| Year |
Citation |
Score |
| 2023 |
Sulheim E, WiderØe M, Bäck M, Nilsson KPR, Hammarström P, Nilsson LNG, Davies CL, Åslund AKO. Contrast Enhanced Magnetic Resonance Imaging of Amyloid-β Plaques in a Murine Alzheimer's Disease Model. Journal of Alzheimer's Disease : Jad. PMID 37038807 DOI: 10.3233/JAD-220198 |
0.34 |
|
| 2023 |
Caesar I, Nilsson KPR, Hammarstrom P, Lindgren M, Prokop S, Heppner FL, Schmeidler J, Haroutunian V, Holtzman DM, Hof PR, Gandy S. ApoE Alzheimer's Disease Aβ-amyloid plaque morphology varies according to APOE isotype. Research Square. PMID 36798327 DOI: 10.21203/rs.3.rs-2524641/v1 |
0.309 |
|
| 2022 |
Larsson JNK, Nyström S, Hammarström P. HSP10 as a Chaperone for Neurodegenerative Amyloid Fibrils. Frontiers in Neuroscience. 16: 902600. PMID 35769706 DOI: 10.3389/fnins.2022.902600 |
0.401 |
|
| 2022 |
Nyström S, Hammarström P. Amyloidogenesis of SARS-CoV-2 Spike Protein. Journal of the American Chemical Society. 144: 8945-8950. PMID 35579205 DOI: 10.1021/jacs.2c03925 |
0.345 |
|
| 2021 |
Liu H, Kim C, Haldiman T, Sigurdson CJ, Nyström S, Nilsson KPR, Cohen ML, Wisniewski T, Hammarström P, Safar JG. Distinct conformers of amyloid beta accumulate in the neocortex of patients with rapidly progressive Alzheimer's disease. The Journal of Biological Chemistry. 101267. PMID 34599965 DOI: 10.1016/j.jbc.2021.101267 |
0.308 |
|
| 2019 |
Jonson M, Nyström S, Sandberg A, Carlback M, Michno W, Hanrieder J, Starkenberg A, Peter K, Nilsson R, Thor S, Hammarström P. Amyloid fibril polymorphism and cell-specific toxicity . Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 26: 136-137. PMID 31343327 DOI: 10.1080/13506129.2019.1582488 |
0.374 |
|
| 2019 |
Mishra R, Elgland M, Begum A, Fyrner T, Konradsson P, Nyström S, Hammarström P. Impact of N-glycosylation site variants during human PrP aggregation and fibril nucleation. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30935958 DOI: 10.1016/J.Bbapap.2019.03.010 |
0.483 |
|
| 2019 |
Michno W, Nyström S, Wehrli P, Lashley T, Brinkmalm G, Guerard L, Syvänen S, Sehlin D, Kaya I, Brinet D, Nilsson KPR, Hammarström P, Blennow K, Zetterberg H, Hanrieder J. Pyroglutamation of amyloid-βx-42 (Aβx-42) followed by Aβ1-40 deposition underlies plaque polymorphism in progressing Alzheimer's disease pathology. The Journal of Biological Chemistry. PMID 30814252 DOI: 10.1074/Jbc.Ra118.006604 |
0.409 |
|
| 2019 |
Zhang J, Konsmo A, Sandberg A, Wu X, Nyström S, Obermueller U, Wegenast-Braun BM, Konradsson P, Lindgren M, Hammarström P. Phenolic bis-styrylbenzo[c]-1,2,5-thiadiazoles as probes for fluorescence microscope mapping of Aβ plaque heterogeneity. Journal of Medicinal Chemistry. PMID 30707834 DOI: 10.1021/Acs.Jmedchem.8B01681 |
0.414 |
|
| 2019 |
Michno W, Nyström S, Lashley T, Brinkmalm G, Syvänen S, Sehlin D, Nilsson KPR, Hammarström P, Blennow K, Zetterberg H, Hanrieder J. PYROGLUTAMATION OF AβX-42 AND Aβ1-40 DEPOSITION UNDERLIE AMYLOID PLAQUE POLYMORPHISM IN PROGRESSING ALZHEIMER’S DISEASE PATHOLOGY Alzheimers & Dementia. 15: 200. DOI: 10.1016/J.Jalz.2019.06.4534 |
0.429 |
|
| 2018 |
Zhang J, Wang J, Sandberg A, Wu X, Nyström S, LeVine Iii H, Konradsson P, Hammarström P, Durbeej B, Lindgren M. Intramolecular proton and charge transfer of pyrene-based trans-stilbene salicylic acids applied to detection of aggregated proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 30183138 DOI: 10.1002/Cphc.201800823 |
0.397 |
|
| 2018 |
Nilsson KPR, Lindgren M, Hammarström P. Luminescent-Conjugated Oligothiophene Probe Applications for Fluorescence Imaging of Pure Amyloid Fibrils and Protein Aggregates in Tissues. Methods in Molecular Biology (Clifton, N.J.). 1779: 485-496. PMID 29886552 DOI: 10.1007/978-1-4939-7816-8_30 |
