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Frans A.A. Mulder, Ph.D. - Publications

Affiliations: 
1994-1998 Utrecht University, Utrecht, Netherlands 
 1999-2001 Department of Medical Genetics University of Toronto, Toronto, ON, Canada 
 2001-2003 Department of Biophysical Chemistry University of Lund, Lund, Skåne län, Sweden 
 2004-2011 Department of Molecular Dynamics University of Groningen, Groningen, Netherlands 
 2011-2023 Department of Chemistry Aarhus University, Aarhus, Denmark 
 2021- Department of Biochemistry Johannes Kepler University Linz 
Area:
Structural biology, NMR spectroscopy, protein biophysics, dynamics of biomolecules, protein electrostatics
Website:
https://pure.au.dk/portal/en/persons/frans-aa-mulder(0c10dd89-6182-482f-9c80-6739f9c9cbb8).html
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64 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2018 Hoffmann F, Xue M, Mulder F, Schäfer L. NMR Relaxation and Molecular Dynamics Simulations of Side Chain Dynamics in Proteins Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.1892  0.357
2017 Yoshimura Y, Holmberg MA, Kukic P, Andersen CB, Mata-Cabana A, Falsone SF, Vendruscolo M, Nollen EA, Mulder FA. MOAG-4 Promotes the Aggregation of α-Synuclein by Competing with Self-Protective Electrostatic Interactions. The Journal of Biological Chemistry. PMID 28336532 DOI: 10.1074/Jbc.M116.764886  0.745
2016 Yoshimura Y, Oktaviani NA, Yonezawa K, Kamikubo H, Mulder FA. Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy. Angewandte Chemie (International Ed. in English). PMID 27897362 DOI: 10.1002/Anie.201609605  0.807
2016 Xue M, Kitahara R, Yoshimura Y, Mulder FA. Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation. Biochemical and Biophysical Research Communications. PMID 27544032 DOI: 10.1016/J.Bbrc.2016.08.092  0.413
2016 Nielsen JT, Mulder FA. There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order". Frontiers in Molecular Biosciences. 3: 4. PMID 26904549 DOI: 10.3389/Fmolb.2016.00004  0.369
2016 Kitahara R, Yoshimura Y, Xue M, Kameda T, Mulder FA. Detecting O2 binding sites in protein cavities. Scientific Reports. 6: 20534. PMID 26830762 DOI: 10.1038/Srep20534  0.405
2015 Kulminskaya NV, Yoshimura Y, Runager K, Sørensen CS, Bjerring M, Andreasen M, Otzen DE, Enghild JJ, Nielsen NC, Mulder FA. Near-complete (1)H, (13)C, (15)N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T. Biomolecular Nmr Assignments. PMID 26275916 DOI: 10.1007/S12104-015-9630-2  0.579
2015 Oktaviani NA, Risør MW, Lee YH, Megens RP, de Jong DH, Otten R, Scheek RM, Enghild JJ, Nielsen NC, Ikegami T, Mulder FA. Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. Journal of Biomolecular Nmr. 62: 129-42. PMID 25820763 DOI: 10.1007/S10858-015-9925-8  0.779
2015 Hass MA, Mulder FA. Contemporary NMR Studies of Protein Electrostatics. Annual Review of Biophysics. 44: 53-75. PMID 25747592 DOI: 10.1146/Annurev-Biophys-083012-130351  0.445
2015 Kitahara R, Mulder FA. Is pressure-induced signal loss in NMR spectra for the Leu99Ala cavity mutant of T4 lysozyme due to unfolding? Proceedings of the National Academy of Sciences of the United States of America. 112: E923. PMID 25630507 DOI: 10.1073/Pnas.1423279112  0.353
2015 Yoshimura Y, Kulminskaya NV, Mulder FA. Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15N or 13C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra. Journal of Biomolecular Nmr. 61: 109-21. PMID 25577242 DOI: 10.1007/S10858-014-9890-7  0.479
2015 Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R. Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme. Biophysical Journal. 108: 133-45. PMID 25564860 DOI: 10.1016/J.Bpj.2014.11.012  0.722
