Pernilla Wittung-Stafshede - Publications

Affiliations: 
1999-2003 Tulane University, New Orleans, LA, United States 
 2004-2008 Rice University, Houston, TX 
 2008-2015 Umeå University, Umeå, Västerbottens län, Sweden 
 2015- Chalmers University of Technology, Sweden 
Area:
Biochemistry
Website:
https://en.wikipedia.org/wiki/Pernilla_Wittung-Stafshede

183 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
2020 Werner TER, Bernson D, Esbjörner EK, Rocha S, Wittung-Stafshede P. Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers. Proceedings of the National Academy of Sciences of the United States of America. PMID 33093204 DOI: 10.1073/pnas.2015503117  1
2020 Hannestad JK, Rocha S, Agnarsson B, Zhdanov VP, Wittung-Stafshede P, Höök F. Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein. Proceedings of the National Academy of Sciences of the United States of America. PMID 32513706 DOI: 10.1073/Pnas.1914670117  1
2019 Rocha S, Kumar R, Horvath I, Wittung-Stafshede P. Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity. Protein Engineering, Design & Selection : Peds. PMID 31566224 DOI: 10.1093/Protein/Gzz021  1
2019 Dedic J, Rocha S, Okur HI, Wittung-Stafshede P, Roke S. Membrane-Protein-Hydration Interaction of α-Synuclein with Anionic Vesicles Probed via Angle-Resolved Second Harmonic Scattering. The Journal of Physical Chemistry. B. PMID 30625272 DOI: 10.1021/Acs.Jpcb.8B11096  1
2018 Jiang K, Rocha S, Westling A, Kk S, Dorfman K, Wittung-Stafshede P, Westerlund F. Alpha-synuclein modulates the physical properties of DNA. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 30102440 DOI: 10.1002/Chem.201803933  1
2018 Horvath I, Rocha S, Wittung-Stafshede P. In Vitro Analysis of α-Synuclein Amyloid Formation and Cross-Reactivity. Methods in Molecular Biology (Clifton, N.J.). 1779: 73-83. PMID 29886528 DOI: 10.1007/978-1-4939-7816-8_6  1
2018 Rocha S, Wittung-Stafshede P. The Role of Lipid Chemistry in Alpha-Synuclein Membrane Binding and Aggregation Biophysical Journal. 114. DOI: 10.1016/J.Bpj.2017.11.1598  1
2017 Bosaeus N, Reymer A, Beke-Somfai T, Brown T, Takahashi M, Wittung-Stafshede P, Rocha S, Nordén B. A stretched conformation of DNA with a biological role? Quarterly Reviews of Biophysics. 50: e11. PMID 29233223 DOI: 10.1017/S0033583517000099  1
2017 Kiskis J, Horvath I, Wittung-Stafshede P, Rocha S. Unraveling amyloid formation paths of Parkinson's disease protein α-synuclein triggered by anionic vesicles. Quarterly Reviews of Biophysics. 50: e3. PMID 29233215 DOI: 10.1017/S0033583517000026  1
2016 Sampson TR, Debelius JW, Thron T, Janssen S, Shastri GG, Ilhan ZE, Challis C, Schretter CE, Rocha S, Gradinaru V, Chesselet MF, Keshavarzian A, Shannon KM, Krajmalnik-Brown R, Wittung-Stafshede P, et al. Gut Microbiota Regulate Motor Deficits and Neuroinflammation in a Model of Parkinson's Disease. Cell. 167: 1469-1480.e12. PMID 27912057 DOI: 10.1016/J.Cell.2016.11.018  1
2016 Kumar R, Ariöz C, Li Y, Bosaeus N, Rocha S, Wittung-Stafshede P. Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 27744583 DOI: 10.1007/S10534-016-9976-7  1
2016 Good JA, Andersson C, Hansen S, Wall J, Krishnan KS, Begum A, Grundström C, Niemiec MS, Vaitkevicius K, Chorell E, Wittung-Stafshede P, Sauer UH, Sauer-Eriksson AE, Almqvist F, Johansson J. Attenuating Listeria monocytogenes Virulence by Targeting the Regulatory Protein PrfA. Cell Chemical Biology. 23: 404-14. PMID 26991105 DOI: 10.1016/J.Chembiol.2016.02.013  1
2016 Mondol T, Åden J, Wittung-Stafshede P. Copper binding triggers compaction in N-terminal tail of human copper pump ATP7B. Biochemical and Biophysical Research Communications. 470: 663-9. PMID 26797276 DOI: 10.1016/J.Bbrc.2016.01.085  1
2016 Kahra D, Kovermann M, Wittung-Stafshede P. The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1. Biophysical Journal. 110: 95-102. PMID 26745413 DOI: 10.1016/J.Bpj.2015.11.016  1
2015 Singh P, Chorell E, Krishnan KS, Kindahl T, Åden J, Wittung-Stafshede P, Almqvist F. Synthesis of Multiring Fused 2-Pyridones via a Nitrene Insertion Reaction: Fluorescent Modulators of α-Synuclein Amyloid Formation. Organic Letters. PMID 26650849 DOI: 10.1021/Acs.Orglett.5B03190  1
2015 Wittung-Stafshede P. Unresolved questions in human copper pump mechanisms. Quarterly Reviews of Biophysics. 48: 471-8. PMID 26537407 DOI: 10.1017/S0033583515000128  1
2015 Chorell E, Andersson E, Evans ML, Jain N, Götheson A, Åden J, Chapman MR, Almqvist F, Wittung-Stafshede P. Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts. Plos One. 10: e0140194. PMID 26465894 DOI: 10.1371/Journal.Pone.0140194  1
2015 Sharma SK, Chorell E, Wittung-Stafshede P. Insulin-degrading enzyme is activated by the C-terminus of α-synuclein. Biochemical and Biophysical Research Communications. 466: 192-5. PMID 26343304 DOI: 10.1016/J.Bbrc.2015.09.002  1
2015 Sharma SK, Chorell E, Steneberg P, Vernersson-Lindahl E, Edlund H, Wittung-Stafshede P. Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner. Scientific Reports. 5: 12531. PMID 26228656 DOI: 10.1038/Srep12531  1
2015 Öhrvik H, Wittung-Stafshede P. Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation? International Journal of Molecular Sciences. 16: 16728-39. PMID 26213915 DOI: 10.3390/Ijms160816728  1
2015 Nors Perdersen M, Foderà V, Horvath I, van Maarschalkerweerd A, Nørgaard Toft K, Weise C, Almqvist F, Wolf-Watz M, Wittung-Stafshede P, Vestergaard B. Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth. Scientific Reports. 5: 10422. PMID 26020724 DOI: 10.1038/Srep10422  1
