School of Molecular Biosciences

Professor Kostas Tokatlidis

  • Cathcart Chair, Director of Research (Molecular Biosciences)

telephone: 01413306775
email: Kostas.Tokatlidis@glasgow.ac.uk
pronouns: He/him/his

University of Glasgow, School of Molecular Biosciences, Room 217 Davidson Building, University Avenue, Glasgow, G12 8QQ

Import to contacts

ORCID iDhttps://orcid.org/0000-0001-6295-8183

Personal assistant: Ms Bohan Yang
email: Bohan.Yang@glasgow.ac.uk

Research interests

'Mitochondria biogenesis (protein targeting/folding/assembly) in health and disease' 

Research groups

Publications

List by: Type | Date

Jump to: 2026 | 2025 | 2024 | 2022 | 2021 | 2020 | 2019 | 2018 | 2017 | 2016 | 2015 | 2014 | 2013 | 2012 | 2011 | 2010 | 2009 | 2008 | 2007 | 2006 | 2005 | 2004 | 2003 | 2002 | 2001 | 2000 | 1999
Number of items: 66.

2026

van der Schans, Fara, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Vitali, Daniela G. ORCID logoORCID: https://orcid.org/0000-0003-4468-1066 (2026) In and out of the mitochondrial intermembrane space. Protein Science, (Accepted for Publication)

2025

Eaglesfield, Ross, Fernandez-Vizarra, Erika, Lacko, Erik, Caldwell, Stuart T. ORCID logoORCID: https://orcid.org/0000-0003-1604-3462, Sloan, Nikki L., Siciarz, Daniel, Hartley, Richard C. ORCID logoORCID: https://orcid.org/0000-0003-1033-5405 and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2025) Sub-organellar mitochondrial hydrogen peroxide observed using a SNAP tag targeted coumarin-based fluorescent reporter. Redox Biology, 80, 103502. (doi: 10.1016/j.redox.2025.103502) (PMID:39864323) (PMCID:PMC11802384)

2024

Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2024) MIMAS is a new giant multifunctional player in the mitochondrial megacomplex playground. Cell Reports, 43(3), 113874. (doi: 10.1016/j.celrep.2024.113874) (PMID:38386551)

2022

Caccavale, Elio, Johnson, Michael Pierre, Brijbassi, Sonya, Andreazza, Ana C. and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2022) Mitochondria and Us: from exploration to global collective. Biochemist, 44(4), pp. 22-28. (doi: 10.1042/bio_2022_122)

Ledahawsky, L. M. et al. (2022) The mitochondrial protein Sideroflexin 3 (SFXN3) influences neurodegeneration pathways in vivo. FEBS Journal, 289(13), pp. 3894-3914. (doi: 10.1111/febs.16377) (PMID:35092170) (PMCID:PMC9542548)

2021

Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Eaglesfield, Ross (2021) Targeting and insertion of membrane proteins in mitochondria. Frontiers in Cell and Developmental Biology, 9, 803205. (doi: 10.3389/fcell.2021.803205) (PMID:35004695) (PMCID:PMC8740019)

Geldon, Stefan, Fernandez-Vizarra, Erika and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) Redox-mediated regulation of mitochondrial biogenesis, dynamics and respiratory chain assembly in yeast and human cells. Frontiers in Cell and Developmental Biology, 9, 720656. (doi: 10.3389/fcell.2021.720656) (PMID:34557489) (PMCID:PMC8452992)

Edwards, Ruairidh, Eaglesfield, Ross and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways. Open Biology, 11(3), 210002. (doi: 10.1098/rsob.210002) (PMID:33715390) (PMCID:PMC8061763)

Dickson-Murray, Eleanor, Nedara, Kenza, Modjtahedi, Nazanine and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) The Mia40/CHCHD4 oxidative folding system: Redox regulation and signaling in the mitochondrial intermembrane space. Antioxidants, 10(4), 592. (doi: 10.3390/antiox10040592) (PMID:33921425) (PMCID:PMC8069373)

Dimogkioka, Anna-Roza, Lees, Jamie, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Lacko, Erik (2021) Protein import in mitochondria biogenesis: Guided by targeting signals and sustained by dedicated chaperones. RSC Advances, 11(51), pp. 32476-32493. (doi: 10.1039/D1RA04497D)

2020

Reinhardt, Camille, Arena, Giuseppe, Nedara, Kenza, Edwards, Ruairidh, Brenner, Catherine, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Modjtahedi, Nazanine (2020) AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway. Biochimica et Biophysica Acta: Molecular Basis of Disease, 1866(6), 165746. (doi: 10.1016/j.bbadis.2020.165746) (PMID:32105825)

Edwards, Ruairidh, Gerlich, Sarah and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2020) The biogenesis of mitochondrial intermembrane space proteins. Biological Chemistry, 401(6-7), pp. 737-747. (doi: 10.1515/hsz-2020-0114) (PMID:32061164)

2019

Edwards, Ruairidh and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2019) The yeast voltage-dependent anion channel Porin: more IMPORTant than just metabolite transport. Molecular Cell, 73(5), pp. 861-862. (doi: 10.1016/j.molcel.2019.02.028) (PMID:30849391)

