Publications

 

Evidence for Age-Dependent in Vivo Conformational Rearrangement within Aβ Amyloid Deposits, Nyström S., Psonka-Antonczyk K.M., Ellingsen P.G., Johansson L.B., Reitan N., Handrick S., Prokop S., Heppner F.L., Wegenast-Braun B.M., Jucker M., Lindgren M., Stokke B.T., Hammarström P., Nilsson K.P. (2013), ACS Chemical Biology

 

Enhanced Fluorescent Assignment of Protein Aggregates by an Oligothiophene-Porphyrin-Based Amyloid Ligand, Arja, K., Sjolander, D., Aslund, A., Prokop, S., Heppner, F. L., Konradsson, P., Lindgren, M., Hammarstrom, P., Aslund, K. O., and Nilsson, K. P. (2013), Macromolecular rapid communications.

 

Spectral discrimination of cerebral amyloid lesions after peripheral application of luminescent conjugated oligothiophenes,Wegenast-Braun, B. M., Skodras, A., Bayraktar, G., Mahler, J., Fritschi, S. K., Klingstedt, T., Mason, J. J., Hammarstrom, P., Nilsson, K. P., Liebig, C., and Jucker, M. (2012) The American journal of pathology 181, 1953-1960.

 

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, Sole-Domenech, S., Sjovall, P., Vukojevic, V., Fernando, R., Codita, A., Salve, S., Bogdanovic, N., Mohammed, A. H., Hammarstrom, P., Nilsson, K. P., LaFerla, F. M., Jacob, S., Berggren, P. O., Gimenez-Llort, L., Schalling, M., Terenius, L., and Johansson, B. (2013) Acta neuropathologica 125, 145-157.

 

Multiple substitutions of methionine 129 in human prion protein reveal its importance in the amyloid fibrillation pathway, Nystrom, S., Mishra, R., Hornemann, S., Aguzzi, A., Nilsson, K. P., and Hammarstrom, P. (2012) The Journal of biological chemistry 287, 25975-25984.

 

Derivatization of a Bioorthogonal Protected Trisaccharide Linker-Toward Multimodal Tools for Chemical Biology,Fyrner, T., Magnusson, K., Nilsson, K. P., Hammarstrom, P., Aili, D., and Konradsson, P. (2012) Bioconjugate chemistry 23 (6), 1333–1340.

 

A pentameric luminescent-conjugated oligothiophene for optical imaging of in vitro-formed amyloid fibrils and protein aggregates in tissue sections,Nilsson, K. P., Lindgren, M., and Hammarstrom, P. (2012) Methods Mol Biol 849, 425-434.

 

Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates, Margalith, I., Suter, C., Ballmer, B., Schwarz, P., Tiberi, C., Sonati, T., Falsig, J., Nystrom, S., Hammarstrom, P., Aslund, A., Nilsson, K. P., Yam, A., Whitters, E., Hornemann, S., and Aguzzi, A. (2012) The Journal of biological chemistry 287, 18872-18887.

 

Power tools for Alzheimer's disease - an electrochemical preamp for Abeta, Zetterberg, H., and Hammarstrom, P. (2012) Journal of neurochemistry.

 

Nanoscopic and photonic ultrastructural characterization of two distinct insulin amyloid States, Psonka-Antonczyk, K. M., Duboisset, J., Stokke, B. T., Zako, T., Kobayashi, T., Maeda, M., Nystrom, S., Mason, J., Hammarstrom, P., Nilsson, K. P., and Lindgren, M. (2012) International journal of molecular sciences 13, 1461-1480.

 

Curcumin promotes A-beta fibrillation and reduces neurotoxicity in transgenic Drosophila, Caesar, I., Jonson, M., Nilsson, K. P., Thor, S., and Hammarstrom, P. (2012) PloS one 7, e31424.

 

Cell interaction study of amyloid by using luminescent conjugated polythiophene: implication that amyloid cytotoxicity is correlated with prolonged cellular binding, Zako, T., Sakono, M., Kobayashi, T., Sorgjerd, K., Nilsson, K. P., Hammarstrom, P., Lindgren, M., and Maeda, M. (2012) Chembiochem 13, 358-363.

 

Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates, Klingstedt, T., Aslund, A., Simon, R. A., Johansson, L. B., Mason, J. J., Nystrom, S., Hammarstrom, P., and Nilsson, K. P. (2011) Organic & biomolecular chemistry 9, 8356-8370.

 

Observations in APP bitransgenic mice suggest that diffuse and compact plaques form via independent processes in Alzheimer's disease, Lord, A., Philipson, O., Klingstedt, T., Westermark, G., Hammarstrom, P., Nilsson, K. P., and Nilsson, L. N. (2011) The American journal of pathology 178, 2286-2298.