0.434 |
|
| 2018 |
Michno W, Kaya I, Nyström S, Guerard L, Nilsson KPR, Hammarström P, Blennow K, Zetterberg H, Hanrieder J. Multimodal Chemical Imaging of Amyloid Plaque Polymorphism Reveals Aβ Aggregation Dependent Anionic Lipid Accumulations and Metabolism. Analytical Chemistry. PMID 29856605 DOI: 10.1021/Acs.Analchem.8B01361 |
0.413 |
|
| 2018 |
Jonson M, Nyström S, Sandberg A, Carlback M, Michno W, Hanrieder J, Starkenberg A, Nilsson KPR, Thor S, Hammarström P. Aggregated Aβ1-42 Is Selectively Toxic for Neurons, Whereas Glial Cells Produce Mature Fibrils with Low Toxicity in Drosophila. Cell Chemical Biology. PMID 29657084 DOI: 10.1016/J.Chembiol.2018.03.006 |
0.447 |
|
| 2018 |
Zhang J, Sandberg A, Konsmo A, Wu X, Nyström S, Nilsson KP, Konradsson P, LeVine H, Lindgren M, Hammarström P. Detection and imaging of Aβ1-42 and Tau fibrils by redesigned fluorescent X-34 analogues. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29543355 DOI: 10.1002/Chem.201800501 |
0.431 |
|
| 2018 |
Aguilar-Calvo P, Bett C, Sevillano AM, Kurt TD, Lawrence J, Soldau K, Hammarström P, Nilsson KPR, Sigurdson CJ. Generation of novel neuroinvasive prions following intravenous challenge. Brain Pathology (Zurich, Switzerland). PMID 29505163 DOI: 10.1111/Bpa.12598 |
0.317 |
|
| 2018 |
Khodaparast L, Khodaparast L, Gallardo R, Louros NN, Michiels E, Ramakrishnan R, Ramakers M, Claes F, Young L, Shahrooei M, Wilkinson H, Desager M, Mengistu Tadesse W, Nilsson KPR, Hammarström P, et al. Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis. Nature Communications. 9: 866. PMID 29491361 DOI: 10.1038/S41467-018-03131-0 |
0.394 |
|
| 2018 |
Fändrich M, Nyström S, Nilsson KPR, Böckmann A, LeVine H, Hammarström P. Amyloid fibril polymorphism - a challenge for molecular imaging and therapy. Journal of Internal Medicine. PMID 29360284 DOI: 10.1111/Joim.12732 |
0.397 |
|
| 2018 |
Zhang J, Wang J, Sandberg A, Wu X, Nyström S, LeVine H, Konradsson P, Hammarström P, Durbeej B, Lindgren M. Cover Feature: Intramolecular Proton and Charge Transfer of Pyrene-based trans
-Stilbene Salicylic Acids Applied to Detection of Aggregated Proteins (ChemPhysChem 22/2018) Chemphyschem. 19: 2969-2969. DOI: 10.1002/Cphc.201800987 |
0.326 |
|
| 2017 |
Schütz AK, Hornemann S, Wälti MA, Greuter L, Tiberi C, Cadalbert R, Gantner M, Riek R, Hammarström P, Nilsson KPR, Böckmann A, Aguzzi A, Meier BH. Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore. Acs Chemical Neuroscience. PMID 29178774 DOI: 10.1021/Acschemneuro.7B00397 |
0.426 |
|
| 2017 |
Rasmussen J, Mahler J, Beschorner N, Kaeser SA, Häsler LM, Baumann F, Nyström S, Portelius E, Blennow K, Lashley T, Fox NC, Sepulveda-Falla D, Glatzel M, Oblak AL, Ghetti B, et al. Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 29158413 DOI: 10.1073/Pnas.1713215114 |
0.454 |
|
| 2017 |
Nyström S, Bäck M, Nilsson KPR, Hammarström P. Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging. Journal of Visualized Experiments : Jove. PMID 29155738 DOI: 10.3791/56279 |
0.472 |
|
| 2017 |
Hahn K, Nilsson KPR, Hammarström P, Urban P, Meliss RR, Behrens HM, Krüger S, Röcken C. Establishing and validating the fluorescent amyloid ligand h-FTAA (heptamer formyl thiophene acetic acid) to identify transthyretin amyloid deposits in carpal tunnel syndrome. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-9. PMID 28434259 DOI: 10.1080/13506129.2017.1316711 |
0.332 |
|
| 2016 |