2015 Hong Z, Nowakowski M, Spronk C, Petersen SV, Andreasen PA, KoźmiÅ„ski W, Mulder FA, Jensen JK. The solution structure of the MANEC-type domain from hepatocyte growth factor activator inhibitor-1 reveals an unexpected PAN/apple domain-type fold. The Biochemical Journal. 466: 299-309. PMID 25510835 DOI: 10.1042/Bj20141236  0.38
2015 Kulminskaya N, Yoshimura Y, Runager K, Sorensen C, Bjerring M, Mulder F, Nielsen N. Backbone and side-chain 13C, 15N resonance assignments of artificially disordered FAS 1-4 A546T domain of TGFBIp dissolved in 95 % of DMSO in presence of water Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr25425  0.358
2014 Chu BC, Otten R, Krewulak KD, Mulder FA, Vogel HJ. The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB. The Journal of Biological Chemistry. 289: 29219-34. PMID 25173704 DOI: 10.1074/Jbc.M114.564021  0.723
2014 Lorenzen N, Nielsen SB, Yoshimura Y, Vad BS, Andersen CB, Betzer C, Kaspersen JD, Christiansen G, Pedersen JS, Jensen PH, Mulder FA, Otzen DE. How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro. The Journal of Biological Chemistry. 289: 21299-310. PMID 24907278 DOI: 10.1074/Jbc.M114.554667  0.754
2014 O'Malley TT, Oktaviani NA, Zhang D, Lomakin A, O'Nuallain B, Linse S, Benedek GB, Rowan MJ, Mulder FA, Walsh DM. Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies. The Biochemical Journal. 461: 413-26. PMID 24785004 DOI: 10.1042/Bj20140219  0.745
2014 Chu B, Otten R, Krewulak K, Mulder F, Vogel H. Solution structure of the Escherichia coli apo ferric enterobactin binding protein Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2M6K/Pdb  0.713
2013 Avanti C, Oktaviani NA, Hinrichs WL, Frijlink HW, Mulder FA. Aspartate buffer and divalent metal ions affect oxytocin in aqueous solution and protect it from degradation. International Journal of Pharmaceutics. 444: 139-45. PMID 23376504 DOI: 10.1016/J.Ijpharm.2013.01.051  0.771
2013 Pool TJ, Oktaviani NA, Kamikubo H, Kataoka M, Mulder FA. (1)H, (13)C, and (15)N resonance assignment of photoactive yellow protein. Biomolecular Nmr Assignments. 7: 97-100. PMID 22528767 DOI: 10.1007/S12104-012-9387-9  0.785
2013 Vandova G, Tamiola K, Oktaviani N, Mulder F. Backbone 1H, 13C,and 15N chemical shift assignments for alpha-synuclein at different pH and temperature Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18857  0.75
2013 Mulder F, Scheek R. Multidimensional NMR spectroscopy Springer Us. 1637-1646. DOI: 10.1007/9783642167126  0.373
2012 Tamiola K, Mulder FA. Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins. Biochemical Society Transactions. 40: 1014-20. PMID 22988857 DOI: 10.1042/Bst20120171  0.799
2012 Oktaviani NA, Pool TJ, Kamikubo H, Slager J, Scheek RM, Kataoka M, Mulder FA. Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy. Biophysical Journal. 102: 579-86. PMID 22325281 DOI: 10.1016/J.Bpj.2011.12.024  0.78
2012 Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomolecular Nmr Assignments. 6: 15-8. PMID 21647611 DOI: 10.1007/S12104-011-9315-4  0.717
2011 Mulder FA, Otten R, Scheek RM. Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra. Journal of Biomolecular Nmr. 51: 199-207. PMID 21947928 DOI: 10.1007/S10858-011-9554-9  0.694
2011 Karasawa A, Erkens GB, Berntsson RP, Otten R, Schuurman-Wolters GK, Mulder FA, Poolman B. Cystathionine β-synthase (CBS) domains 1 and 2 fulfill different roles in ionic strength sensing of the ATP-binding cassette (ABC) transporter OpuA. The Journal of Biological Chemistry. 286: 37280-91. PMID 21878634 DOI: 10.1074/Jbc.M111.284059  0.701
