FINStruct

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Structural Biology Finland and Instruct-ERIC Centre Finland research infrastructures

Structural Biology Finland (FINStruct)

FINStruct is a national, coordinated, multi-institution, open-access, research infrastructure network (previous Instruct Finland, Instruct-FI until 2020). It provides integrated structural biology services and training to support research and innovation in life science. FINStruct services are provided by core facilities in five universities (Helsinki, Oulu, Eastern Finland, Turku, and Åbo Academi), and coordinated by the University of Helsinki. FINStruct is included on the Finnish Research Infrastructure 2014-2020 roadmap and 2021-2024 roadmap. FINStruct is the Structural Biology Platform of Biocenter Finland, and coordinates all research infrastructure requirements of the national structural biology network.

FINStruct Coordination Hub at the University of Helsinki

  • Director, Professor Sarah Butcher
  • Coordinator, Adjunct Professor Hanna Oksanen
  • Coordinates FINStruct and Instruct-ERIC Centre Finland

FINStruct services

FINStruct spearheads international research and development in biomolecular complex purification (Biocomplex); cryo-electron microscopy (cryoEM); nuclear magnetic resonance (NMR); native mass spectrometry (native-MS); structural bioinformatics, X-ray crystallography and data management. Each unit is a core facility of the research providing organizations. FINStruct serves the entire research community, academia and industry, nationally and internationally. CryoEM, Biocomplex, NMR, SCoPE-MS, Biocenter Oulu, and Biocenter Kuopio services can be also accessed through Instruct-ERIC (see below and funding possibilities for Instruct-ERIC access).

Instruct-ERIC Centre Finland

Instruct-ERIC is one of the successful operators at the European Strategy Forum on Research Infrastructures (ESFRI) with s a landmark status on the ESFRI Roadmap (2016). Accesses are provided at the scientifically evaluated and accepted Instruct-ERIC Centres that are located across the Europe. Instruct-ERIC member states host Instruct Centres that provide infrastructure and expertise supporting the mission and objectives of the Instruct-ERIC. Instruct-ERIC provides also the following resources:

Finland became a full member of Instruct-ERIC in 2019. In February 2020, Instruct Centre Finland services were opened and are available through the Instruct-ERIC catalogue for international and national use (Instruct-ERIC News). FINStruct provides a distributed Instruct Centre Finland, which is a national node of Instruct-ERIC. Being a member of Instruct-ERIC allows scientists from Finland to access the wide catalogue of cutting-edge structural biology technologies, including funding to enable important research discoveries in molecular bioscience.

Instruct-ERIC Centre Finland services

Funding for Instruct-ERIC Access

See funded access. Who can apply?

How to acknowledge FINStruct and Instruct-ERIC

For all publication and theses of research resulting from FINStruct or Instruct-ERIC Centre Finland access and use of services, there should be acknowledgement of FINStruct and/or Instruct-ERIC. Please acknowledge, use of the service, expertise and resources using the following texts in the Acknowledgements:

Service units operating both in FINStruct  and Instruct-ERIC: CryoEM, Biocomplex and NMR (University of Helsinki), Biocenter Oulu unit (University of Oulu), and Biocenter Kuopio unit (University of Eastern Finland)
The facilities and expertise of the “RI facility name at the University of X”, a member of Instruct-ERIC Centre Finland, FINStruct, and Biocenter Finland are gratefully acknowledged.
Example: The facilities and expertise of the CryoEM facility at the University of Helsinki, a member of Instruct-ERIC Centre Finland, FINStruct, and Biocenter Finland are gratefully acknowledged.

SCoPE-MS unit in Instruct-ERIC
The facilities and expertise of the SCoPE-MS at the University of Helsinki, a member of Instruct-ERIC Centre Finland are gratefully acknowledged.

For projects with Instruct-ERIC access funding: see guidelines here

Service units operating in FINStruct: Protein crystallization facilities at the Universities of Helsinki and Turku, and Åbo Akademi University
The facilities and expertise of the “RI facility name at the University of X”, a member of FINStruct and Biocenter Finland are gratefully acknowledged.
Example: The facilities and expertise of the crystallization facility at the University of Helsinki, a member of FINStruct and Biocenter Finland are gratefully acknowledged.