2015 Niemiec MS, Dingeldein AP, Wittung-Stafshede P. Enthalpy-entropy compensation at play in human copper ion transfer. Scientific Reports. 5: 10518. PMID 26013029 DOI: 10.1038/Srep10518  1
2015 Kahra D, Mondol T, Niemiec MS, Wittung-Stafshede P. Human Copper Chaperone Atox1 Translocates to the Nucleus but does not Bind DNA In Vitro. Protein and Peptide Letters. 22: 532-8. PMID 25962064 DOI: 10.2174/0929866522666150506094546  1
2015 Petzoldt S, Kahra D, Kovermann M, Dingeldein AP, Niemiec MS, Ådén J, Wittung-Stafshede P. Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 28: 577-85. PMID 25673218 DOI: 10.1007/S10534-015-9832-1  1
2015 Evans ML, Chorell E, Taylor JD, Ã…den J, Götheson A, Li F, Koch M, Sefer L, Matthews SJ, Wittung-Stafshede P, Almqvist F, Chapman MR. The bacterial curli system possesses a potent and selective inhibitor of amyloid formation. Molecular Cell. 57: 445-55. PMID 25620560 DOI: 10.1016/J.Molcel.2014.12.025  1
2014 Mikaelsson T, Adén J, Wittung-Stafshede P, Johansson LB. Macromolecular crowding effects on two homologs of ribosomal protein s16: protein-dependent structural changes and local interactions. Biophysical Journal. 107: 401-10. PMID 25028882 DOI: 10.1016/J.Bpj.2014.05.038  1
2014 Niemiec MS, Dingeldein AP, Wittung-Stafshede P. T versus D in the MTCXXC motif of copper transport proteins plays a role in directional metal transport. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 19: 1037-47. PMID 24824562 DOI: 10.1007/S00775-014-1147-0  1
2014 Adén J, Wittung-Stafshede P. Folding of an unfolded protein by macromolecular crowding in vitro. Biochemistry. 53: 2271-7. PMID 24665900 DOI: 10.1021/Bi500222G  1
2014 Christiansen A, Wittung-Stafshede P. Synthetic crowding agent dextran causes excluded volume interactions exclusively to tracer protein apoazurin. Febs Letters. 588: 811-4. PMID 24491997 DOI: 10.1016/J.Febslet.2014.01.043  1
2014 Palm-Espling ME, Lundin C, Björn E, Naredi P, Wittung-Stafshede P. Interaction between the anticancer drug Cisplatin and the copper chaperone Atox1 in human melanoma cells. Protein and Peptide Letters. 21: 63-8. PMID 23988033 DOI: 10.2174/09298665113209990036  1
2013 Christiansen A, Wittung-Stafshede P. Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitro. Biophysical Journal. 105: 1689-99. PMID 24094410 DOI: 10.1016/J.Bpj.2013.08.038  1
2013 Andersson EK, Bengtsson C, Evans ML, Chorell E, Sellstedt M, Lindgren AE, Hufnagel DA, Bhattacharya M, Tessier PM, Wittung-Stafshede P, Almqvist F, Chapman MR. Modulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones. Chemistry & Biology. 20: 1245-54. PMID 24035282 DOI: 10.1016/J.Chembiol.2013.07.017  1
2013 Palm-Espling ME, Andersson CD, Björn E, Linusson A, Wittung-Stafshede P. Determinants for simultaneous binding of copper and platinum to human chaperone Atox1: hitchhiking not hijacking. Plos One. 8: e70473. PMID 23936210 DOI: 10.1371/Journal.Pone.0070473  1
2013 Nilsson L, Ã…dén J, Niemiec MS, Nam K, Wittung-Stafshede P. Small pH and salt variations radically alter the thermal stability of metal-binding domains in the copper transporter, Wilson disease protein. The Journal of Physical Chemistry. B. 117: 13038-50. PMID 23675861 DOI: 10.1021/Jp402415Y  1
2013 Mikaelsson T, Adén J, Johansson LB, Wittung-Stafshede P. Direct observation of protein unfolded state compaction in the presence of macromolecular crowding. Biophysical Journal. 104: 694-704. PMID 23442920 DOI: 10.1016/J.Bpj.2012.12.020  1
2013 Horvath I, Sellstedt M, Weise C, Nordvall LM, Krishna Prasad G, Olofsson A, Larsson G, Almqvist F, Wittung-Stafshede P. Modulation of α-synuclein fibrillization by ring-fused 2-pyridones: templation and inhibition involve oligomers with different structure. Archives of Biochemistry and Biophysics. 532: 84-90. PMID 23399432 DOI: 10.1016/J.Abb.2013.01.012  1
2013 Christiansen A, Wang Q, Cheung MS, Wittung-Stafshede P. Effects of macromolecular crowding agents on protein folding in vitro and in silico Biophysical Reviews. 5: 137-145. DOI: 10.1007/s12551-013-0108-0  1
2012 Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekström F, Linusson A. Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase. Angewandte Chemie (International Ed. in English). 51: 12716-20. PMID 23161758 DOI: 10.1002/anie.201205113  1
2012 Chen E, Christiansen A, Wang Q, Cheung MS, Kliger DS, Wittung-Stafshede P. Effects of macromolecular crowding on burst phase kinetics of cytochrome c folding. Biochemistry. 51: 9836-45. PMID 23145850 DOI: 10.1021/Bi301324Y  1
2012 Andersson CD, Karlberg T, Ekblad T, Lindgren AE, Thorsell AG, Spjut S, Uciechowska U, Niemiec MS, Wittung-Stafshede P, Weigelt J, Elofsson M, Schüler H, Linusson A. Discovery of ligands for ADP-ribosyltransferases via docking-based virtual screening. Journal of Medicinal Chemistry. 55: 7706-18. PMID 22823910 DOI: 10.1021/Jm300746D  1
2012 Niemiec MS, Weise CF, Wittung-Stafshede P. In vitro thermodynamic dissection of human copper transfer from chaperone to target protein. Plos One. 7: e36102. PMID 22574136 DOI: 10.1371/Journal.Pone.0036102  1
2012 Blomberg J, Aguilar X, Brännström K, Rautio L, Olofsson A, Wittung-Stafshede P, Björklund S. Interactions between DNA, transcriptional regulator Dreb2a and the Med25 mediator subunit from Arabidopsis thaliana involve conformational changes. Nucleic Acids Research. 40: 5938-50. PMID 22447446 DOI: 10.1093/Nar/Gks265  1
