Per Hammarstrom, Ph.D. - Publications

Biochemistry Linköping University, Linköping, Östergötlands län, Sweden 
Protein Folding and Misfolding

62 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
2015 Bednarska NG, Van Eldere J, Gallardo R, Ganesan A, Ramakers M, Vogel I, Baatsen P, Staes A, Goethals M, Hammarström P, Nilsson KP, Gevaert K, Schymkowitz J, Rousseau F. Protein aggregation as an antibiotic design strategy. Molecular Microbiology. PMID 26559925 DOI: 10.1111/mmi.13269  0.96
2015 Sekijima Y, Campos RI, Hammarström P, Nilsson KP, Yoshinaga T, Nagamatsu K, Yazaki M, Kametani F, Ikeda SI. Pathological, biochemical, and biophysical characteristics of the transthyretin variant Y114H (p.Y134H) explain its very mild clinical phenotype. Journal of the Peripheral Nervous System : Jpns. PMID 26306725 DOI: 10.1111/jns.12143  0.96
2015 Herrmann US, Schütz AK, Shirani H, Huang D, Saban D, Nuvolone M, Li B, Ballmer B, Åslund AK, Mason JJ, Rushing E, Budka H, Nyström S, Hammarström P, Böckmann A, et al. Structure-based drug design identifies polythiophenes as antiprion compounds. Science Translational Medicine. 7: 299ra123. PMID 26246168 DOI: 10.1126/scitranslmed.aab1923  0.96
2015 Jonson M, Pokrzywa M, Starkenberg A, Hammarstrom P, Thor S. Systematic Aβ Analysis in Drosophila Reveals High Toxicity for the 1-42, 3-42 and 11-42 Peptides, and Emphasizes N- and C-Terminal Residues. Plos One. 10: e0133272. PMID 26208119 DOI: 10.1371/journal.pone.0133272  0.96
2014 Magnusson K, Simon R, Sjölander D, Sigurdson CJ, Hammarström P, Nilsson KP. Multimodal fluorescence microscopy of prion strain specific PrP deposits stained by thiophene-based amyloid ligands. Prion. 8: 319-29. PMID 25495506 DOI: 10.4161/pri.29239  0.96
2014 Fritschi SK, Cintron A, Ye L, Mahler J, Bühler A, Baumann F, Neumann M, Nilsson KP, Hammarström P, Walker LC, Jucker M. Aβ seeds resist inactivation by formaldehyde. Acta Neuropathologica. 128: 477-84. PMID 25193240 DOI: 10.1007/s00401-014-1339-2  0.96
2014 Usmani SM, Zirafi O, Müller JA, Sandi-Monroy NL, Yadav JK, Meier C, Weil T, Roan NR, Greene WC, Walther P, Nilsson KP, Hammarström P, Wetzel R, Pilcher CD, Gagsteiger F, et al. Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen. Nature Communications. 5: 3508. PMID 24691351 DOI: 10.1038/ncomms4508  0.96
2013 Arja K, Sjölander D, Ã…slund A, Prokop S, Heppner FL, Konradsson P, Lindgren M, Hammarström P, Ã…slund KO, Nilsson KP. Enhanced fluorescent assignment of protein aggregates by an oligothiophene-porphyrin-based amyloid ligand. Macromolecular Rapid Communications. 34: 723-30. PMID 23468206 DOI: 10.1002/marc.201200817  0.6
2013 Solé-Domènech S, Sjövall P, Vukojević V, Fernando R, Codita A, Salve S, Bogdanović N, Mohammed AH, Hammarström P, Nilsson KP, LaFerla FM, Jacob S, Berggren PO, Giménez-Llort L, Schalling M, et al. Localization of cholesterol, amyloid and glia in Alzheimer's disease transgenic mouse brain tissue using time-of-flight secondary ion mass spectrometry (ToF-SIMS) and immunofluorescence imaging. Acta Neuropathologica. 125: 145-57. PMID 22996963 DOI: 10.1007/s00401-012-1046-9  0.96
2012 Fyrner T, Magnusson K, Nilsson KP, Hammarström P, Aili D, Konradsson P. Derivatization of a bioorthogonal protected trisaccharide linker-toward multimodal tools for chemical biology. Bioconjugate Chemistry. 23: 1333-40. PMID 22568531 DOI: 10.1021/bc300160a  0.6