Publications

updated on March 2, 2021

2021

  1. Eesmaa A, Yu L-Y, Göös H, Nõges K, Kovaleva V, Hellman M, Zimmermann R, Jung M, Permi P, Varjosalo M, Lindholm P, Saarma M. 2021. The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor. J. Biol. Chem, in press.
  2. Flatt, J.W.,  Domanska, A., Seppälä, A.L., Butcher, S.J. 2021. Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. Comms Biol. accepted
  3. Georgakis N, Poudel N, Vlachakis D, Papageorgiou AC, Labrou NE. 2021. Phi class glutathione transferases as molecular targets towards multiple-herbicide resistance: Inhibition analysis and pharmacophore design. Plant Physiol Biochem 158:342-352.
  4. Gludovacz E, Schuetzenberger K, Resch M, Tillmann K, Petroczi K, Vondra S, Vakal S, Schosserer M, Virgolini N, Pollheimer J, Salminen TA, Jilma B, Borth N, Boehm T. 2021. Human diamine oxidase cellular binding and internalization in vitro and rapid clearance in vivo are not mediated by N-glycans but by heparan sulfate proteoglycan interactions. Glycobiology. cwaa090. Epub ahead of print.
  5. Kurkela J, Fredman J, Salminen TA, Tyystjärvi T. 2021. Revealing secrets of the enigmatic omega subunit of bacterial RNA polymerase. Mol Microbiol. 115:1-11.
  6. Mustonen V, Muruganandam G, Loris R, Kursula P, Ruskamo S. 2021. Crystal and solution structure of NDRG1, a membrane-binding protein linked to myelination and tumour suppression. FEBS J. 2020. Epub ahead of print.
  7. Myllykoski M, Sutinen A, Koski MK, Kallio JP, Raasakka A, Myllyharju J, Wierenga RK, Koivunen P. 2021. Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. J Biol Chem. Epub ahead of print.
  8. Papageorgiou AC, Poudel N, Matsson J. 2021. Protein analysis with X-ray crystallography. Methods Mol. Biol. 2178:377-404.
  9. Platis M, Vlachakis D, Foudah AI, Muharram MM, Alqarni MH, Papageorgiou AC, Labrou NE. 2021. The interaction of Schistosoma japonicum glutathione transferase with Cibacron blue 3GA and its fragments. Med Chem (in press)
  10. Sowa ST, Moilanen A, Biterova E, Saaranen MJ, Lehtiö L, Ruddock LW. High-resolution crystal structure of human pERp1, a saposin-like protein involved in IgA, IgM and integrin maturation in the endoplasmic reticulum. J Mol Biol. 2021. Epub ahead of print.
  11. Schwarzer S, Rodriguez-Franco M, Oksanen HM, Quax TEF. 2021. Growth phase dependent cell shape of Haloarcula. Microorganisms. 9:231.
  12. Tittes C, Schwarzer S, Pfeiffer F, Dyall-Smith M, Rodriguez-Franco M, Oksanen HM, Quax TEF. 2021. Cellular and genomic properties of Haloferax gibbonsii LR2-5, the host of euryarchaeal virus HFTV1. Front. Microbiol. In Press
  13. Wazir S, Maksimainen MM, Alanen HI, Galera-Prat A, Lehtiö L. 2021. Activity-based screening assay for mono-ADP-ribosylhydrolases. SLAS Discov. 26:67-76.