2011 Meinema AC, Laba JK, Hapsari RA, Otten R, Mulder FA, Kralt A, van den Bogaart G, Lusk CP, Poolman B, Veenhoff LM. Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science (New York, N.Y.). 333: 90-3. PMID 21659568 DOI: 10.1126/Science.1205741  0.7
2011 Tamiola K, Mulder FA. ncIDP-assign: a SPARKY extension for the effective NMR assignment of intrinsically disordered proteins. Bioinformatics (Oxford, England). 27: 1039-40. PMID 21372082 DOI: 10.1093/Bioinformatics/Btr054  0.787
2011 Oktaviani NA, Otten R, Dijkstra K, Scheek RM, Thulin E, Akke M, Mulder FA. 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G. Biomolecular Nmr Assignments. 5: 79-84. PMID 21069485 DOI: 10.1007/S12104-010-9272-3  0.751
2011 Maeno A, Kitahara R, Dahlquist F, Yokoyama S, Mulder F, Akasaka K. 1H1348 Cavity hydration as a gateway to internal mobility : A high pressure ^<13>C and ^<15>N-NMR study of T4 lysozyme(Protein: Property 2,The 49th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51: S49. DOI: 10.2142/Biophys.51.S49_1  0.381
2010 Tamiola K, Acar B, Mulder FA. Sequence-specific random coil chemical shifts of intrinsically disordered proteins. Journal of the American Chemical Society. 132: 18000-3. PMID 21128621 DOI: 10.1021/Ja105656T  0.809
2010 Otten R, Villali J, Kern D, Mulder FA. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r). Journal of the American Chemical Society. 132: 17004-14. PMID 21058670 DOI: 10.1021/Ja107410X  0.757
2010 Wood K, Tobias DJ, Kessler B, Gabel F, Oesterhelt D, Mulder FA, Zaccai G, Weik M. The low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations. Journal of the American Chemical Society. 132: 4990-1. PMID 20302295 DOI: 10.1021/Ja910502G  0.353
2010 Otten R, Chu B, Krewulak KD, Vogel HJ, Mulder FA. Comprehensive and cost-effective NMR spectroscopy of methyl groups in large proteins. Journal of the American Chemical Society. 132: 2952-60. PMID 20148553 DOI: 10.1021/Ja907706A  0.741
2010 Mulder FA, Filatov M. NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination. Chemical Society Reviews. 39: 578-90. PMID 20111782 DOI: 10.1039/B811366C  0.402
2010 Hansen DF, Neudecker P, Vallurupalli P, Mulder FA, Kay LE. Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion. Journal of the American Chemical Society. 132: 42-3. PMID 20000605 DOI: 10.1021/Ja909294N  0.579
2009 Mulder FA. Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts. Chembiochem : a European Journal of Chemical Biology. 10: 1477-9. PMID 19466705 DOI: 10.1002/Cbic.200900086  0.443
2008 Paquin R, Ferrage F, Mulder FA, Akke M, Bodenhausen G. Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. Journal of the American Chemical Society. 130: 15805-7. PMID 18975903 DOI: 10.1021/Ja803794G  0.659
2008 Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. Biophysical Journal. 95: 1928-44. PMID 18456828 DOI: 10.1529/Biophysj.107.126995  0.362
2007 André I, Linse S, Mulder FA. Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin. Journal of the American Chemical Society. 129: 15805-13. PMID 18044888 DOI: 10.1021/Ja0721824  0.452
2007 Helgstrand M, Mandava CS, Mulder FA, Liljas A, Sanyal S, Akke M. The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain. Journal of Molecular Biology. 365: 468-79. PMID 17070545 DOI: 10.1016/J.Jmb.2006.10.025  0.617
2007 Lindman S, Linse S, Mulder FA, André I. pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability. Biophysical Journal. 92: 257-66. PMID 17040982 DOI: 10.1529/Biophysj.106.088682  0.387
2006 Lindman S, Linse S, Mulder FA, André I. Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein. Biochemistry. 45: 13993-4002. PMID 17115694 DOI: 10.1021/Bi061555V  0.356
2006 Brath U, Akke M, Yang D, Kay LE, Mulder FA. Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 128: 5718-27. PMID 16637639 DOI: 10.1021/Ja0570279  0.735