Purohit, Paresh Kumar, Edwards, Ruairidh, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Saini, Neeru (2019) MiR-195 regulates mitochondrial function by targeting mitofusin-2 in breast cancer cells. RNA Biology, 16(7), pp. 918-929. (doi: 10.1080/15476286.2019.1600999) (PMID:30932749) (PMCID:PMC6546347)

2018

Tokatlidis, Konstas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2018) Shaping the import system of mitochondria. eLife, 7, e38209. (doi: 10.7554/elife.38209) (PMID:29923828) (PMCID:PMC6010340)

Cardenas-Rodriguez, Mauricio, Chatzi, Afroditi and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2018) Iron–sulfur clusters: from metals through mitochondria biogenesis to disease. Journal of Biological Inorganic Chemistry, 23(4), pp. 509-520. (doi: 10.1007/s00775-018-1548-6) (PMID:29511832) (PMCID:PMC6006200)

Egea, J. et al. (2018) Corrigendum to “European contribution to the study of ROS: a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)” [Redox Biol. 13 (2017) 94–162]. Redox Biology, 14, pp. 694-696. (doi: 10.1016/j.redox.2017.10.001) (PMID:29107648)

2017

Egea, J. et al. (2017) European contribution to the study of ROS: a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS). Redox Biology, 13, pp. 94-162. (doi: 10.1016/j.redox.2017.05.007) (PMID:28577489)

Cardenas-Rodriguez, Mauricio and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space. FEBS Letters, 591(17), pp. 2661-2670. (doi: 10.1002/1873-3468.12766) (PMID:28746987) (PMCID:PMC5601281)

MacPherson, Lisa ORCID logoORCID: https://orcid.org/0000-0003-3224-9233 and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease. Biochemical Journal, 474(15), pp. 2533-2545. (doi: 10.1042/BCJ20160627) (PMID:28701417) (PMCID:PMC5509380)

Kritsiligkou, Paraskevi, Chatzi, Afroditi, Charalampous, Georgia, Mironov, Alexsandr, Grant, Chris M. and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Unconventional targeting of a thiol peroxidase to the mitochondrial intermembrane space facilitates oxidative protein folding. Cell Reports, 18(11), pp. 2729-2741. (doi: 10.1016/j.celrep.2017.02.053) (PMID:28297675) (PMCID:PMC5368413)

Manganas, Phanee, MacPherson, Lisa and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space. Cell and Tissue Research, 367(1), pp. 43-57. (doi: 10.1007/s00441-016-2488-5) (PMID:27632163) (PMCID:PMC5203823)

2016

Nuebel, Esther, Manganas, Phanee and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: new pathways and metabolic cross-talk. Biochimica et Biophysica Acta: Molecular Cell Research, 1863(11), pp. 2613-2623. (doi: 10.1016/j.bbamcr.2016.07.004) (PMID:27425144) (PMCID:PMC5404111)

Kalef-Ezra, Ester, Kotzamani, Dimitra, Zaganas, Ioannis, Katrakili, Nitsa, Plaitakis, Andreas and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence. Biochemical Journal, 473(18), pp. 2813-2829. (doi: 10.1042/BCJ20160535) (PMID:27422783) (PMCID:PMC5095901)

Chatzi, Afroditi, Manganas, Phanee and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Oxidative folding in the mitochondrial intermembrane space: a regulated process important for cell physiology and disease. Biochimica et Biophysica Acta: Molecular Cell Research, 1863(6 Pt.A), pp. 1298-1306. (doi: 10.1016/j.bbamcr.2016.03.023) (PMID:27033519)

Modjtahedi, Nazanine, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183, Dessen, Philippe and Kroemer, Guido (2016) Mitochondrial proteins containing coiled-coil-helix-coiled-coil-helix (CHCH) domains in health and disease. Trends in Biochemical Sciences, 41(3), pp. 245-260. (doi: 10.1016/j.tibs.2015.12.004) (PMID:26782138)

2015

Hangen, E. et al. (2015) Interaction between AIF and CHCHD4 regulates respiratory chain biogenesis. Molecular Cell, 58(6), pp. 1001-1014. (doi: 10.1016/j.molcel.2015.04.020) (PMID:26004228)

Mordas, Amelia and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2015) The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis. Accounts of Chemical Research, 48(8), pp. 2191-2199. (doi: 10.1021/acs.accounts.5b00150) (PMID:26214018) (PMCID:PMC4551283)

2014

Kallergi, E., Kalef-Ezra, E., Karagouni-Dalakoura, K. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2014) Common players in mitochondria biogenesis and neuronal protection against stress-induced apoptosis. Neurochemical Research, 39(3), pp. 546-555. (doi: 10.1007/s11064-013-1109-x)

2013

Chatzi, A., Sideris, D.P., Katrakili, N., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2013) Biogenesis of yeast Mia40 - uncoupling folding from import and atypical recognition features. FEBS Journal, 280(20), pp. 4960-4969. (doi: 10.1111/febs.12482)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Brown, G.C. (2013) Introduction: focus on mitochondria. FEBS Journal, 280(20), p. 4932. (doi: 10.1111/febs.12504)

