Using core stengths in electron tomography and protein bioengineering the cellular structural biology group focuses on analysis of 3D structures of biological macromolecules in the cell, in particular using cryo-electron tomography.
Our Research
Our focus is electron and X-ray imaging and related methodological development. Takashi Ishikawa is interested in eukaryotic cilia/flagella, which are microtubule-based organelles and enable cellular motility, extracellular flow as well as sensing. His group pursues 3D imaging of motor, regulatory, and cytoskeletal proteins, intact cilia and ciliated cells and tissues, employing single particle cryo-EM, cryo-electron tomography and ptychographic X-ray tomography. Their aim is to reveal molecular mechanism of ciliary function. The Benoit group is interested in molecular and cellular structures of membrane proteins, especially receptors. They use single particle cryo-EM to analyze molecular structure of membrane proteins, developing related genetic engineering techniques.
for more information please contact:
Takashi Ishikawa, Group leader
Cellular and molecular structural biology on eukaryotic cilia and flagella
Roger Benoit, Scientist
Engineered scaffolds for protein structure elucidation by cryo-EM and crystallography
Group members
Former group members
| Tobias Bierig | Ph.D. Student |
| Gabriella Collu | Ph.D. Student |
| Khanh Huy Bui | Postdoc |
| Aditi Maheshwari | Ph.D. Student |
| Malkova Barbora | Postdoc |
| Akira Noga | Postdoc |
| Tandis Movassagh | Ph.D. Student |
| Jagan Mohan Obbineni | Ph.D. Student |
| Gaia Pigino | Postdoc |
| Emiliya Poghosyan | Ph.D. Student |
| Farooque Razvi Shaik | Postdoc |
| Iman Rostami | Postdoc |
| Sarah Shahmoradian | Scientist |
| Hung Tri Tran | Ph.D. Student |
| Hironori Ueno | Postdoc |
| Valtteri Järvinen | Ph.D. Student |
Publications
Group publications since 2010
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Christen P, Jaussi R, Benoit R
Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
2nd ed. Berlin: Springer Nature; 2024. https://doi.org/10.1007/978-3-662-65477-4
DORA PSI -
Wang J, Beyer D, Vaccarin C, He Y, Tanriver M, Benoit R, et al.
Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2
European Journal of Nuclear Medicine and Molecular Imaging. 2024. https://doi.org/10.1007/s00259-024-06831-6
DORA PSI -
Zimmermann N, Ishikawa T
Comparative structural study on axonemal and cytoplasmic dyneins
Cytoskeleton. 2024. https://doi.org/10.1002/cm.21897
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Behbahanipour M, Benoit R, Navarro S, Ventura S
OligoBinders: bioengineered soluble amyloid-like nanoparticles to bind and neutralize SARS-CoV-2
ACS Applied Materials and Interfaces. 2023; 15(9): 11444-11457. https://doi.org/10.1021/acsami.2c18305
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Cvjetan N, Schuler LD, Ishikawa T, Walde P
Optimization and enhancement of the peroxidase-like activity of hemin in aqueous solutions of sodium dodecylsulfate
ACS Omega. 2023; 8(45): 42878-42899. https://doi.org/10.1021/acsomega.3c05915
DORA PSI -
Farnung J, Muhar M, Liang JR, Tolmachova KA, Benoit RM, Corn JE, et al.