2005 Lundström P, Mulder FA, Akke M. Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins. Proceedings of the National Academy of Sciences of the United States of America. 102: 16984-9. PMID 16278300 DOI: 10.1073/Pnas.0504361102  0.673
2004 Mulder FA, Bouakaz L, Lundell A, Venkataramana M, Liljas A, Akke M, Sanyal S. Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome. Biochemistry. 43: 5930-6. PMID 15147176 DOI: 10.1021/Bi0495331  0.658
2002 Mittermaier T, Mulder F, Dahlquist R, Kay LE. Studying Protein-Excited States by Nmr. Thescientificworldjournal. 2: 45-46. PMID 29973797 DOI: 10.1100/tsw.2002.23  0.483
2002 Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 124: 1443-51. PMID 11841314 DOI: 10.1021/Ja0119806  0.721
2002 Choy WY, Mulder FA, Crowhurst KA, Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. Journal of Molecular Biology. 316: 101-12. PMID 11829506 DOI: 10.1006/Jmbi.2001.5328  0.519
2001 Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE. Slow dynamics in folded and unfolded states of an SH3 domain. Journal of the American Chemical Society. 123: 11341-52. PMID 11707108 DOI: 10.1021/Ja011300Z  0.735
2001 Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE. Studying excited states of proteins by NMR spectroscopy. Nature Structural Biology. 8: 932-5. PMID 11685237 DOI: 10.1038/Nsb1101-932  0.723
2001 Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 4556-66. PMID 11457242 DOI: 10.1021/Ja004179P  0.727
2001 Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE. Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme. Journal of the American Chemical Society. 123: 967-75. PMID 11456632 DOI: 10.1021/Ja003447G  0.745
2000 Mulder FA, Hon B, Muhandiram DR, Dahlquist FW, Kay LE. Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry. 39: 12614-22. PMID 11027141 DOI: 10.1021/Bi001351T  0.582
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  0.781
1999 Mulder FA, Schipper D, Bott R, Boelens R. Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. Journal of Molecular Biology. 292: 111-23. PMID 10493861 DOI: 10.1006/Jmbi.1999.3034  0.665
1999 Mulder FA, van Tilborg PJ, Kaptein R, Boelens R. Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements. Journal of Biomolecular Nmr. 13: 275-88. PMID 10212986 DOI: 10.1023/A:1008354232281  0.765
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  0.745
1998 Düx P, Rubinstenn G, Vuister GW, Boelens R, Mulder FA, Hård K, Hoff WD, Kroon AR, Crielaard W, Hellingwerf KJ, Kaptein R. Solution structure and backbone dynamics of the photoactive yellow protein. Biochemistry. 37: 12689-99. PMID 9737845 DOI: 10.1021/Bi9806652  0.796
1998 Rubinstenn G, Vuister GW, Mulder FA, Düx PE, Boelens R, Hellingwerf KJ, Kaptein R. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution. Nature Structural Biology. 5: 568-70. PMID 9665170 DOI: 10.1038/823  0.8
1997 Martin JR, Mulder FA, Karimi-Nejad Y, van der Zwan J, Mariani M, Schipper D, Boelens R. The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site. Structure (London, England : 1993). 5: 521-32. PMID 9115441 DOI: 10.1016/S0969-2126(97)00208-6  0.626
1997 Tessari M, Mulder FA, Boelens R, Vuister GW. Determination of Amide Proton CSA in15N-Labeled Proteins Using1H CSA/15N–1H Dipolar and15N CSA/15N–1H Dipolar Cross-Correlation Rates Journal of Magnetic Resonance. 127: 128-133. DOI: 10.1006/Jmre.1997.1199  0.723
1996 Mulder FA, Spronk CA, Slijper M, Kaptein R, Boelens R. Improved HSQC experiments for the observation of exchange broadened signals. Journal of Biomolecular Nmr. 8: 223-8. PMID 22911143 DOI: 10.1007/Bf00211169  0.751
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