2012 Margalith I, Suter C, Ballmer B, Schwarz P, Tiberi C, Sonati T, Falsig J, Nyström S, Hammarström P, Aslund A, Nilsson KP, Yam A, Whitters E, Hornemann S, Aguzzi A. Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates. The Journal of Biological Chemistry. 287: 18872-87. PMID 22493452 DOI: 10.1074/jbc.M112.355958  0.96
2012 Caesar I, Jonson M, Nilsson KP, Thor S, Hammarström P. Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic Drosophila. Plos One. 7: e31424. PMID 22348084 DOI: 10.1371/journal.pone.0031424  0.6
2011 Lord A, Philipson O, Klingstedt T, Westermark G, Hammarström P, Nilsson KP, Nilsson LN. Observations in APP bitransgenic mice suggest that diffuse and compact plaques form via independent processes in Alzheimer's disease. The American Journal of Pathology. 178: 2286-98. PMID 21514441 DOI: 10.1016/j.ajpath.2011.01.052  0.6
2011 Groenning M, Campos RI, Fagerberg C, Rasmussen AA, Eriksen UH, Powers ET, Hammarström P. Thermodynamic stability and denaturation kinetics of a benign natural transthyretin mutant identified in a Danish kindred. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 18: 35-46. PMID 21406045 DOI: 10.3109/13506129.2011.560215  0.96
2010 Hammarström P, Simon R, Nyström S, Konradsson P, Aslund A, Nilsson KP. A fluorescent pentameric thiophene derivative detects in vitro-formed prefibrillar protein aggregates. Biochemistry. 49: 6838-45. PMID 20604540 DOI: 10.1021/bi100922r  0.6
2010 Berg I, Nilsson KP, Thor S, Hammarström P. Efficient imaging of amyloid deposits in Drosophila models of human amyloidoses. Nature Protocols. 5: 935-44. PMID 20431539 DOI: 10.1038/nprot.2010.41  0.6
2009 Aslund A, Sigurdson CJ, Klingstedt T, Grathwohl S, Bolmont T, Dickstein DL, Glimsdal E, Prokop S, Lindgren M, Konradsson P, Holtzman DM, Hof PR, Heppner FL, Gandy S, Jucker M, et al. Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses. Acs Chemical Biology. 4: 673-84. PMID 19624097 DOI: 10.1021/cb900112v  0.96
2009 Hammarström P. Protein folding, misfolding and disease. Febs Letters. 583: 2579-80. PMID 19616000 DOI: 10.1016/j.febslet.2009.07.016  0.6
2009 Almstedt K, Rafstedt T, Supuran CT, Carlsson U, Hammarström P. Small-molecule suppression of misfolding of mutated human carbonic anhydrase II linked to marble brain disease. Biochemistry. 48: 5358-64. PMID 19415900 DOI: 10.1021/bi900128e  0.6
2009 Berg I, Thor S, Hammarström P. Modeling familial amyloidotic polyneuropathy (Transthyretin V30M) in Drosophila melanogaster. Neuro-Degenerative Diseases. 6: 127-38. PMID 19372706 DOI: 10.1159/000213761  0.6
2009 Moparthi SB, Hammarström P, Carlsson U. A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding. Protein Science : a Publication of the Protein Society. 18: 475-9. PMID 19185003 DOI: 10.1002/pro.28  0.6
2009 Philipson O, Hammarström P, Nilsson KP, Portelius E, Olofsson T, Ingelsson M, Hyman BT, Blennow K, Lannfelt L, Kalimo H, Nilsson LN. A highly insoluble state of Abeta similar to that of Alzheimer's disease brain is found in Arctic APP transgenic mice. Neurobiology of Aging. 30: 1393-405. PMID 18192084 DOI: 10.1016/j.neurobiolaging.2007.11.022  0.96
