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DNA-like double helix formed by peptide nucleic acid P Wittung, PE Nielsen, O Buchardt, M Egholm, B Norde´ n Nature 368 (6471), 561-563, 1994 | 691 | 1994 |
Gold nanoparticles can induce the formation of protein-based aggregates at physiological pH D Zhang, O Neumann, H Wang, VM Yuwono, A Barhoumi, M Perham, ... Nano letters 9 (2), 666-671, 2009 | 432 | 2009 |
Ionic effects on the stability and conformation of peptide nucleic acid complexes S Tomac, M Sarkar, T Ratilainen, P Wittung, PE Nielsen, B Nordén, ... Journal of the American Chemical Society 118 (24), 5544-5552, 1996 | 407 | 1996 |
A gut bacterial amyloid promotes α-synuclein aggregation and motor impairment in mice TR Sampson, C Challis, N Jain, A Moiseyenko, MS Ladinsky, GG Shastri, ... elife 9, e53111, 2020 | 336 | 2020 |
Molecular crowding enhances native structure and stability of α/β protein flavodoxin L Stagg, SQ Zhang, MS Cheung, P Wittung-Stafshede Proceedings of the National Academy of Sciences 104 (48), 18976-18981, 2007 | 303 | 2007 |
Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins KL Maxwell, D Wildes, A Zarrine‐Afsar, MA De Los Rios, AG Brown, ... Protein Science 14 (3), 602-616, 2005 | 259 | 2005 |
Crowded, cell-like environment induces shape changes in aspherical protein D Homouz, M Perham, A Samiotakis, MS Cheung, P Wittung-Stafshede Proceedings of the National Academy of Sciences 105 (33), 11754-11759, 2008 | 238 | 2008 |
Role of cofactors in protein folding P Wittung-Stafshede Accounts of chemical research 35 (4), 201-208, 2002 | 222 | 2002 |
The bacterial curli system possesses a potent and selective inhibitor of amyloid formation ML Evans, E Chorell, JD Taylor, J Åden, A Götheson, F Li, M Koch, ... Molecular cell 57 (3), 445-455, 2015 | 220 | 2015 |
Defining the human copper proteome and analysis of its expression variation in cancers S Blockhuys, E Celauro, C Hildesjö, A Feizi, O Stål, JC Fierro-González, ... Metallomics 9 (2), 112-123, 2017 | 213 | 2017 |
Structure-activity studies of the binding of modified peptide nucleic acids (PNAs) to DNA B Hyrup, M Egholm, PE Nielsen, P Wittung, B Norden, O Buchardt Journal of the American Chemical Society 116 (18), 7964-7970, 1994 | 196 | 1994 |
Phospholipid membrane permeability of peptide nucleic acid P Wittung, J Kajanus, K Edwards, P Nielsen, B Nordén, BG Malmström FEBS letters 365 (1), 27-29, 1995 | 188 | 1995 |
Effects of folding on metalloprotein active sites JR Winkler, P Wittung-Stafshede, J Leckner, BG Malmström, HB Gray Proceedings of the National Academy of Sciences 94 (9), 4246-4249, 1997 | 187 | 1997 |
Cytochrome b562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein P Wittung-Stafshede, JC Lee, JR Winkler, HB Gray Proceedings of the National Academy of Sciences 96 (12), 6587-6590, 1999 | 158 | 1999 |
Water-soluble, recombinant CuA-domain of the cytochrome ba 3 subunit II from Thermus thermophilus CE Slutter, D Sanders, P Wittung, BG Malmström, R Aasa, JH Richards, ... Biochemistry 35 (11), 3387-3395, 1996 | 156 | 1996 |
Factors Defining Effects of Macromolecular Crowding on Protein Stability: An in Vitro/in Silico Case Study Using Cytochrome c A Christiansen, Q Wang, A Samiotakis, MS Cheung, P Wittung-Stafshede Biochemistry 49 (31), 6519-6530, 2010 | 150 | 2010 |
Direct observation of strand invasion by peptide nucleic acid (PNA) into double-stranded DNA P Wittung, P Nielsen, B Nordén Journal of the American Chemical Society 118 (30), 7049-7054, 1996 | 150 | 1996 |
Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson’s disease I Horvath, P Wittung-Stafshede Proceedings of the National Academy of Sciences 113 (44), 12473-12477, 2016 | 149 | 2016 |
Extended DNA-recognition repertoire of peptide nucleic acid (PNA): PNA− dsDNA triplex formed with cytosine-rich homopyrimidine PNA P Wittung, P Nielsen, B Nordén Biochemistry 36 (26), 7973-7979, 1997 | 149 | 1997 |