Per Hammarström

9.2k total citations
145 papers, 7.2k citations indexed

About

Per Hammarström is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Per Hammarström has authored 145 papers receiving a total of 7.2k indexed citations (citations by other indexed papers that have themselves been cited), including 96 papers in Molecular Biology, 72 papers in Physiology and 24 papers in Materials Chemistry. Recurrent topics in Per Hammarström's work include Alzheimer's disease research and treatments (71 papers), Prion Diseases and Protein Misfolding (36 papers) and Amyloidosis: Diagnosis, Treatment, Outcomes (25 papers). Per Hammarström is often cited by papers focused on Alzheimer's disease research and treatments (71 papers), Prion Diseases and Protein Misfolding (36 papers) and Amyloidosis: Diagnosis, Treatment, Outcomes (25 papers). Per Hammarström collaborates with scholars based in Sweden, United States and Norway. Per Hammarström's co-authors include Jeffery W. Kelly, K. Peter R. Nilsson, Mikaël Lindgren, Sofie Nyström, Evan T. Powers, R. Luke Wiseman, Karin Sörgjerd, Uno Carlsson, Frank Schneider and Olle Inganäs and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Per Hammarström

144 papers receiving 7.1k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Per Hammarström Sweden 45 4.5k 3.2k 1.1k 995 697 145 7.2k
Niccolò Taddei Italy 46 6.6k 1.5× 3.6k 1.1× 1.7k 1.6× 1.1k 1.1× 774 1.1× 112 9.1k
Evan T. Powers United States 52 7.2k 1.6× 2.5k 0.8× 850 0.8× 2.1k 2.1× 588 0.8× 108 9.9k
Jesús Zurdo United Kingdom 28 5.6k 1.2× 3.8k 1.2× 1.1k 1.1× 668 0.7× 1.2k 1.7× 35 7.2k
Wolfgang Hoyer Germany 31 2.8k 0.6× 3.4k 1.1× 537 0.5× 440 0.4× 753 1.1× 73 5.8k
K. Peter R. Nilsson Sweden 48 4.1k 0.9× 3.5k 1.1× 1.6k 1.5× 384 0.4× 1.2k 1.8× 189 8.6k
Ralf Langen United States 58 6.4k 1.4× 3.1k 1.0× 1.1k 1.0× 2.1k 2.1× 545 0.8× 128 10.2k
Marcus Fändrich Germany 52 7.2k 1.6× 6.4k 2.0× 1.1k 1.0× 708 0.7× 1.9k 2.8× 131 10.5k
David Eliezer United States 57 4.7k 1.0× 3.5k 1.1× 1.2k 1.1× 1.9k 1.9× 308 0.4× 125 10.2k
Ronald Wetzel United States 69 11.8k 2.6× 5.2k 1.6× 1.5k 1.4× 1.1k 1.1× 1.3k 1.9× 166 15.0k
Gunilla T. Westermark Sweden 46 5.2k 1.2× 4.5k 1.4× 370 0.3× 1.4k 1.4× 693 1.0× 153 9.4k

Countries citing papers authored by Per Hammarström

Since Specialization
Citations

This map shows the geographic impact of Per Hammarström's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Per Hammarström with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Per Hammarström more than expected).

Fields of papers citing papers by Per Hammarström

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Per Hammarström. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Per Hammarström. The network helps show where Per Hammarström may publish in the future.

