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Reconstitution of the Mia40-Erv1 Oxidative Folding Pathway for the Small Tim Proteins

Tienson, H. L., Dabir, D. V., Neal, S. E., Loo, R. O., Hasson, S. A., Boontheung, P., Kim, S., Loo, J. A., & Koehler, C. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-10-1062 · Cited by 69 · see citing works

The MIA Pathway: A Key Regulator of Mitochondrial Oxidative Protein Folding and Biogenesis

Mordas, A. V., & Tokatlidis, K. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00150 · Cited by 67 · see citing works

Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochromecoxidase

Bode, M., Woellhaf, M. W., Bohnert, M., van der Laan, M., Sommer, F., Jung, M., Zimmermann, R., Schroda, M., & Herrmann, J. M. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-11-1526 · Cited by 67 · see citing works

The complex of cytochrome c and cytochrome c peroxidase: The end of the road?

Volkov, A. N., Nicholls, P. J., & Worrall, J. A. R. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.07.010 · Cited by 64 · see citing works

Augmenter of Liver Regeneration: Substrate Specificity of a Flavin-Dependent Oxidoreductase from the Mitochondrial Intermembrane Space

Daithankar, V. N., Farrell, S. R., & Thorpe, C. (2009) · Biochemistry · doi:10.1021/bi900347v · Cited by 63 · see citing works

Enhancement of perfluorooctanoic acid and perfluorooctane sulphonic acid removal in constructed wetland using iron mineral: Performance and mechanisms

Ma, H., Kang, Y., Li, M., Dong, J., Wang, Y., Xiao, J., & Guo, Z. (2023) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2023.130819 · Cited by 62 · see citing works

Redox regulation of protein folding in the mitochondrial intermembrane space

Koehler, C. M., & Tienson, H. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.08.002 · Cited by 62 · see citing works

A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import

Ramesh, A., Peleh, V., Martinez‐Caballero, S., Wollweber, F., Sommer, F., van der Laan, M., Schroda, M., Alexander, R. T., Campo, M. L., & Herrmann, J. M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201602074 · Cited by 62 · see citing works

Mechanisms of Protein Sorting in MitochondriaPreprint

Stojanovski, D., Bohnert, M., Pfanner, N., & van der Laan, M. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011320 · Cited by 63 · see citing works

Biophysical Characterization of Iron in Mitochondria Isolated from Respiring and Fermenting Yeast

Morales, J. G., Holmes‐Hampton, G. P., Miao, R., Guo, Y., Münck, E., & Lindahl, P. A. (2010) · Biochemistry · doi:10.1021/bi100558z · Cited by 60 · see citing works

Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system

Gross, D., Burgard, C., Reddehase, S., Leitch, J. M., Culotta, V., & Hell, K. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0296 · Cited by 59 · see citing works

Oxidation-driven protein import into mitochondria: Insights and blind spots

Riemer, J., Fischer, M., & Herrmann, J. M. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.06.003 · Cited by 58 · see citing works

AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway

Reinhardt, C., Arena, G., Nedara, K., Edwards, R., Brenner, C., Tokatlidis, K., & Modjtahedi, N. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165746 · Cited by 58 · see citing works

Redox-Mediated Regulation of Mitochondrial Biogenesis, Dynamics, and Respiratory Chain Assembly in Yeast and Human Cells

Geldon, S., Fernández‐Vizarra, E., & Tokatlidis, K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.720656 · Cited by 55 · see citing works

Augmenter of liver regeneration: Mitochondrial function and steatohepatitis

Verma, A. K., Sharma, A., Nithyananthan, S., & Gandhi, C. R. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2022.06.019 · Cited by 56 · see citing works

Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum

Roscoe, J. M., & Sevier, C. S. (2020) · Cells · doi:10.3390/cells9102314 · Cited by 55 · see citing works

Distinctive biochemistry in the trypanosome mitochondrial intermembrane space suggests a model for stepwise evolution of the MIA pathway for import of cysteine‐rich proteins

Allen, J. W. A., Ferguson, S. J., & Ginger, M. L. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.07.015 · Cited by 55 · see citing works

Cysteine Oxidations in Mitochondrial Membrane Proteins: The Case of VDAC Isoforms in Mammals

Reina, S., Pittalà, M. G. G., Guarino, F., Messina, A. A., Pinto, V. D., Foti, S., & Saletti, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00397 · Cited by 55 · see citing works

Thiol oxidation in bacteria, mitochondria and chloroplasts: Common principles but three unrelated machineries?

