Dr. Jinghui Luo

In neurodegenerative diseases like Alzheimer’s (AD) and Parkinson’s (PD), proteins such as Aβ and α-synuclein can misfold and form toxic, transient oligomers before aggregating into insoluble fibrils. These oligomers disrupt cellular function—often by damaging membranes—and play a central role in disease progression. However, their highly dynamic and heterogeneous nature makes them difficult to study and target therapeutically. At PSI, my group is addressing this challenge by applying nanopore engineering and single-molecule trapping to investigate how these oligomers form and behave. We recently engineered stable and uniform Aβ oligomers by grafting Alzheimer’s peptides onto the α-hemolysin (αHL) nanopore scaffold. These synthetic oligomers closely mimic the toxic properties of native ones and, crucially, have a defined structure confirmed by cryo-EM. This opens up exciting possibilities for structural analysis, drug screening, and antibody development targeting specific oligomer conformations. In parallel, we've used nanopore trapping techniques to dissect the membrane-binding kinetics of α-synuclein and how these interactions are influenced by metal ions and therapeutic helix mimetics. Our studies have also revealed unique oligomeric equilibrium behaviors of peptides that are relevant not only for amyloid research but also for understanding supermolecular assembly and cellular function more broadly. Together, our work advances both the fundamental understanding of protein oligomer formation and the development of novel nanopore-based tools for biomedical research, diagnostics, and therapeutic discovery.

• _{Chang Liu, Yoav Dan, Ji Yun, Lihi Adler-Abramovich, Jinghui Luo*. Unveiling the Assembly Transition of Di-phenylalanine and its Analogs: From Oligomer Equilibrium to Nanocluster Formation. ACS Nano (in press). https://doi.org/10.1021/acsnano.5c00433}
• _{Chang Liu, Anja Henning-Knechtel, Nicklas Österlund, Jinming Wu, Guangshun Wang, Astrid Gräslund, Serdal Kirmizialtin, Jinghui Luo*. Oligomer Dynamics of LL-37 Truncated Fragments Probed by α-Hemolysin Pore and Molecular Simulations. Small, 2023, 12: e2206232.}
• _{Chang Liu, Jinghui Luo*. Advances in Oligomer Engineering and Design: From Biological Function, Toxicity to Application. Angewandte Chemie International Edition, 2023, e202216480.}
• _{Jinming Wu, Tohru Yamashita, Andrew David Hamilton, Sam Thompson, Jinghui Luo*. Single-Molecule Nanopore Dielectrophoretic Trapping of α-Synuclein with Lipid Membranes. Cell Reports Physical Science, 2023, 4: 101243.}
• _{Jinming Wu, Thorsten B. Blum, Daniel P. Farrell, Frank DiMaio, Jan Pieter Abrahams, Jinghui Luo*. Cryo-Electron Microscopy Imaging of Alzheimer's Amyloid-β42 Oligomer Displayed on a Functionally and Structurally Relevant Scaffold. Angewandte Chemie International Edition, 2021, doi:10.1002/anie.202104497.}
• _{Jinming Wu, Chan Cao, Rolf Antonie Loch, Ann Tiiman, Jinghui Luo*. Single-Molecule Studies of Amyloid Proteins: From Biophysical Properties to Diagnostic Perspectives. Quarterly Reviews of Biophysics, 2020, 53: e12.}

(2) Exploring the Molecular Foundations of Neurodegeneration by using X-ray Spectroscopy, Scattering and Imaging Techniques

A growing body of evidence underscores the pivotal role of early-stage amyloid protein condensation in driving fibril formation in vitro. However, how disease-associated molecules modulate this transition—either by promoting or preventing condensation—in vivo remains largely unresolved. At the Paul Scherrer Institute (PSI), we have leveraged a suite of X-ray spectroscopy, scattering, and imaging techniques to investigate this transition in detail. Our focus has been on amyloidogenic proteins such as Tau and their interactions with molecular partners, including heat shock protein 90 (Hsp90), small-molecule compounds, and various metal ions. Through these studies, we have elucidated the molecular mechanisms by which these partners influence amyloid aggregation. This includes their effects on the kinetics of conformational transitions from intrinsically disordered monomers to β-sheet-rich aggregates, as well as the toxicological profiles of intermediate oligomeric species, using established biophysical and biochemical methods. Time-resolved small-angle X-ray scattering (SAXS) has enabled us to capture rapid changes in the radius of gyration of amyloid protein monomers at the millisecond timescale, providing insight into early condensation or oligomerization dynamics.