Psonka-Antonczyk KM, Hammarström P, Johansson LB, Lindgren M, Stokke BT, Nilsson KP, Nyström S. Nanoscale Structure and Spectroscopic Probing of Aβ1-40 Fibril Bundle Formation. Frontiers in Chemistry. 4: 44. PMID 27921029 DOI: 10.3389/Fchem.2016.00044 |
0.458 |
|
| 2016 |
Gallardo R, Ramakers M, De Smet F, Claes F, Khodaparast L, Khodaparast L, Couceiro JR, Langenberg T, Siemons M, Nyström S, Young LJ, Laine RF, Young L, Radaelli E, Benilova I, et al. De novo design of a biologically active amyloid. Science (New York, N.Y.). 354. PMID 27846578 DOI: 10.1126/Science.Aah4949 |
0.446 |
|
| 2016 |
Moparthi SB, Carlsson U, Vincentelli R, Jonsson BH, Hammarström P, Wenger J. Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components. Scientific Reports. 6: 28386. PMID 27328749 DOI: 10.1038/Srep28386 |
0.369 |
|
| 2016 |
Campos RI, Wu X, Elgland M, Konradsson P, Hammarstrom P. Novel Trans-Stilbene-based Fluorophores as Probes for Spectral Discrimination of Native and Protofibrillar Transthyretin. Acs Chemical Neuroscience. PMID 27144293 DOI: 10.1021/Acschemneuro.6B00062 |
0.384 |
|
| 2016 |
Nordeman P, Johansson LB, Bäck M, Estrada S, Hall H, Sjölander D, Westermark GT, Westermark P, Nilsson L, Hammarström P, Nilsson KP, Antoni G. (11)C and (18)F Radiolabeling of Tetra- and Pentathiophenes as PET-Ligands for Amyloid Protein Aggregates. Acs Medicinal Chemistry Letters. 7: 368-73. PMID 27096043 DOI: 10.1021/Acsmedchemlett.5B00309 |
0.364 |
|
| 2016 |
Sjölander D, Röcken C, Westermark P, Westermark GT, Nilsson KP, Hammarström P. Establishing the fluorescent amyloid ligand h-FTAA for studying human tissues with systemic and localized amyloid. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 23: 98-108. PMID 26987044 DOI: 10.3109/13506129.2016.1158159 |
0.391 |
|
| 2016 |
Gabrielsson EO, Armgarth A, Hammarström P, Nilsson KPR, Berggren M. Spatiotemporal Control of Amyloid-Like Aβ Plaque Formation Using a Multichannel Organic Electronic Device Macromolecular Materials and Engineering. 301: 359-363. DOI: 10.1002/Mame.201500428 |
0.375 |
|
| 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 |
0.362 |
|
| 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 |
0.642 |
|
| 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 |
0.438 |
|
| 2015 |
Hammarström P, Nyström S. Porcine prion protein amyloid. Prion. 9: 266-77. PMID 26218890 DOI: 10.1080/19336896.2015.1065373 |
0.369 |
|
| 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 |
0.379 |
|
| 2015 |
Groenning M, Campos RI, Hirschberg D, Hammarström P, Vestergaard B. Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils. Scientific Reports. 5: 11443. PMID 26108284 DOI: 10.1038/Srep11443 |
0.38 |
|
| 2015 |
Nyström S, Hammarström P. Generic amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prions. Scientific Reports. 5: 10101. PMID 25960067 DOI: 10.1038/Srep10101 |
0.416 |
|
| 2015 |
Sjölander D, Bijzet J, Hazenberg BP, Nilsson KP, Hammarström P. Sensitive and rapid assessment of amyloid by oligothiophene fluorescence in subcutaneous fat tissue. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 22: 19-25. PMID 25847117 DOI: 10.3109/13506129.2014.984063 |
0.308 |
|
| 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 |
0.437 |
|
| 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 |
0.456 |
|
| 2014 |
Nyström S, Hammarström P. Is the prevalent human prion protein 129M/V mutation a living fossil from a Paleolithic panzootic superprion pandemic? Prion. 8: 2-10. PMID 24398570 DOI: 10.4161/Pri.27601 |
0.427 |
|
| 2013 |
Moparthi SB, Sjölander D, Villebeck L, Jonsson BH, Hammarström P, Carlsson U. Transient conformational remodeling of folding proteins by GroES-individually and in concert with GroEL. Journal of Chemical Biology. 7: 1-15. PMID 24386013 DOI: 10.1007/S12154-013-0106-5 |