2012 Palm-Espling ME, Niemiec MS, Wittung-Stafshede P. Role of metal in folding and stability of copper proteins in vitro. Biochimica Et Biophysica Acta. 1823: 1594-603. PMID 22306006 DOI: 10.1016/J.Bbamcr.2012.01.013  1
2012 Palm-Espling ME, Wittung-Stafshede P. Reaction of platinum anticancer drugs and drug derivatives with a copper transporting protein, Atox1. Biochemical Pharmacology. 83: 874-81. PMID 22285228 DOI: 10.1016/J.Bcp.2012.01.018  1
2012 Horvath I, Weise CF, Andersson EK, Chorell E, Sellstedt M, Bengtsson C, Olofsson A, Hultgren SJ, Chapman M, Wolf-Watz M, Almqvist F, Wittung-Stafshede P. Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation. Journal of the American Chemical Society. 134: 3439-44. PMID 22260746 DOI: 10.1021/Ja209829M  1
2011 Wang Q, Christiansen A, Samiotakis A, Wittung-Stafshede P, Cheung MS. Comparison of chemical and thermal protein denaturation by combination of computational and experimental approaches. II. The Journal of Chemical Physics. 135: 175102. PMID 22070324 DOI: 10.1016/J.Bpj.2011.11.2510  1
2011 Wittung-Stafshede P. Protein folding inside the cell. Biophysical Journal. 101: 265-6. PMID 21767477 DOI: 10.1016/J.Bpj.2011.06.018  1
2011 Palm ME, Weise CF, Lundin C, Wingsle G, Nygren Y, Björn E, Naredi P, Wolf-Watz M, Wittung-Stafshede P. Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro. Proceedings of the National Academy of Sciences of the United States of America. 108: 6951-6. PMID 21482801 DOI: 10.1073/Pnas.1012899108  1
2011 Aguilar X, F Weise C, Sparrman T, Wolf-Watz M, Wittung-Stafshede P. Macromolecular crowding extended to a heptameric system: the Co-chaperonin protein 10. Biochemistry. 50: 3034-44. PMID 21375247 DOI: 10.1021/Bi2002086  1
2011 Stagg L, Christiansen A, Wittung-Stafshede P. Macromolecular crowding tunes folding landscape of parallel α/β protein, apoflavodoxin. Journal of the American Chemical Society. 133: 646-8. PMID 21175168 DOI: 10.1021/Ja107638E  1
2010 Miller C, Davlieva M, Wilson C, White KI, Couñago R, Wu G, Myers JC, Wittung-Stafshede P, Shamoo Y. Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability. Biophysical Journal. 99: 887-96. PMID 20682267 DOI: 10.1016/J.Bpj.2010.04.076  1
2010 Christiansen A, Wang Q, Samiotakis A, Cheung MS, Wittung-Stafshede P. Factors defining effects of macromolecular crowding on protein stability: an in vitro/in silico case study using cytochrome c. Biochemistry. 49: 6519-30. PMID 20593812 DOI: 10.1016/J.Bpj.2010.12.2354  1
2010 Rodriguez-Granillo A, Crespo A, Estrin DA, Wittung-Stafshede P. Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of Wilson disease protein. The Journal of Physical Chemistry. B. 114: 3698-706. PMID 20166696 DOI: 10.1021/Jp911208Z  1
2010 Rodriguez-Granillo A, Crespo A, Wittung-Stafshede P. Interdomain interactions modulate collective dynamics of the metal-binding domains in the Wilson disease protein. The Journal of Physical Chemistry. B. 114: 1836-48. PMID 20078131 DOI: 10.1021/Jp909450X  1
2010 Pozdnyakova I, Wittung-Stafshede P. Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase. Biochimica Et Biophysica Acta. 1804: 740-4. PMID 19932772 DOI: 10.1016/J.Bbapap.2009.11.013  1
2010 Stagg L, Samiotakis A, Homouz D, Cheung MS, Wittung-Stafshede P. Residue-specific analysis of frustration in the folding landscape of repeat beta/alpha protein apoflavodoxin. Journal of Molecular Biology. 396: 75-89. PMID 19913555 DOI: 10.1016/J.Jmb.2009.11.008  1
2009 Shaikhibrahim Z, Rahaman H, Wittung-Stafshede P, Björklund S. Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation. Proceedings of the National Academy of Sciences of the United States of America. 106: 20728-33. PMID 19934057 DOI: 10.1073/Pnas.0907645106  1
2009 Neumann O, Zhang D, Tam F, Lal S, Wittung-Stafshede P, Halas NJ. Direct optical detection of aptamer conformational changes induced by target molecules. Analytical Chemistry. 81: 10002-6. PMID 19928834 DOI: 10.1021/Ac901849K  1
2009 Hussain F, Rodriguez-Granillo A, Wittung-Stafshede P. Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain. Journal of the American Chemical Society. 131: 16371-3. PMID 19863064 DOI: 10.1021/Ja9058266  1
2009 Guelker M, Stagg L, Wittung-Stafshede P, Shamoo Y. Pseudosymmetry, high copy number and twinning complicate the structure determination of Desulfovibrio desulfuricans (ATCC 29577) flavodoxin. Acta Crystallographica. Section D, Biological Crystallography. 65: 523-34. PMID 19465766 DOI: 10.1107/S0907444909010075  1
2009 Rodriguez-Granillo A, Crespo A, Wittung-Stafshede P. Conformational dynamics of metal-binding domains in Wilson disease protein: molecular insights into selective copper transfer. Biochemistry. 48: 5849-63. PMID 19449859 DOI: 10.1021/Bi900235G  1
2009 Samiotakis A, Wittung-Stafshede P, Cheung MS. Folding, stability and shape of proteins in crowded environments: experimental and computational approaches. International Journal of Molecular Sciences. 10: 572-88. PMID 19333422 DOI: 10.3390/Ijms10020572  1
2009 Zhang D, Neumann O, Wang H, Yuwono VM, Barhoumi A, Perham M, Hartgerink JD, Wittung-Stafshede P, Halas NJ. Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH. Nano Letters. 9: 666-71. PMID 19199758 DOI: 10.1021/Nl803054H  1
2009 Rodriguez-Granillo A, Wittung-Stafshede P. Tuning of copper-loop flexibility in Bacillus subtilis CopZ copper chaperone: role of conserved residues. The Journal of Physical Chemistry. B. 113: 1919-32. PMID 19170606 DOI: 10.1021/Jp807594Q  1
2009 Homouz D, Stagg L, Wittung-Stafshede P, Cheung MS. Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin. Biophysical Journal. 96: 671-80. PMID 19167312 DOI: 10.1016/J.Bpj.2008.10.014  1