Co-authorship network of co-authors of Per Hammarström

This figure shows the co-authorship network connecting the top 25 collaborators of Per Hammarström. A scholar is included among the top collaborators of Per Hammarström based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Per Hammarström. Per Hammarström is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Westermark, Gunilla T., et al.. (2025). The question of strains in AA amyloidosis. Scientific Reports. 15(1). 3684–3684.
2.
Wegenast‐Braun, Bettina M., Mathias Jucker, Takashi Saito, et al.. (2024). Divergent Age-Dependent Conformational Rearrangement within Aβ Amyloid Deposits in APP23, APPPS1, and App NL-F Mice. ACS Chemical Neuroscience. 15(10). 2058–2069. 5 indexed citations
3.
Swaminathan, Parasuraman, Therése Klingstedt, Hjalte Gram, et al.. (2024). In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging. International Journal of Molecular Sciences. 25(22). 12458–12458. 2 indexed citations
4.
Johansson, Lovisa, et al.. (2024). Amyloid beta 1‐40 and 1‐42 fibril ratios and maturation level cause conformational differences with minimal impact on autophagy and cytotoxicity. Journal of Neurochemistry. 168(9). 3308–3322. 2 indexed citations
5.
6.
Knight, Ashley C., Daniel Sohn, Junchao Tong, et al.. (2021). Radiosynthesis, In Vitro and In Vivo Evaluation of [18F]CBD-2115 as a First-in-Class Radiotracer for Imaging 4R-Tauopathies. ACS Chemical Neuroscience. 12(4). 596–602. 36 indexed citations
7.
Bäck, Marcus, Robert Selegård, Sofie Nyström, et al.. (2020). Tyrosine Side‐Chain Functionalities at Distinct Positions Determine the Chirooptical Properties and Supramolecular Structures of Pentameric Oligothiophenes. ChemistryOpen. 9(11). 1100–1108. 4 indexed citations
8.
Ling, Helen, Marla Gearing, Beth A. Dombroski, et al.. (2020). Fibrillation and molecular characteristics are coherent with clinical and pathological features of 4-repeat tauopathy caused by MAPT variant G273R. Neurobiology of Disease. 146. 105079–105079. 4 indexed citations
9.
Michno, Wojciech, Sofie Nyström, Tammaryn Lashley, et al.. (2019). Pyroglutamation of amyloid-βx-42 (Aβx-42) followed by Aβ1–40 deposition underlies plaque polymorphism in progressing Alzheimer’s disease pathology. Journal of Biological Chemistry. 294(17). 6719–6732. 53 indexed citations
10.
Åslund, Andreas, Frédéric Lerouge, Sofie Nyström, et al.. (2018). Two-Photon Fluorescence and Magnetic Resonance Specific Imaging of Aβ Amyloid Using Hybrid Nano-GdF3 Contrast Media. ACS Applied Bio Materials. 1(2). 462–472. 19 indexed citations
11.
Michno, Wojciech, Ibrahim Kaya, Sofie Nyström, et al.. (2018). Multimodal Chemical Imaging of Amyloid Plaque Polymorphism Reveals Aβ Aggregation Dependent Anionic Lipid Accumulations and Metabolism. Analytical Chemistry. 90(13). 8130–8138. 42 indexed citations
12.
Schütz, Anne K., Simone Hornemann, Marielle Aulikki Wälti, et al.. (2017). Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore. ACS Chemical Neuroscience. 9(3). 475–481. 32 indexed citations
13.
Prokop, Stefan, Frank L. Heppner, Peter Konradsson, et al.. (2013). Enhanced Fluorescent Assignment of Protein Aggregates by an Oligothiophene–Porphyrin‐Based Amyloid Ligand. Macromolecular Rapid Communications. 34(9). 723–730. 25 indexed citations
14.
Lord, Anna, Ola Philipson, Therése Klingstedt, et al.. (2011). Observations in APP Bitransgenic Mice Suggest that Diffuse and Compact Plaques Form via Independent Processes in Alzheimer's Disease. American Journal Of Pathology. 178(5). 2286–2298. 33 indexed citations
15.
Mishra, Rajesh, et al.. (2011). Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dyeNile red. Molecular BioSystems. 7(4). 1232–1240. 124 indexed citations
16.
Lindgren, Mikaël & Per Hammarström. (2010). Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states. FEBS Journal. 277(6). 1380–1388. 86 indexed citations
17.
18.
Sekijima, Yoshiki, R. Luke Wiseman, Jeanne Matteson, et al.. (2005). The Biological and Chemical Basis for Tissue-Selective Amyloid Disease. Cell. 121(1). 73–85. 391 indexed citations
19.
Hammarström, Per, et al.. (2002). Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. Proceedings of the National Academy of Sciences. 99(suppl_4). 16427–16432. 296 indexed citations
20.
Hammarström, Per, Malin Persson, & Uno Carlsson. (2000). Compactness measurements at unfolding of carbonic anhydrase by Trp-AEDANS fluorescence energy transfer. Evidence for forced unfolding by GroEL.. Biophysical Journal. 78(1). 1 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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