0.384 |
|
| 2013 |
Bagheri M, Rezakhani A, Nyström S, Turkina MV, Roghani M, Hammarström P, Mohseni S. Amyloid beta(1-40)-induced astrogliosis and the effect of genistein treatment in rat: a three-dimensional confocal morphometric and proteomic study. Plos One. 8: e76526. PMID 24130779 DOI: 10.1371/Journal.Pone.0076526 |
0.328 |
|
| 2013 |
Heilbronner G, Eisele YS, Langer F, Kaeser SA, Novotny R, Nagarathinam A, Aslund A, Hammarström P, Nilsson KP, Jucker M. Seeded strain-like transmission of β-amyloid morphotypes in APP transgenic mice. Embo Reports. 14: 1017-22. PMID 23999102 DOI: 10.1038/Embor.2013.137 |
0.379 |
|
| 2013 |
Nyström S, Psonka-Antonczyk KM, Ellingsen PG, Johansson LB, Reitan N, Handrick S, Prokop S, Heppner FL, Wegenast-Braun BM, Jucker M, Lindgren M, Stokke BT, Hammarström P, Nilsson KP. Evidence for age-dependent in vivo conformational rearrangement within Aβ amyloid deposits. Acs Chemical Biology. 8: 1128-33. PMID 23521783 DOI: 10.1021/Cb4000376 |
0.437 |
|
| 2012 |
Wegenast-Braun BM, Skodras A, Bayraktar G, Mahler J, Fritschi SK, Klingstedt T, Mason JJ, Hammarström P, Nilsson KP, Liebig C, Jucker M. Spectral discrimination of cerebral amyloid lesions after peripheral application of luminescent conjugated oligothiophenes. The American Journal of Pathology. 181: 1953-60. PMID 23041059 DOI: 10.1016/J.Ajpath.2012.08.031 |
0.452 |
|
| 2012 |
Nyström S, Mishra R, Hornemann S, Aguzzi A, Nilsson KP, Hammarström P. Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway. The Journal of Biological Chemistry. 287: 25975-84. PMID 22669942 DOI: 10.1074/Jbc.M112.372136 |
0.49 |
|
| 2012 |
Nilsson KP, Lindgren M, Hammarström P. A pentameric luminescent-conjugated oligothiophene for optical imaging of in vitro-formed amyloid fibrils and protein aggregates in tissue sections. Methods in Molecular Biology (Clifton, N.J.). 849: 425-34. PMID 22528107 DOI: 10.1007/978-1-61779-551-0_29 |
0.448 |
|
| 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 |
0.423 |
|
| 2012 |
Zetterberg H, Hammarström P. Power tools for Alzheimer's disease - an electrochemical preamp for Aβ. Journal of Neurochemistry. 122: 231-2. PMID 22409410 DOI: 10.1111/J.1471-4159.2012.07730.X |
0.34 |
|
| 2012 |
Psonka-Antonczyk KM, Duboisset J, Stokke BT, Zako T, Kobayashi T, Maeda M, Nyström S, Mason J, Hammarström P, Nilsson KP, Lindgren M. Nanoscopic and photonic ultrastructural characterization of two distinct insulin amyloid states. International Journal of Molecular Sciences. 13: 1461-80. PMID 22408402 DOI: 10.3390/Ijms13021461 |
0.393 |
|
| 2012 |
Zako T, Sakono M, Kobayashi T, Sörgjerd K, Nilsson KP, Hammarström P, Lindgren M, Maeda M. Cell interaction study of amyloid by using luminescent conjugated polythiophene: implication that amyloid cytotoxicity is correlated with prolonged cellular binding. Chembiochem : a European Journal of Chemical Biology. 13: 358-63. PMID 22262644 DOI: 10.1002/Cbic.201100467 |
0.441 |
|
| 2011 |
Klingstedt T, Aslund A, Simon RA, Johansson LB, Mason JJ, Nyström S, Hammarström P, Nilsson KP. Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates. Organic & Biomolecular Chemistry. 9: 8356-70. PMID 22051883 DOI: 10.1039/C1Ob05637A |
0.498 |
|
| 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 |
0.652 |
|
| 2011 |
Mishra R, Sjölander D, Hammarström P. Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red. Molecular Biosystems. 7: 1232-40. PMID 21279219 DOI: 10.1039/C0Mb00236D |
0.464 |
|
| 2011 |