In collaboration with the Xtreme beamline at the Swiss Light Source, we apply soft X-ray spectroscopy to simultaneously probe the electronic structures of Alzheimer’s disease–related copper ions and amyloid peptides/proteins at the N K and Cu L₂,₃ absorption edges. Our findings reveal a distinct Cu(I) spectroscopic signature indicative of peptide/protein coordination, offering a potential biomarker for pathological metal states and a mechanistic link to reactive oxygen species (ROS) generation. 

Building on these biochemical and spectroscopic insights, we are now extending our investigations to the spatial and mesoscale dimensions of amyloid condensation and metal/compound interactions in disease-relevant contexts. Using tomographic and correlative imaging approaches, we aim to reconstruct the ultrastructural organization of amyloid condensates and associated cellular organelles, and correlate these with metal ion deposition in Alzheimer’s and Parkinson’s disease brain tissue, transgenic mouse models, and live C. elegans. These efforts are supported by collaborations with the Tomcat, SIM, and Pollux beamlines, as well as the application of light-sheet fluorescence microscopy for 3D correlative imaging.

This integrated platform allows us to spatially resolve both the oxidation states of metals and the distribution of amyloid aggregates at nanometer resolution—bridging molecular events with mesoscale pathological manifestations. By linking metal chemistry, amyloid structure, and cellular context, our work aims to uncover new mechanistic pathways in neurodegeneration. Ultimately, this interdisciplinary research provides a foundational framework for the development of diagnostic tools and targeted therapeutic strategies for neurodegenerative diseases such as Alzheimer’s and Parkinson’s.

• _{Rebecca Sternke-Hoffmann, Xun Sun, Andreas Menzel, Miriam Dos Santos Pinto, Urte Venclovaite, Michael Wördehoff, Wolfgang Hoyer, Wenwei Zheng*, Jinghui Luo*. Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions. Advanced Science, 2024, Jul 7: e2308279.}
• _{Jinming Wu, Nicklas Österlund, Hongzhi Wang, Rebecca Sternke-Hoffmann, Astrid Gräslund, Jinghui Luo*. Identifying the Role of Co-Aggregation of Alzheimer’s Amyloid-β with Amorphous Protein Aggregates of Non-Amyloid Proteins. Cell Reports Physical Science, 2022, 3: 101028.}
• _{Jinghui Luo*, Hongzhi Wang, Jinming Wu, Vladyslav Romankov, Niéli Daffé, Jan Dreiser*. Amyloid-β–Copper Interaction Studied by Simultaneous Nitrogen K and Copper L₂,₃-Edge Soft X-ray Absorption Spectroscopy. iScience, 2021, 24: 103465.}
• _{Hongzhi Wang, Max Lallemang, Bianca Hermann, Cecilia Wallin, Rolf Loch, Alain Blanc, Bizan N. Balzer, Thorsten Hugel, Jinghui Luo*. ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation. Journal of Molecular Biology, 2021, 433(2): 166717.}
• _{Cecilia Wallin, Yoshitaka Hiruma, Sebastian K T S Wärmländer, Isabelle Huvent, Jüri Jarvet, Jan Pieter Abrahams, Astrid Gräslund, Guy Lippens, Jinghui Luo *. The Neuronal Tau Protein Blocks In Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage. Journal of the American Chemical Society, 2018, 140: 8138–8146.}
  
   

• Dimitris Lymperopoulos, (2024, Trainee, next destination: Freiburg University)
• Miriam Pinto, (2023-2024, Trainee, next destination: Roche)
• Ariane Melissa Schwitter,  (2024, Guest Ph.D student from the University of Tokyo)
• Sigrid Kirss,  (2024, Guest Ph.D student from Tallin University of Technology
• Duan Fangyuan, (2022, Guest Ph.D student from Harbin Institute of Technology)
• Jinming Wu, (2018-2022, Ph.D student, next destination: Lund University)
• Hongzhi Wang, (2018-2021, Ph.D student, next destination: Chinese Academy of Sciences)
• Hegne Pupart, (2018, Summer intern, next destination: Ph.D student at Tallinn University of Technology)

• Pathogenic mutation ΔK280 promotes hydrophobic interactions involving microtubule-binding domain and enhances liquid-liquid phase separation of tau.
  Yujie Chen, Xun Sun, Yiming Tang, Yuan Tan, Cong Guo, Tong Pan, Xuefeng Zhang, Jinghui Luo*, Guanghong Wei*. 
  Small. 2024 Oct 18:e2406429. 
  DOI: 10.1002/smll.202406429.