2008 Sörgjerd K, Klingstedt T, Lindgren M, Kågedal K, Hammarström P. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochemical and Biophysical Research Communications. 377: 1072-8. PMID 18983977 DOI: 10.1016/j.bbrc.2008.10.121  0.6
2008 Maas C, Govers-Riemslag JW, Bouma B, Schiks B, Hazenberg BP, Lokhorst HM, Hammarström P, ten Cate H, de Groot PG, Bouma BN, Gebbink MF. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. The Journal of Clinical Investigation. 118: 3208-18. PMID 18725990 DOI: 10.1172/JCI35424  0.6
2008 Sjöberg AP, Nyström S, Hammarström P, Blom AM. Native, amyloid fibrils and beta-oligomers of the C-terminal domain of human prion protein display differential activation of complement and bind C1q, factor H and C4b-binding protein directly. Molecular Immunology. 45: 3213-21. PMID 18406463 DOI: 10.1016/j.molimm.2008.02.023  0.6
2008 Mishra R, Olofsson L, Karlsson M, Carlsson U, Nicholls IA, Hammarström P. A conformationally isoformic thermophilic protein with high kinetic unfolding barriers. Cellular and Molecular Life Sciences : Cmls. 65: 827-39. PMID 18217202 DOI: 10.1007/s00018-008-7517-4  0.6
2008 Almstedt K, Mårtensson LG, Carlsson U, Hammarström P. Thermodynamic interrogation of a folding disease. Mutant mapping of position 107 in human carbonic anhydrase II linked to marble brain disease. Biochemistry. 47: 1288-98. PMID 18189416 DOI: 10.1021/bi701720p  0.6
2007 Sigurdson CJ, Nilsson KP, Hornemann S, Manco G, Polymenidou M, Schwarz P, Leclerc M, Hammarström P, Wüthrich K, Aguzzi A. Prion strain discrimination using luminescent conjugated polymers. Nature Methods. 4: 1023-30. PMID 18026110 DOI: 10.1038/nmeth1131  0.96
2007 Aslund A, Herland A, Hammarström P, Nilsson KP, Jonsson BH, Inganäs O, Konradsson P. Studies of luminescent conjugated polythiophene derivatives: enhanced spectral discrimination of protein conformational states. Bioconjugate Chemistry. 18: 1860-8. PMID 17939727 DOI: 10.1021/bc700180g  0.6
2007 Villebeck L, Moparthi SB, Lindgren M, Hammarström P, Jonsson BH. Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC). Biochemistry. 46: 12639-47. PMID 17939680 DOI: 10.1021/bi700658n  0.6
2007 Nilsson KP, Aslund A, Berg I, Nyström S, Konradsson P, Herland A, Inganäs O, Stabo-Eeg F, Lindgren M, Westermark GT, Lannfelt L, Nilsson LN, Hammarström P. Imaging distinct conformational states of amyloid-beta fibrils in Alzheimer's disease using novel luminescent probes. Acs Chemical Biology. 2: 553-60. PMID 17672509 DOI: 10.1021/cb700116u  0.96
2007 Hammarström P. The bloody path of amyloids and prions. Journal of Thrombosis and Haemostasis : Jth. 5: 1136-8. PMID 17567445 DOI: 10.1111/j.1538-7836.2007.02575.x  0.6
2007 Villebeck L, Persson M, Luan SL, Hammarström P, Lindgren M, Jonsson BH. Conformational rearrangements of tail-less complex polypeptide 1 (TCP-1) ring complex (TRiC)-bound actin. Biochemistry. 46: 5083-93. PMID 17417821 DOI: 10.1021/bi062093o  0.6
2007 Mishra R, Sörgjerd K, Nyström S, NordigÃ¥rden A, Yu YC, Hammarström P. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. Journal of Molecular Biology. 366: 1029-44. PMID 17196616 DOI: 10.1016/j.jmb.2006.11.084  0.6