 

Thermodynamic stability and denaturation kinetics of a benign natural transthyretin mutant identified in a Danish kindred, Groenning, M., Campos, R. I., Fagerberg, C., Rasmussen, A. A., Eriksen, U. H., Powers, E. T., and Hammarstrom, P. (2011) Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis 18, 35-46.

 

Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red, Mishra, R., Sjolander, D., and Hammarstrom, P. (2011) Molecular bioSystems 7, 1232-1240.

 

An auto-catalytic surface for conformational replication of amyloid fibrils--genesis of an amyloid world? Hammarstrom, P., Ali, M. M., Mishra, R., Salagic, B., Svensson, S., Tengvall, P., and Lundstrom, I. (2011) Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life 41, 373-383.

 

Spatially controlled amyloid reactions using organic electronics, Gabrielsson, E. O., Tybrandt, K., Hammarstrom, P., Berggren, M., and Nilsson, K. P. (2010) Small 6, 2153-2161.

 

A fluorescent pentameric thiophene derivative detects in vitro-formed prefibrillar protein aggregates, Hammarstrom, P., Simon, R., Nystrom, S., Konradsson, P., Aslund, A., and Nilsson, K. P. (2010) Biochemistry 49, 6838-6845.

 

Efficient imaging of amyloid deposits in Drosophila models of human amyloidoses, Berg, I., Nilsson, K. P., Thor, S., and Hammarstrom, P. (2010) Nature protocols 5, 935-944.

Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states, Lindgren, M., and Hammarstrom, P. (2010) The FEBS journal 277, 1380-1388.

 

Chaperone activity of Cyp18 through hydrophobic condensation that enables rescue of transient misfolded molten globule intermediates, Moparthi, S. B., Fristedt, R., Mishra, R., Almstedt, K., Karlsson, M., Hammarstrom, P., and Carlsson, U. (2010) Biochemistry 49, 1137-1145.

 

GroEL-induced topological dislocation of a substrate protein beta-sheet core: a solution EPR spin-spin distance study, Owenius, R., Jarl, A., Jonsson, B. H., Carlsson, U., and Hammarstrom, P. (2010) Journal of chemical biology 3, 127-139.

 

Luminescence and two-photon absorption cross section of novel oligomeric luminescent conjugated polythiophenes for diagnostics of amyloid fibrils Lindgren, M. Glimsdal, E. Åslund, A. Simon, R., Hammarström, P., Nilsson, P. (2010) Nonlinear Optics Quantum Optics 40, 241-251

 

Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates, Almstedt, K., Nystrom, S., Nilsson, K. P., and Hammarstrom, P. (2009) Prion 3, 224-235.

 

Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses, Aslund, A., Sigurdson, C. J., Klingstedt, T., Grathwohl, S., Bolmont, T., Dickstein, D. L., Glimsdal, E., Prokop, S., Lindgren, M., Konradsson, P., Holtzman, D. M., Hof, P. R., Heppner, F. L., Gandy, S., Jucker, M., Aguzzi, A., Hammarstrom, P., and Nilsson, K. P. (2009) ACS chemical biology 4, 673-684.

 

Protein folding, misfolding and disease, Hammarstrom, P. (2009) FEBS letters 583, 2579-2580.

 

Small-molecule suppression of misfolding of mutated human carbonic anhydrase II linked to marble brain disease, Almstedt, K., Rafstedt, T., Supuran, C. T., Carlsson, U., and Hammarstrom, P. (2009) Biochemistry 48, 5358-5364.

 

Modeling familial amyloidotic polyneuropathy (Transthyretin V30M) in Drosophila melanogaster, Berg, I., Thor, S., and Hammarstrom, P. (2009) Neuro-degenerative diseases 6, 127-138.

 

A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding, Moparthi, S. B., Hammarstrom, P., and Carlsson, U. (2009) Protein science : a publication of the Protein Society 18, 475-479.

 

A highly insoluble state of Abeta similar to that of Alzheimer's disease brain is found in Arctic APP transgenic mice, Philipson, O., Hammarstrom, P., Nilsson, K. P., Portelius, E., Olofsson, T., Ingelsson, M., Hyman, B. T., Blennow, K., Lannfelt, L., Kalimo, H., and Nilsson, L. N. (2009) Neurobiology of aging 30, 1393-1405.

 

Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture, Sorgjerd, K., Klingstedt, T., Lindgren, M., Kagedal, K., and Hammarstrom, P. (2008) Biochemical and biophysical research communications 377, 1072-1078.

 

Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation, Maas, C., Govers-Riemslag, J. W., Bouma, B., Schiks, B., Hazenberg, B. P., Lokhorst, H. M., Hammarstrom, P., ten Cate, H., de Groot, P. G., Bouma, B. N., and Gebbink, M. F. (2008) The Journal of clinical investigation 118, 3208-3218.