   

• Phase Separation and Aggregation of α-Synuclein diverge at different salt conditions. 
  Rebecca Sternke-Hoffmann, Xun Sun, Andreas Menzel, Miriam Dos Santos Pinto, Urte Venclovaite, Michael Wördehoff, Wolfgang Hoyer, Wenwei Zheng*, Jinghui Luo*. 
  Advanced Science. 2024 Jul 7:e2308279.
  DOI:10.1002/advs.202308279.

   

• Self-Adaptive Synthesis of Non-Covalent Crosslinkers while Folding Single-Chain Polymers. 
  Dawei Qi, Xuncheng Shi, Caihong Lin, Ferdinand Holzhausen, Liljeström Ville, Xun Su, Jinghui Luo, Leena Pitkänen , Ya Zhu, Jessica Rosenholm, Sirpa Jalkanen, Jianwei Li. 
  Angew Chem Int Ed Engl. 2024. 29:e202408670.
  DOI:10.1002/anie.202408670.

   

• Channel Activities of the Full-Length Prion and Truncated Proteins.
  Jinming Wu, Xue Wang, Asvin Lakkaraju, Rebecca Sternke-Hoffmann, Bilal M Qureshi, Adriano Aguzzi, Jinghui Luo*.
  ACS Chem Neurosci. 2024;15(1):98-107. 
  DOI:10.1021/acschemneuro.3c00412. 
   
• Visualizing alpha-synuclein and iron deposition in M83 mouse model of Parkinson's disease in vivo. 
  Nadja Straumann, Benjamin F Combes, Xose Luis Dean Ben, Rebecca Sternke-Hoffmann, Juan A Gerez, Ines Dias, Zhenyue Chen, Benjamin Watts, Iman Rostami, Kuangyu Shi, Axel Rominger, Christian R Baumann, Jinghui Luo, Daniela Noain, Roger M Nitsch, Nobuyuki Okamura, Daniel Razansky, Ruiqing Ni.  
  Brain Pathol. 2024 9:e13288. 
  DOI:10.1111/bpa.13288.

   

• Oligomer Dynamics of LL-37 Truncated Fragments Probed by α-Hemolysin Pore and Molecular Simulations.
  Chang Liu#, Anja Henning-Knechtel#, Nicklas Österlund, Jinming Wu, Guangshun Wang, Ruth Astrid Olivia Gräslund, Serdal Kirmizialtin, Jinghui Luo*
  Small, e2206232
  DOI:/10.1002/smll.202206232

   

• Protein Oligomer Engineering: A New Frontier for Studying Protein Structure, Function, and Toxicity.
  Chang Liu, Jinghui Luo*
  Angewandte Chemie, e202216480
  DOI:/10.1002/ange.202216480

   

• Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases
  Rolf Antonie Loch#, Hongzhi Wang#, Alex Perálvarez Marín, Philipp Berger, Henrietta Nielsen, Angeliki Chroni, Jinghui Luo*
  Computational and Structural Biotechnology Journal. 2023 20:21:1189-1204.
  DOI:10.1016/j.csbj.2023.01.022

   

• Single-molecule nanopore dielectrophoretic trapping of a-synuclein with lipid membranes
  Jinming Wu, Tohru Yamashita, Andrew D. Hamilton, Sam Thompson, Jinghui Luo*
  Cell Reports Physical Science, 4, 2023: 101243
  DOI:10.1016/j.xcrp.2022.101243
   

• Multivariate effects of pH, salt, and Zn2+ ions on Aβ40 fibrillation
  Hongzhi Wang, Jinming Wu, Rebecca Sternke-Hoffmann, Wenwei Zheng, Cecilia Mörman, Jinghui Luo*
  Communications Chemistry 5, 2022: 171
  DOI:10.1038/s42004-022-00786-1

   

• Identifying the role of co-aggregation of Alzheimer’s Amyloid-beta with amorphous protein aggregates of non-amyloid proteins
  Jinming Wu, Nicklas Österlund, Hongzhi Wang, Rebecca Sternke-Hoffmann, Hegne Pupart, Leopold L. Ilag,  Astrid Gräslund, Jinghui Luo* 
  Cell Reports Physical Science, 3, 2022: 101028
  DOI:110.1016/j.xcrp.2022.101028

