Mitochondria & Redox Biology

Our research is focused on mitochondria biogenesis and function in health and disease, signaling processes underpinning mitophagy, mitochondria in ageing, and redox and unfolded protein stress responses in the mitochondria and the ER.




Kowalczyk, D., Nakasone, M. A., Smith, B. O., Huang, D. T. (2022) Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function Life Science Alliance, 5, (doi: 10.26508/lsa.202201472)

Martínez Corrales, G., Li, M., Svermova, T., Goncalves, A., Voicu, D., Dobson, A. J., Southall, T. D., Alic, N. (2022) Transcriptional memory of dFOXO activation in youth curtails later-life mortality through chromatin remodelling and Xbp1 Nature Aging, 2, pp. 1176-1190. (doi: 10.1038/s43587-022-00312-x)

Kataura, T., Sedlackova, L., Otten, E. G., Kumari, R., Shapira, D., Scialo, F., Stefanatos, R., Ishikawa, K.-I., Kelly, G., Seranova, E., Sun, C., Maetzel, D., Kenneth, N., Trushin, S., Zhang, T., Trushina, E., Bascom, C. C., Tasseff, R., Isfort, R. J., Oblong, J. E., Miwa, S., Lazarou, M., Jaenisch, R., Imoto, M., Saiki, S., Papamichos-Chronakis, M., Manjithaya, R., Maddocks, O. D.K., Sanz Montero, A., Sarkar, S., Korolchuk, V. I. (2022) Autophagy promotes cell survival by maintaining NAD levels Developmental Cell, 57, pp. 2584-2598.e11. (doi: 10.1016/j.devcel.2022.10.008)

Teige, M., Jones, M., Toledo-Ortiz, G. (2022) Plant organellar signalling—back and forth and intertwined with cellular signalling Journal of Experimental Botany, 73, pp. 7103-7104. (doi: 10.1093/jxb/erac383)

Gracie, J., Zamberlan, F., Andrews, I. B., Smith, B. O., Peveler, W. J. (2022) Growth of plasmonic nanoparticles for aging cask-matured whisky ACS Applied Nano Materials, 5, pp. 15362-15368. (doi: 10.1021/acsanm.2c03406)

Ryan, S. M., Ruscher, R., Johnston, W. A., Pickering, D. A., Kennedy, M. W., Smith, B. O., Jones, L., Buitrago, G., Field, M. A., Esterman, A. J., McHugh, C. P., Browne, D. J., Cooper, M. M., Ryan, R. Y. M., Doolan, D. L., Engwerda, C. R., Miles, K., Mitreva, M., Croese, J., Rahman, T., Alexandrov, K., Giacomin, P. R., Loukas, A. (2022) Novel antiinflammatory biologics shaped by parasite–host coevolution Proceedings of the National Academy of Sciences of the United States of America, 119, (doi: 10.1073/pnas.2202795119)

Caccavale, E., Johnson, M. P., Brijbassi, S., Andreazza, A. C., Tokatlidis, K. (2022) Mitochondria and Us: from exploration to global collective Biochemist, 44, pp. 22-28. (doi: 10.1042/bio_2022_122)

Graham, C., Stefanatos, R., Yek, A. E.H., Spriggs, R. V., Loh, S. H.Y., Huerta Uribe, A., Zhang, T., Martins, L. M., Maddocks, O. D.K., Scialo, F., Sanz, A. (2022) Mitochondrial ROS signalling requires uninterrupted electron flow and is lost during ageing in flies GeroScience, 44, pp. 1961-1974. (doi: 10.1007/s11357-022-00555-x)

Kjeldsen, A., Kay, J. E., Baxter, S., McColm, S., Serrano-Amatriain, C., Parker, S., Robb, E., Arnold, S. A., Gilmour, C., Raper, A., Robertson, G., Fleming, R., Smith, B. O., Fotheringham, I. G., Christie, J. M., Magneschi, L. (2022) The fluorescent protein iLOV as a reporter for screening of high‐yield production of antimicrobial peptides in Pichia pastoris Microbial Biotechnology, 15, pp. 2126-2139. (doi: 10.1111/1751-7915.14034)

Ledahawsky, L. M., Terzenidou, M. E., Edwards, R., Kline, R. A., Graham, L. C., Eaton, S. L., van der Hoorn, D., Chaytow, H., Huang, Y.‐T., Groen, E. J.N., Motyl, A. A. L., Lamont, D. J., Tokatlidis, K., Wishart, T. M., Gillingwater, T. H. (2022) The mitochondrial protein Sideroflexin 3 (SFXN3) influences neurodegeneration pathways in vivo FEBS Journal, 289, pp. 3894-3914. (doi: 10.1111/febs.16377)

de Carbonnel, M., Stormonth-Darling, J. M., Liu, W., Kuziak, D., Jones, M. A. (2022) Realising the environmental potential of vertical farming systems through advances in plant photobiology Biology, 11, (doi: 10.3390/biology11060922)