2009 Rodriguez-Granillo A, Wittung-Stafshede P. Differential roles of Met10, Thr11, and Lys60 in structural dynamics of human copper chaperone Atox1. Biochemistry. 48: 960-72. PMID 19146392 DOI: 10.1021/Bi8018652  1
2009 Chen M, Dousis AD, Wu Y, Wittung-Stafshede P, Ma J. Predicting protein folding cores by empirical potential functions. Archives of Biochemistry and Biophysics. 483: 16-22. PMID 19135974 DOI: 10.1016/J.Abb.2008.12.011  1
2008 Sedlák E, Ziegler L, Kosman DJ, Wittung-Stafshede P. In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site. Proceedings of the National Academy of Sciences of the United States of America. 105: 19258-63. PMID 19033465 DOI: 10.1073/Pnas.0806431105  1
2008 Sedlák E, Stagg L, Wittung-Stafshede P. Effect of Hofmeister ions on protein thermal stability: roles of ion hydration and peptide groups? Archives of Biochemistry and Biophysics. 479: 69-73. PMID 18782555 DOI: 10.1016/J.Abb.2008.08.013  1
2008 Homouz D, Perham M, Samiotakis A, Cheung MS, Wittung-Stafshede P. Crowded, cell-like environment induces shape changes in aspherical protein. Proceedings of the National Academy of Sciences of the United States of America. 105: 11754-9. PMID 18697933 DOI: 10.1073/Pnas.0803672105  1
2008 Rodriguez-Granillo A, Sedlak E, Wittung-Stafshede P. Stability and ATP binding of the nucleotide-binding domain of the Wilson disease protein: effect of the common H1069Q mutation. Journal of Molecular Biology. 383: 1097-111. PMID 18692069 DOI: 10.1016/J.Jmb.2008.07.065  1
2008 Hussain F, Olson JS, Wittung-Stafshede P. Conserved residues modulate copper release in human copper chaperone Atox1. Proceedings of the National Academy of Sciences of the United States of America. 105: 11158-63. PMID 18685091 DOI: 10.1073/Pnas.0802928105  1
2008 Guu TS, Dong L, Wittung-Stafshede P, Tao YJ. Mapping the domain structure of the influenza A virus polymerase acidic protein (PA) and its interaction with the basic protein 1 (PB1) subunit. Virology. 379: 135-42. PMID 18657841 DOI: 10.1016/J.Virol.2008.06.022  1
2008 Chen DH, Luke K, Zhang J, Chiu W, Wittung-Stafshede P. Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques. Journal of Molecular Biology. 381: 707-17. PMID 18588898 DOI: 10.1016/J.Jmb.2008.06.021  1
2008 Rodriguez-Granillo A, Wittung-Stafshede P. Structure and dynamics of Cu(I) binding in copper chaperones Atox1 and CopZ: a computer simulation study. The Journal of Physical Chemistry. B. 112: 4583-93. PMID 18361527 DOI: 10.1021/Jp711787X  1
2008 Sedlák E, Stagg L, Wittung-Stafshede P. Role of cations in stability of acidic protein Desulfovibrio desulfuricans apoflavodoxin. Archives of Biochemistry and Biophysics. 474: 128-35. PMID 18342618 DOI: 10.1016/J.Abb.2008.02.037  1
2008 Couñago R, Wilson CJ, Peña MI, Wittung-Stafshede P, Shamoo Y. An adaptive mutation in adenylate kinase that increases organismal fitness is linked to stability-activity trade-offs. Protein Engineering, Design & Selection : Peds. 21: 19-27. PMID 18093993 DOI: 10.1093/Protein/Gzm072  1
2008 Sedlák E, Zoldák G, Wittung-Stafshede P. Role of copper in thermal stability of human ceruloplasmin. Biophysical Journal. 94: 1384-91. PMID 17965133 DOI: 10.1529/Biophysj.107.113696  1
2008 Wittung-Stafshede P. Response to Harve et al: Effects on protein folding speed and shape despite possible size changes in Ficoll 70 Proceedings of the National Academy of Sciences of the United States of America. 105. DOI: 10.1073/Pnas.0810638106  1
2007 Stagg L, Zhang SQ, Cheung MS, Wittung-Stafshede P. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin. Proceedings of the National Academy of Sciences of the United States of America. 104: 18976-81. PMID 18024596 DOI: 10.1073/Pnas.0705127104  1
2007 Perham M, Stagg L, Wittung-Stafshede P. Macromolecular crowding increases structural content of folded proteins. Febs Letters. 581: 5065-9. PMID 17919600 DOI: 10.1016/J.Febslet.2007.09.049  1
2007 Hussain F, Sedlak E, Wittung-Stafshede P. Role of copper in folding and stability of cupredoxin-like copper-carrier protein CopC. Archives of Biochemistry and Biophysics. 467: 58-66. PMID 17889826 DOI: 10.1016/J.Abb.2007.08.014  1
2007 Hussain F, Wittung-Stafshede P. Impact of cofactor on stability of bacterial (CopZ) and human (Atox1) copper chaperones. Biochimica Et Biophysica Acta. 1774: 1316-22. PMID 17881304 DOI: 10.1016/J.Bbapap.2007.07.020  1
2007 Luke KA, Higgins CL, Wittung-Stafshede P. Thermodynamic stability and folding of proteins from hyperthermophilic organisms. The Febs Journal. 274: 4023-33. PMID 17683332 DOI: 10.1111/J.1742-4658.2007.05955.X  1
2007 Sedlak E, Wittung-Stafshede P. Discrete roles of copper ions in chemical unfolding of human ceruloplasmin. Biochemistry. 46: 9638-44. PMID 17661447 DOI: 10.1021/bi700715e  1
2007 Perham M, Wittung-Stafshede P. Folding and assembly of co-chaperonin heptamer probed by forster resonance energy transfer. Archives of Biochemistry and Biophysics. 464: 306-13. PMID 17521602 DOI: 10.1016/J.Abb.2007.04.020  1
2007 Zong C, Wilson CJ, Shen T, Wittung-Stafshede P, Mayo SL, Wolynes PG. Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin. Proceedings of the National Academy of Sciences of the United States of America. 104: 3159-64. PMID 17301232 DOI: 10.1073/Pnas.0611149104  1
2006 Luke K, Wittung-Stafshede P. Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability. Archives of Biochemistry and Biophysics. 456: 8-18. PMID 17084377 DOI: 10.1016/J.Abb.2006.10.003  1
