| Year |
Citation |
Score |
| 2021 |
Werner TER, Horvath I, Wittung-Stafshede P. Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein. Qrb Discovery. 2: e2. PMID 37529678 DOI: 10.1017/qrd.2020.17 |
0.313 |
|
| 2021 |
Rocha S, Kumar R, Nordén B, Wittung-Stafshede P. Orientation of α-Synuclein at Negatively Charged Lipid Vesicles: Linear Dichroism Reveals Time-Dependent Changes in Helix Binding Mode. Journal of the American Chemical Society. PMID 34748321 DOI: 10.1021/jacs.1c05344 |
0.452 |
|
| 2021 |
Zegarra FC, Homouz D, Wittung-Stafshede P, Cheung MS. The Zero-Order Loop in Apoazurin Modulates Folding Mechanism In Silico. The Journal of Physical Chemistry. B. PMID 33818090 DOI: 10.1021/acs.jpcb.1c00219 |
0.333 |
|
| 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 |
0.321 |
|
| 2020 |
Lorentzon E, Kumar R, Horvath I, Wittung-Stafshede P. Differential effects of Cu and Fe ions on in vitro amyloid formation of biologically-relevant α-synuclein variants. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 32170541 DOI: 10.1007/S10534-020-00234-4 |
0.335 |
|
| 2020 |
Sampson TR, Challis C, Jain N, Moiseyenko A, Ladinsky MS, Shastri GG, Thron T, Needham BD, Horvath I, Debelius JW, Janssen S, Knight R, Wittung-Stafshede P, Gradinaru V, Chapman M, et al. A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice. Elife. 9. PMID 32043464 DOI: 10.7554/Elife.53111 |
0.315 |
|
| 2020 |
Zhang X, Wesén E, Kumar R, Bernson D, Gallud A, Paul A, Wittung-Stafshede P, Esbjörner EK. Correlation between cellular uptake and cytotoxicity of fragmented α-synuclein amyloid fibrils suggests intracellular basis for toxicity. Acs Chemical Neuroscience. PMID 31894960 DOI: 10.1021/Acschemneuro.9B00562 |
0.31 |
|
| 2019 |
Horvath I, Blockhuys S, Sulskis D, Holgersson S, Kumar R, Burmann BM, Wittung-Stafshede P. Interaction between copper chaperone Atox1 and Parkinson's disease protein -synuclein includes metal-binding sites and occurs in living cells. Acs Chemical Neuroscience. PMID 31600047 DOI: 10.1021/Acschemneuro.9B00476 |
0.425 |
|
| 2019 |
Shanmugavel KP, Kumar R, Li Y, Wittung-Stafshede P. Wilson disease missense mutations in ATP7B affect metal-binding domain structural dynamics. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 31598802 DOI: 10.1007/S10534-019-00219-Y |
0.327 |
|
| 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 |
0.351 |
|
| 2019 |
Shanmugavel KP, Wittung-Stafshede P. Copper relay path through the N-terminus of Wilson disease protein, ATP7B. Metallomics : Integrated Biometal Science. PMID 31321400 DOI: 10.1039/C9Mt00147F |
0.34 |
|
| 2019 |
Zegarra FC, Homouz D, Gasic A, Babel L, Kovermann M, Wittung-Stafshede P, Cheung MS. Crowding-induced Elongated Conformation of Urea-unfolded Apoazurin: Investigating the Role of Crowder Shape In Silico. The Journal of Physical Chemistry. B. PMID 30963769 DOI: 10.1021/Acs.Jpcb.9B00782 |
0.404 |
|
| 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 |
0.36 |
|
| 2019 |
Kiskis J, Horvath I, Wittung-Stafshede P, Rocha S. [The processes of α-synuclein amyloid protein complexes involved in the pathogenesis of Parkinson's disease]. Zhurnal Nevrologii I Psikhiatrii Imeni S.S. Korsakova. 118: 75-81. PMID 30251982 DOI: 10.17116/Jnevro201811808175 |
0.343 |
|
| 2018 |
Ariöz C, Wittung-Stafshede P. Folding of copper proteins: role of the metal? Quarterly Reviews of Biophysics. 51: e4. PMID 30912494 DOI: 10.1017/S0033583518000021 |
0.482 |
|
| 2018 |
Horvath I, Werner T, Kumar R, Wittung-Stafshede P. Copper chaperone blocks amyloid formation via ternary complex. Quarterly Reviews of Biophysics. 51: e6. PMID 30912493 DOI: 10.1017/S0033583518000045 |
0.447 |
|
| 2018 |
Matson Dzebo M, Blockhuys S, Valenzuela S, Celauro E, Esbjörner EK, Wittung-Stafshede P. Copper Chaperone Atox1 Interacts with Cell Cycle Proteins. Computational and Structural Biotechnology Journal. 16: 443-449. PMID 30455854 DOI: 10.1016/J.Csbj.2018.10.018 |
0.328 |
|
| 2018 |
Köhn B, Ponnandai Shanmugavel K, Wu M, Kovermann M, Wittung-Stafshede P. A Luminal Loop of Wilson Disease Protein Binds Copper and Is Required for Protein Activity. Biophysical Journal. PMID 30173886 DOI: 10.1016/J.Bpj.2018.07.040 |
0.367 |
|
| 2018 |
Kozak JJ, Gray HB, Wittung-Stafshede P. Geometrical Description of Protein Structural Motifs. The Journal of Physical Chemistry. B. PMID 30141936 DOI: 10.1021/Acs.Jpcb.8B07130 |
0.441 |
|
| 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 |
0.337 |
|
| 2018 |
Werner T, Kumar R, Horvath I, Scheers N, Wittung-Stafshede P. Abundant fish protein inhibits α-synuclein amyloid formation. Scientific Reports. 8: 5465. PMID 29615738 DOI: 10.1038/S41598-018-23850-0 |
0.348 |
|
| 2018 |
Sedlák E, Žoldák G, Wittung-Stafshede P. Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p. International Journal of Molecular Sciences. 19. PMID 29337899 DOI: 10.3390/Ijms19010269 |