Hammarström P, Ali MM, Mishra R, Salagic B, Svensson S, Tengvall P, Lundström I. An auto-catalytic surface for conformational replication of amyloid fibrils--genesis of an amyloid world? Origins of Life and Evolution of the Biosphere : the Journal of the International Society For the Study of the Origin of Life. 41: 373-83. PMID 21127982 DOI: 10.1007/S11084-010-9230-1 |
0.401 |
|
| 2011 |
Solé-Domènech S, Sjövall P, Vukojevic V, Codita A, Salve S, Schalling M, LaFerla F, Giménez-Llort L, Nilsson P, Hammarström P, Terenius L, Johansson B. Cholesterol accumulates in the vicinity of amyloid-beta deposits in brain tissue Alzheimers & Dementia. 7. DOI: 10.1016/J.Jalz.2011.05.2093 |
0.322 |
|
| 2011 |
Dahlqvist C, Hagstrom E, Olsson R, Karlsson U, Nyström S, Radesater A, Simon S, Nordvall G, Gravenfors Y, Lundkvist J, Svensson S, Hammarström P. P2-226: Exploring the specificity of small molecules exhibiting anti-Abeta aggregating activity Alzheimer's & Dementia. 7: S384-S384. DOI: 10.1016/J.Jalz.2011.05.1109 |
0.353 |
|
| 2010 |
Owenius R, Jarl A, Jonsson BH, Carlsson U, Hammarström P. GroEL-induced topological dislocation of a substrate protein β-sheet core: a solution EPR spin-spin distance study. Journal of Chemical Biology. 3: 127-39. PMID 21479077 DOI: 10.1007/S12154-010-0038-2 |
0.34 |
|
| 2010 |
Gabrielsson EO, Tybrandt K, Hammarström P, Berggren M, Nilsson KP. Spatially controlled amyloid reactions using organic electronics. Small (Weinheim An Der Bergstrasse, Germany). 6: 2153-61. PMID 20814927 DOI: 10.1002/Smll.201001157 |
0.409 |
|
| 2010 |
Lindgren M, Hammarström P. Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states. The Febs Journal. 277: 1380-8. PMID 20148961 DOI: 10.1111/J.1742-4658.2010.07571.X |
0.439 |
|
| 2009 |
Almstedt K, Nyström S, Nilsson KP, Hammarström P. Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates. Prion. 3: 224-35. PMID 19923901 DOI: 10.4161/Pri.3.4.10112 |
0.447 |
|
| 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 |
0.477 |
|
| 2009 |
Hammarström P. Protein folding, misfolding and disease. Febs Letters. 583: 2579-80. PMID 19616000 DOI: 10.1016/J.Febslet.2009.07.016 |
0.431 |
|
| 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 |
0.346 |
|
| 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 |
0.359 |
|
| 2009 |
Zako T, Kobayashi T, Sakono M, Lindgren M, Hammarström P, Nilsson P, Maeda M. Structure and cytotoxicity of novel insulin noodle-like filamentous amyloids Febs Journal. 276: 173-173. DOI: 10.1111/J.1742-4658.2009.07049.X |
0.336 |
|
| 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 |
0.466 |
|
| 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 |
0.34 |
|
| 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 |
0.429 |
|
| 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 |
0.443 |
|
| 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 |
0.347 |
|
| 2008 |
Nilsson KPR, Hammarström P. Luminescent Conjugated Polymers: Illuminating the Dark Matters of Biology and Pathology Advanced Materials. 20: 2639-2645. DOI: 10.1002/Adma.200800663 |
0.407 |
|
| 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 |
0.417 |
|
| 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 |
0.314 |
|
| 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 |
0.423 |
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| 2007 |
Stabo-Eeg F, Lindgren M, Nilsson KPR, Inganäs O, Hammarström P. Quantum efficiency and two-photon absorption cross-section of conjugated polyelectrolytes used for protein conformation measurements with applications on amyloid structures Chemical Physics. 336: 121-126. DOI: 10.1016/J.Chemphys.2007.06.020 |
0.389 |
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| 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 |