 

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, Sjoberg, A. P., Nystrom, S., Hammarstrom, P., and Blom, A. M. (2008) Molecular immunology 45, 3213-3221.

 

A conformationally isoformic thermophilic protein with high kinetic unfolding barriers, Mishra, R., Olofsson, L., Karlsson, M., Carlsson, U., Nicholls, I. A., and Hammarstrom, P. (2008) Cellular and molecular life sciences : CMLS 65, 827-839.

 

Luminescent conjugated polymers: Illuminating the Dark Matters of Biology and Pathology Nilsson, K. P. R., and Hammarström, P.  (2008) Advanced  Materials 20:2639-2645

 

Thermodynamic interrogation of a folding disease. Mutant mapping of position 107 in human carbonic anhydrase II linked to marble brain disease, Almstedt, K., Martensson, L. G., Carlsson, U., and Hammarstrom, P. (2008) Biochemistry 47, 1288-1298.

 

Prion strain discrimination using luminescent conjugated polymers, Sigurdson, C. J., Nilsson, K. P., Hornemann, S., Manco, G., Polymenidou, M., Schwarz, P., Leclerc, M., Hammarstrom, P., Wuthrich, K., and Aguzzi, A. (2007) Nature methods 4, 1023-1030.

 

Studies of luminescent conjugated polythiophene derivatives: enhanced spectral discrimination of protein conformational states, Aslund, A., Herland, A., Hammarstrom, P., Nilsson, K. P., Jonsson, B. H., Inganas, O., and Konradsson, P. (2007) Bioconjugate chemistry 18, 1860-1868.

 

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), Villebeck, L., Moparthi, S. B., Lindgren, M., Hammarstrom, P., and Jonsson, B. H. (2007) Biochemistry 46, 12639-12647.

 

Imaging distinct conformational states of amyloid-beta fibrils in Alzheimer's disease using novel luminescent probes, Nilsson, K. P., Aslund, A., Berg, I., Nystrom, S., Konradsson, P., Herland, A., Inganas, O., Stabo-Eeg, F., Lindgren, M., Westermark, G. T., Lannfelt, L., Nilsson, L. N., and Hammarstrom, P. (2007) ACS chemical biology 2, 553-560.

 

The bloody path of amyloids and prions, Hammarstrom, P. (2007) Journal of thrombosis and haemostasis : JTH 5, 1136-1138.

 

Conformational rearrangements of tail-less complex polypeptide 1 (TCP-1) ring complex (TRiC)-bound actin, Villebeck, L., Persson, M., Luan, S. L., Hammarstrom, P., Lindgren, M., and Jonsson, B. H. (2007) Biochemistry 46, 5083-5093.

 

Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion, Mishra, R., Sorgjerd, K., Nystrom, S., Nordigarden, A., Yu, Y. C., and Hammarstrom, P. (2007) Journal of molecular biology 366, 1029-1044.

 

Conjugated polyelectrolytes--conformation-sensitive optical probes for staining and characterization of amyloid deposits, Nilsson, K. P., Hammarstrom, P., Ahlgren, F., Herland, A., Schnell, E. A., Lindgren, M., Westermark, G. T., and Inganas, O. (2006) Chembiochem 7, 1096-1104.

 

Retention of misfolded mutant transthyretin by the chaperone BiP/GRP78 mitigates amyloidogenesis, Sorgjerd, K., Ghafouri, B., Jonsson, B. H., Kelly, J. W., Blond, S. Y., and Hammarstrom, P. (2006) Journal of molecular biology 356, 469-482.

 

The cyclooxygenase-2 inhibitor celecoxib is a potent inhibitor of human carbonic anhydrase II, Knudsen, J. F., Carlsson, U., Hammarstrom, P., Sokol, G. H., and Cantilena, L. R. (2004) Inflammation 28, 285-290.

 

Activity, folding, misfolding, and aggregation in vitro of the naturally occurring human tissue factor mutant R200W, Wirehn, J., Carlsson, K., Herland, A., Persson, E., Carlsson, U., Svensson, M., and Hammarstrom, P. (2005) Biochemistry 44, 6755-6763.

 

The biological and chemical basis for tissue-selective amyloid disease, Sekijima, Y., Wiseman, R. L., Matteson, J., Hammarstrom, P., Miller, S. R., Sawkar, A. R., Balch, W. E., and Kelly, J. W. (2005) Cell 121, 73-85.

 

Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy, Lindgren, M., Sorgjerd, K., and Hammarstrom, P. (2005) Biophysical journal 88, 4200-4212.

 

Conjugated polyelectrolytes: conformation-sensitive optical probes for detection of amyloid fibril formation, Nilsson, K. P., Herland, A., Hammarstrom, P., and Inganas, O. (2005) Biochemistry 44, 3718-3724.