0.345 |
|
| 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 |
0.511 |
|
| 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 |
0.328 |
|
| 2017 |
Ariöz C, Li Y, Wittung-Stafshede P. The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 29063292 DOI: 10.1007/S10534-017-0058-2 |
0.36 |
|
| 2017 |
Ponnandai Shanmugavel K, Petranovic D, Wittung-Stafshede P. Probing functional roles of Wilson disease protein (ATP7B) copper-binding domains in yeast. Metallomics : Integrated Biometal Science. PMID 28653724 DOI: 10.1039/C7Mt00101K |
0.368 |
|
| 2017 |
Blockhuys S, Wittung-Stafshede P. Roles of Copper-Binding Proteins in Breast Cancer. International Journal of Molecular Sciences. 18. PMID 28425924 DOI: 10.3390/Ijms18040871 |
0.417 |
|
| 2017 |
Blockhuys S, Celauro E, Hildesjö C, Feizi A, Stål O, Fierro-González JC, Wittung-Stafshede P. Defining the human copper proteome and analysis of its expression variation in cancers. Metallomics : Integrated Biometal Science. 9: 112-123. PMID 27942658 DOI: 10.1039/C6Mt00202A |
0.336 |
|
| 2017 |
Wittung-Stafshede P. Cross-Reactivity of Alpha-Synuclein with Other Cellular Components Can Dramatically Modulate Amyloid Formation Biophysical Journal. 112: 365. DOI: 10.1016/J.Bpj.2016.11.1980 |
0.364 |
|
| 2016 |
Blockhuys S, Wittung-Stafshede P. Copper chaperone Atox1 plays role in breast cancer cell migration. Biochemical and Biophysical Research Communications. PMID 28027931 DOI: 10.1016/J.Bbrc.2016.12.148 |
0.3 |
|
| 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 |
0.381 |
|
| 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 |
0.353 |
|
| 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 |
0.41 |
|
| 2016 |
Matson Dzebo M, Ariöz C, Wittung-Stafshede P. Extended functional repertoire for human copper chaperones. Biomolecular Concepts. 7: 29-39. PMID 26745464 DOI: 10.1515/Bmc-2015-0030 |
0.341 |
|
| 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 |
0.33 |
|
| 2016 |
Wittung-Stafshede P. Protein Interactions that Enable Safe and Efficient Copper Ion Transport in the Human Cytoplasm Biophysical Journal. 110: 179a. DOI: 10.1016/J.Bpj.2015.11.998 |
0.381 |
|
| 2016 |
Wittung-Stafshede P. A Copper Story: From Protein Folding and Metal Transport to Cancer Israel Journal of Chemistry. 56: 671-681. DOI: 10.1002/Ijch.201600019 |
0.381 |
|
| 2015 |
Wittung-Stafshede P. Unresolved questions in human copper pump mechanisms. Quarterly Reviews of Biophysics. 48: 471-8. PMID 26537407 DOI: 10.1017/S0033583515000128 |
0.321 |
|
| 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 |
0.348 |
|
| 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 |
0.316 |
|
| 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 |
0.326 |
|
| 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 |
0.398 |
|
| 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 |
0.319 |
|
| 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 |
0.401 |
|
| 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 |
0.4 |
|
| 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 |
0.352 |
|
| 2015 |
Evans ML, Chorell E, Taylor JD, Åden 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 |
0.312 |
|
| 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 |
0.414 |
|
| 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 |
0.401 |
|
| 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 |
0.486 |
|
| 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 |
0.36 |
|
| 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 |
0.352 |
|
| 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. PMID 28510156 DOI: 10.1007/S12551-013-0108-0 |
0.487 |
|
| 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 |
0.383 |
|
| 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 |
0.394 |
|
| 2013 |
Nilsson L, Ådén 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 |
0.376 |
|
| 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 |
0.495 |
|
| 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 |
0.328 |
|
| 2013 |
Wittung-Stafshede P. In Vitro effects of Macromolecular Crowding on Protein Stability, Structure and Folding Biophysical Journal. 104: 576a. DOI: 10.1016/J.Bpj.2012.11.3199 |
0.481 |
|
| 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 |
0.396 |
|
| 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 |
0.324 |
|
| 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 |
0.464 |
|
| 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 |
0.305 |
|
| 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 |
0.458 |
|
| 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 |
0.327 |
|
| 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 |
0.358 |
|
| 2012 |
Wittung-stafshede P. Effects of Macromolecular Crowding on Protein Biophysics Biophysical Journal. 102: 475a. DOI: 10.1016/J.Bpj.2011.11.2604 |