   

• Evaluation of Zn2+- and Cu2+-Binding Affinities of Native Cu,Zn-SOD1 and Its G93A Mutant by LC-ICP MS
  Julia Smirnova, Julia Gavrilova, Andra Noormägi, Karin Valmsen, Hegne Pupart, Jinghui Luo, Vello Tõugu, Peep Palumaa
  Molecules, 27, 2022: 3160
  DOI:10.3390/molecules27103160

   

• Cu2+ ions modulate the interaction between α-synuclein and lipid membranes
  Hongzhi Wang, Cecilia Mörman, Rebecca Sternke-Hoffmann, Chia-Ying Huang, Andrea Prota, Pikyee Ma, Jinghui Luo*
  Journal of Inorganic Biochemistry, 236, 2022: 111945
  DOI:10.1016/j.jinorgbio.2022.111945

   

• Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation
  Clementine E Bavinton, Rebecca Sternke-Hoffmann, Tohru Yamashita, Peter C Knipe, Andrew D Hamilton, Jinghui Luo*, Sam Thompson*
  Chemical Communications, 58, 2022: 5132-5135
  DOI:10.1039/D2CC00212D

• Editorial: The Biochemistry of Amyloids in Neurodegenerative Diseases, Volume I
  Gomes C*, Hoyer W*, Luo J*.
  Frontiers in Neuroscience, 819481, 2021 
  DOI:10.3389/fnins.2021.819481

   

• Amyloid-beta–copper interaction studied by simultaneous nitrogen K and copper L2,3- edge soft X-ray absorption spectroscopy
  Luo J*,  Wang H, Wu J, Romankov V, Daffe N,  Dreiser J*
  iScience 24, 103465, 2021 
  DOI:10.1016/j.isci. 2021.103465

   

• Cryo-electron microscopy imaging of Alzheimer's amyloid-beta 42 oligomer displayed on a functionally and structurally relevant scaffold
  Wu J, Blum TB, Farrell DP, DiMaio F, Abrahams JP, Luo J*.
  Angew Chem Int Ed Engl. 2021 May 27.
  DOI:10.1002/anie.202104497.

   

• ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation
  Wang H , Lallemang M , Hermann B , Wallin C , Loch R, Blanc A, Balzer BN, Hugel T, Luo J*
  Journal of Molecular Biology 433 (2), 166717 (2021).
  DOI:10.1016/j.jmb.2020.11.016
   

• Antimicrobial Peptide Mimetics Based on a Diphenylacetylene Scaffold: Synthesis, Conformational Analysis, and Activity
  Peacock H, Henriques ST, Benfield AH, Elliott AG, Luo J, J Luccarelli, Nagano M, Craik D, Hamilton A
  ChemMedChem. 15 (20), 1932-1939 (2020).
  DOI: 10.1002/cmdc.202000474
   
• Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives
  Wu J, Cao C, Loch RA, Tiiman A, Luo J*
  Quarterly Reviews of Biophysics. 53:e12 (2020).
  DOI: 10.1017/S0033583520000086

• Nuclear Pore Membrane Proteins Self-Assemble into Nanopores Panatala R, Barbato S, Kozai T, Luo J, Kapinos Larisa E, Lim Roderick YH

  BIOCHEMISTRY 58, 484 (2019).

  DOI: 10.1021/acs.biochem.8b01179

• Membrane-mimetic systems for biophysical studies of the amyloid-beta peptide 
  Österlund N, Luo J, Wärmländer Sebastian KTS, Gräslund A
  BIOCHIMICA ET BIOPHYSICA ACTA (BBA) - PROTEINS AND PROTEOMICS , S1570963918302036 (2018).
  DOI: 10.1016/j.bbapap.2018.11.005
• The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-beta Peptide at the Oligomeric Stage.
  Wallin C, Hiruma Y, Wärmländer SKTS, Huvent I, Jarvet J, Abrahams J, Gräslund A, Lippens G, Luo J
  Journal of the American Chemical Society 140, 8138 (2018).
  DOI: 10.1021/jacs.7b13623