Semisynthetic LC3 probes for autophagy pathways reveal a noncanonical LC3 interacting region motif crucial for the enzymatic activity of human ATG3
ACS Central Science. 2023; 9(5): 1025-1034. https://doi.org/10.1021/acscentsci.3c00009
DORA PSI -
Ishikawa T
Architecture of intraflagellar transport complexes
Nature Structural and Molecular Biology. 2023; 30(5): 570-573. https://doi.org/10.1038/s41594-023-00986-w
DORA PSI -
Ishikawa T
Cryo-electron tomography
In: Bradshaw RA, Hart GW, Stahl PD, eds. Organizational aspects of cell biology - part 1. Encyclopedia of cell biology. Amsterdam: Elsevier; 2023:28-36. https://doi.org/10.1016/B978-0-12-821618-7.00084-5
DORA PSI -
Ishikawa T
Mass-spec, cryo-EM and AI join forces for a close look at the transporter complex in cilia
EMBO Journal. 2023; 42: e113010 (3 pp.). https://doi.org/10.15252/embj.2022113010
DORA PSI -
Yildiz A, Ishikawa T
Dyneins
In: Bradshaw RA, Hart GW, Stahl PD, eds. Organizational aspects of cell biology - part 2. Encyclopedia of cell biology. Amsterdam: Elsevier; 2023:110-137. https://doi.org/10.1016/B978-0-12-821618-7.00094-8
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Zimmermann N, Noga A, Obbineni JM, Ishikawa T
ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography
EMBO Journal. 2023; 42(12): e112466 (15 pp.). https://doi.org/10.15252/embj.2022112466
DORA PSI -
Collu G, Bierig T, Krebs A-S, Engilberge S, Varma N, Guixà-González R, et al.
Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
Structure. 2022; 30(1): 95-106. https://doi.org/10.1016/j.str.2021.09.002
DORA PSI -
Ishikawa T
Structure of motile cilia
In: Harris RJ, Marles-Wright J, eds. Macromolecular protein complexes IV. Structure and function. Subcellular biochemistry. Cham: Springer Nature; 2022:471-494. https://doi.org/10.1007/978-3-031-00793-4_15
DORA PSI -
Noga A, Horii M, Goto Y, Toyooka K, Ishikawa T, Hirono M
Bld10p/Cep135 determines the number of triplets in the centriole independently of the cartwheel
EMBO Journal. 2022; 41(20): e104582 (14 pp.). https://doi.org/10.15252/embj.2020104582
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Galaz-Montoya JG, Shahmoradian SH, Shen K, Frydman J, Chiu W
Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates
Communications Biology. 2021; 4(1): 849 (9 pp.). https://doi.org/10.1038/s42003-021-02360-2
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Kutomi O, Yamamoto R, Hirose K, Mizuno K, Nakagiri Y, Imai H, et al.
A dynein-associated photoreceptor protein prevents ciliary acclimation to blue light
Science Advances. 2021; 7(9): eabf3621 (12 pp.). https://doi.org/10.1126/sciadv.abf3621
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Panneels V, Diaz A, Imsand C, Guizar-Sicairos M, Müller E, Bittermann AG, et al.
Imaging of retina cellular and subcellular structures using ptychographic hard X-ray tomography
Journal of Cell Science. 2021; 134(19): jcs258561 (8 pp.). https://doi.org/10.1242/jcs.258561
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Tran HT, Lucas MS, Ishikawa T, Shahmoradian SH, Padeste C
A compartmentalized neuronal cell-culture platform compatible with cryo-fixation by high-pressure freezing for ultrastructural imaging
Frontiers in Neuroscience. 2021; 15: 726763 (15 pp.). https://doi.org/10.3389/fnins.2021.726763
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Yamamoto R, Hwang J, Ishikawa T, Kon T, Sale WS
Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii
Cytoskeleton. 2021; 78(3): 77-96. https://doi.org/10.1002/cm.21662
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Bierig T, Collu G, Blanc A, Poghosyan E, Benoit RM
Design, expression, purification, and characterization of a YFP-tagged 2019-n CoV spike receptor-binding domain construct
Frontiers in Bioengineering and Biotechnology. 2020; 8: 618615 (10 pp.). https://doi.org/10.3389/fbioe.2020.618615
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Holler M, Ihli J, Tsai EHR, Nudelman F, Verezhak M, van de Berg WDJ, et al.
A lathe system for micrometre-sized cylindrical sample preparation at room and cryogenic temperatures
Journal of Synchrotron Radiation. 2020; 27(2): 472-476. https://doi.org/10.1107/S1600577519017028
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Poghosyan E, Iacovache I, Faltova L, Leitner A, Yang P, Diener DR, et al.