2006 Luke K, Perham M, Wittung-Stafshede P. Kinetic folding and assembly mechanisms differ for two homologous heptamers. Journal of Molecular Biology. 363: 729-42. PMID 16979655 DOI: 10.1016/J.Jmb.2006.08.058  1
2006 Chen M, Wilson CJ, Wu Y, Wittung-Stafshede P, Ma J. Correlation between protein stability cores and protein folding kinetics: a case study on Pseudomonas aeruginosa apo-azurin. Structure (London, England : 1993). 14: 1401-10. PMID 16962971 DOI: 10.1016/J.Str.2006.07.007  1
2006 Perham M, Liao J, Wittung-Stafshede P. Differential effects of alcohols on conformational switchovers in alpha-helical and beta-sheet protein models. Biochemistry. 45: 7740-9. PMID 16784225 DOI: 10.1021/Bi060464V  1
2006 Muralidhara BK, Rathinakumar R, Wittung-Stafshede P. Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting. Archives of Biochemistry and Biophysics. 451: 51-8. PMID 16730634 DOI: 10.1016/J.Abb.2006.03.032  1
2006 Zong C, Wilson CJ, Shen T, Wolynes PG, Wittung-Stafshede P. Phi-value analysis of apo-azurin folding: comparison between experiment and theory. Biochemistry. 45: 6458-66. PMID 16700556 DOI: 10.1021/Bi060025W  1
2006 Wilson CJ, Apiyo D, Wittung-Stafshede P. Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal: Solvation of azurin's folding nucleus. Protein Science : a Publication of the Protein Society. 15: 843-52. PMID 16522792 DOI: 10.1110/Ps.051838206  1
2006 de los Rios MA, Muralidhara BK, Wildes D, Sosnick TR, Marqusee S, Wittung-Stafshede P, Plaxco KW, Ruczinski I. On the precision of experimentally determined protein folding rates and phi-values. Protein Science : a Publication of the Protein Society. 15: 553-63. PMID 16501226 DOI: 10.1110/Ps.051870506  1
2005 Perham M, Chen M, Ma J, Wittung-Stafshede P. Unfolding of heptameric co-chaperonin protein follows "fly casting" mechanism: observation of transient nonnative heptamer. Journal of the American Chemical Society. 127: 16402-3. PMID 16305220 DOI: 10.1021/Ja055574O  1
2005 Luke K, Apiyo D, Wittung-Stafshede P. Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10. Biochemistry. 44: 14385-95. PMID 16262239 DOI: 10.1021/Bi051131L  1
2005 Wilson CJ, Das P, Clementi C, Matthews KS, Wittung-Stafshede P. The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates. Proceedings of the National Academy of Sciences of the United States of America. 102: 14563-8. PMID 16203983 DOI: 10.1073/Pnas.0505808102  1
2005 Das P, Wilson CJ, Fossati G, Wittung-Stafshede P, Matthews KS, Clementi C. Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment. Proceedings of the National Academy of Sciences of the United States of America. 102: 14569-74. PMID 16203982 DOI: 10.1073/Pnas.0505844102  1
2005 Luke K, Apiyo D, Wittung-Stafshede P. Dissecting homo-heptamer thermodynamics by isothermal titration calorimetry: entropy-driven assembly of co-chaperonin protein 10. Biophysical Journal. 89: 3332-6. PMID 16100270 DOI: 10.1529/Biophysj.105.067223  1
2005 Wilson CJ, Wittung-Stafshede P. Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin. Biochemistry. 44: 10054-62. PMID 16042382 DOI: 10.1021/Bi050342N  1
2005 Brown C, Liao J, Wittung-Stafshede P. Interface mutation in heptameric co-chaperonin protein 10 destabilizes subunits but not interfaces. Archives of Biochemistry and Biophysics. 439: 175-83. PMID 15978542 DOI: 10.1016/J.Abb.2005.05.019  1
2005 Apiyo D, Wittung-Stafshede P. Unique complex between bacterial azurin and tumor-suppressor protein p53. Biochemical and Biophysical Research Communications. 332: 965-8. PMID 15913547 DOI: 10.1016/J.Bbrc.2005.05.038  1
2005 Muralidhara BK, Chen M, Ma J, Wittung-Stafshede P. Effect of inorganic phosphate on FMN binding and loop flexibility in Desulfovibrio desulfuricans apo-flavodoxin. Journal of Molecular Biology. 349: 87-97. PMID 15876370 DOI: 10.1016/J.Jmb.2005.03.054  0.48
2005 Wilson CJ, Wittung-Stafshede P. Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin. Proceedings of the National Academy of Sciences of the United States of America. 102: 3984-7. PMID 15753320 DOI: 10.1073/Pnas.0501038102  1
2005 Higgins CL, Muralidhara BK, Wittung-Stafshede P. How do cofactors modulate protein folding? Protein and Peptide Letters. 12: 165-70. PMID 15723643 DOI: 10.2174/0929866053005782  1
2005 Muralidhara BK, Wittung-Stafshede P. FMN binding and unfolding of Desulfovibrio desulfuricans flavodoxin: "hidden" intermediates at low denaturant concentrations. Biochimica Et Biophysica Acta. 1747: 239-50. PMID 15698959 DOI: 10.1016/J.Bbapap.2004.11.012  1
2005 Maxwell KL, Wildes D, Zarrine-Afsar A, De Los Rios MA, Brown AG, Friel CT, Hedberg L, Horng JC, Bona D, Miller EJ, Vallée-Bélisle A, Main ER, Bemporad F, Qiu L, Teilum K, ... ... Wittung-Stafshede P, et al. Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Science : a Publication of the Protein Society. 14: 602-16. PMID 15689503 DOI: 10.1110/Ps.041205405  1
2004 Wilson CJ, Apiyo D, Wittung-Stafshede P. Role of cofactors in metalloprotein folding. Quarterly Reviews of Biophysics. 37: 285-314. PMID 16194296 DOI: 10.1017/S003358350500404X  1
2004 Wittung-Stafshede P. Role of cofactors in folding of the blue-copper protein azurin. Inorganic Chemistry. 43: 7926-33. PMID 15578826 DOI: 10.1021/Ic049398G  1
2004 Muralidhara BK, Wittung-Stafshede P. Thermal unfolding of Apo and Holo Desulfovibrio desulfuricans flavodoxin: cofactor stabilizes folded and intermediate states. Biochemistry. 43: 12855-64. PMID 15461458 DOI: 10.1021/Bi048944E  1