0.46 |
|
| 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 |
0.368 |
|
| 2011 |
Wittung-Stafshede P. Protein folding inside the cell. Biophysical Journal. 101: 265-6. PMID 21767477 DOI: 10.1016/J.Bpj.2011.06.018 |
0.481 |
|
| 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 |
0.409 |
|
| 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 |
0.434 |
|
| 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 |
0.445 |
|
| 2011 |
Horvath I, Rosenbaum E, Olofsson A, Johansson LBÅ, Almqvist F, Wittung-Stafshede P. In Vitro Interactions Between Model Proteins and Amyloid Inhibitors Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.2374 |
0.383 |
|
| 2011 |
Aguilar X, Wittung-Stafshede P. Effects of Macromolecular Crowding on Oligomeric Protein Unfolding: Case Study with Human Co-Chaperonin Protein 10 (cpn10) Biophysical Journal. 100: 2-3. DOI: 10.1016/J.Bpj.2010.12.1377 |
0.461 |
|
| 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 |
0.392 |
|
| 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 |
0.426 |
|
| 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 |
0.387 |
|
| 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 |
0.355 |
|
| 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 |
0.744 |
|
| 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 |
0.376 |
|
| 2010 |
Samiotakis A, Stagg L, Homouz D, Cheung MS, Wittung-Stafshede P. Residue Specific Analysis of Frustration in Folding Landscape of Repeat Alpha/Beta Protein Apoflavodoxin Biophysical Journal. 98: 200a. DOI: 10.1016/J.Bpj.2009.12.1066 |
0.432 |
|
| 2010 |
Wittung-Stafshede P. Protein Structure, Stability and Folding in the Cell - in vitro Biophysical Approaches Biophysical Journal. 98: 5a. DOI: 10.1016/J.Bpj.2009.12.031 |
0.455 |
|
| 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 |
0.415 |
|
| 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 |
0.393 |
|
| 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 |
0.409 |
|
| 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 |
0.471 |
|
| 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 |
0.312 |
|
| 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 |
0.355 |
|
| 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 |
0.434 |
|
| 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 |
0.394 |
|
| 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 |
0.454 |
|
| 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 |
0.37 |
|
| 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 |
0.428 |
|
| 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 |
0.415 |
|
| 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 |
0.342 |
|
| 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 |
0.306 |
|
| 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 |
0.396 |
|
| 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 |
0.422 |
|
| 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 |
0.422 |
|
| 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 |
0.393 |
|
| 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 |
0.424 |
|
| 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 |
0.422 |
|
| 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 |
0.442 |
|
| 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 |
0.411 |
|
| 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 |
0.459 |
|
| 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 |
0.706 |
|
| 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 |
0.348 |
|
| 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 |
0.395 |
|
| 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 |
0.4 |
|
| 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 |
0.423 |
|
| 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 |
0.452 |
|
| 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 |
0.476 |
|
| 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 |
0.39 |
|
| 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 |
0.496 |
|
| 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 |
0.392 |
|
| 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 |
0.783 |
|
| 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 |
0.338 |
|
| 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 |
0.457 |
|
| 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 |
0.809 |
|
| 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 |
0.464 |
|
| 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 |
0.434 |
|
| 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 |
0.79 |
|
| 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 |
0.404 |
|
| 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 |
0.365 |
|
| 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 |
0.788 |
|
| 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 |
0.428 |
|