0.483 |
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| 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 |
0.617 |
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| 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 |
0.482 |
|
| 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 |
0.718 |
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| 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 |
0.467 |
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| 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 |
0.465 |
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| 2005 |
Lindgren M, Stabo-Eeg F, Schnell EA, Nilsson KPR, Hammarström P, Inganæs O. Biosensing and -imaging with enantiomeric luminescent conjugated polythiophenes using multiphoton excitation Proceedings of Spie - the International Society For Optical Engineering. 5935: 1-10. DOI: 10.1117/12.624438 |
0.358 |
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| 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 |
0.442 |
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| 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 |
0.372 |
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| 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 DOI: 10.1097/01.Lab.0000059937.11023.1F |
0.692 |
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| 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 |
0.785 |
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| 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 |
0.71 |
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| 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 |
0.607 |
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| 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+ |
0.75 |
|
| 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 |
0.75 |
|
| 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 |
0.494 |
|
| 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 |
0.4 |
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| 2001 |
Hammarstrom P, Persson M, Carlsson U. Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL. The Journal of Biological Chemistry. 276: 21765-75. PMID 11278767 DOI: 10.1074/Jbc.M010858200 |
0.33 |
|
| 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 |
0.404 |
|
| 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 |
0.346 |
|
| 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 |
0.452 |
|
| 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 |
0.305 |
|
| 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 |
0.349 |
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| Low-probability matches (unlikely to be authored by this person) |
| 2023 |
Hammarström P, Nyström S. Viruses and amyloids - a vicious liaison. Prion. 17: 82-104. PMID 36998202 DOI: 10.1080/19336896.2023.2194212 |
0.296 |
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| 2020 |
Yuzu K, Lindgren M, Nyström S, Zhang J, Mori W, Kunitomi R, Nagase T, Iwaya K, Hammarström P, Zako T. Insulin amyloid polymorphs: implications for iatrogenic cytotoxicity. Rsc Advances. 10: 37721-37727. PMID 35515176 DOI: 10.1039/d0ra07742a |
0.292 |
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| 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 |
0.29 |
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| 2009 |
Kobayashi T, Zako T, Sakono M, Lindgren M, Nilsson P, Hammarstrom P, Maeda M. 1P-056 Cell toxicity and inner structure analysis of novel insulin filaments using novel luminescent conjugate polymers(Protein:Property, The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S72. DOI: 10.2142/Biophys.49.S72_1 |