• Alzheimer'ss disease and cigarette smoke components: effects of nicotine, PAHs, and Cd(II), Cr(III), Pb(II), Pb(IV) ions on amyloid-beta peptide aggregation 
  Wallin C, Sholts Sabrina B, Österlund N, Luo J, Jarvet J, Roos Per M, Ilag L, Gräslund A, Wärmländer Sebastian KTS
  Scientific Reports 7, 14423 (2017).
  DOI: 10.1038/s41598-017-13759-5
• Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin Pavicevic A, Luo J, Popovic-Bijelic A, Mojovic M
  European Biophysics Journal 46, 773 (2017).
  DOI: 10.1007/s00249-017-1257-z

• Characterization of Mn(II) ion binding to the amyloid-beta peptide in Alzheimer's disease. 
  Wallin C, Kulkarni Yashraj S, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams J, Sholts Sabrina B, Roos Per M, Kamerlin Shina CL, Gräslund A, Wärmländer Sebastian KTS
  JOURNAL OF TRACE ELEMENTS IN MEDICINE AND BIOLOGY, (2016).
  DOI: 10.1016/j.jtemb.2016.03.009
• Cross-interactions between the Alzheimer Disease Amyloid-? Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis. 
  Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
  JOURNAL OF BIOLOGICAL CHEMISTRY 291, 16485 (2016).
  DOI: 10.1074/jbc.R116.714576
• Non-covalent S?O interactions control conformation in a scaffold that disrupts islet amyloid polypeptide fibrillation Peacock H, Luo J, Yamashita T, Luccarelli J, Thompson S, Hamilton Andrew D
  CHEMICAL SCIENCE 7, 6435 (2016).
  DOI: 10.1039/C6SC00756B
• Reciprocal Molecular Interactions between the A? Peptide Linked to Alzheimer?s Disease and Insulin Linked to Diabetes Mellitus Type II.
  Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
  ACS Chemical Neuroscience 7, 269 (2016).
  DOI: 10.1021/acschemneuro.5b00325
• Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.
   Tiiman A, Luo J, Wallin C, Olsson L, Lindgren J, Jarvet J, Per R, Sholts Sabrina B, Rahimipour S, Abrahams J, Karlström A, Gräslund A, Wärmländer Sebastian KTS
  Journal of Alzheimer's Disease 54, 971 (2016).
  DOI: 10.3233/JAD-160427
• The Amyloid-beta Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions Wallin C, Luo J, Jarvet J, Wärmländer Sebastian KTS, Gräslund A
  ISRAEL JOURNAL OF CHEMISTRY 57, 674 (2016).
  DOI: 10.1002/ijch.201600105

• Alzheimer Peptides Aggregate into Transient Nanoglobules That Nucleate Fibrils 
  Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
  BIOCHEMISTRY 53, 6302 (2014).
  DOI: 10.1021/bi5003579
• Cyclic Peptides as Inhibitors of Amyloid Fibrillation 
  Luo J, Abrahams J
  CHEMISTRY - A EUROPEAN JOURNAL 20, 2410 (2014).
  DOI: 10.1002/chem.201304253
• Endogenous Polyamines Reduce the Toxicity of Soluble A? Peptide Aggregates Associated with Alzheimer's Disease Luo J, Mohammed I, Wärmländer Sebastian KTS, Hiruma Y, Gräslund A, Abrahams J
  BIOMACROMOLECULES 15, 1985 (2014).
  DOI: 10.1021/bm401874j
• Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide 
  Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
  JOURNAL OF BIOLOGICAL CHEMISTRY 289, 27766 (2014).
  DOI: 10.1074/jbc.M114.574947
• The Abeta peptide forms non-amyloid fibrils in the presence of carbon nanotubes 
  Luo J, Waermlaender Sebastian KTS, Yu C, Muhammad K, Graeslund A, Abrahams JP
  NANOSCALE 6, 6720 (2014).
  DOI: 10.1039/c4nr00291a
• The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway Abelein A, Abrahams J, Danielsson J, Gräslund A, Jarvet J, Luo J, Tiiman A, Wärmländer Sebastian KTS
  JBIC JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY 19, 623 (2014).
  DOI: 10.1007/s00775-014-1131-8