Chatzi, Afroditi and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2013) The mitochondrial intermembrane space: a hub for oxidative folding linked to protein biogenesis. Antioxidants and Redox Signaling, 19(1), pp. 54-62. (doi: 10.1089/ars.2012.4855) (PMID:22901034)

Banci, L. et al. (2013) An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control. Journal of Molecular Biology, 425(3), pp. 594-608. (doi: 10.1016/j.jmb.2012.11.032)

2012

Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2012) An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR. Journal of the American Chemical Society, 134(3), pp. 1442-1445. (doi: 10.1021/ja209881f)

Kallergi, E. et al. (2012) Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space. ACS Chemical Biology, 7(4), pp. 707-714. (doi: 10.1021/cb200485b)

2011

Banci, L., Bertini, I., Ciofi-Baffoni, S., Boscaro, F., Chatzi, A., Mikolajczyk, M., Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Winkelmann, J. (2011) Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. Chemistry and Biology, 18(6), pp. 794-804. (doi: 10.1016/j.chembiol.2011.03.015) (PMID:21700214)

Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A., Kallergi, E., Lionaki, E., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2011) Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR. Proceedings of the National Academy of Sciences of the United States of America, 108(12), pp. 4811-4816. (doi: 10.1073/pnas.1014542108)

2010

Banci, L. et al. (2010) Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import. Proceedings of the National Academy of Sciences of the United States of America, 107(47), pp. 20190-20195. (doi: 10.1073/pnas.1010095107)

Lionaki, E., Aivaliotis, M., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria. Antioxidants and Redox Signaling, 13(9), pp. 1327-1339. (doi: 10.1089/ars.2010.3200)

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) Oxidative protein folding in the mitochondrial intermembrane space. Antioxidants and Redox Signaling, 13(8), pp. 1189-1204. (doi: 10.1089/ars.2010.3157)

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) Trapping oxidative folding intermediates during translocation to the intermembrane space of mitochondria: in vivo and in vitro studies. In: Economou, A. (ed.) Protein Secretion. Series: Methods in molecular biology (619). Humana Press: New York, NY, USA, pp. 411-423. ISBN 9781603271677 (doi: 10.1007/978-1-60327-412-8_25)

2009

Sideris, D.P., Petrakis, N., Katrakili, N., Mikropoulou, D., Gallo, A., Ciofi-Baffoni, S., Banci, L., Bertini, I. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding. Journal of Cell Biology, 187(7), pp. 1007-1022. (doi: 10.1083/jcb.200905134)

Petrakis, N., Alcock, F. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) Mitochondrial ATP-independent chaperones. IUBMB Life, 61(9), pp. 909-914. (doi: 10.1002/iub.235)

Banci, Lucia, Bertini, Ivano, Ciofi-Baffoni, Simone and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) The coiled coil-helix-coiled coil-helix proteins may be redox proteins. FEBS Letters, 583(11), pp. 1699-1702. (doi: 10.1016/j.febslet.2009.03.061)

Banci, L., Bertini, I., Cefaro, C., Ciofi-Baffoni, S., Gallo, A., Martinelli, M., Sideris, D.P., Katrakili, N. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. Nature Structural and Molecular Biology, 16(2), pp. 198-206. (doi: 10.1038/nsmb.1553)

2008

Roussakis, E., Voutsadaki, S., Pinakoulaki, E., Sideris, D.P., Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Katerinopoulos, H.E. (2008) ICPBCZin: a red emitting ratiometric fluorescent indicator with nanomolar affinity for Zn2+ ions. Cell Calcium, 44(3), pp. 270-275. (doi: 10.1016/j.ceca.2007.12.008)

Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) Complementing structural information of modular proteins with small angle neutron scattering and contrast variation. European Biophysics Journal with Biophysics Letters, 37(5), pp. 603-611. (doi: 10.1007/s00249-008-0278-z)

Alcock, F.H., Grossmann, J.G., Gentle, I.E., Likić, V.A., Lithgow, T. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space. Biochemical Journal, 409(2), pp. 377-387. (doi: 10.1042/BJ20070877)

Lionaki, E., de Marcos Lousa, C., Baud, C., Vougioukalaki, M., Panayotou, G. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain. Journal of Biological Chemistry, 283(23), pp. 15747-15753. (doi: 10.1074/jbc.M800350200)

2007

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space. Molecular Microbiology, 65(5), pp. 1360-1373. (doi: 10.1111/j.1365-2958.2007.05880.x)

Vergnolle, M.A.S., Alcock, F.H., Petrakis, N. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Mutation of conserved charged residues in mitochondrial TIM10 subunits precludes TIM10 complex assembly, but does not abolish growth of yeast cells. Journal of Molecular Biology, 371(5), pp. 1315-1324. (doi: 10.1016/j.jmb.2007.06.025)