2004 Wittung-Stafshede P. Slow unfolding explains high stability of thermostable ferredoxins: common mechanism governing thermostability? Biochimica Et Biophysica Acta. 1700: 1-4. PMID 15210118 DOI: 10.1016/J.Bbapap.2004.04.002  1
2004 Higgins CL, Wittung-Stafshede P. Formation of linear three-iron clusters in Aquifex aeolicus two-iron ferredoxins: effect of protein-unfolding speed. Archives of Biochemistry and Biophysics. 427: 154-63. PMID 15196989 DOI: 10.1016/J.Abb.2004.04.026  1
2004 Bascos N, Guidry J, Wittung-Stafshede P. Monomer topology defines folding speed of heptamer. Protein Science : a Publication of the Protein Society. 13: 1317-21. PMID 15075408 DOI: 10.1110/Ps.03559504  1
2004 Guidry J, Wittung-Stafshede P. First characterization of co-chaperonin protein 10 from hyper-thermophilic Aquifex aeolicus. Biochemical and Biophysical Research Communications. 317: 176-80. PMID 15047164 DOI: 10.1016/J.Bbrc.2004.03.025  1
2004 Marks J, Pozdnyakova I, Guidry J, Wittung-Stafshede P. Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin Journal of Biological Inorganic Chemistry. 9: 281-288. PMID 14758526 DOI: 10.1007/S00775-004-0523-6  1
2003 Griffin S, Higgins CL, Soulimane T, Wittung-Stafshede P. High thermal and chemical stability of Thermus thermophilus seven-iron ferredoxin. Linear clusters form at high pH on polypeptide unfolding. European Journal of Biochemistry / Febs. 270: 4736-43. PMID 14622262 DOI: 10.1046/J.1432-1033.2003.03873.X  1
2003 Muralidhara BK, Wittung-Stafshede P. Can Cofactor-Binding Sites in Proteins Be Flexible? Desulfovibrio desulfuricans Flavodoxin Binds FMN Dimer Biochemistry. 42: 13074-13080. PMID 14596623 DOI: 10.1021/Bi035073K  1
2003 Pozdnyakova I, Wittung-Stafshede P. Approaching the speed limit for Greek Key β-barrel formation: Transition-state movement tunes folding rate of zinc-substituted azurin Biochimica Et Biophysica Acta - Proteins and Proteomics. 1651: 1-4. PMID 14499583 DOI: 10.1016/S1570-9639(03)00240-1  1
2003 Jones K, Wittung-Stafshede P. The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation Journal of the American Chemical Society. 125: 9606-9607. PMID 12904024 DOI: 10.1021/Ja0358807  1
2003 Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ. The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochemistry. 42: 4937-44. PMID 12718535 DOI: 10.1021/Bi027333O  1
2003 Smith J, Guidry J, Wittung-Stafshede P. Novel "three-in-one" peptide device for genetic drug delivery Protein and Peptide Letters. 10: 1-7. PMID 12625820 DOI: 10.2174/0929866033408291  1
2003 Mitou G, Higgins C, Wittung-Stafshede P, Conover RC, Smith AD, Johnson MK, Gaillard J, Stubna A, Münck E, Meyer J. An Isc-type extremely thermostable [2Fe-2S] ferredoxin from Aquifex aeolicus. Biochemical, spectroscopic, and unfolding studies. Biochemistry. 42: 1354-64. PMID 12564939 DOI: 10.1021/Bi027116N  1
2002 Higgins CL, Meyer J, Wittung-Stafshede P. Exceptional stability of a [2Fe-2S] ferredoxin from hyperthermophilic bacterium Aquifex aeolicus. Biochimica Et Biophysica Acta. 1599: 82-9. PMID 12479408 DOI: 10.1016/S1570-9639(02)00405-3  1
2002 Pereira MM, Jones KL, Campos MG, Melo AMP, Saraiva LM, Louro RO, Wittung-Stafshede P, Teixeira M. A ferredoxin from the thermohalophilic bacterium Rhodothermus marinus Biochimica Et Biophysica Acta - Proteins and Proteomics. 1601: 1-8. PMID 12429497 DOI: 10.1016/S1570-9639(02)00406-5  1
2002 Pozdnyakova I, Wittung-Stafshede P. If space is provided, bulky modification on the rim of Azurin's β-barrel results in folded protein Febs Letters. 531: 209-214. PMID 12417314 DOI: 10.1016/S0014-5793(02)03505-6  1
2002 Guidry JJ, Wittung-Stafshede P. Low stability for monomeric human chaperonin protein 10: Interprotein interactions contribute majority of oligomer stability Archives of Biochemistry and Biophysics. 405: 280-282. PMID 12220543 DOI: 10.1016/S0003-9861(02)00406-X  1
2002 Griffin S, Vitello A, Wittung-Stafshede P. Buried water molecules contribute to cytochrome f stability Archives of Biochemistry and Biophysics. 404: 335-337. PMID 12147273 DOI: 10.1016/S0003-9861(02)00333-8  1
2002 Sabahi A, Wittung-Stafshede P. Unfolding the unique c-type heme protein, Chlamydomonas reinhardtii cytochrome f Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1596: 163-171. PMID 11983431 DOI: 10.1016/S0167-4838(02)00214-5  1
2002 Apiyo D, Wittung-Stafshede P. Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin Protein Science. 11: 1129-1135. PMID 11967369 DOI: 10.1110/Ps.3840102  1
2002 Pozdnyakova I, Guidry J, Wittung-Stafshede P. Studies of Pseudomonas aeruginosa azurin mutants: Cavities in β-barrel do not affect refolding speed Biophysical Journal. 82: 2645-2651. PMID 11964251 DOI: 10.1016/S0006-3495(02)75606-3  1
2002 Jones K, Gomes CM, Huber H, Teixeira M, Wittung-Stafshede P. Formation of a linear [3Fe-4S] cluster in a seven-iron ferredoxin triggered by polypeptide unfolding Journal of Biological Inorganic Chemistry. 7: 357-362. PMID 11941493 DOI: 10.1007/S00775-001-0304-4  1
2002 Meyer J, Clay MD, Johnson MK, Stubna A, Münck E, Higgins C, Wittung-Stafshede P. A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond. Biochemistry. 41: 3096-108. PMID 11863449 DOI: 10.1021/Bi015981M  1
2002 Wittung-Stafshede P. Role of cofactors in protein folding Accounts of Chemical Research. 35: 201-208. DOI: 10.1021/Ar010106E  1
2001 Jones K, Guidry J, Wittung-Stafshede P. Characterization of surface antigen from Lyme disease spirochete Borrelia burgdorferi Biochemical and Biophysical Research Communications. 289: 389-394. PMID 11716485 DOI: 10.1006/Bbrc.2001.5983  1