The structure and symmetry of the radial spoke protein complex in Chlamydomonas flagella
Journal of Cell Science. 2020; 133(16): jcs245233 (9 pp.). https://doi.org/10.1242/jcs.245233
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Rösner B, Finizio S, Koch F, Döring F, Guzenko VA, Langer M, et al.
Soft x-ray microscopy with 7 nm resolution
Optica. 2020; 7(11): 1602-1608. https://doi.org/10.1364/OPTICA.399885
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Skopintsev P, Ehrenberg D, Weinert T, James D, Kar RK, Johnson PJM, et al.
Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Nature. 2020; 583: 314-318. https://doi.org/10.1038/s41586-020-2307-8
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Tran HT, Tsai EHR, Lewis AJ, Moors T, Bol JGJM, Rostami I, et al.
Alterations in sub-axonal architecture between normal aging and Parkinson's diseased human brains using label-free cryogenic X-ray nanotomography
Frontiers in Neuroscience. 2020; 14: 570019 (22 pp.). https://doi.org/10.3389/fnins.2020.570019
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Guerrero-Ferreira RC, Hupfeld M, Nazarov S, Taylor NMI, Shneider MM, Obbineni JM, et al.
Structure and transformation of bacteriophage A511 baseplate and tail upon infection of Listeria cells
EMBO Journal. 2019; 38(3): e99455 (20 pp.). https://doi.org/10.15252/embj.201899455
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Kashima K, Fujisaki T, Serrano-Luginbühl S, Kissner R, Janošević Ležaić A, Bajuk-Bogdanović D, et al.
Effect of template type on the Trametes versicolor laccase-catalyzed oligomerization of the aniline dimer p-aminodiphenylamine (PADPA)
ACS Omega. 2019; 4(2): 2931-2947. https://doi.org/10.1021/acsomega.8b03441
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Krebs A-S, Bierig T, Collu G, Benoit RM
Seamless insert-plasmid assembly at sub-terminal homologous sequences
Plasmid. 2019; 106: 102445 (9 pp.). https://doi.org/10.1016/j.plasmid.2019.102445
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Lewis AJ, Genoud C, Pont M, van de Berg WDJ, Frank S, Stahlberg H, et al.
Imaging of post-mortem human brain tissue using electron and X-ray microscopy
Current Opinion in Structural Biology. 2019; 58: 138-148. https://doi.org/10.1016/j.sbi.2019.06.003
DORA PSI -
Li T, Krumeich F, Ihli J, Ma Z, Ishikawa T, Pinar AB, et al.
Heavy atom labeling enables silanol defect visualization in silicalite-1 crystals
Chemical Communications. 2019; 55(4): 482-485. https://doi.org/10.1039/c8cc07912a
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Rostami I, Alanagh HR, Hu Z, Shahmoradian SH
Breakthroughs in medicine and bioimaging with up-conversion nanoparticles
International Journal of Nanomedicine. 2019; 14: 7759-7780. https://doi.org/10.2147/IJN.S221433
DORA PSI -
Shahmoradian SH, Lewis AJ, Genoud C, Hench J, Moors T, Navarro PP, et al.
Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes
Nature Neuroscience. 2019; 22(7): 1099-1109. https://doi.org/10.1038/s41593-019-0423-2
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Zhu X, Poghosyan E, Rezabkova L, Mehall B, Sakakibara H, Hirono M, et al.
The roles of a flagellar HSP40 ensuring rhythmic beating
Molecular Biology of the Cell. 2019; 30(2): 228-241. https://doi.org/10.1091/mbc.E18-01-0047
DORA PSI -
Benoit RM
Botulinum neurotoxin diversity from a gene-centered view
Toxins. 2018; 10(8): 310 (14 pp.). https://doi.org/10.3390/toxins10080310
DORA PSI -
Holler M, Raabe J, Diaz A, Guizar-Sicairos M, Wepf R, Odstrcil M, et al.
OMNY – a tOMography Nano crYo stage
Review of Scientific Instruments. 2018; 89(4): 043706 (13 pp.). https://doi.org/10.1063/1.5020247
DORA PSI -
Isabettini S, Stucki S, Massabni S, Baumgartner ME, Reckey PQ, Kohlbrecher J, et al.