Gentle, I.E. et al. (2007) Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space. Molecular Biology and Evolution, 24(5), pp. 1149-1160. (doi: 10.1093/molbev/msm031)

Baud, C., de Marcos-Lousa, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Molecular interactions of the mitochondrial Tim12 translocase subunit. Protein and Peptide Letters, 14(6), pp. 597-600. (doi: 10.2174/092986607780990019)

2006

de Marcos-Lousa, C., P Sideris, D. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2006) Translocation of mitochondrial inner-membrane proteins: conformation matters. Trends in Biochemical Sciences, 31(5), pp. 259-267. (doi: 10.1016/j.tibs.2006.03.006)

2005

Allen, S., Balabanidou, V., Sideris, D.P., Lisowsky, T. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. Journal of Molecular Biology, 353(5), pp. 937-944. (doi: 10.1016/j.jmb.2005.08.049)

Vergnolle, M.A.S., Baud, C., Golovanov, A.P., Alcock, F., Luciano, P., Lian, L.-Y. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) Distinct domains of small tims involved in subunit interaction and substrate recognition. Journal of Molecular Biology, 351(4), pp. 839-849. (doi: 10.1016/j.jmb.2005.06.010)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) A disulfide relay system in mitochondria. Cell, 121(7), pp. 965-967. (doi: 10.1016/j.cell.2005.06.019)

Sawney, H., Vergnolle, M.A.S., Junne, T., Dolfini, L. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery. Biochemical Journal, 385(1), pp. 173-180. (doi: 10.1042/BJ20040650)

2004

Lu, H., Allen, S., Wardleworth, L., Savory, P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2004) Functional TIM10 chaperone assembly is redox-regulated in vivo. Journal of Biological Chemistry, 279(18), pp. 18952-18958. (doi: 10.1074/jbc.M313045200)

2003

Allen, S., Lu, H., Thornton, D. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2003) Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10. Journal of Biological Chemistry, 278(40), pp. 38505-38513. (doi: 10.1074/jbc.M306027200)

Dyall, S.D., Agius, S.C., De Marcos Lousa, C., Trézéguet, V. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2003) The dynamic dimerization of the yeast ADP/ATP carrier in the iunner mitochondrial membrane is affected by conserved cysteine residues. Journal of Biological Chemistry, 278(29), pp. 26757-26764. (doi: 10.1074/jbc.M302700200)

2002

Minczuk, M. et al. (2002) Localisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNA. Nucleic Acids Research, 30(23), pp. 5074-5086. (doi: 10.1093/nar/gkf647)

Vial, S., Lu, H., Allen, S., Savory, P., Thornton, D., Sheerhan, J. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2002) Assembly of Tim9 and Tim10 into a functional chaperone. Journal of Biological Chemistry, 277(39), pp. 36100-36108. (doi: 10.1074/jbc.M202310200)

2001

Luciano, P., Vial, S., Vegnolle, M.A.S., Dyall, S.D., Robinson, D.R. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2001) Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex. EMBO Journal, 20(15), pp. 4099-4106. (doi: 10.1093/emboj/20.15.4099)

2000

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183, Vial, S., Luciano, P., Vergnolle, M. and Clémence, S. (2000) Membrane protein import in yeast mitochondria. Biochemical Society Transactions, 28(4), pp. 495-499. (doi: 10.1042/0300-5127:0280495)

1999

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Schatz, G. (1999) Biogenesis of mitochondrial inner membrane proteins. Journal of Biological Chemistry, 274(50), pp. 35285-35288. (doi: 10.1074/jbc.274.50.35285)

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Number of items: 66.

Articles

van der Schans, Fara, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Vitali, Daniela G. ORCID logoORCID: https://orcid.org/0000-0003-4468-1066 (2026) In and out of the mitochondrial intermembrane space. Protein Science, (Accepted for Publication)

Eaglesfield, Ross, Fernandez-Vizarra, Erika, Lacko, Erik, Caldwell, Stuart T. ORCID logoORCID: https://orcid.org/0000-0003-1604-3462, Sloan, Nikki L., Siciarz, Daniel, Hartley, Richard C. ORCID logoORCID: https://orcid.org/0000-0003-1033-5405 and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2025) Sub-organellar mitochondrial hydrogen peroxide observed using a SNAP tag targeted coumarin-based fluorescent reporter. Redox Biology, 80, 103502. (doi: 10.1016/j.redox.2025.103502) (PMID:39864323) (PMCID:PMC11802384)

Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2024) MIMAS is a new giant multifunctional player in the mitochondrial megacomplex playground. Cell Reports, 43(3), 113874. (doi: 10.1016/j.celrep.2024.113874) (PMID:38386551)

Caccavale, Elio, Johnson, Michael Pierre, Brijbassi, Sonya, Andreazza, Ana C. and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2022) Mitochondria and Us: from exploration to global collective. Biochemist, 44(4), pp. 22-28. (doi: 10.1042/bio_2022_122)

Ledahawsky, L. M. et al. (2022) The mitochondrial protein Sideroflexin 3 (SFXN3) influences neurodegeneration pathways in vivo. FEBS Journal, 289(13), pp. 3894-3914. (doi: 10.1111/febs.16377) (PMID:35092170) (PMCID:PMC9542548)

Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Eaglesfield, Ross (2021) Targeting and insertion of membrane proteins in mitochondria. Frontiers in Cell and Developmental Biology, 9, 803205. (doi: 10.3389/fcell.2021.803205) (PMID:35004695) (PMCID:PMC8740019)

Geldon, Stefan, Fernandez-Vizarra, Erika and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) Redox-mediated regulation of mitochondrial biogenesis, dynamics and respiratory chain assembly in yeast and human cells. Frontiers in Cell and Developmental Biology, 9, 720656. (doi: 10.3389/fcell.2021.720656) (PMID:34557489) (PMCID:PMC8452992)

Edwards, Ruairidh, Eaglesfield, Ross and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways. Open Biology, 11(3), 210002. (doi: 10.1098/rsob.210002) (PMID:33715390) (PMCID:PMC8061763)

Dickson-Murray, Eleanor, Nedara, Kenza, Modjtahedi, Nazanine and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2021) The Mia40/CHCHD4 oxidative folding system: Redox regulation and signaling in the mitochondrial intermembrane space. Antioxidants, 10(4), 592. (doi: 10.3390/antiox10040592) (PMID:33921425) (PMCID:PMC8069373)

Dimogkioka, Anna-Roza, Lees, Jamie, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Lacko, Erik (2021) Protein import in mitochondria biogenesis: Guided by targeting signals and sustained by dedicated chaperones. RSC Advances, 11(51), pp. 32476-32493. (doi: 10.1039/D1RA04497D)

Reinhardt, Camille, Arena, Giuseppe, Nedara, Kenza, Edwards, Ruairidh, Brenner, Catherine, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Modjtahedi, Nazanine (2020) AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway. Biochimica et Biophysica Acta: Molecular Basis of Disease, 1866(6), 165746. (doi: 10.1016/j.bbadis.2020.165746) (PMID:32105825)

Edwards, Ruairidh, Gerlich, Sarah and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2020) The biogenesis of mitochondrial intermembrane space proteins. Biological Chemistry, 401(6-7), pp. 737-747. (doi: 10.1515/hsz-2020-0114) (PMID:32061164)

Edwards, Ruairidh and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2019) The yeast voltage-dependent anion channel Porin: more IMPORTant than just metabolite transport. Molecular Cell, 73(5), pp. 861-862. (doi: 10.1016/j.molcel.2019.02.028) (PMID:30849391)

Purohit, Paresh Kumar, Edwards, Ruairidh, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Saini, Neeru (2019) MiR-195 regulates mitochondrial function by targeting mitofusin-2 in breast cancer cells. RNA Biology, 16(7), pp. 918-929. (doi: 10.1080/15476286.2019.1600999) (PMID:30932749) (PMCID:PMC6546347)

Tokatlidis, Konstas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2018) Shaping the import system of mitochondria. eLife, 7, e38209. (doi: 10.7554/elife.38209) (PMID:29923828) (PMCID:PMC6010340)

Cardenas-Rodriguez, Mauricio, Chatzi, Afroditi and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2018) Iron–sulfur clusters: from metals through mitochondria biogenesis to disease. Journal of Biological Inorganic Chemistry, 23(4), pp. 509-520. (doi: 10.1007/s00775-018-1548-6) (PMID:29511832) (PMCID:PMC6006200)

Egea, J. et al. (2018) Corrigendum to “European contribution to the study of ROS: a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)” [Redox Biol. 13 (2017) 94–162]. Redox Biology, 14, pp. 694-696. (doi: 10.1016/j.redox.2017.10.001) (PMID:29107648)

Egea, J. et al. (2017) European contribution to the study of ROS: a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS). Redox Biology, 13, pp. 94-162. (doi: 10.1016/j.redox.2017.05.007) (PMID:28577489)

Cardenas-Rodriguez, Mauricio and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space. FEBS Letters, 591(17), pp. 2661-2670. (doi: 10.1002/1873-3468.12766) (PMID:28746987) (PMCID:PMC5601281)

MacPherson, Lisa ORCID logoORCID: https://orcid.org/0000-0003-3224-9233 and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease. Biochemical Journal, 474(15), pp. 2533-2545. (doi: 10.1042/BCJ20160627) (PMID:28701417) (PMCID:PMC5509380)

Kritsiligkou, Paraskevi, Chatzi, Afroditi, Charalampous, Georgia, Mironov, Alexsandr, Grant, Chris M. and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Unconventional targeting of a thiol peroxidase to the mitochondrial intermembrane space facilitates oxidative protein folding. Cell Reports, 18(11), pp. 2729-2741. (doi: 10.1016/j.celrep.2017.02.053) (PMID:28297675) (PMCID:PMC5368413)

Manganas, Phanee, MacPherson, Lisa and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2017) Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space. Cell and Tissue Research, 367(1), pp. 43-57. (doi: 10.1007/s00441-016-2488-5) (PMID:27632163) (PMCID:PMC5203823)