2001 Pozdnyakova I, Wittung-Stafshede P. Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin Biochemistry. 40: 13728-13733. PMID 11695922 DOI: 10.1021/Bi011591O  1
2001 Pozdnyakova I, Wittung-Stafshede P. Biological relevance of metal binding before protein folding [19] Journal of the American Chemical Society. 123: 10135-10136. PMID 11592908 DOI: 10.1021/Ja016252X  1
2001 Moczygemba C, Guidry J, Jones KL, Gomes CM, Teixeira M, Wittung-Stafshede P. High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: Involvement of electrostatic interactions and cofactors Protein Science. 10: 1539-1548. PMID 11468351 DOI: 10.1110/Ps.49401  1
2001 Griffin S, Guidry J, Wittung-Stafshede P. The rate of formation of cytochrome c553 is not dependent on the nature of the unfolded state Archives of Biochemistry and Biophysics. 389: 150-152. PMID 11370667 DOI: 10.1006/Abbi.2001.2326  1
2001 Pozdnyakova I, Guidry J, Wittung-Stafshede P. Copper stabilizes azurin by decreasing the unfolding rate Archives of Biochemistry and Biophysics. 390: 146-148. PMID 11368526 DOI: 10.1006/Abbi.2000.2369  1
2001 Sabahi A, Guidry J, Inamati GB, Manoharan M, Wittung-Stafshede P. Hybridization of 2′-ribose modified mixed-sequence oligonucleotides: Thermodynamic and kinetic studies Nucleic Acids Research. 29: 2163-2170. PMID 11353086 DOI: 10.1093/Nar/29.10.2163  1
2001 Apiyo D, Jones K, Guidry J, Wittung-Stafshede P. Equilibrium unfolding of dimeric desulfoferrodoxin involves a monomeric intermediate: Iron cofactors dissociate after polypeptide unfolding Biochemistry. 40: 4940-4948. PMID 11305909 DOI: 10.1021/Bi002653Y  1
2001 Pozdnyakova I, Guidry J, Wittung-Stafshede P. Probing copper ligands in denatured Pseudomonas aeruginosa azurin: Unfolding His117Gly and His46Gly mutants Journal of Biological Inorganic Chemistry. 6: 182-188. PMID 11293412 DOI: 10.1007/S007750000189  1
2000 Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Protein Science : a Publication of the Protein Society. 9: 2109-17. PMID 11152122 DOI: 10.1110/Ps.9.11.2109  1
2000 Guidry J, Wittung-Stafshede P. Cytochrome c553, a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics Journal of Molecular Biology. 301: 769-773. PMID 10966783 DOI: 10.1006/Jmbi.2000.3993  1
2000 Guidry J, Wittung-Stafshede P. Stability determines formation rate of four-helix-bundle protein Archives of Biochemistry and Biophysics. 378: 190-191. PMID 10871060 DOI: 10.1006/Abbi.2000.1814  1
2000 Apiyo D, Guidry J, Wittung-Stafshede P. No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1479: 214-224. PMID 10862971 DOI: 10.1016/S0167-4838(00)00032-7  1
2000 Moczygemba C, Guidry J, Wittung-Stafshede P. Heme orientation affects holo-myoglobin folding and unfolding kinetics Febs Letters. 470: 203-206. PMID 10734234 DOI: 10.1016/S0014-5793(00)01319-3  1
2000 Wittung-Stafshede P, Gomes CM, Teixeira M. Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens Journal of Inorganic Biochemistry. 78: 35-41. PMID 10714703 DOI: 10.1016/S0162-0134(99)00202-0  1
2000 Pozdnyakova I, Guidry J, Wittung-Stafshede P. Copper-triggered β-hairpin formation initiation site for azurin folding? [26] Journal of the American Chemical Society. 122: 6337-6338. DOI: 10.1021/Ja0011010  1
2000 Wittung-Stafshede P, Rodahl M, Kasemo B, Nielsen P, Norden B. Detection of point mutations in DNA by PNA-based quartz-crystal biosensor Colloids and Surfaces a: Physicochemical and Engineering Aspects. 174: 269-273. DOI: 10.1016/S0927-7757(00)00537-9  1
2000 DeBeer S, Wittung-Stafshede P, Leckner J, Karlsson G, Winkler JR, Gray HB, Malmström BG, Solomon EI, Hedman B, Hodgson KO. X-ray absorption spectroscopy of folded and unfolded copper(I) azurin Inorganica Chimica Acta. 297: 278-282. DOI: 10.1016/S0020-1693(99)00315-1  1
1999 Ardhammar M, Nordén B, Nielsen PE, Malmström BG, Wittung-Stafshede P. In vitro membrane penetration of modified peptide nucleic acid (PNA). Journal of Biomolecular Structure & Dynamics. 17: 33-40. PMID 10496419 DOI: 10.1080/07391102.1999.10508338  1
1999 Wittung-Stafshede P. Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris Protein Science. 8: 1523-1529. PMID 10422842 DOI: 10.1110/Ps.8.7.1523  1
1999 Wittung-Stafshede P. Effect of redox state on unfolding energetics of heme proteins Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1432: 401-405. PMID 10407162 DOI: 10.1016/S0167-4838(99)00116-8  1
1999 Wittung-Stafshede P, Lee JC, Winkler JR, Gray HB. Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a four-helix-bundle protein. Proceedings of the National Academy of Sciences of the United States of America. 96: 6587-90. PMID 10359755 DOI: 10.1073/Pnas.96.12.6587  1
1999 Selmane T, Wittung-Stafshede P, Maraboeuf F, Voloshin ON, Nordén B, Camerini-Otero DR, Takahashi M. The L2 loop peptide of RecA stiffens and restricts base motions of single-stranded DNA similar to the intact protein Febs Letters. 446: 30-34. PMID 10100609 DOI: 10.1016/S0014-5793(99)00181-7  1
1999 Chen E, Wittung-Stafshede P, Kliger DS. Far-UV time-resolved circular dichroism detection of electron-transfer- triggered cytochrome c folding Journal of the American Chemical Society. 121: 3811-3817. DOI: 10.1021/Ja983169+  1
1999 Malmström BG, Wittung-Stafshede P. Effects of protein folding on metalloprotein redox-active sites: Electron-transfer properties of blue and purple copper proteins Coordination Chemistry Reviews. 185: 127-140. DOI: 10.1016/S0010-8545(98)00257-4  1
1999 Chen E, Wittung-Stafshede P, Kliger DS. Far-UV time-resolved circular dichroism detection of electron-transfer-triggered cytochrome c folding Journal of the American Chemical Society. 121: X.  1