Torres Cabán, C. C., Yang, M., Lai, C., Yang, L., Subach, F. V., Smith, B. O., Piatkevich, K. D., Boyden, E. S. (2022) Tuning the sensitivity of genetically encoded fluorescent potassium indicators through structure-guided and genome mining strategies ACS Sensors, 7, pp. 1336-1346. (doi: 10.1021/acssensors.1c02201)

Tibbo, A. J., Mika, D., Dobi, S., Ling, J., McFall, A., Tejeda, G. S., Blair, C., MacLeod, R., MacQuaide, N., Gök, C., Fuller, W., Smith, B. O., Smith, G. L., Vandecasteele, G., Brand, T., Baillie, G. S. (2022) Phosphodiesterase type 4 anchoring regulates cAMP signaling to Popeye domain-containing proteins Journal of Molecular and Cellular Cardiology, 165, pp. 86-102. (doi: 10.1016/j.yjmcc.2022.01.001)

Nakasone, M. A., Majorek, K. A., Gabrielsen, M., Sibbet, G. J., Smith, B. O., Huang, D. T. (2022) Structure of UBE2K-Ub/E3/polyUb reveals mechanisms of K48-linked Ub chain extension Nature Chemical Biology, 18, pp. 422-431. (doi: 10.1038/s41589-021-00952-x)

Neckebroeck, A., Kelly, S. M., Smith, B. O., Clark, J. S. (2022) Synthesis of the prototypical cyclopropyl dipeptide mimic and evaluation of its turn-inducing capability Journal of Organic Chemistry, 87, pp. 258-270. (doi: 10.1021/acs.joc.1c02344)


Tokatlidis, K., Eaglesfield, R. (2021) Targeting and insertion of membrane proteins in mitochondria Frontiers in Cell and Developmental Biology, 9, (doi: 10.3389/fcell.2021.803205)

Castejón-Vega, B., Rubio, A., Pérez-Pulido, A. J., Quiles, J. L., Lane, J. D., Fernández-Domínguez, B., Cachón-González, M. B., Martín-Ruiz, C., Sanz, A., Cox, T. M., Alcocer-Gómez, E., Cordero, M. D. (2021) L-arginine ameliorates defective autophagy in GM2 gangliosidoses by mTOR modulation Cells, 10, (doi: 10.3390/cells10113122)

Prabhakar, A. T., James, C. D., Das, D., Otoa, R., Day, M., Burgner, J., Fontan, C. T., Wang, X., Wieland, A., Donaldson, M. M., Bristol, M. L., Li, R., Oliver, A. W., Pearl, L. H., Smith, B. O., Glass, S., Morgan, I. M. (2021) CK2 phosphorylation of human papillomavirus 16 E2 on serine 23 promotes interaction with TopBP1 and is critical for E2 interaction with mitotic chromatin and the viral life cycle mBio, 12, (doi: 10.1128/mbio.01163-21)

Bonfini, A., Dobson, A. J., Duneau, D., Revah, J., Liu, X., Houtz, P., Buchon, N. (2021) Multiscale analysis reveals that diet-dependent midgut plasticity emerges from alterations in both stem cell niche coupling and enterocyte size eLife, 10, (doi: 10.7554/elife.64125)

Buist, H. K., Luchowska-Stańska, U., van Basten, B., Valli, J., Smith, B. O., Baillie, G. S., Rickman, C., Ricketts, B., Davidson, A., Hannam, R., Sunderland, J., Yarwood, S. J. (2021) Identification and characterization of an affimer affinity reagent for the detection of the cAMP sensor, EPAC1 Cells, 10, (doi: 10.3390/cells10092307)

Geldon, S., Fernandez-Vizarra, E., Tokatlidis, K. (2021) Redox-mediated regulation of mitochondrial biogenesis, dynamics and respiratory chain assembly in yeast and human cells Frontiers in Cell and Developmental Biology, 9, (doi: 10.3389/fcell.2021.720656)

Ahwazi, D., Neopane, K., Markby, G. R., Kopietz, F., Ovens, A. J., Dall, M., Hassing, A. S., Graesle, P., Alshuweishi, Y. A. I., Treebak, J. T., Salt, I., Göransson, O., Zeqiraj, E., Scott, J. W., Sakamoto, K. (2021) Investigation of the specificity and mechanism of action of the ULK1/AMPK inhibitor SBI-0206965 Biochemical Journal, 478, pp. 2977-2997. (doi: 10.1042/BCJ20210284)

Palmer, T. M., Salt, I. P. (2021) Nutrient regulation of inflammatory signalling in obesity and vascular disease Clinical Science, 135, pp. 1563-1590. (doi: 10.1042/CS20190768)

Morgan, D. C., Morris, C., Mahindra, A., Blair, C. M., Tejeda, G., Herbert, I., Turnbull, M. L., Lieber, G., Willett, B. J., Logan, N., Smith, B., Tobin, A. B., Bhella, D., Baillie, G. S., Jamieson, A. G. (2021) Stapled ACE2 peptidomimetics designed to target the SARS-CoV-2 spike protein do not prevent virus internalisation Peptide Science, 113, (doi: 10.1002/pep2.24217)