Herrmann, J. M., Kauff, F., & Neuhaus, H. E. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.05.001 · Cited by 54 · see citing works

Disulphide Bond Formation in the Intermembrane Space of Mitochondria

Deponte, M., & Hell, K. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp133 · Cited by 52 · see citing works

The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways

Edwards, R., Eaglesfield, R., & Tokatlidis, K. (2021) · Open Biology · doi:10.1098/rsob.210002 · Cited by 50 · see citing works

Structure of the Human Sulfhydryl Oxidase Augmenter of Liver Regeneration and Characterization of a Human Mutation Causing an Autosomal Recessive Myopathy,

Daithankar, V. N., Schaefer, S., Dong, M., Bahnson, B. J., & Thorpe, C. (2010) · Biochemistry · doi:10.1021/bi100912m · Cited by 51 · see citing works

Deciphering Structural and Functional Roles of Individual Disulfide Bonds of the Mitochondrial Sulfhydryl Oxidase Erv1p

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The Mitochondrial Disulfide Relay System: Roles in Oxidative Protein Folding and Beyond

Fischer, M., & Riemer, J. (2013) · International Journal of Cell Biology · doi:10.1155/2013/742923 · Cited by 50 · see citing works

Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation

Sayyed, U. M. H., & Mahalakshmi, R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101870 · Cited by 47 · see citing works

Genetic and phylogenetic analysis of dissimilatory iodate-reducing bacteria identifies potential niches across the world’s oceans

Reyes-Umana, V., Henning, Z., Lee, K., Barnum, T. P., & Coates, J. D. (2021) · The ISME Journal · doi:10.1038/s41396-021-01034-5 · Cited by 47 · see citing works

Structural Basis for the Disulfide Relay System in the Mitochondrial Intermembrane Space

Endo, T., Yamano, K., & Kawano, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3099 · Cited by 46 · see citing works

The biogenesis of mitochondrial intermembrane space proteins

Edwards, R., Gerlich, S., & Tokatlidis, K. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0114 · Cited by 46 · see citing works

Divergence of Erv1-Associated Mitochondrial Import and Export Pathways in Trypanosomes and Anaerobic Protists

Basu, S., Leonard, J. C., Desai, N., Mavridou, D. A. I., Tang, K. H., Goddard, A. D., Ginger, M. L., Lukeš, J., & Allen, J. W. A. (2012) · Eukaryotic Cell · doi:10.1128/ec.00304-12 · Cited by 45 · see citing works

Energetics of protein translocation into mitochondria

Mokranjac, D., & Neupert, W. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.009 · Cited by 45 · see citing works

Oxidative Protein-Folding Systems in Plant Cells

Onda, Y. (2013) · International Journal of Cell Biology · doi:10.1155/2013/585431 · Cited by 45 · see citing works

The power of yeast to model diseases of the powerhouse of the cell

Claypool, S. M. (2012) · Frontiers in bioscience · doi:10.2741/4098 · Cited by 42 · see citing works

Biogenesis of Mitochondrial Proteins

Herrmann, J. M., Longen, S., Weckbecker, D., & Depuydt, M. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_3 · Cited by 43 · see citing works

Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and disease

Chatzi, A., Manganas, P., & Tokatlidis, K. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.03.023 · Cited by 42 · see citing works

Osm1 facilitates the transfer of electrons from Erv1 to fumarate in the redox-regulated import pathway in the mitochondrial intermembrane space

Neal, S. E., Dabir, D. V., Wijaya, J., Boon, C., & Koehler, C. M. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-10-0712 · Cited by 41 · see citing works

Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40

Peleh, V., Zannini, F., Backes, S., Rouhier, N., & Herrmann, J. M. (2017) · BMC Biology · doi:10.1186/s12915-017-0445-8 · Cited by 41 · see citing works

Post-Translational Modifications of Cytochrome c in Cell Life and Disease

Guerra‐Castellano, A., Márquez, I., Pérez‐Mejías, G., Dı́az-Quintana, A., la Rosa, M. Á. D., & Díaz‐Moreno, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228483 · Cited by 41 · see citing works