2006 Nilsson KP, Hammarström P, Ahlgren F, Herland A, Schnell EA, Lindgren M, Westermark GT, Inganäs O. Conjugated polyelectrolytes--conformation-sensitive optical probes for staining and characterization of amyloid deposits. Chembiochem : a European Journal of Chemical Biology. 7: 1096-104. PMID 16729336 DOI: 10.1002/cbic.200500550  0.96
2006 Sörgjerd K, Ghafouri B, Jonsson BH, Kelly JW, Blond SY, Hammarström P. Retention of misfolded mutant transthyretin by the chaperone BiP/GRP78 mitigates amyloidogenesis. Journal of Molecular Biology. 356: 469-82. PMID 16376939 DOI: 10.1016/j.jmb.2005.11.051  0.96
2005 Wiréhn J, Carlsson K, Herland A, Persson E, Carlsson U, Svensson M, Hammarström P. Activity, folding, misfolding, and aggregation in vitro of the naturally occurring human tissue factor mutant R200W. Biochemistry. 44: 6755-63. PMID 15865421 DOI: 10.1021/bi047388l  0.6
2005 Sekijima Y, Wiseman RL, Matteson J, Hammarström P, Miller SR, Sawkar AR, Balch WE, Kelly JW. The biological and chemical basis for tissue-selective amyloid disease. Cell. 121: 73-85. PMID 15820680 DOI: 10.1016/j.cell.2005.01.018  0.96
2005 Lindgren M, Sörgjerd K, Hammarström P. Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy. Biophysical Journal. 88: 4200-12. PMID 15764666 DOI: 10.1529/biophysj.104.049700  0.6
2005 Nilsson KP, Herland A, Hammarström P, Inganäs O. Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation. Biochemistry. 44: 3718-24. PMID 15751948 DOI: 10.1021/bi047402u  0.6
2005 Herland A, Nilsson KP, Olsson JD, Hammarström P, Konradsson P, Inganäs O. Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH. Journal of the American Chemical Society. 127: 2317-23. PMID 15713111 DOI: 10.1021/ja045835e  0.6
2004 Knudsen JF, Carlsson U, Hammarström P, Sokol GH, Cantilena LR. The cyclooxygenase-2 inhibitor celecoxib is a potent inhibitor of human carbonic anhydrase II. Inflammation. 28: 285-90. PMID 16134002 DOI: 10.1007/s10753-004-6052-1  0.6
2004 Almstedt K, Lundqvist M, Carlsson J, Karlsson M, Persson B, Jonsson BH, Carlsson U, Hammarström P. Unfolding a folding disease: folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II. Journal of Molecular Biology. 342: 619-33. PMID 15327960 DOI: 10.1016/j.jmb.2004.07.024  0.6
2004 Borén K, Grankvist H, Hammarström P, Carlsson U. Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase. Febs Letters. 566: 95-9. PMID 15147875 DOI: 10.1016/j.febslet.2004.03.105  0.6
2004 Tiihonen M, Pasiskevicius V, Laurell F, Hammarstrom P, Lindgren M. A UV laser source for biological and chemical sensing Proceedings of Spie - the International Society For Optical Engineering. 5240: 127-136.  0.96
2003 Hammarström P, Sekijima Y, White JT, Wiseman RL, Lim A, Costello CE, Altland K, Garzuly F, Budka H, Kelly JW. D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? Biochemistry. 42: 6656-63. PMID 12779320 DOI: 10.1021/bi027319b  0.96
2003 Sekijima Y, Hammarström P, Matsumura M, Shimizu Y, Iwata M, Tokuda T, Ikeda S, Kelly JW. Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology. Laboratory Investigation; a Journal of Technical Methods and Pathology. 83: 409-17. PMID 12649341  0.96
2003 Hammarström P, Wiseman RL, Powers ET, Kelly JW. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science (New York, N.Y.). 299: 713-6. PMID 12560553 DOI: 10.1126/science.1079589  0.96