Navas, P., Sanz, A. (2021) Editorial: "Mitochondrial Coenzyme Q Homeostasis: signalling, respiratory chain stability and diseases." Free Radical Biology and Medicine, 169, pp. 12-13. (doi: 10.1016/j.freeradbiomed.2021.04.005)

Stevens, J., Jones, M. A., Lawson, T. (2021) Diverse physiological and physical responses among wild, landrace and elite barley varieties point to novel breeding opportunities Agronomy, 11, (doi: 10.3390/agronomy11050921)

Salt, I. P., Nunes, J. R.C., Fullerton, M. D. (2021) Metformin again? Atheroprotection mediated by macrophage AMPK and ATF1 Cardiovascular Research, 117, pp. 1233-1234. (doi: 10.1093/cvr/cvab065)

Edwards, R., Eaglesfield, R., Tokatlidis, K. (2021) The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways Open Biology, 11, (doi: 10.1098/rsob.210002)

Scialo, F., Sanz, A. (2021) Coenzyme Q redox signalling and longevity Free Radical Biology and Medicine, 164, pp. 187-205. (doi: 10.1016/j.freeradbiomed.2021.01.018)

Kopietz, F., Alshuweishi, Y., Bijland, S., Alghamdi, F., Degerman, E., Sakamoto, K., Salt, I. P., Göransson, O. (2021) A-769662 inhibits adipocyte glucose uptake in an AMPK-independent manner Biochemical Journal, 478, pp. 633-646. (doi: 10.1042/BCJ20200659)

Navarro-Pando, J. M., Alcocer-Gómez, E., Castejón-Vega, B., Navarro-Villarán, E., Condés-Hervás, M., Mundi-Roldan, M., Muntané, J., Pérez-Pulido, A. J., Bullon, P., Wang, C., Hoffman, H. M., Sanz, A., Mbalaviele, G., Ryffel, B., Cordero, M. D. (2021) Inhibition of the NLRP3 inflammasome prevents ovarian aging Science Advances, 7, (doi: 10.1126/sciadv.abc7409)

Knuhtsen, A., Whiting, R., McWhinnie, F. S., Whitmore, C., Smith, B. O., Green, A. C., Timperley, C. M., Kinnear, K. I., Jamieson, A. G. (2021) μ-conotoxin KIIIA peptidomimetics that block human voltage-gated sodium channels Peptide Science, 113, (doi: 10.1002/pep2.24203)

Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gómez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Álvarez, É. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. Y., Antas, P., Antebi, A., Antón, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araújo, W. L., Araya, J., Arden, C., Arévalo, M.-A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A. R., Armstrong-James, D., Arnauné-Pelloquin, L., Aroca, A., Arroyo, D. S., Arsov, I., Artero, R., Asaro, D. M. L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A. G., Au, A. K., Auberger, P., Auner, H. W., Aurelian, L., Autelli, R., Avagliano, L., Ávalos, Y., Aveic, S., Aveleira, C. A., Avin-Wittenberg, T., Aydin, Y., Ayton, S., Ayyadevara, S., Azzopardi, M., Baba, M., Backer, J. M., Backues, S. K., Bae, D.-H., Bae, O.-N., Bae, S. H., Baehrecke, E. H., Baek, A., Baek, S.-H., Baek, S. H., Bagetta, G., Bagniewska-Zadworna, A., Bai, H., Bai, J., Bai, X., Bai, Y., Bairagi, N., Baksi, S., Balbi, T., Baldari, C. T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banerjee, S., Bánréti, Á., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barilà, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touzé, N., Bellarosa, C., Belleudi, F., Belló Pérez, M., Bello-Morales, R., Beltran, J. S. d. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. G., Besteiro, S., Betin, V. M., Beyaert, R., Bezbradica, J. S., Bhaskar, K., Bhatia-Kissova, I., Bhattacharya, R., Bhattacharya, S., Bhattacharyya, S., Bhuiyan, M. S., Bhutia, S. K., Bi, L., Bi, X., Biden, T. J., Bijian, K., Billes, V. A., Binart, N., Bincoletto, C., Birgisdottir, A. B., Bjorkoy, G., Blanco, G., Blas-Garcia, A., Blasiak, J., Blomgran, R., Blomgren, K., Blum, J. S., Boada-Romero, E., Boban, M., Boesze-Battaglia, K., Boeuf, P., Boland, B., Bomont, P., Bonaldo, P., Bonam, S. R., Bonfili, L., Bonifacino, J. S., Boone, B. A., Bootman, M. D., Bordi, M., Borner, C., Bornhauser, B. C., Borthakur, G., Bosch, J., Bose, S., Botana, L. M., Botas, J., Boulanger, C. M., Boulton, M. E., Bourdenx, M., Bourgeois, B., Bourke, N. M., Bousquet, G., Boya, P., Bozhkov, P. V., Bozi, L. H. M., Bozkurt, T. O., Brackney, D. E., Brandts, C. H., Braun, R. J., Braus, G. H., Bravo-Sagua, R., Bravo-San Pedro, J. M., Brest, P., Bringer, M.-A., Briones-Herrera, A., Broaddus, V. C., Brodersen, P., Brodsky, J. L., Brody, S. L., Bronson, P. G., Bronstein, J. M., Brown, C. N., Brown, R. E., Brum, P. C., Brumell, J. H., Brunetti-Pierri, N., Bruno, D., Bryson-Richardson, R. J., Bucci, C., Buchrieser, C., Bueno, M., Buitrago-Molina, L. E., Buraschi, S., Buch, S., Buchan, J. R., Buckingham, E. M., Budak, H., Budini, M., Bultynck, G., Burada, F., Burgoyne, J. R., Burón, M. I., Bustos, V., Büttner, S., Butturini, E., Byrd, A., Cabas, I., Cabrera-Benitez, S., Cadwell, K., Cai, J., Cai, L., Cai, Q., Cairó, M., Calbet, J. A., Caldwell, G. A., Caldwell, K. A., Call, J. A., Calvani, R., Calvo, A. C., Calvo-Rubio Barrera, M., Camara, N. O., Camonis, J. H., Camougrand, N., Campanella, M., Campbell, E. M., Campbell-Valois, F.-X., Campello, S., Campesi, I., Campos, J. C., Camuzard, O., Cancino, J., Candido de Almeida, D., Canesi, L., Caniggia, I., Canonico, B., Cantí, C., Cao, B., Caraglia, M., Caramés, B., Carchman, E. H., Cardenal-Muñoz, E., Cardenas, C., Cardenas, L., Cardoso, S. M., Carew, J. S., Carle, G. F., Carleton, G., Carloni, S., Carmona-Gutierrez, D., Carneiro, L. A., Carnevali, O., Carosi, J. M., Carra, S., Carrier, A., Carrier, L., Carroll, B., Carter, A. B., Carvalho, A. N., Casanova, M., Casas, C., Casas, J., Cassioli, C., Castillo, E. F., Castillo, K., Castillo-Lluva, S., Castoldi, F., Castori, M., Castro, A. F., Castro-Caldas, M., Castro-Hernandez, J., Castro-Obregon, S., Catz, S. D., Cavadas, C., Cavaliere, F., Cavallini, G., Cavinato, M., Cayuela, M. L., Cebollada Rica, P., Cecarini, V., Cecconi, F., Cechowska-Pasko, M., Cenci, S., Ceperuelo-Mallafré, V., Cerqueira, J. J., Cerutti, J. M., Cervia, D., Cetintas, V. B., Cetrullo, S., Chae, H.-J., Chagin, A. S., Chai, C.-Y., Chakrabarti, G., Chakrabarti, O., Chakraborty, T., Chakraborty, T., Chami, M., Chamilos, G., Chan, D. W., Chan, E. Y. W., Chan, E. D., Chan, H. Y. E., Chan, H. H., Chan, H., Chan, M. T. V., Chan, Y. S., Chandra, P. K., Chang, C.