0.285 |
|
| 2018 |
Mpambani F, Åslund AKO, Lerouge F, Nyström S, Reitan N, Huuse EM, Widerøe M, Chaput F, Monnereau C, Andraud C, Lecouvey M, Handrick S, Prokop S, Heppner FL, Nilsson P, et al. Two-Photon Fluorescence and Magnetic Resonance Specific Imaging of Aβ Amyloid Using Hybrid Nano-GdF Contrast Media. Acs Applied Bio Materials. 1: 462-472. PMID 35016367 DOI: 10.1021/acsabm.8b00191 |
0.284 |
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| 2010 |
Klingstedt T, Kostareva A, Sjöberg G, Gudkova A, Nilsson P, Hammarström P, Sejersen T. Desmin L345P transgenic mice exhibit morphological and biochemical features of amyloidosis of two distinct types European Heart Journal. 31: 924-925. DOI: 10.1093/Eurheartj/Ehq290 |
0.28 |
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| 2010 |
Moparthi SB, Fristedt R, Mishra R, Almstedt K, Karlsson M, Hammarström P, Carlsson U. Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates. Biochemistry. 49: 1137-45. PMID 20070121 DOI: 10.1021/Bi901997Q |
0.268 |
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| 2005 |
Herland A, Björk P, Nilsson KPR, Olsson JDM, Åsberg P, Konradsson P, Hammarström P, Inganäs O. Electroactive Luminescent Self-Assembled Bio-organic Nanowires: Integration of Semiconducting Oligoelectrolytes within Amyloidogenic Proteins Advanced Materials. 17: 1466-1471. DOI: 10.1002/Adma.200500183 |
0.266 |
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| 2005 |
Herland A, Björk P, Nilsson KPR, Olsson JDM, Åsberg P, Konradsson P, Hammarström P, Inganäs O. Electroactive Luminescent Self-Assembled Bio-organic Nanowires: Integration of Semiconducting Oligoelectrolytes within Amyloidogenic Proteins (Adv. Mater. 2005, 12, 1466) Advanced Materials. 17: 1703-1703. DOI: 10.1002/Adma.200590069 |
0.266 |
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| 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 |
0.261 |
|
| 2023 |
Lerouge F, Ong E, Rositi H, Mpambani F, Berner LP, Bolbos R, Olivier C, Peyrin F, Apputukan VK, Monnereau C, Andraud C, Chaput F, Berthezène Y, Braun B, Jucker M, et al. targeting and multimodal imaging of cerebral amyloid-β aggregates using hybrid GdF nanoparticles. Nanomedicine (London, England). PMID 36927004 DOI: 10.2217/nnm-2022-0252 |
0.253 |
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| 2017 |
Zhang J, Sandberg A, Wu X, Nyström S, Lindgren M, Konradsson P, Hammarström P. -Stilbenoids with Extended Fluorescence Lifetimes for the Characterization of Amyloid Fibrils. Acs Omega. 2: 4693-4704. PMID 31457755 DOI: 10.1021/acsomega.7b00535 |
0.252 |
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| 1997 |
Lindgren M, Eaton GR, Eaton SS, Jonsson B, Hammarström P, Svensson M, Carlsson U. Electron spin echo decay as a probe of aminoxyl environment in spin-labeled mutants of human carbonic anhydrase II† Journal of the Chemical Society-Perkin Transactions 1. 2549-2554. DOI: 10.1039/A702470C |
0.244 |
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| 2022 |
Jiang R, Smailovic U, Haytural H, Tijms BM, Li H, Haret RM, Shevchenko G, Chen G, Abelein A, Gobom J, Frykman S, Sekiguchi M, Fujioka R, Watamura N, Sasaguri H, et al. Increased CSF-decorin predicts brain pathological changes driven by Alzheimer's Aβ amyloidosis. Acta Neuropathologica Communications. 10: 96. PMID 35787306 DOI: 10.1186/s40478-022-01398-5 |
0.243 |
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| 2009 |