Mitochondrial protein import machineries and lipids: A functional connection

Gebert, N., Ryan, M. T., Pfanner, N., Wiedemann, N., & Stojanovski, D. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.08.003 · Cited by 38 · see citing works

The Mia40/CHCHD4 Oxidative Folding System: Redox Regulation and Signaling in the Mitochondrial Intermembrane Space

Dickson-Murray, E., Nedara, K., Modjtahedi, N., & Tokatlidis, K. (2021) · Antioxidants · doi:10.3390/antiox10040592 · Cited by 38 · see citing works

Novel insights into the mechanism of electron transfer in mitochondrial cytochrome c

Pérez‐Mejías, G., Dı́az-Quintana, A., Guerra‐Castellano, A., Díaz‐Moreno, I., & la Rosa, M. Á. D. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214233 · Cited by 37 · see citing works

The N-terminal Shuttle Domain of Erv1 Determines the Affinity for Mia40 and Mediates Electron Transfer to the Catalytic Erv1 Core in Yeast Mitochondria

Lionaki, E., Aivaliotis, M., Pozidis, C., & Tokatlidis, K. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3200 · Cited by 35 · see citing works

Role of the Mitochondrial Protein Import Machinery and Protein Processing in Heart Disease

Zhao, F., & Zou, M.-H. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.749756 · Cited by 28 · see citing works

Three Approaches to One Problem: Protein Folding in the Periplasm, the Endoplasmic Reticulum, and the Intermembrane Space

Herrmann, J. M., & Riemer, J. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5841 · Cited by 33 · see citing works

Electron Transfer Interactome of Cytochrome c

Volkov, A. N., & van Nuland, N. A. J. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002807 · Cited by 33 · see citing works

Fe/S protein biogenesis in trypanosomes — A review

Lukeš, J., & Basu, S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.08.015 · Cited by 31 · see citing works

Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding

Moilanen, A., Korhonen, K., Saaranen, M. J., & Ruddock, L. W. (2018) · Life Science Alliance · doi:10.26508/lsa.201800090 · Cited by 31 · see citing works

The Journey of Mitochondrial Protein Import and the Roadmap to Follow

Haastrup, M. O., Vikramdeo, K. S., Singh, S., Singh, A. P., & Dasgupta, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032479 · Cited by 30 · see citing works

The oxidative protein folding machinery in plant cells

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The Mitochondrial Intermembrane Space: A Hub for Oxidative Folding Linked to Protein Biogenesis

Chatzi, A., & Tokatlidis, K. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4855 · Cited by 29 · see citing works

Cytochrome c signalosome in mitochondria

Díaz‐Moreno, I., García-Heredia, J. M., Dı́az-Quintana, A., & la Rosa, M. Á. D. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0774-4 · Cited by 28 · see citing works

Mitochondrial disulfide relay and its substrates: mechanisms in health and disease

Erdogan, A. J., & Riemer, J. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2481-z · Cited by 28 · see citing works

Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones

Dimogkioka, A. R., Lees, J., Lacko, E., & Tokatlidis, K. (2021) · RSC Advances · doi:10.1039/d1ra04497d · Cited by 27 · see citing works

Mitochondrial sulphydryl oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles

Ang, S. K., Zhang, M., Lodi, T., & Lu, H. (2014) · Research Explorer (The University of Manchester)

Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles

Ang, S. K., Zhang, M., Lodi, T., & Lu, H. (2014) · Biochemical Journal · doi:10.1042/bj20131540 · Cited by 16 · see citing works

Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria

Ceh‐Pavia, E., Tang, X., Liu, Y., Heyes, D. J., Zhao, B., Xiao, P., & Lu, H. (2019) · FEBS Journal · doi:10.1111/febs.15136 · Cited by 7 · see citing works

Erv1 Mediates the Mia40-dependent Protein Import Pathway and Provides a Functional Link to the Respiratory Chain by Shuttling Electrons to Cytochrome c

Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., & Tokatlidis, K. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.049 · Cited by 235 · see citing works

Determination of the Redox Properties of Mitochondrial Sulfhydryl Oxidase Erv1

Ceh‐Pavia, E., & Lu, H. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.065 · Cited by 2 · see citing works