2020

  1. Asthana P,  Singh D, Pedersen JS, Hynönen MJ, Sulu R, Murthy VA, Laitaoja M, Jänis J, Riley LW, Venkatesan R. 2020. Structural insights on the substrate-binding proteins of the Mycobacterium tuberculosis mammalian-cell-entry (Mce) 1 and 4 complexes. BioRxiv. doi: https://doi.org/10.1101/2020.09.29.317909
  2. Ashok Y, Maksimainen MM, Kallio T, Kilpeläinen P, Lehtiö L. 2020. FMN-dependent oligomerization of putative lactate oxidase from Pediococcus acidilactici. PLoS One. 15:e0223870.
  3. Ashok Y, Miettinen M, Oliveira DKH, Tamirat MZ, Näreoja K, Tiwari A, Hottiger MO, Johnson MS, Lehtiö L, Pulliainen AT. 2020. Discovery of compounds inhibiting the ADP-ribosyltransferase activity of pertussis toxin. ACS Infect Dis. 6:588-602.
  4. Barrass SV, Butcher SJ. Advances in high-throughput methods for the identification of virus receptors. 2020. Med Microbiol Immunol. 209:309-323.
  5. Barylski J, Enault F, Dutilh BE, Schuller MBP, Edwards RA, Gillis A, Klumpp J, Knezevic P, Krupovic M, Kuhn JH, Lavigne R, Oksanen HM, Sullivan MB, Jang HB, Simmonds P, Aiewsakun P, Wittmann J, Tolstoy I, Brister JR, Kropinski AM, Adriaenssens EM. 2020. Analysis of spounaviruses as a case study for the overdue reclassification of tailed phages. Syst Biol. 69:110-123.
  6. Bendes AA, Kursula P,  Kursula I. 2020. Structure of an atypical homodimeric actin capping protein from the malaria parasite. BioRxiv. doi: https://doi.org/10.1101/2020.08.16.253187
  7. Beyer HM, Mikula KM, Li M, Wlodawer A, Iwaï H. 2020. The crystal structure of the naturally split gp41-1 intein guides the engineering of orthogonal split inteins from cis-splicing inteins. FEBS J. 287:1886-1898.
  8. Beyer HM, Virtanen SI, Aranko AS, Mikula KM, Lountos GT, Wlodawer A, Ollila OHS, Iwaï H. 2020. The convergence of the hedgehog/intein fold in different protein splicing mechanisms.  Int J Mol Sci. 21:8367.
  9. Carvalho DMD, Lahtinen, MH, Lawoko M, Mikkonen KS. 2020. Enrichment and identification of lignin–carbohydrate complexes in softwood extract, ACS Sustainable Chem. Eng. 8:11795–11804
  10. Ciragan A, Backlund SM, Mikula KM, Beyer HM, Ollila OHS, Iwaï H. 2020. NMR structure and dynamics of TonB investigated by scar-less segmental isotopic labeling using a salt-inducible split intein. Front. Chem. 8:136.
  11. Cuellar J, Åstrand M, Elovaara H, Pietikäinen A, Sirén S, Liljeblad A, Guédez G, Salminen TA, Hytönen J. 2020. Structural and biomolecular analyses of Borrelia burgdorferi BmpD reveal a substrate-binding protein of an ABC-type nucleoside transporter family. Infect Immun. 88:e00962-19.
  12. De S, Pollari M, Varjosalo M, Mäkinen K. 2020. Association of host protein VARICOSE with HCPro within a multiprotein complex is crucial for RNA silencing suppression, translation, encapsidation and systemic spread of potato virus A infection. PLoS Pathog. 16:e1008956.
  13. Demina TA, Oksanen HM. 2020. Pleomorphic archaeal viruses: the family Pleolipoviridae is expanding by seven new species. Arch Virol. 165:2723-2731.
  14. Flatt, J.W.,  Domanska, A., Seppälä, A.L., Butcher, S.J. 2020. Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enteroviruses. BioRxiv: doi: https://doi.org/10.1101/2020.07.06.189373
  15. Georgakis N, Poudel N, Papageorgiou AC, Labrou NE. 2020. Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops. Plant Physiol Biochem. 149:266-276.  
  16. Harrus D, Harduin-Lepers A, Glumoff T. 2020. Unliganded and CMP-Neu5Ac bound structures of human α-2,6-sialyltransferase ST6Gal I at high resolution. J Struct Biol. 212:107628