Nuebel, Esther, Manganas, Phanee and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: new pathways and metabolic cross-talk. Biochimica et Biophysica Acta: Molecular Cell Research, 1863(11), pp. 2613-2623. (doi: 10.1016/j.bbamcr.2016.07.004) (PMID:27425144) (PMCID:PMC5404111)

Kalef-Ezra, Ester, Kotzamani, Dimitra, Zaganas, Ioannis, Katrakili, Nitsa, Plaitakis, Andreas and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence. Biochemical Journal, 473(18), pp. 2813-2829. (doi: 10.1042/BCJ20160535) (PMID:27422783) (PMCID:PMC5095901)

Chatzi, Afroditi, Manganas, Phanee and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2016) Oxidative folding in the mitochondrial intermembrane space: a regulated process important for cell physiology and disease. Biochimica et Biophysica Acta: Molecular Cell Research, 1863(6 Pt.A), pp. 1298-1306. (doi: 10.1016/j.bbamcr.2016.03.023) (PMID:27033519)

Modjtahedi, Nazanine, Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183, Dessen, Philippe and Kroemer, Guido (2016) Mitochondrial proteins containing coiled-coil-helix-coiled-coil-helix (CHCH) domains in health and disease. Trends in Biochemical Sciences, 41(3), pp. 245-260. (doi: 10.1016/j.tibs.2015.12.004) (PMID:26782138)

Hangen, E. et al. (2015) Interaction between AIF and CHCHD4 regulates respiratory chain biogenesis. Molecular Cell, 58(6), pp. 1001-1014. (doi: 10.1016/j.molcel.2015.04.020) (PMID:26004228)

Mordas, Amelia and Tokatlidis, Konstantinos ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2015) The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis. Accounts of Chemical Research, 48(8), pp. 2191-2199. (doi: 10.1021/acs.accounts.5b00150) (PMID:26214018) (PMCID:PMC4551283)

Kallergi, E., Kalef-Ezra, E., Karagouni-Dalakoura, K. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2014) Common players in mitochondria biogenesis and neuronal protection against stress-induced apoptosis. Neurochemical Research, 39(3), pp. 546-555. (doi: 10.1007/s11064-013-1109-x)

Chatzi, A., Sideris, D.P., Katrakili, N., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2013) Biogenesis of yeast Mia40 - uncoupling folding from import and atypical recognition features. FEBS Journal, 280(20), pp. 4960-4969. (doi: 10.1111/febs.12482)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Brown, G.C. (2013) Introduction: focus on mitochondria. FEBS Journal, 280(20), p. 4932. (doi: 10.1111/febs.12504)

Chatzi, Afroditi and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2013) The mitochondrial intermembrane space: a hub for oxidative folding linked to protein biogenesis. Antioxidants and Redox Signaling, 19(1), pp. 54-62. (doi: 10.1089/ars.2012.4855) (PMID:22901034)

Banci, L. et al. (2013) An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control. Journal of Molecular Biology, 425(3), pp. 594-608. (doi: 10.1016/j.jmb.2012.11.032)

Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2012) An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR. Journal of the American Chemical Society, 134(3), pp. 1442-1445. (doi: 10.1021/ja209881f)

Kallergi, E. et al. (2012) Targeting and maturation of Erv1/ALR in the mitochondrial intermembrane space. ACS Chemical Biology, 7(4), pp. 707-714. (doi: 10.1021/cb200485b)

Banci, L., Bertini, I., Ciofi-Baffoni, S., Boscaro, F., Chatzi, A., Mikolajczyk, M., Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Winkelmann, J. (2011) Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. Chemistry and Biology, 18(6), pp. 794-804. (doi: 10.1016/j.chembiol.2011.03.015) (PMID:21700214)

Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A., Kallergi, E., Lionaki, E., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2011) Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR. Proceedings of the National Academy of Sciences of the United States of America, 108(12), pp. 4811-4816. (doi: 10.1073/pnas.1014542108)

Banci, L. et al. (2010) Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import. Proceedings of the National Academy of Sciences of the United States of America, 107(47), pp. 20190-20195. (doi: 10.1073/pnas.1010095107)

Lionaki, E., Aivaliotis, M., Pozidis, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria. Antioxidants and Redox Signaling, 13(9), pp. 1327-1339. (doi: 10.1089/ars.2010.3200)

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) Oxidative protein folding in the mitochondrial intermembrane space. Antioxidants and Redox Signaling, 13(8), pp. 1189-1204. (doi: 10.1089/ars.2010.3157)

Sideris, D.P., Petrakis, N., Katrakili, N., Mikropoulou, D., Gallo, A., Ciofi-Baffoni, S., Banci, L., Bertini, I. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding. Journal of Cell Biology, 187(7), pp. 1007-1022. (doi: 10.1083/jcb.200905134)

Petrakis, N., Alcock, F. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) Mitochondrial ATP-independent chaperones. IUBMB Life, 61(9), pp. 909-914. (doi: 10.1002/iub.235)