-P., Chang, C., Chang, H.-C., Chang, K., Chao, J., Chapman, T., Charlet-Berguerand, N., Chatterjee, S., Chaube, S. K., Chaudhary, A., Chauhan, S., Chaum, E., Checler, F., Cheetham, M. E., Chen, C.-S., Chen, G.-C., Chen, J.-F., Chen, L. L., Chen, L., Chen, L., Chen, M., Chen, M.-K., Chen, N., Chen, Q., Chen, R.-H., Chen, S., Chen, W., Chen, W., Chen, X.-M., Chen, X.-W., Chen, X., Chen, Y., Chen, Y.-G., Chen, Y., Chen, Y., Chen, Y.-J., Chen, Y.-Q., Chen, Z. S., Chen, Z., Chen, Z.-H., Chen, Z. J., Chen, Z., Cheng, H., Cheng, J., Cheng, S.-Y., Cheng, W., Cheng, X., Cheng, X.-T., Cheng, Y., Cheng, Z., Chen, Z., Cheong, H., Cheong, J. K., Chernyak, B. V., Cherry, S., Cheung, C. F. R., Cheung, C. H. A., Cheung, K.-H., Chevet, E., Chi, R. J., Chiang, A. K. S., Chiaradonna, F., Chiarelli, R., Chiariello, M., Chica, N., Chiocca, S., Chiong, M., Chiou, S.-H., Chiramel, A. I., Chiurchiù, V., Cho, D.-H., Choe, S.-K., Choi, A. M. K., Choi, M. E., Choudhury, K. R., Chow, N. S., Chu, C. T., Chua, J. P., Chua, J. J. E., Chung, H., Chung, K. P., Chung, S., Chung, S.-H., Chung, Y.-L., Cianfanelli, V., Ciechomska, I. A., Cifuentes, M., Cinque, L., Cirak, S., Cirone, M., Clague, M. J., Clarke, R., Clementi, E., Coccia, E. M., Codogno, P., Cohen, E., Cohen, M. M., Colasanti, T., Colasuonno, F., Colbert, R. A., Colell, A., Čolić, M., Coll, N. S., Collins, M. O., Colombo, M. I., Colón-Ramos, D. A., Combaret, L., Comincini, S., Cominetti, M. R., Consiglio, A., Conte, A., Conti, F., Contu, V. R., Cookson, M. R., Coombs, K. M., Coppens, I., Corasaniti, M. T., Corkery, D. P., Cordes, N., Cortese, K., Costa, M. d. C., Costantino, S., Costelli, P., Coto-Montes, A., Crack, P. J., Crespo, J. L., Criollo, A., Crippa, V., Cristofani, R., Csizmadia, T., Cuadrado, A., Cui, B., Cui, J., Cui, Y., Cui, Y., Culetto, E., Cumino, A. C., Cybulsky, A. V., Czaja, M. J., Czuczwar, S. J., D'Adamo, S., D'Amelio, M., D'Arcangelo, D., D'Lugos, A. C., D'Orazi, G., da Silva, J. A., Dafsari, H. S., Dagda, R. K., Dagdas, Y., Daglia, M., Dai, X., Dai, Y., Dai, Y., Dal Col, J., Dalhaimer, P., Dalla Valle, L., Dallenga, T., Dalmasso, G., Damme, M., Dando, I., Dantuma, N. P., Darling, A. L., Das, H., Dasarathy, S., Dasari, S. K., Dash, S., Daumke, O., Dauphinee, A. N., Davies, J. S., Dávila, V. A., Davis, R. J., Davis, T., Dayalan Naidu, S., De Amicis, F., De Bosscher, K., De Felice, F., De Franceschi, L., De Leonibus, C., de Mattos Barbosa, M. G., De Meyer, G. R. Y., De Milito, A., De Nunzio, C., De Palma, C., De Santi, M., De Virgilio, C., De Zio, D., Debnath, J., DeBosch, B. J., Decuypere, J.-P., Deehan, M. A., Deflorian, G., DeGregori, J., Dehay, B., Del Rio, G., Delaney, J. R., Delbridge, L. M. D., Delorme-Axford, E., Delpino, M. V., Demarchi, F., Dembitz, V., Demers, N. D., Deng, H., Deng, Z., Dengjel, J., Dent, P., Denton, D., DePamphilis, M. L., Der, C. J., Deretic, V., Descoteaux, A., Devis, L., Devkota, S., Devuyst, O., Dewson, G., Dharmasivam, M., Dhiman, R., di Bernardo, D., Di Cristina, M., Di Domenico, F., Di Fazio, P., Di Fonzo, A., Di Guardo, G., Di Guglielmo, G. M., Di Leo, L., Di Malta, C., Di Nardo, A., Di Rienzo, M., Di Sano, F., Diallinas, G., Diao, J., Diaz-Araya, G., Díaz-Laviada, I., Dickinson, J. M., Diederich, M., Dieudé, M., Dikic, I., Ding, S., Ding, W.-X., Dini, L., Dinić, J., Dinic, M., Dinkova-Kostova, A. T., Dionne, M. S., Distler, J. H. W., Diwan, A., Dixon, I. M. C., Djavaheri-Mergny, M., Dobrinski, I., Dobrovinskaya, O., Dobrowolski, R., Dobson, R. C. J., Đokić, J., Dokmeci Emre, S., Donadelli, M., Dong, B., Dong, X., Dong, Z., Dorn Ii, G. W., Dotsch, V., Dou, H., Dou, J., Dowaidar, M., Dridi, S., Drucker, L., Du, A., Du, C., Du, G., Du, H.-N., Du, L.-L., du Toit, A., Duan, S.-B., Duan, X., Duarte, S. P., Dubrovska, A., Dunlop, E. A., Dupont, N., Durán, R. V., Dwarakanath, B. S., Dyshlovoy, S. 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Battle, M. W., Vegliani, F., Jones, M. A. (2020) Shades of green: untying the knots of green photoperception Journal of Experimental Botany, 71, pp. 5764-5770. (doi: 10.1093/jxb/eraa312)