  17. Heliste J, Chheda H, Paatero I, Salminen TA, Akimov Y, Paavola J, Elenius K, Aittokallio T. 2020. Genetic and functional implications of an exonic TRIM55 variant in heart failure. J Mol Cell Cardiol. 138:222-233.
  18. Hongisto H, Dewing JM, Christensen DR, Scott J, Cree AJ, Nättinen J, Määttä J, Jylhä A, Aapola U, Uusitalo H, Kaarniranta K, Ratnayaka JA, Skottman H, Lotery AJ. 2020. In vitro stem cell modelling demonstrates a proof-of-concept for excess functional mutant TIMP3 as the cause of Sorsby fundus dystrophy. J Pathol. 252:138-150.
  19. Jaakkonen A, Volkmann G, Iwaï H. 2020. An off-the-shelf approach for the production of Fc fusion proteins by protein trans-splicing towards generating a lectibody in vitro. Int. J. Mol. Sci. 21: 4011.
  20. Jiang M, Österlund P, Poranen MM, Julkunen I. 2020. In vitro production of synthetic viral RNAs and their delivery into mammalian cells and the application of viral RNAs in the study of innate interferon responses. Methods. 183:21-29.
  21. Johansson MM, Bélurier E, Papageorgiou AC, Sundin AP, Rahkila J, Kallonen T, Nilsson UJ, Maatsola S, Nyholm TKM, Käpylä J, Corander J, Leino R, Finne J, Teneberg S, Haataja S. 2020. The binding mechanism of the virulence factor Streptococcus suis adhesin P subtype to globotetraosylceramide is associated with systemic disease. J. Biol. Chem. 295: 14305-14324
  22. Johansson MM, Bélurier E, Papageorgiou AC, Sundin AP, Rahkila J, Kallonen T, Nilsson UJ, Maatsola S, Nyholm TKM, Käpylä J, Corander J, Leino R, Finne J, Teneberg S, Haataja S. 2020. The binding mechanism of the virulence factor Streptococcus suis adhesin P subtype to globotetraosylceramide is associated with systemic disease. bioRxiv 2020.05.29.122762; doi: https://doi.org/10.1101/2020.05.29.122762
  23. Johansson NG, Turku A, Vidilaseris K, Dreano L, Khattab A, Ayuso Pérez D, Wilkinson A, Zhang Y, Tamminen M, Grazhdankin E, Kiriazis A, Fishwick CWG, Meri S, Yli-Kauhaluoma J, Goldman A, Boije Af Gennäs G, Xhaard H. 2020. Discovery of membrane-bound pyrophosphatase inhibitors derived from an isoxazole fragment. ACS Med Chem Lett. 11:605-610.
  24. Kalke K, Lehtinen J, Gnjatovic J, Lund LM, Nyman MC, Paavilainen H, Orpana J, Lasanen T, Frejborg F, Levanova AA, Vuorinen T, Poranen MM, Hukkanen V. 2020. Herpes simplex virus type 1 clinical isolates respond to UL29-targeted siRNA swarm treatment independent of their acyclovir sensitivity. Viruses. 12:1434.
  25. Karki S, Shkumatov AV, Bae S, Kim H, Ko J, Kajander T. 2020. Structural basis of SALM3 dimerization and synaptic adhesion complex formation with PTPσ. Sci Rep. 10:11557.
  26. Kukkurainen S, Azizi L, Zhang P, Jacquier MC, Baikoghli M, von Essen M, Tuukkanen A, Laitaoja M, Liu X, Rahikainen R, Orłowski A, Jänis J, Määttä JAE, Varjosalo M, Vattulainen I, Róg T, Svergun D, Cheng RH, Wu J, Hytönen VP, Wehrle-Haller B. 2020. The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. J Cell Sci. 133:jcs239202.
  27. Leppänen VM, Brouillard P, Korhonen EA, Sipilä T, Jha SK, Revencu N, Labarque V, Fastré E, Schlögel M, Ravoet M, Singer A, Luzzatto C, Angelone D, Crichiutti G, D'Elia A, Kuurne J, Elamaa H, Koh GY, Saharinen P, Vikkula M, Alitalo K. 2020. Characterization of ANGPT2 mutations associated with primary lymphedema. Sci Transl Med. 12:eaax8013.
  28. Levanova AA, Kalke KM, Lund LM, Sipari N, Sadeghi M, Nyman MC, Paavilainen H, Hukkanen V, Poranen MM. 2020. Enzymatically synthesized 2'-fluoro-modified Dicer-substrate siRNA swarms against herpes simplex virus demonstrate enhanced antiviral efficacy and low cytotoxicity. Antiviral Res. 182:104916.