Development of smart optical gels with highly magnetically responsive bicelles
ACS Applied Materials and Interfaces. 2018; 10(10): 8926-8936. https://doi.org/10.1021/acsami.7b17134
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Navarro PP, Genoud C, Castaño-Díez D, Graff-Meyer A, Lewis AJ, de Gier Y, et al.
Cerebral Corpora amylacea are dense membranous labyrinths containing structurally preserved cell organelles
Scientific Reports. 2018; 8(1): 18046 (13 pp.). https://doi.org/10.1038/s41598-018-36223-4
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Neuhaus F, Mueller D, Tanasescu R, Stefaniu C, Zaffalon P-L, Balog S, et al.
Against the rules: pressure induced transition from high to reduced order
Soft Matter. 2018; 14(19): 3978-3986. https://doi.org/10.1039/c8sm00212f
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Neuhaus F, Mueller D, Tanasescu R, Balog S, Ishikawa T, Brezesinski G, et al.
Synthesis and biophysical characterization of an odd-numbered 1,3-diamidophospholipid
Langmuir. 2018; 34(10): 3215-3220. https://doi.org/10.1021/acs.langmuir.7b04227
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Benoit RM, Schärer MA, Wieser MM, Li X, Frey D, Kammerer RA
Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C
Scientific Reports. 2017; 7: 43588 (7 pp.). https://doi.org/10.1038/srep43588
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Buscema M, Matviykiv S, Mészáros T, Gerganova G, Weinberger A, Mettal U, et al.
Immunological response to nitroglycerin-loaded shear-responsive liposomes in vitro and in vivo
Journal of Controlled Release. 2017; 264: 14-23. https://doi.org/10.1016/j.jconrel.2017.08.010
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Heydenreich FM, Miljuš T, Jaussi R, Benoit R, Milić D, Veprintsev DB
High-throughput mutagenesis using a two-fragment PCR approach
Scientific Reports. 2017; 7: 6787 (11 pp.). https://doi.org/10.1038/s41598-017-07010-4
DORA PSI -
Holler M, Raabe J, Wepf R, Shahmoradian SH, Diaz A, Sarafimov B, et al.
OMNY PIN - a versatile sample holder for tomographic measurements at room and cryogenic temperatures
Review of Scientific Instruments. 2017; 88(11): 113701 (9 pp.). https://doi.org/10.1063/1.4996092
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Isabettini S, Liebi M, Kohlbrecher J, Ishikawa T, Fischer P, Windhab EJ, et al.
Mastering the magnetic susceptibility of magnetically responsive bicelles with 3β-amino-5-cholestene and complexed lanthanide ions
Physical Chemistry Chemical Physics. 2017; 19(17): 10820-10824. https://doi.org/10.1039/c7cp01025g
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Isabettini S, Baumgartner ME, Reckey PQ, Kohlbrecher J, Ishikawa T, Fischer P, et al.
Methods for generating highly magnetically responsive lanthanide-chelating phospholipid polymolecular assemblies
Langmuir. 2017; 33(25): 6363-6371. https://doi.org/10.1021/acs.langmuir.7b00725
DORA PSI -
Isabettini S, Massabni S, Hodzic A, Durovic D, Kohlbrecher J, Ishikawa T, et al.
Molecular engineering of lanthanide ion chelating phospholipids generating assemblies with a switched magnetic susceptibility
Physical Chemistry Chemical Physics. 2017; 19(31): 20991-21002. https://doi.org/10.1039/c7cp03994h
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Ishikawa T
Axoneme structure from motile cilia
Cold Spring Harbor Perspectives in Biology. 2017; 9(1): a028076 (18 pp.). https://doi.org/10.1101/cshperspect.a028076
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Neuhaus F, Mueller D, Tanasescu R, Balog S, Ishikawa T, Brezesinski G, et al.