Banci, Lucia, Bertini, Ivano, Ciofi-Baffoni, Simone and Tokatlidis, Kostas ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) The coiled coil-helix-coiled coil-helix proteins may be redox proteins. FEBS Letters, 583(11), pp. 1699-1702. (doi: 10.1016/j.febslet.2009.03.061)

Banci, L., Bertini, I., Cefaro, C., Ciofi-Baffoni, S., Gallo, A., Martinelli, M., Sideris, D.P., Katrakili, N. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2009) MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. Nature Structural and Molecular Biology, 16(2), pp. 198-206. (doi: 10.1038/nsmb.1553)

Roussakis, E., Voutsadaki, S., Pinakoulaki, E., Sideris, D.P., Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Katerinopoulos, H.E. (2008) ICPBCZin: a red emitting ratiometric fluorescent indicator with nanomolar affinity for Zn2+ ions. Cell Calcium, 44(3), pp. 270-275. (doi: 10.1016/j.ceca.2007.12.008)

Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) Complementing structural information of modular proteins with small angle neutron scattering and contrast variation. European Biophysics Journal with Biophysics Letters, 37(5), pp. 603-611. (doi: 10.1007/s00249-008-0278-z)

Alcock, F.H., Grossmann, J.G., Gentle, I.E., Likić, V.A., Lithgow, T. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space. Biochemical Journal, 409(2), pp. 377-387. (doi: 10.1042/BJ20070877)

Lionaki, E., de Marcos Lousa, C., Baud, C., Vougioukalaki, M., Panayotou, G. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2008) The essential function of Tim12 in vivo is ensured by the assembly interactions of its C-terminal domain. Journal of Biological Chemistry, 283(23), pp. 15747-15753. (doi: 10.1074/jbc.M800350200)

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space. Molecular Microbiology, 65(5), pp. 1360-1373. (doi: 10.1111/j.1365-2958.2007.05880.x)

Vergnolle, M.A.S., Alcock, F.H., Petrakis, N. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Mutation of conserved charged residues in mitochondrial TIM10 subunits precludes TIM10 complex assembly, but does not abolish growth of yeast cells. Journal of Molecular Biology, 371(5), pp. 1315-1324. (doi: 10.1016/j.jmb.2007.06.025)

Gentle, I.E. et al. (2007) Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space. Molecular Biology and Evolution, 24(5), pp. 1149-1160. (doi: 10.1093/molbev/msm031)

Baud, C., de Marcos-Lousa, C. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2007) Molecular interactions of the mitochondrial Tim12 translocase subunit. Protein and Peptide Letters, 14(6), pp. 597-600. (doi: 10.2174/092986607780990019)

de Marcos-Lousa, C., P Sideris, D. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2006) Translocation of mitochondrial inner-membrane proteins: conformation matters. Trends in Biochemical Sciences, 31(5), pp. 259-267. (doi: 10.1016/j.tibs.2006.03.006)

Allen, S., Balabanidou, V., Sideris, D.P., Lisowsky, T. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. Journal of Molecular Biology, 353(5), pp. 937-944. (doi: 10.1016/j.jmb.2005.08.049)

Vergnolle, M.A.S., Baud, C., Golovanov, A.P., Alcock, F., Luciano, P., Lian, L.-Y. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) Distinct domains of small tims involved in subunit interaction and substrate recognition. Journal of Molecular Biology, 351(4), pp. 839-849. (doi: 10.1016/j.jmb.2005.06.010)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) A disulfide relay system in mitochondria. Cell, 121(7), pp. 965-967. (doi: 10.1016/j.cell.2005.06.019)

Sawney, H., Vergnolle, M.A.S., Junne, T., Dolfini, L. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2005) A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery. Biochemical Journal, 385(1), pp. 173-180. (doi: 10.1042/BJ20040650)

Lu, H., Allen, S., Wardleworth, L., Savory, P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2004) Functional TIM10 chaperone assembly is redox-regulated in vivo. Journal of Biological Chemistry, 279(18), pp. 18952-18958. (doi: 10.1074/jbc.M313045200)

Allen, S., Lu, H., Thornton, D. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2003) Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10. Journal of Biological Chemistry, 278(40), pp. 38505-38513. (doi: 10.1074/jbc.M306027200)

Dyall, S.D., Agius, S.C., De Marcos Lousa, C., Trézéguet, V. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2003) The dynamic dimerization of the yeast ADP/ATP carrier in the iunner mitochondrial membrane is affected by conserved cysteine residues. Journal of Biological Chemistry, 278(29), pp. 26757-26764. (doi: 10.1074/jbc.M302700200)

Minczuk, M. et al. (2002) Localisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNA. Nucleic Acids Research, 30(23), pp. 5074-5086. (doi: 10.1093/nar/gkf647)

Vial, S., Lu, H., Allen, S., Savory, P., Thornton, D., Sheerhan, J. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2002) Assembly of Tim9 and Tim10 into a functional chaperone. Journal of Biological Chemistry, 277(39), pp. 36100-36108. (doi: 10.1074/jbc.M202310200)