Chatrin, C., Gabrielsen, M., Buetow, L., Nakasone, M. A., Ahmed, S. F., Sumpton, D., Sibbet, G. J., Smith, B. O., Huang, D. T. (2020) Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases Science Advances, 6, (doi: 10.1126/sciadv.abc0418)

Reinhardt, C., Arena, G., Nedara, K., Edwards, R., Brenner, C., Tokatlidis, K., Modjtahedi, N. (2020) AIF meets the CHCHD4/Mia40-dependent mitochondrial import pathway Biochimica et Biophysica Acta: Molecular Basis of Disease, 1866, (doi: 10.1016/j.bbadis.2020.165746)

Crecente Garcia, S., Neckebroeck, A., Clark, J. S., Smith, B. O., Thomson, A. R. (2020) β-turn mimics by chemical ligation Organic Letters, 22, pp. 4424-4428. (doi: 10.1021/acs.orglett.0c01427)

Scialò, F., Sriram, A., Stefanatos, R., Spriggs, R. V., Loh, S. H.Y., Martins, L. M., Sanz, A. (2020) Mitochondrial complex I derived ROS regulate stress adaptation in Drosophila melanogaster Redox Biology, 32, (doi: 10.1016/j.redox.2020.101450)

Edwards, R., Gerlich, S., Tokatlidis, K. (2020) The biogenesis of mitochondrial intermembrane space proteins Biological Chemistry, 401, pp. 737-747. (doi: 10.1515/hsz-2020-0114)

Woodling, N. S., Aleyakpo, B., Dyson, M. C., Minkley, L. J., Rajasingam, A., Dobson, A. J., Leung, K. H. C., Pomposova, S., Fuentealba, M., Alic, N., Partridge, L. (2020) The neuronal receptor tyrosine kinase Alk is a target for longevity Aging Cell, 19, (doi: 10.1111/acel.13137)

Battle, M. W., Jones, M. A. (2020) Cryptochromes integrate green light signals into the circadian system Plant, Cell and Environment, 43, pp. 16-27. (doi: 10.1111/pce.13643)


Gubina, N., Naudi, A., Stefanatos, R., Jove, M., Scialo, F., Fernandez-Ayala, D. J., Rantapero, T., Yurkevych, I., Portero-Otin, M., Nykter, M., Lushchak, O., Navas, P., Pamplona, R., Sanz, A., Anderson, R. (2019) Essential physiological differences characterize short- and long-lived strains of Drosophila melanogaster Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 74, pp. 1835-1843. (doi: 10.1093/gerona/gly143)

Pulli, I., Löf, C., Blom, T., Asghar, M.Y., Lassila, T., Bäck, N., Lin, K.-L., Nyström, J.H., Kemppainen, K., Toivola, D.M., Dufour, E., Sanz, A., Cooper, H.M., Parys, J.B., Törnquist, K. (2019) Sphingosine kinase 1 overexpression induces MFN2 fragmentation and alters mitochondrial matrix Ca2+ handling in HeLa cells Biochimica et Biophysica Acta: Molecular Cell Research, 1866, pp. 1475-1486. (doi: 10.1016/j.bbamcr.2019.06.006)

Ibáñez-Shimabukuro, M., Rey-Burusco, M. F., Gabrielsen, M., Franchini, G. R., Riboldi-Tunnicliffe, A., Roe, A. J., Griffiths, K., Cooper, A., Córsico, B., Kennedy, M. W., Smith, B. O. (2019) Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode Bioscience Reports, 39, (doi: 10.1042/BSR20191292)

Dobson, A. J., Boulton-McDonald, R., Houchou, L., Svermova, T., Ren, Z., Subrini, J., Vazquez-Prada, M., Hoti, M., Rodriguez-Lopez, M., Ibrahim, R., Gregoriou, A., Gkantiragas, A., Bähler, J., Ezcurra, M., Alic, N. (2019) Longevity is determined by ETS transcription factors in multiple tissues and diverse species PLoS Genetics, 15, (doi: 10.1371/journal.pgen.1008212)

Katwan, O. J., Alghamdi, F., Almabrouk, T. A., Mancini, S. J., Kennedy, S., Oakhill, J. S., Scott, J. W., Salt, I. P. (2019) AMP-activated protein kinase complexes containing the β2 regulatory subunit are upregulated during and contribute to adipogenesis Biochemical Journal, 476, pp. 1725-1740. (doi: 10.1042/BCJ20180714)

Edwards, R., Tokatlidis, K. (2019) The yeast voltage-dependent anion channel Porin: more IMPORTant than just metabolite transport Molecular Cell, 73, pp. 861-862. (doi: 10.1016/j.molcel.2019.02.028)

Jones, M. A. (2019) Retrograde signalling as an informant of circadian timing New Phytologist, 221, pp. 1749-1753. (doi: 10.1111/nph.15525)

Knuhtsen, A., Whitmore, C., McWhinnie, F. S., McDougall, L., Whiting, R., Smith, B. O., Timperley, C. M., Green, A. C., Kinnear, K. I., Jamieson, A. G. (2019) α-conotoxin GI triazole-peptidomimetics: potent and stable blockers of a human acetylcholine receptor Chemical Science, 10, pp. 1671-1676. (doi: 10.1039/C8SC04198A)

Jones, M. A., Morohashi, K., Grotewold, E., Harmer, S. L. (2019) Arabidopsis JMJD5/JMJ30 acts independently of LUX ARRHYTHMO within the plant circadian clock to enable temperature compensation Frontiers in Plant Science, 10, (doi: 10.3389/fpls.2019.00057)

Petrie, J. R., Salt, I. P. (2019) Diabetes and vascular disease Springer

Rezig, I. M., Bremner, S. K., Bhutta, M. S., Salt, I. P., Gould, G. W., McInerny, C. J. (2019) Genetic and cytological methods to study ESCRT cell cycle function in fission yeast Humana Press

Simon, N. M.L., Litthauer, S., Jones, M. A., Dodd, A. N. (2019) Interactions between circadian rhythms, ROS and redox Springer