Vesicle origami: cuboid phospholipid vesicles formed by template-free self-assembly
Angewandte Chemie International Edition. 2017; 56(23): 6515-6518. https://doi.org/10.1002/anie.201701634
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Obbineni JM, Yamamoto R, Ishikawa T
A simple and fast approach for missing-wedge invariant classification of subtomograms extracted from filamentous structures
Journal of Structural Biology. 2017; 197(2): 145-154. https://doi.org/10.1016/j.jsb.2016.08.003
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Shahmoradian SH, Tsai EHR, Diaz A, Guizar-Sicairos M, Raabe J, Spycher L, et al.
Three-dimensional imaging of biological tissue by cryo X-ray ptychography
Scientific Reports. 2017; 7: 6291 (12 pp.). https://doi.org/10.1038/s41598-017-05587-4
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Yamamoto R, Obbineni JM, Alford LM, Ide T, Owa M, Hwang J, et al.
Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms
PLoS Genetics. 2017; 13(10): e1006996 (21 pp.). https://doi.org/10.1371/journal.pgen.1006996
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Zhu X, Poghosyan E, Gopal R, Liu Y, Ciruelas KS, Maizy Y, et al.
General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase
Molecular Biology of the Cell. 2017; 28(22): 3029-3042. https://doi.org/10.1091/mbc.E17-03-0156
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Aroua S, Tiu EGV, Ishikawa T, Yamakoshi Y
Well-defined amphiphilic C60-PEG conjugates: water-soluble and thermoresponsive materials
Helvetica Chimica Acta. 2016; 99(10): 805-813. https://doi.org/10.1002/hlca.201600171
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Benoit RM, Ostermeier C, Geiser M, Li JSZ, Widmer H, Auer M
Seamless insert-plasmid assembly at high efficiency and low cost
PLoS One. 2016; 11(4): e0153158 (13 pp.). https://doi.org/10.1371/journal.pone.0153158
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Bianchi S, van Riel WE, Kraatz SHW, Olieric N, Frey D, Katrukha EA, et al.
Structural basis for misregulation of kinesin KIF21A autoinhibition by CFEOM1 disease mutations
Scientific Reports. 2016; 6: 30668 (16 pp.). https://doi.org/10.1038/srep30668
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Christen P, Jaussi R, Benoit R
Biochemie und Molekularbiologie. Eine Einführung in 40 Lerneinheiten
Berlin, Heidelberg: Springer; 2016. https://doi.org/10.1007/978-3-662-46430-4
DORA PSI -
Isabettini S, Liebi M, Kohlbrecher J, Ishikawa T, Windhab EJ, Fischer P, et al.
Tailoring bicelle morphology and thermal stability with lanthanide-chelating cholesterol conjugates
Langmuir. 2016; 32(35): 9005-9014. https://doi.org/10.1021/acs.langmuir.6b01968
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Pfister B, Sánchez-Ferrer A, Diaz A, Lu K, Otto C, Holler M, et al.
Recreating the synthesis of starch granules in yeast
eLife. 2016; 5: e15552 (29 pp.). https://doi.org/10.7554/eLife.15552
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Shen K, Calamini B, Fauerbach JA, Ma B, Shahmoradian SH, Serrano Lachapel IL, et al.
Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract
eLife. 2016; 5: e18065 (29 pp.). https://doi.org/10.7554/eLife.18065
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Tanasescu R, Lanz MA, Mueller D, Tassler S, Ishikawa T, Reiter R, et al.
Vesicle origami and the influence of cholesterol on lipid packing
Langmuir. 2016; 32(19): 4896-4903. https://doi.org/10.1021/acs.langmuir.6b01143
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Aroua S, Tiu EGV, Ayer M, Ishikawa T, Yamakoshi Y
RAFT synthesis of poly(vinylpyrrolidone) amine and preparation of a water-soluble C60-PVP conjugate
Polymer Chemistry. 2015; 6(14): 2616-2619. https://doi.org/10.1039/c4py01333f
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Benoit RM, Frey D, Wieser MM, Thieltges KM, Jaussi R, Capitani G, et al.