  29. Laurinmäki, P., Shakeel, S., Ekström, J., Mohammadi, P., Hultmark, D. , Butcher, S.J. (2020) Structure of Nora virus at 2.7 Å resolution and implications for receptor binding, capsid stability and taxonomy. Scientific Reports 10:19675 https://doi.org/10.1038/s41598-020-76613-1
  30. Mahato AK, Kopra J, Renko JM, Visnapuu T, Korhonen I, Pulkkinen N, Bespalov MM, Domanskyi A, Ronken E, Piepponen TP, Voutilainen MH, Tuominen RK, Karelson M, Sidorova YA, Saarma M. 2020. Glial cell line-derived neurotrophic factor receptor Rearranged during transfection agonist supports dopamine neurons in Vitro and enhances dopamine release In Vivo. Mov Disord. 35:245-255.
  31. Mattila ALK, Jiggins CD, Opedal ØH, Montejo-Kovacevich G, de Castro É, McMillan WO, Bacquet C, Saastamoinen M. 2020. High evolutionary potential in the chemical defenses of an aposematic Heliconius butterfly, bioRxiv 2020.01.14.905950
  32. Mofikoya OO, Mäkinen M, Jänis J. 2020. Chemical fingerprinting of conifer needle essential oils and solvent extracts by ultrahigh-resolution fourier transform ion cyclotron resonance mass spectrometry. ACS Omega. 5:10543-10552.
  33. Myllykoski M, Sutinen A, Koski MK, Kallio JP,  Raasakka A,  Myllyharju J, Wierenga R, Koivunen P. 2020. Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. BioRxiv. doi: https://doi.org/10.1101/2020.10.25.354423
  34. Mäntynen S, Laanto E, Sundberg LR, Poranen MM, Oksanen HM, ICTV Report Consortium. 2020. ICTV Virus Taxonomy Profile: Finnlakeviridae. J Gen Virol. 101:894-895.
  35. Nguyen GTT, Sutinen A, Raasakka A, Muruganandam G, Loris R, Kursula P. 2020. Structure of the complete dimeric human GDAP1 core domain provides insights into ligand binding and clustering of disease mutations. BioRxiv. doi: https://doi.org/10.1101/2020.11.13.381293
  36. Nji Wandi B, Siitonen V, Dinis P, Vukic V, Salminen TA, Metsä-Ketelä M. 2020. Evolution-guided engineering of non-heme iron enzymes involved in nogalamycin biosynthesis. FEBS J. 287:2998-3011.
  37. Oeemig JS, Beyer HM, Aranko AS, Mutanen J, Iwaï H. 2020. Substrate specificities of inteins investigated by QuickDrop-cassette mutagenesis. FEBS Lett. 594:3338-3355.
  38. Orengo C, Velankar S, Wodak S, Zoete V, Bonvin AMJJ, Elofsson A, Feenstra KA, Gerloff DL, Hamelryck T, Hancock JM, Helmer-Citterich M, Hospital A, Orozco M, Perrakis A, Rarey M, Soares C, Sussman JL, Thornton JM, Tuffery P, Tusnady G, Wierenga R, Salminen T, Schneider B. 2020. A community proposal to integrate structural bioinformatics activities in ELIXIR (3D-Bioinfo Community). F1000Res. 9:ELIXIR-278.
  39. Papageorgiou AC, Mohsin I. 2020.  The SARS-CoV-2 spike glycoprotein as a drug and vaccine target: structural insights into its complexes with ACE2 and antibodies. Cells 9: 2343.
  40. Premetis G, Marugas P, Fanos G, Vlachakis D, Chronopoulou EG, Perperopoulou F, Dubey KK, Shukla P, Foudah AI, Muharram MM, Aldwsari MF, Papageorgiou AC, Labrou NE. 2020. The interaction of the microtubule targeting anticancer drug colchicine with human glutathione transferases. Curr Pharm Des 26: 5205-5212
  41. Saari H, Turunen T, Lõhmus A, Turunen M, Jalasvuori M, Butcher SJ, Ylä-Herttuala S, Viitala T, Cerullo V, Siljander PRM, Yliperttula M. 2020. Extracellular vesicles provide a capsid-free vector for oncolytic adenoviral DNA delivery. J Extracell Vesicles. 9:1747206.
  42. Sah-Teli SK, Hynönen MJ, Sulu R, Dalwani S, Schmitz W, Wierenga RK, Venkatesan R. 2020. Insights into the stability and substrate specificity of the E. coli aerobic β-oxidation trifunctional enzyme complex. J Struct Biol.  210:107494.