2002 Hammarström P, Jiang X, Hurshman AR, Powers ET, Kelly JW. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proceedings of the National Academy of Sciences of the United States of America. 99: 16427-32. PMID 12351683 DOI: 10.1073/pnas.202495199  0.96
2001 Huber M, Lindgren M, Hammarström P, MÃ¥rtensson LG, Carlsson U, Eaton GR, Eaton SS. Phase memory relaxation times of spin labels in human carbonic anhydrase II: pulsed EPR to determine spin label location. Biophysical Chemistry. 94: 245-56. PMID 11804734 DOI: 10.1016/S0301-4622(01)00239-3  0.96
2001 Hammarström P, Schneider F, Kelly JW. Trans-suppression of misfolding in an amyloid disease. Science (New York, N.Y.). 293: 2459-62. PMID 11577236 DOI: 10.1126/science.1062245  0.96
2001 Hammarström P, Jiang X, Deechongkit S, Kelly JW. Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy. Biochemistry. 40: 11453-9. PMID 11560493 DOI: 10.1021/bi010673+  0.96
2001 Jiang X, Smith CS, Petrassi HM, Hammarström P, White JT, Sacchettini JC, Kelly JW. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. Biochemistry. 40: 11442-52. PMID 11560492 DOI: 10.1021/bi011194d  0.96
2001 Schneider F, Hammarström P, Kelly JW. Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins. Protein Science : a Publication of the Protein Society. 10: 1606-13. PMID 11468357 DOI: 10.1110/ps.8901  0.96
2001 Persson M, Harbridge JR, Hammarström P, Mitri R, MÃ¥rtensson LG, Carlsson U, Eaton GR, Eaton SS. Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II. Biophysical Journal. 80: 2886-97. PMID 11371461 DOI: 10.1016/S0006-3495(01)76254-6  0.96
2001 Hammarström P, Owenius R, Mårtensson LG, Carlsson U, Lindgren M. High-resolution probing of local conformational changes in proteins by the use of multiple labeling: unfolding and self-assembly of human carbonic anhydrase II monitored by spin, fluorescent, and chemical reactivity probes. Biophysical Journal. 80: 2867-85. PMID 11371460 DOI: 10.1016/S0006-3495(01)76253-4  0.6
2001 Andersson D, Hammarström P, Carlsson U. Cofactor-induced refolding: refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II). Biochemistry. 40: 2653-61. PMID 11258876 DOI: 10.1021/bi000957e  0.6
2000 Hammarström P, Carlsson U. Is the unfolded state the Rosetta Stone of the protein folding problem? Biochemical and Biophysical Research Communications. 276: 393-8. PMID 11027486 DOI: 10.1006/bbrc.2000.3360  0.6
2000 Hammarström P, Persson M, Owenius R, Lindgren M, Carlsson U. Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity. The Journal of Biological Chemistry. 275: 22832-8. PMID 10811634 DOI: 10.1074/jbc.M000649200  0.6
1999 Hammarström P, Persson M, Freskgârd PO, Mârtensson LG, Andersson D, Jonsson BH, Carlsson U. Structural mapping of an aggregation nucleation site in a molten globule intermediate. The Journal of Biological Chemistry. 274: 32897-903. PMID 10551854 DOI: 10.1074/jbc.274.46.32897  0.6
1999 Persson M, Hammarström P, Lindgren M, Jonsson BH, Svensson M, Carlsson U. EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction. Biochemistry. 38: 432-41. PMID 9890926 DOI: 10.1021/bi981442e  0.6
1997 Hammarström P, Kalman B, Jonsson BH, Carlsson U. Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II. Febs Letters. 420: 63-8. PMID 9450551 DOI: 10.1016/S0014-5793(97)01488-9  0.6
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