Structure of the BoNT/A1 - Receptor complex
Toxicon. 2015; 107(Part A): 25-31. https://doi.org/10.1016/j.toxicon.2015.08.002
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Diaz A, Malkova B, Holler M, Guizar-Sicairos M, Lima E, Panneels V, et al.
Three-dimensional mass density mapping of cellular ultrastructure by ptychographic X-ray nanotomography
Journal of Structural Biology. 2015; 192(3): 461-469. https://doi.org/10.1016/j.jsb.2015.10.008
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Fodor D, Ishikawa T, Krumeich F, van Bokhoven JA
Synthesis of single crystal nanoreactor materials with multiple catalytic functions by incipient wetness impregnation and ion exchange
Advanced Materials. 2015; 27(11): 1919-1923. https://doi.org/10.1002/adma.201404628
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Geertsma ER, Chang Y-N, Shaik FR, Neldner Y, Pardon E, Steyaert J, et al.
Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family
Nature Structural and Molecular Biology. 2015; 22(10): 803-808. https://doi.org/10.1038/nsmb.3091
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Ishikawa T
Cryo-electron tomography of motile cilia and flagella
Cilia. 2015; 4(Suppl. 1): 3 (20 pp.). https://doi.org/10.1186/s13630-014-0012-7
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Liebi M, Kuster S, Kohlbrecher J, Ishikawa T, Walde P, Windhab EJ, et al.
Design of magnetically responsive phospholipid bicelles towards switchable optical hydrogels
Swiss Neutron News. 2015:4-13.
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Maheshwari A, Obbineni JM, Bui KH, Shibata K, Toyoshima YY, Ishikawa T
α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography
Structure. 2015; 23(9): 1584-1595. https://doi.org/10.1016/j.str.2015.06.017
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Weinberger A, Tanasescu R, Stefaniu C, Fedotenko LA, Favarger F, Ishikawa T, et al.
Bilayer properties of 1,3-diamidophospholipids
Langmuir. 2015; 31(6): 1879-1884. https://doi.org/10.1021/la5041745
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Benoit RM, Frey D, Hilbert M, Kevenaar JT, Wieser MM, Stirnimann CU, et al.
Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A
Nature. 2014; 505(7481): 108-111. https://doi.org/10.1038/nature12732
DORA PSI -
Ishikawa T
Protein tagging reveals new insights into signaling in flagella
Journal of Cell Biology. 2014; 204(5): 631-633. https://doi.org/10.1083/jcb.201401142
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Kammerer RA, Benoit RM
Botulinum neurotoxins: new questions arising from structural biology
Trends in Biochemical Sciences. 2014; 39(11): 517-526. https://doi.org/10.1016/j.tibs.2014.08.009
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Liebi M, Kuster S, Kohlbrecher J, Ishikawa T, Fischer P, Walde P, et al.
Magnetically enhanced bicelles delivering switchable anisotropy in optical gels
ACS Applied Materials and Interfaces. 2014; 6(2): 1100-1105. https://doi.org/10.1021/am4046469
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Ueno H, Bui KH, Ishikawa T, Imai Y, Yamaguchi T, Ishikawa T
Structure of dimeric axonemal dynein in cilia suggests an alternative mechanism of force generation
Cytoskeleton. 2014; 71(7): 412-422. https://doi.org/10.1002/cm.21180
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Ishikawa T
3D structure of eukaryotic flagella/cilia by cryo-electron tomography
Biophysics. 2013; 9: 141-148. https://doi.org/10.2142/biophysics.9.141
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Liebi M, Kuster S, Kohlbrecher J, Ishikawa T, Fischer P, Walde P, et al.
Cholesterol-diethylenetriaminepentaacetate complexed with thulium ions integrated into bicelles to increase their magnetic alignability
Journal of Physical Chemistry B. 2013; 117(47): 14743-14748. https://doi.org/10.1021/jp406599c
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Bui KH, Yagi T, Yamamoto R, Kamiya R, Ishikawa T
Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme
Journal of Cell Biology. 2012; 198(5): 913-925. https://doi.org/10.1083/jcb.201201120
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Ishikawa T
Structural biology of cytoplasmic and axonemal dyneins
Journal of Structural Biology. 2012; 179(2): 229-234. https://doi.org/10.1016/j.jsb.2012.05.016
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Junker K, Zandomeneghi G, Guo Z, Kissner R, Ishikawa T, Kohlbrecher J, et al.