Purohit, P. K., Edwards, R., Tokatlidis, K., Saini, N. (2019) MiR-195 regulates mitochondrial function by targeting mitofusin-2 in breast cancer cells RNA Biology, 16, pp. 918-929. (doi: 10.1080/15476286.2019.1600999)


Strembitska, A., Mancini, S. J., Gamwell, J. M., Palmer, T. M., Baillie, G. S., Salt, I. P. (2018) A769662 inhibits insulin-stimulated Akt activation in human macrovascular endothelial cells independent of AMP-activated protein kinase International Journal of Molecular Sciences, 19, (doi: 10.3390/ijms19123886)

Thompson, K., Mai, N., Oláhová, M., Scialó, F., Formosa, L. E., Stroud, D. A., Garrett, M., Lax, N. Z., Robertson, F. M., Jou, C., Nascimento, A., Ortez, C., Jimenez‐Mallebrera, C., Hardy, S. A., He, L., Brown, G. K., Marttinen, P., McFarland, R., Sanz Montero, A., Battersby, B. J., Bonnen, P. E., Ryan, M. T., Chrzanowska‐Lightowlers, Z. M.A., Lightowlers, R. N., Taylor, R. W. (2018) OXA 1L mutations cause mitochondrial encephalopathy and a combined oxidative phosphorylation defect EMBO Molecular Medicine, 10, (doi: 10.15252/emmm.201809060)

Jones, M. A. (2018) Using light to improve commercial value Horticulture Research, 5, (doi: 10.1038/s41438-018-0049-7)

Tokatlidis, K. (2018) Shaping the import system of mitochondria eLife, 7, (doi: 10.7554/elife.38209)

Cardenas-Rodriguez, M., Chatzi, A., Tokatlidis, K. (2018) Iron–sulfur clusters: from metals through mitochondria biogenesis to disease Journal of Biological Inorganic Chemistry, 23, pp. 509-520. (doi: 10.1007/s00775-018-1548-6)

Dobson, A. J., He, X., Blanc, E., Bolukbasi, E., Feseha, Y., Yang, M., Piper, M. D.W. (2018) Tissue-specific transcriptome profiling of Drosophila reveals roles for GATA transcription factors in longevity by dietary restriction npj Aging and Mechanisms of Disease, 4, (doi: 10.1038/s41514-018-0024-4)

Egea, J., Fabregat, I., Frapart, Y.M., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K., Knaus, U.G., Lopez, M.G., Olaso-Gonzalez, G., Petry, A., Schulz, R., Vina, J., Winyard, P., Abbas, K., Ademowo, O.S., Afonso, C.B., Andreadou, I., Antelmann, H., Antunes, F., Aslan, M., Bachschmid, M.M., Barbosa, R.M., Belousov, V., Berndt, C., Bernlohr, D., Bertrán, E., Bindoli, A., Bottari, S.P., Brito, P.M., Carrara, G., Casas, A.I., Chatzi, A., Chondrogianni, N., Conrad, M., Cooke, M.S., Costa, J.G., Cuadrado, A., My-Chan Dang, P., De Smet, B., Debelec-Butuner, B., Dias, I.H.K., Dunn, J.D., Edson, A.J., El Assar, M., El-Benna, J., Ferdinandy, P., Fernandes, A.S., Fladmark, K.E., Förstermann, U., Giniatullin, R., Giricz, Z., Görbe, A., Griffiths, H., Hampl, V., Hanf, A., Herget, J., Hernansanz-Agustín, P., Hillion, M., Huang, J., Ilikay, S., Jansen-Dürr, P., Jaquet, V., Joles, J.A., Kalyanaraman, B., Kaminskyy, D., Karbaschi, M., Kleanthous, M., Klotz, L.O., Korac, B., Korkmaz, K.S., Koziel, R., Kračun, D., Krause, K.H., Křen, V., Krieg, T., Laranjinha, J., Lazou, A., Li, H., Martínez-Ruiz, A., Matsui, R., McBean, G.J., Meredith, S.P., Messens, J., Miguel, V., Mikhed, Y., Milisav, I., Milković, L., Miranda-Vizuete, A., Mojović, M., Monsalve, M., Mouthuy, P.A., Mulvey, J., Münzel, T., Muzykantov, V., Nguyen, I.T.N., Oelze, M., Oliveira, N.G., Palmeira, C.M., Papaevgeniou, N., Pavićević, A., Pedre, B., Peyrot, F., Phylactides, M., Pircalabioru, G.G., Pitt, A.R., Poulsen, H.E., Prieto, I., Rigobello, M.P., Robledinos-Antón, N., Rodríguez-Mañas, L., Rolo, A.P., Rousset, F., Ruskovska, T., Saraiva, N., Sasson, S., Schröder, K., Semen, K., Seredenina, T., Shakirzyanova, A., Smith, G.L., Soldati, T., Sousa, B.C., Spickett, C.M., Stancic, A., Stasia, M.J., Steinbrenner, H., Stepanić, V., Steven, S., Tokatlidis, K., Tuncay, E., Turan, B., Ursini, F., Vacek, J., Vajnerova, O., Valentová, K., Van Breusegem, F., Varisli, L., Veal, E.A., Yalçın, A.S., Yelisyeyeva, O., Žarković, N., Zatloukalová, M., Zielonka, J., Touyz, R.M., Papapetropoulos, A., Grune, T., Lamas, S., Schmidt, H.H.H.W., Di Lisa, F., Daiber, A. (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)