• An efficient nanolitre-volume multi-channel device for highly viscous materials used in membrane protein crystallization Luo J, Zwier R, Abrahams J
  JOURNAL OF APPLIED CRYSTALLOGRAPHY 46, 829 (2013).
  DOI: 10.1107/S0021889813006742
• Biophysical Studies of the Amyloid ?-Peptide: Interactions with Metal Ions and Small Molecules Wärmländer S, Tiiman A, Abelein A, Luo J, Jarvet J, Söderberg Kajsa L, Danielsson J, Gräslund A
  CHEMBIOCHEM 14, 1692 (2013).
  DOI: 10.1002/cbic.201300262
• Cellular Polyamines Promote Amyloid-Beta (A?) Peptide Fibrillation and Modulate the Aggregation Pathways 
  Luo J, Yu C, Yu H, Borstnar R, Kamerlin Shina CL, Gräslund A, Abrahams J, Wärmländer Sebastian KTS
  ACS Chemical Neuroscience 4, 454 (2013).
  DOI: 10.1021/cn300170x
• Exploiting preQ 1 Riboswitches To Regulate Ribosomal Frameshifting 
  Yu C, Luo J, Iwata-Reuyl D, Olsthoorn RCL
  ACS CHEMICAL BIOLOGY 8, 733 (2013).
  DOI: 10.1021/cb300629b
• Human lysozyme inhibits the in vitro aggregation of A? peptides, which in vivo are associated with Alzheimer's disease Luo J, Wärmländer Sebastian KTS, Gräslund A, Abrahams J
  CHEMICAL COMMUNICATIONS 49, 6507 (2013).
  DOI: 10.1039/c3cc42325e
• Inhibiting and Reversing Amyloid-beta Peptide (1-40) Fibril Formation with Gramicidin S and Engineered Analogues 
  Luo J, Otero José M, Yu C, Wärmländer Sebastian KTS, Gräslund A, Overhand M, Abrahams J
  CHEMISTRY - A EUROPEAN JOURNAL 19, 17338 (2013).
  DOI: 10.1002/chem.201301535

• Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution 
  Luo J, van Loo B, Kamerlin Shina CL
  FEBS LETTERS 586, 1622 (2012).
  DOI: 10.1016/j.febslet.2012.04.012
• Conformation Effects of CpG Methylation on Single-Stranded DNA Oligonucleotides: Analysis of the Opioid Peptide Dynorphin-Coding Sequences 
  Taqi M, Wärmländer Sebastian KTS, Yamskova O, Madani F, Bazov I, Luo J, Zubarev R, Verbeek D, Gräslund A, Bakalkin G
  PLOS ONE 7, e39605 (2012).
  DOI: 10.1371/journal.pone.0039605
• Examining the promiscuous phosphatase activity of Pseudomonas aeruginosa arylsulfatase: A comparison to analogous phosphatases 
  Luo J, van Loo B, Kamerlin SCL
  PROTEINS: STRUCTURE, FUNCTION, AND BIOINFORMATICS 80, 1211 (2012).
  DOI: 10.1002/prot.24020

• A Straightforward and Robust Method for Introducing Human Hair as a Nucleant into High Throughput Crystallization Trials 
  Nederlof I, Hosseini R, Georgieva D, Luo J, Li D, Abrahams J
  CRYSTAL GROWTH & DESIGN 11, 1170 (2011).
  DOI: 10.1021/cg101374r
• Inhibition of chlamydial class Ic ribonucleotide reductase by C-terminal peptides from protein R2 
  Öhrström M, Popovic-Bijelic A, Luo J, Stenmark P, Högbom M, Gräslund A
  JOURNAL OF PEPTIDE SCIENCE 17, 756 (2011).
  DOI: 10.1002/psc.1399
• Ribonucleotide reductase inhibition by metal complexes of Triapine (3-aminopyridine-2-carboxaldehyde thiosemicarbazone): A combined experimental and theoretical study.
  Popovic-Bijelic A, Kowol CR, Lind Maria ES, Luo J, Himo F, Enyedy EA, Arion VB, Graeslund A
  JOURNAL OF INORGANIC BIOCHEMISTRY 105, 1422 (2011).
  DOI: 10.1016/j.jinorgbio.2011.07.003
• Ribonucleotide reductase inhibition by p-alkoxyphenols studied by molecular docking and molecular dynamics simulations.
  Luo J, Gräslund A
  ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 516, 29 (2011).
  DOI: 10.1016/j.abb.2011.09.003

• In Silico Analysis of the Apolipoprotein E and the Amyloid ? Peptide Interaction: Misfolding Induced by Frustration of the Salt Bridge Network 
  Luo J, Maréchal J, Wärmländer S, Gräslund A, Perálvarez-Marín A
  PLOS COMPUTATIONAL BIOLOGY 6, e1000663 (2010).
  DOI: 10.1371/journal.pcbi.1000663