Mechanistic aspects of the horseradish peroxidase-catalysed polymerisation of aniline in the presence of AOT vesicles as templates
RSC Advances. 2012; 2(16): 6478-6495. https://doi.org/10.1039/c2ra20566a
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Liebi M, Kohlbrecher J, Ishikawa T, Fischer P, Walde P, Windhab EJ
Cholesterol increases the magnetic aligning of bicellar disks from an aqueous mixture of DMPC and DMPE-DTPA with complexed thulium ions
Langmuir. 2012; 28(29): 10905-10915. https://doi.org/10.1021/la3019327
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Lowell AN, Qiao H, Liu T, Ishikawa T, Zhang H, Oriana S, et al.
Functionalized low-density lipoprotein nanoparticles for in vivo enhancement of atherosclerosis on magnetic resonance images
Bioconjugate Chemistry. 2012; 23(11): 2313-2319. https://doi.org/10.1021/bc300561e
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Maheshwari A, Ishikawa T
Heterogeneity of dynein structure implies coordinated suppression of dynein motor activity in the axoneme
Journal of Structural Biology. 2012; 179(2): 235-241. https://doi.org/10.1016/j.jsb.2012.04.018
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Pigino G, Maheshwari A, Bui KH, Shingyoji C, Kamimura S, Ishikawa T
Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins
Journal of Structural Biology. 2012; 178(2): 199-206. https://doi.org/10.1016/j.jsb.2012.02.012
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Tokutsu R, Kato N, Bui KH, Ishikawa T, Minagawa J
Revisiting the supramolecular organization of photosystem II in Chlamydomonas reinhardtii
Journal of Biological Chemistry. 2012; 287(37): 31574-31581. https://doi.org/10.1074/jbc.M111.331991
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Ueno H, Ishikawa T, Bui KH, Gonda K, Ishikawa T, Yamaguchi T
Analysis of ciliary motion and the axonemal structure in the mouse respiratory cilia
In: ASME 2012 summer bioengineering conference, SBC 2012. ; 2012:(2 pp.). https://doi.org/10.1115/SBC2012-80232
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Ueno H, Ishikawa T, Bui KH, Gonda K, Ishikawa T, Yamaguchi T
Mouse respiratory cilia with the asymmetric axonemal structure on sparsely distributed ciliary cells can generate overall directional flow
Nanomedicine: Nanotechnology, Biology and Medicine. 2012; 8(7): 1081-1087. https://doi.org/10.1016/j.nano.2012.01.004
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Bui KH, Pigino G, Ishikawa T
Three-dimensional structural analysis of eukaryotic flagella/cilia by electron cryo-tomography
Journal of Synchrotron Radiation. 2011; 18(1): 2-5. https://doi.org/10.1107/S0909049510036812
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Ishikawa T
3D structures of axonemes
In: Hirose K, ed. Handbook of Dynein. New York: Jenny Stanford Publishing; 2011:245-266. https://doi.org/10.1201/b11622
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Ishikawa T
Organization of dyneins in the axoneme
In: King SM, ed. Dyneins. Structure, biology and disease. Elsevier; 2011:244-271. https://doi.org/10.1016/B978-0-12-382004-4.10008-1
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Pigino G, Bui KH, Maheshwari A, Lupetti P, Diener D, Ishikawa T
Cryoelectron tomography of radial spokes in cilia and flagella
Journal of Cell Biology. 2011; 195(4): 673-687. https://doi.org/10.1083/jcb.201106125
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Benoit RM, Meisner N-C, Kallen J, Graff P, Hemmig R, Cèbe R, et al.
The X-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible hur redox sensing mechanism
Journal of Molecular Biology. 2010; 397(5): 1231-1244. https://doi.org/10.1016/j.jmb.2010.02.043
DORA PSI