MV, Pon CL, Boelens R, Gualerzi CO. The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor. Proceedings of the National Academy of Sciences of the United States of America. 103: 13962-7. PMID 16968770 DOI: 10.1073/Pnas.0606384103 |
0.554 |
|
| 2006 |
Jonker HR, Wechselberger RW, Pinkse M, Kaptein R, Folkers GE. Gradual phosphorylation regulates PC4 coactivator function. The Febs Journal. 273: 1430-44. PMID 16689930 DOI: 10.1111/j.1742-4658.2006.05165.x |
0.508 |
|
| 2006 |
Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. Biochemistry. 45: 5067-81. PMID 16605275 DOI: 10.1021/Bi052531B |
0.738 |
|
| 2006 |
Limacher A, Kloer DP, Flückiger S, Folkers G, Crameri R, Scapozza L. The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element Structure. 14: 185-195. PMID 16472738 DOI: 10.1016/J.Str.2005.10.015 |
0.374 |
|
| 2006 |
de Jong RN, Ab E, Diercks T, Truffault V, Daniëls M, Kaptein R, Folkers GE. Solution structure of the human ubiquitin-specific protease 15 DUSP domain. The Journal of Biological Chemistry. 281: 5026-31. PMID 16298993 DOI: 10.1074/jbc.M510993200 |
0.575 |
|
| 2006 |
Grenha R, Rzechorzek NJ, Brannigan JA, Ab E, Folkers GE, Jong RND, Diercks T, Wilkinson AJ, Kaptein R, Wilson KS. Nmr Solution Structure Of A Protein Aspartic Acid Phosphate Phosphatase From Bacillus Anthracis Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr7349 |
0.458 |
|
| 2005 |
Tripsianes K, Folkers G, Ab E, Das D, Odijk H, Jaspers NG, Hoeijmakers JH, Kaptein R, Boelens R. The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair. Structure (London, England : 1993). 13: 1849-58. PMID 16338413 DOI: 10.1016/J.Str.2005.08.014 |
0.769 |
|
| 2005 |
Kopke Salinas R, Folkers GE, Bonvin AM, Das D, Boelens R, Kaptein R. Altered specificity in DNA binding by the lac repressor: a mutant lac headpiece that mimics the gal repressor. Chembiochem : a European Journal of Chemical Biology. 6: 1628-37. PMID 16094693 DOI: 10.1002/Cbic.200500049 |
0.717 |
|
| 2005 |
Patterson HM, Brannigan JA, Cutting SM, Wilson KS, Wilkinson AJ, Ab E, Diercks T, de Jong RN, Truffault V, Folkers GE, Kaptein R. The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus. The Journal of Biological Chemistry. 280: 36214-20. PMID 16049010 DOI: 10.1074/jbc.M506910200 |
0.514 |
|
| 2005 |
Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. Structural properties of the promiscuous VP16 activation domain. Biochemistry. 44: 827-39. PMID 15654739 DOI: 10.1021/Bi0482912 |
0.673 |
|
| 2004 |
Perozzo R, Folkers G, Scapozza L. Thermodynamics of protein-ligand interactions: History, presence, and future aspects Journal of Receptors and Signal Transduction. 24: 1-52. PMID 15344878 DOI: 10.1081/Rrs-120037896 |
0.3 |
|
| 2004 |
Folkers GE, van Buuren BN, Kaptein R. Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. Journal of Structural and Functional Genomics. 5: 119-31. PMID 15263851 DOI: 10.1023/B:JSFG.0000029200.66197.0c |
0.493 |
|
| 2004 |
Cavalli A, Prota AE, Stehle T, Dermody TS, Recanatini M, Folkers G, Scapozza L. A molecular dynamics study of reovirus attachment protein sigma1 reveals conformational changes in sigma1 structure. Biophysical Journal. 86: 3423-31. PMID 15189844 DOI: 10.1529/Biophysj.103.030825 |
0.347 |
|
| 2002 |
Singh S, Folkers GE, Bonvin AM, Boelens R, Wechselberger R, Niztayev A, Kaptein R. Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli. The Embo Journal. 21: 6257-66. PMID 12426397 DOI: 10.1093/Emboj/Cdf627 |
0.736 |
|
| 2001 |
Kalodimos CG, Folkers GE, Boelens R, Kaptein R. Strong DNA binding by covalently linked dimeric Lac headpiece: evidence for the crucial role of the hinge helices. Proceedings of the National Academy of Sciences of the United States of America. 98: 6039-44. PMID 11353825 DOI: 10.1073/Pnas.101129898 |
0.696 |
|
| 2000 |
Nooren IM, Folkers GE, Kaptein R, Sauer RT, Boelens R. Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex. Journal of Biomolecular Structure & Dynamics. 17: 113-22. PMID 22607414 DOI: 10.1080/07391102.2000.10506611 |
0.73 |
|
| 2000 |
van Tilborg PJ, Czisch M, Mulder FA, Folkers GE, Bonvin AM, Nair M, Boelens R, Kaptein R. Changes in dynamical behavior of the retinoid X receptor DNA-binding domain upon binding to a 14 base-pair DNA half site. Biochemistry. 39: 8747-57. PMID 10913286 DOI: 10.1021/Bi991550G |
0.69 |
|
| 1999 |
Spronk CA, Folkers GE, Noordman AM, Wechselberger R, van den Brink N, Boelens R, Kaptein R. Hinge-helix formation and DNA bending in various lac repressor-operator complexes. The Embo Journal. 18: 6472-80. PMID 10562559 DOI: 10.1093/Emboj/18.22.6472 |
0.652 |
|
| 1999 |
van Tilborg PJ, Mulder FA, de Backer MM, Nair M, van Heerde EC, Folkers G, van der Saag PT, Karimi-Nejad Y, Boelens R, Kaptein R. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry. 38: 1951-6. PMID 10026278 DOI: 10.1021/Bi982526Q |
0.708 |
|
| 1995 |
Kern P, Brunne RM, Folkers G. Nucleotide-binding properties of adenylate kinase from Escherichia coli: a molecular dynamics study in aqueous and vacuum environments. Journal of Computer-Aided Molecular Design. 8: 367-88. PMID 7815090 DOI: 10.1007/Bf00125373 |
0.335 |
|
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