  43. Seifert M, van Nies P, Papini FS, Arnold JJ, Poranen MM, Cameron CE, Depken M, Dulin D. 2020. Temperature controlled high-throughput magnetic tweezers show striking difference in activation energies of replicating viral RNA-dependent RNA polymerases. Nucleic Acids Res. 48:5591-5602.
  44. Seifert M, van Nies P, Papini FS, Arnold JJ, Poranen MM, Cameron CE, Depken M, Dulin D. 2020. Temperature controlled high-throughput magnetic tweezers show striking difference in activation energies of replicating viral RNA-dependent RNA polymerases. bioRxiv 2020.01.15.906032
  45. Sridhar S, Schmitz W, Hiltunen JK, Venkatesan R, Bergmann U, Kiema TR, Wierenga RK. 2020. Crystallographic binding studies of rat peroxisomal multifunctional enzyme type 1 with 3-ketodecanoyl-CoA: capturing active and inactive states of its hydratase and dehydrogenase catalytic sites. Acta Crystallogr D Struct Biol. 76:1256-1269.
  46. Sirén S, Dahlström KM, Puttreddy R, Rissanen K, Salminen TA, Scheinin M, Li XG, Liljeblad A. 2020. Candida antarctica lipase A-based enantiorecognition of a highly strained 4-dibenzocyclooctynol (DIBO) used for PET imaging. Molecules. 25:879.
  47. Sowa ST, Vela-Rodríguez C, Galera-Prat A, Cázares-Olivera M, Prunskaite-Hyyryläinen R, Ignatev A, Lehtiö L. 2020. A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases. Sci Rep. 10:12357.
  48. Storey D, McNally A, Åstrand M, Sa-Pessoa Graca Santos J, Rodriguez-Escudero I, Elmore B, Palacios L, Marshall H, Hobley L, Molina M, Cid VJ, Salminen TA, Bengoechea JA. 2020. Klebsiella pneumoniae type VI secretion system-mediated microbial competition is PhoPQ controlled and reactive oxygen species dependent. PLoS Pathog. 16:e1007969.
  49. Thapa R, Nissinen T, Turhanen P, Määttä J, Vepsäläinen J, Lehto V-P, Riikonen J. 2020. Bisphosphonate modified mesoporous silicon for scandium adsorption. Microporous and Mesoporous Materials 296:109980
  50. Tittes C, Schwarzer S, Pfeiffer F, Dyall-Smith M, Rodriguez-Franco M, Oksanen HM, Quax TEF. 2020. Cellular and genomic properties of Haloferax gibbonsii LR2-5, the host of euryarchaeal virus HFTV1. bioRxiv. 2020.10.26.354720
  51. Tuusa J, Koski MK, Ruskamo S, Tasanen K. 2020. The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment. Amino Acids. 52:619-627.
  52. Vakal S, Jalkanen S, Dahlström KM, Salminen TA. 2020. Human copper-containing amine oxidases in drug design and development. Molecules. 25:1293.
  53. Valanne S, Järvelä-Stölting M, Harjula SE, Myllymäki H, Salminen TS, Rämet M. 2020. Osa-containing brahma complex regulates innate immunity and the expression of metabolic genes in Drosophila. J Immunol. 204:2143-2155.
  54. Viisanen H, Nuotio U, Kambur O, Mahato AK, Jokinen V, Lilius T, Li W, Santos HA, Karelson M, Rauhala P, Kalso E, & Sidorova YA. 2020. Novel RET agonist for the treatment of experimental neuropathies. Molecular Pain. 16:1744806920950866.
  55. Virtanen SI, Kiirikki AM, Mikula KM, Iwaï H, Ollila OHS. 2020. Heterogeneous dynamics in partially disordered proteins. Phys. Chem. Chem. Phys. 22:21185-21196.
  56. Wang L, Borghei M, Ishfaq A, Lahtinen P, Ago M, Papageorgiou AC, Lundahl M, Johansson LS, Kallio T, Rojas OJ. 2020. Mesoporous carbon microfibers for electroactive materials derived from lignin-containing nanocellulose ACS Sustain Chem Eng 8 (23): 8549-8561.
  57. Wazir S, Maksimainen MM, Lehtiö L. Multiple crystal forms of human MacroD2. 2020. Acta Crystallogr F Struct Biol Commun. 76477-482.
  58. Zhang P, Azizi L, Kukkurainen S, Gao T, Baikoghli M, Jacquier MC, Sun Y, Määttä JAE, Cheng RH, Wehrle-Haller B, Hytönen VP, Wu J. 2020. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding. Proc Natl Acad Sci U S A. 117:32402-32412.

2013-2021, see the PDF, below.