Luciano, P., Vial, S., Vegnolle, M.A.S., Dyall, S.D., Robinson, D.R. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2001) Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex. EMBO Journal, 20(15), pp. 4099-4106. (doi: 10.1093/emboj/20.15.4099)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183, Vial, S., Luciano, P., Vergnolle, M. and Clémence, S. (2000) Membrane protein import in yeast mitochondria. Biochemical Society Transactions, 28(4), pp. 495-499. (doi: 10.1042/0300-5127:0280495)

Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 and Schatz, G. (1999) Biogenesis of mitochondrial inner membrane proteins. Journal of Biological Chemistry, 274(50), pp. 35285-35288. (doi: 10.1074/jbc.274.50.35285)

Book Sections

Sideris, D.P. and Tokatlidis, K. ORCID logoORCID: https://orcid.org/0000-0001-6295-8183 (2010) Trapping oxidative folding intermediates during translocation to the intermembrane space of mitochondria: in vivo and in vitro studies. In: Economou, A. (ed.) Protein Secretion. Series: Methods in molecular biology (619). Humana Press: New York, NY, USA, pp. 411-423. ISBN 9781603271677 (doi: 10.1007/978-1-60327-412-8_25)

This list was generated on Sat Jan 31 19:54:06 2026 GMT.

Grants

Grants and Awards listed are those received whilst working with the University of Glasgow.

  • MAINSTREAM: EPSRC Research and Partnership Hub for Health Technologies in Manufacturing Stem Cells
    Engineering and Physical Sciences Research Council
    2025 - 2031
     
  • Mitotrapin
    Medical Research Council
    2024 - 2025
     
  • Strengthening international partnerships
    Biotechnology and Biological Sciences Research Council
    2024 - 2024
     
  • Mitotargin stability ADME
    Medical Research Council
    2023 - 2023
     
  • Establishing global partnerships and KE activities for the Mitochondria Research Centre
    Biotechnology and Biological Sciences Research Council
    2022 - 2023
     
  • Defining the market for a novel mitochondria diagnostics platform
    Scottish Enterprise
    2022 - 2022
     
  • Mitochondrial proteostasis and reductive metabolic stress in ageing
    Biotechnology and Biological Sciences Research Council
    2021 - 2024
     
  • A first-in-class peptide-based platform delivery technology to modulate mitochondria function in disease
    Medical Research Council
    2021 - 2022
     
  • A first-in-class peptie-based platform delivery technology to modulate mitochondria function in disease
    Medical Research Council
    2021 - 2022
     
  • A first-in-class peptide-based platform delivery technology to modulate mitochondria function in disease
    Medical Research Council
    2021 - 2022
     
  • Host mitochrondria dysfunction by viral hijacking as a key pathogenicity mechanism in COVID-19
    Wellcome Trust
    2020 - 2021
     
  • How does a novel targeting peptide direct proteins to mitochondria in response to oxidative stress?
    University of Edinburgh
    2020 - 2021
     
  • Mitochondrial ROS mapping and control with sub-organellar resolution
    Biotechnology and Biological Sciences Research Council
    2020 - 2023
     
  • Market research for commercial development of a novel peptide tool
    Medical Research Council
    2019 - 2020
     
  • Mitochondria salvage via a novel antioxidant protein import pathway
    Biotechnology and Biological Sciences Research Council
    2018 - 2021
     
  • Analysis of a novel protein translocation pathway of the mitchondrial intermembrane space
    Lister Institute of Preventive Medicine
    2018 - 2018
     
  • Thiol Modification and Redox Signalling
    Medical Research Council
    2016 - 2018
     
  • Oxidative Folding and Redox Signalling in the Mitochondria Intermembrane Space.
    The Royal Society
    2013 - 2018
     

Supervision

  • Lacko, Erik
    Temperature regulation of mitochondria function, architecture and biogenesis
  • McNulty, Flora Elisabeth
    The impact of cancer-associated mitochondrial DNA mutations on tumour metabolism
  • Sabha, Bassam Hassan A
    Using a molecular biology approach to understand the role of heat shock protein co-chaperones in normal physiology and disease.
  • Siciarz, Daniel
    Mitochondria redox biogenesis and metabolic Raman imaging in insulin signalling
  • Van Der Schans, Fara
    Targeting therapy-resistant cancer cells via mitochondrial biogenesis
  • Wang, Lei
    Dissecting how and why damage mitochondria accumulate during ageing
  • Wang, Zejia
    Unconventional protein import into the mitochondrial intermembrane space as a backup mechanism to sustain Erv1/ALR function under stress conditions
  • Zhang, Naichuan
    Regulation of mitochondrial dynamics, mitophagy and biogenesis by the redox balance of the intermembrane space

Teaching

Coordinator - Level 4 Mitochondrial Biology option course

Coordinator and Lecturer - Redox Biology module of MSc in Chemical Biology

Lectures in 

Level 4 Central Approaches in Biochemistry

Level 4 Cell compartmentalisation

Level 4 Mitochondrial Biology

Tutorials in Level 3 Biochemistry


Kostas Tokatlidis

Professor Kostas Tokatlidis on Twitter