 

Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH, Herland, A., Nilsson, K. P., Olsson, J. D., Hammarstrom, P., Konradsson, P., and Inganas, O. (2005) Journal of the American Chemical Society 127, 2317-2323.

 

Unfolding a folding disease: folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II, Almstedt, K., Lundqvist, M., Carlsson, J., Karlsson, M., Persson, B., Jonsson, B. H., Carlsson, U., and Hammarstrom, P. (2004) Journal of molecular biology 342, 619-633.

 

Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase, Boren, K., Grankvist, H., Hammarstrom, P., and Carlsson, U. (2004) FEBS letters 566, 95-99.

 

D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis? Hammarstrom, P., Sekijima, Y., White, J. T., Wiseman, R. L., Lim, A., Costello, C. E., Altland, K., Garzuly, F., Budka, H., and Kelly, J. W. (2003) Biochemistry 42, 6656-6663.

 

Energetic characteristics of the new transthyretin variant A25T may explain its atypical central nervous system pathology, Sekijima, Y., Hammarstrom, P., Matsumura, M., Shimizu, Y., Iwata, M., Tokuda, T., Ikeda, S., and Kelly, J. W. (2003) Laboratory investigation; a journal of technical methods and pathology 83, 409-417.

 

Prevention of transthyretin amyloid disease by changing protein misfolding energetics, Hammarstrom, P., Wiseman, R. L., Powers, E. T., and Kelly, J. W. (2003) Science (New York, N.Y 299, 713-716.

 

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity, Hammarstrom, P., Jiang, X., Hurshman, A. R., Powers, E. T., and Kelly, J. W. (2002) Proceedings of the National Academy of Sciences of the United States of America 99 Suppl 4, 16427-16432.

 

Phase memory relaxation times of spin labels in human carbonic anhydrase II: pulsed EPR to determine spin label location, Huber, M., Lindgren, M., Hammarstrom, P., Martensson, L. G., Carlsson, U., Eaton, G. R., and Eaton, S. S. (2001) Biophysical chemistry 94, 245-256.

 

Trans-suppression of misfolding in an amyloid disease, Hammarstrom, P., Schneider, F., and Kelly, J. W. (2001) Science (New York, N.Y 293, 2459-2462.

 

Anion shielding of electrostatic repulsions in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy, Hammarstrom, P., Jiang, X., Deechongkit, S., and Kelly, J. W. (2001) Biochemistry 40, 11453-11459.

 

An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured, Jiang, X., Smith, C. S., Petrassi, H. M., Hammarstrom, P., White, J. T., Sacchettini, J. C., and Kelly, J. W. (2001) Biochemistry 40, 11442-11452.

 

Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins, Schneider, F., Hammarstrom, P., and Kelly, J. W. (2001) Protein science : a publication of the Protein Society 10, 1606-1613.

 

Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II, Persson, M., Harbridge, J. R., Hammarstrom, P., Mitri, R., Martensson, L. G., Carlsson, U., Eaton, G. R., and Eaton, S. S. (2001) Biophysical journal 80, 2886-2897.

 

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, Hammarstrom, P., Owenius, R., Martensson, L. G., Carlsson, U., and Lindgren, M. (2001) Biophysical journal 80, 2867-2885.

 

Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL, Hammarstrom, P., Persson, M., and Carlsson, U. (2001) The Journal of biological chemistry 276, 21765-21775.

 

Cofactor-induced refolding: refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II), Andersson, D., Hammarstrom, P., and Carlsson, U. (2001) Biochemistry 40, 2653-2661.

 

Is the unfolded state the Rosetta Stone of the protein folding problem?, Hammarstrom, P., and Carlsson, U. (2000) Biochemical and biophysical research communications 276, 393-398.

 

Protein substrate binding induces conformational changes in the chaperonin GroEL. A suggested mechanism for unfoldase activity, Hammarstrom, P., Persson, M., Owenius, R., Lindgren, M., and Carlsson, U. (2000) The Journal of biological chemistry 275, 22832-22838.

 

Structural mapping of an aggregation nucleation site in a molten globule intermediate, Hammarstrom, P., Persson, M., Freskgard, P. O., Martensson, L. G., Andersson, D., Jonsson, B. H., and Carlsson, U. (1999) The Journal of biological chemistry 274, 32897-32903.

 

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, Persson, M., Hammarstrom, P., Lindgren, M., Jonsson, B. H., Svensson, M., and Carlsson, U. (1999) Biochemistry 38, 432-441.

 

Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II, Hammarstrom, P., Kalman, B., Jonsson, B. H., and Carlsson, U. (1997) FEBS letters 420, 63-68.

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Last updated: 2010-02-08