Kobayashi T, Zako T, Sakono M, Lindgren M, Nilsson P, Hammarstrom P, Maeda M. 1TP3-04 Cell toxicity and inner structure analysis of novel insulin filaments using novel luminescent conjugate polymers(The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S34. DOI: 10.2142/Biophys.49.S34_5 |
0.243 |
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| 2008 |
Kobayashi T, Zako T, Sakono M, Lindgren M, Nilsson KPR, Hammarstrom P, Maeda M. 1P-075 Structural Properties and Cytotoxicity of Novel Insulin 'Noodle'-like Filaments(The 46th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 48: S32. DOI: 10.2142/Biophys.48.S32_6 |
0.239 |
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| 2023 |
Thi Minh NN, Begum A, Zhang J, Leira P, Todarwal Y, Linares M, Norman P, Derbyshire D, von Castelmur E, Lindgren M, Hammarström P, König C. Binding of a Pyrene-Based Fluorescent Amyloid Ligand to Transthyretin: A Combined Crystallographic and Molecular Dynamics Study. The Journal of Physical Chemistry. B. PMID 37477604 DOI: 10.1021/acs.jpcb.3c02147 |
0.236 |
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| 2020 |
Sandberg A, Ling H, Gearing M, Dombroski B, Cantwell L, R'Bibo L, Levey A, Schellenberg GD, Hardy J, Wood N, Fernius J, Nyström S, Svensson S, Thor S, Hammarström P, et al. Fibrillation and molecular characteristics are coherent with clinical and pathological features of 4-repeat tauopathy caused by MAPT variant G273R. Neurobiology of Disease. 105079. PMID 32961270 DOI: 10.1016/j.nbd.2020.105079 |
0.234 |
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| 2013 |
LeVine H, Peter K, Nilsson R, Hammarström P. Reporters of Amyloid Structural Polymorphism Bio-Nanoimaging: Protein Misfolding and Aggregation. 69-79. DOI: 10.1016/B978-0-12-394431-3.00007-9 |
0.228 |
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| 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. DOI: 10.1117/12.510471 |
0.221 |
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| 2017 |
Nyström S, Vahdat Shariat Panahi A, Nilsson KPR, Westermark P, Westermark GT, Hammarström P, Lundmark K. Seed-dependent templating of murine AA amyloidosis. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 24: 140-141. PMID 28434369 DOI: 10.1080/13506129.2017.1290599 |
0.194 |
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| 2020 |
Bäck M, Selegård R, Todarwal Y, Nyström S, Norman P, Linares M, Hammarström P, Lindgren M, Nilsson KPR. Tyrosine Side-Chain Functionalities at Distinct Positions Determine the Chirooptical Properties and Supramolecular Structures of Pentameric Oligothiophenes. Chemistryopen. 9: 1100-1108. PMID 33163327 DOI: 10.1002/open.202000144 |
0.162 |
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| 2021 |
Lindberg A, Knight AC, Sohn D, Rakos L, Tong J, Radelet A, Mason NS, Stehouwer JS, Lopresti BJ, Klunk WE, Sandell J, Sandberg A, Hammarström P, Svensson S, Mathis CA, et al. Radiosynthesis, and Evaluation of [F]CBD-2115 as a First-in-Class Radiotracer for Imaging 4R-Tauopathies. Acs Chemical Neuroscience. PMID 33497190 DOI: 10.1021/acschemneuro.0c00801 |
0.132 |
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| 2023 |
Begum A, Zhang J, Derbyshire D, Wu X, Konradsson P, Hammarström P, von Castelmur E. Transthyretin Binding Mode Dichotomy of Fluorescent -Stilbene Ligands. Acs Chemical Neuroscience. PMID 36780206 DOI: 10.1021/acschemneuro.2c00700 |
0.113 |
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| 2008 |
Hammarström P. Judarna och stadsbranden: Judisk invandring och integration i det sena 1800-talets Sverige Nordisk Judaistik/Scandinavian Jewish Studies. 26: 107-132. DOI: 10.30752/nj.69619 |
0.01 |
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| Hide low-probability matches. |