| 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 |
0.457 |
|
| 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 |
0.739 |
|
| 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 |
0.422 |
|
| 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 |
0.402 |
|
| 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 |
0.813 |
|
| 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 |
0.438 |
|
| 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 |
0.408 |
|
| 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 |
0.405 |
|
| 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 |
0.659 |
|
| 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 |
0.408 |
|
| 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 |
0.387 |
|
| 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 |
0.76 |
|
| 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 |
0.684 |
|
| 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 |
0.387 |
|
| 2003 |
Guidry JJ, Shewmaker F, Maskos K, Landry S, Wittung-Stafshede P. Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified. Bmc Biochemistry. 4: 14. PMID 14525625 DOI: 10.1186/1471-2091-4-14 |
0.364 |
|
| 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 |
0.783 |
|
| 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 |
0.464 |
|
| 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 |
0.34 |
|
| 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 |
0.683 |
|
| 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 |
0.697 |
|
| 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 |
0.381 |
|
| 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 |
0.762 |
|
| 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 |
0.393 |
|
| 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 |
0.337 |
|
| 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 |
0.813 |
|
| 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 |
0.779 |
|
| 2002 |
Wittung-Stafshede P. Role of cofactors in protein folding. Accounts of Chemical Research. 35: 201-8. PMID 11955048 DOI: 10.1021/ar010106e |
0.414 |
|
| 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 |
0.33 |
|
| 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 |
0.666 |
|
| 2002 |
Wittung-Stafshede P. Role of cofactors in protein folding Accounts of Chemical Research. 35: 201-208. DOI: 10.1021/Ar010106E |
0.509 |
|
| 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 |
0.396 |
|
| 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 |
0.791 |
|
| 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 |
0.76 |
|
| 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 |
0.39 |
|
| 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 |
0.301 |
|
| 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 |
0.734 |
|
| 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 |
0.794 |
|
| 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 |
0.758 |
|
| 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 |
0.431 |
|
| 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 |
0.385 |
|
| 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 |
0.416 |
|
| 2000 |
Wittung-Stafshede P. Protein folding. Chemistry & Biology. 7: R74. PMID 10866491 DOI: 10.1016/S1074-5521(00)00096-X |
0.459 |
|
| 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 |
0.804 |
|
| 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 |
0.362 |
|
| 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 |
0.419 |
|
| 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 |
0.733 |
|
| 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 |
0.445 |
|
| 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 |
0.384 |
|
| 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 |
0.453 |
|
| 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 |
0.368 |
|
| 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 |
0.448 |
|
| 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 |
0.349 |
|
| 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 |
0.495 |
|
| 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+ |
0.388 |
|
| 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 |
0.481 |
|
| 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 |
0.456 |
|
| 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 |
0.453 |
|
| 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 |
0.395 |
|
| 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 |
0.452 |
|
| 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 |
0.388 |
|
| 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 |
0.428 |
|
| 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 |
0.335 |
|
| 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 |
0.464 |
|
| 1997 |
Wittung-Stafshede P, Wilkler JR, Gray HB. Rapid folding of a four-helix-bundle protein Faseb Journal. 11. |
0.332 |
|
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