1998 Wittung-Stafshede P, Gomez E, Ohman A, Aasa R, Villahermosa RM, Leckner J, Karlsson BG, Sanders D, Fee JA, Winkler JR, Malmström BG, Gray HB, Hill MG. High-potential states of blue and purple copper proteins. Biochimica Et Biophysica Acta. 1388: 437-43. PMID 9858778 DOI: 10.1016/S0167-4838(98)00205-2  1
1998 Wittung-Stafshede P. Genetic medicine - When will it come to the drugstore? Science. 281: 657-658. PMID 9714674 DOI: 10.1126/Science.281.5377.657  1
1998 Nordén B, Wittung-Stafshede P, Ellouze C, Kim HK, Mortensen K, Takahashi M. Base orientation of second DNA in recA-DNA filaments: Analysis by combination of linear dichroism and small angle neutron scattering in flow- oriented solution Journal of Biological Chemistry. 273: 15682-15686. PMID 9624163 DOI: 10.1074/Jbc.273.25.15682  1
1998 Wittung-Stafshede P. A stable, molten-globule-like cytochrome c Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1382: 324-332. PMID 9540804 DOI: 10.1016/S0167-4838(97)00176-3  1
1998 Wittung-Stafshede P, Malmstrom BG, Sanders D, Fee JA, Winkler JR, Gray HB. Effect of redox state on the folding free energy of a thermostable electron-transfer metalloprotein: the CuA domain of cytochrome oxidase from Thermus thermophilus. Biochemistry. 37: 3172-7. PMID 9485471 DOI: 10.1021/Bi972901Z  1
1998 Wittung-Stafshede P, Malmström BG, Winkler JR, Gray HB. Folding of deoxymyoglobin triggered by electron transfer Journal of Physical Chemistry A. 102: 5599-5601. DOI: 10.1021/Jp9802228  1
1998 Wittung-Stafshede P, Hill MG, Gomez E, Di Bilio AJ, Karlsson BG, Leckner J, Winkler JR, Gray HB, Malmström BG. Reduction potentials of blue and purple copper proteins in their unfolded states: A closer look at rack-induced coordination Journal of Biological Inorganic Chemistry. 3: 367-370. DOI: 10.1007/S007750050246  1
1997 Leckner J, Bonander N, Wittung-Stafshede P, Malmström BG, Karlsson BG. The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc and apoprotein. Biochimica Et Biophysica Acta. 1342: 19-27. PMID 9366266 DOI: 10.1016/S0167-4838(97)00074-5  1
1997 Wittung P, Nielsen P, Nordén B. Extended DNA-recognition repertoire of peptide nucleic acid (PNA): PNA-dsDNA triplex formed with cytosine-rich homopyrimidine PNA. Biochemistry. 36: 7973-9. PMID 9201944 DOI: 10.1021/Bi963136B  0.4
1997 Wittung P, Ellouze C, Maraboeuf F, Takahashi M, Nordèn B. Thermochemical and kinetic evidence for nucleotide-sequence-dependent RecA-DNA interactions. European Journal of Biochemistry. 245: 715-9. PMID 9183010 DOI: 10.1111/J.1432-1033.1997.00715.X  0.4
1997 Winkler JR, Wittung-Stafshede P, Leckner J, Malmström BG, Gray HB. Effects of folding on metalloprotein active sites. Proceedings of the National Academy of Sciences of the United States of America. 94: 4246-9. PMID 9113974 DOI: 10.1073/Pnas.94.9.4246  1
1997 Wittung-Stafshede P, Gray HB, Winkler JR. Rapid formation of a four-helix bundle. Cytochrome b562 folding triggered by electron transfer Journal of the American Chemical Society. 119: 9562-9563. DOI: 10.1021/Ja971855N  1
1997 Wittung-Stafshede P, Wilkler JR, Gray HB. Rapid folding of a four-helix-bundle protein Faseb Journal. 11.  1
1996 Wittung P, Bazemore LR, Takahashi M, Nordén B, Radding C. Second-site RecA-DNA interactions: lack of identical recognition. Biochemistry. 35: 15349-55. PMID 8952486 DOI: 10.1021/Bi961755E  0.32
1995 Wittung P, Nordén B, Takahashi M. Secondary structure of RecA in solution. The effects of cofactor, DNA and ionic conditions. European Journal of Biochemistry. 228: 149-54. PMID 7882996 DOI: 10.1111/J.1432-1033.1995.0149O.X  0.48
1995 Wittung P, Kajanus J, Edwards K, Nielsen P, Nordén B, Malmström BG. Phospholipid membrane permeability of peptide nucleic acid. Febs Letters. 365: 27-9. PMID 7774709 DOI: 10.1016/0014-5793(95)00409-3  0.12
1995 Wittung P, Funk M, Jernström B, Nordén B, Takahashi M. Fluorescence-detected interactions of oligonucleotides in RecA complexes. Febs Letters. 368: 64-8. PMID 7615090 DOI: 10.1016/0014-5793(95)00600-E  0.24
1995 Ellouze C, Takahashi M, Wittung P, Mortensen K, Schnarr M, Nordén B. Evidence for elongation of the helical pitch of the RecA filament upon ATP and ADP binding using small-angle neutron scattering. European Journal of Biochemistry. 233: 579-83. PMID 7588804 DOI: 10.1111/J.1432-1033.1995.579_2.X  0.16
1995 Wittung P, Kajanus J, Edwards K, Haaima G, Nielsen PE, Nordén B, Malmström BG. Phospholipid membrane permeability of peptide nucleic acid. Febs Letters. 375: 27-9. PMID 7498515 DOI: 10.1016/0014-5793(95)00409-3  0.36
1994 Wittung P, Nielsen PE, Buchardt O, Egholm M, Nordén B. DNA-like double helix formed by peptide nucleic acid. Nature. 368: 561-3. PMID 8139692 DOI: 10.1038/368561A0  0.24
1994 Wittung P, Nordén B, Kim SK, Takahashi M. Interactions between DNA molecules bound to RecA filament. Effects of base complementarity. The Journal of Biological Chemistry. 269: 5799-803. PMID 8119921  0.24
1994 Wittung P, Nordén B, Takahashi M. Spectroscopic observation of renaturation between polynucleotides with RecA in the presence of ATP hydrolysis. European Journal of Biochemistry. 224: 39-45. PMID 8076649 DOI: 10.1111/J.1432-1033.1994.Tb19992.X  0.36
1994 Wittung P, Kim SK, Buchardt O, Nielsen P, Nordèn B. Interactions of DNA binding ligands with PNA-DNA hybrids. Nucleic Acids Research. 22: 5371-7. PMID 7816628 DOI: 10.1093/Nar/22.24.5371  0.32
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