Mancini, S. J., Boyd, D., Katwan, O. J., Strembitska, A., Almabrouk, T. A., Kennedy, S., Palmer, T. M., Salt, I. P. (2018) Canagliflozin inhibits interleukin-1β-stimulated cytokine and chemokine secretion in vascular endothelial cells by AMP-activated protein kinase-dependent and -independent mechanisms Scientific Reports, 8, (doi: 10.1038/s41598-018-23420-4)

Stefanatos, R., Sanz, A. (2018) The role of mitochondrial ROS in the aging brain FEBS Letters, 592, pp. 743-758. (doi: 10.1002/1873-3468.12902)

Sannino, D. R., Dobson, A. J., Edwards, K., Angert, E. R., Buchon, N. (2018) The Drosophila melanogaster gut microbiota provisions thiamine to its host mBio, 9, (doi: 10.1128/mBio.00155-18)

Litthauer, S., Chan, K. X., Jones, M. (2018) 3'-phosphoadenosine 5'-phosphate accumulation delays the circadian system Plant Physiology, 176, pp. 3120-3135. (doi: 10.1104/pp.17.01611)

Almabrouk, T. A.M., White, A. D., Ugusman, A. B., Skiba, D. S., Katwan, O. J., Alganga, H., Guzik, T. J., Touyz, R. M., Salt, I. P., Kennedy, S. (2018) High fat diet attenuates the anticontractile activity of aortic PVAT via a mechanism involving AMPK and reduced adiponectin secretion Frontiers in Physiology, 9, (doi: 10.3389/fphys.2018.00051)

Speirs, C., Williams, J. J.L., Riches, K., Salt, I. P., Palmer, T. M. (2018) Linking energy sensing to suppression of JAK-STAT signalling: a potential route for repurposing AMPK activators? Pharmacological Research, 128, pp. 88-100. (doi: 10.1016/j.phrs.2017.10.001)

Carroll, B., Otten, E. G., Manni, D., Stefanatos, R., Menzies, F. M., Smith, G. R., Jurk, D., Kenneth, N., Wilkinson, S., Passos, J. F., Attems, J., Veal, E. A., Teyssou, E., Seilhean, D., Millecamps, S., Eskelinen, E.-L., Bronowska, A. K., Rubinsztein, D. C., Sanz, A., Korolchuk, V. I. (2018) Oxidation of SQSTM1/p62 mediates the link between redox state and protein homeostasis Nature Communications, 9, (doi: 10.1038/s41467-017-02746-z)

Mancini, S. J., Salt, I. P. (2018) Investigating the role of AMPK in inflammation Humana Press

Litthauer, S., Jones, M. A. (2018) SAL1-PAP retrograde signalling extends circadian period by reproducing the loss of exoribonuclease (XRN) activity Plant Signaling and Behavior, 13,


Filer, D., Thompson, M. A., Takhaveev, V., Dobson, A. J., Kotronaki, I., Green, J. W.M., Heinemann, M., Tullet, J. M.A., Alic, N. (2017) RNA polymerase III limits longevity downstream of TORC1 Nature, 552, pp. 263-267. (doi: 10.1038/nature25007)

Cooper, A., Vance, S. J., Smith, B. O., Kennedy, M. W. (2017) Frog foams and natural protein surfactants Colloids and Surfaces A: Physicochemical and Engineering Aspects, 534, pp. 120-129. (doi: 10.1016/j.colsurfa.2017.01.049)

Jones, M. A. (2017) Interplay of circadian rhythms and light in the regulation of photosynthesis-derived metabolism Springer

Gabrielsen, M., Buetow, L., Nakasone, M. A., Ahmed, S. F., Sibbet, G. J., Smith, B. O., Zhang, W., Sidhu, S. S., Huang, D. T. (2017) A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants Molecular Cell, 68, pp. 456-470.e10. (doi: 10.1016/j.molcel.2017.09.027)

Almabrouk, T. A. M., Ugusman, A. B., Katwan, O. J., Salt, I. P., Kennedy, S. (2017) Deletion of AMPKα1 attenuates the anticontractile effect of perivascular adipose tissue (PVAT) and reduces adiponectin release British Journal of Pharmacology, 174, pp. 3398-3410. (doi: 10.1111/bph.13633)

Egea, J., Fabregat, I., Frapart, Y. M., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K., Knaus, U. G., Lopez, M. G., Olaso-Gonzalez, G., Petry, A., Schulz, R., Vina, J., Winyard, P., Abbas, K., Ademowo, O. S., Afonso, C. B., Andreadou, I., Antelmann, H., Antunes, F., Aslan, M., Bachschmid, M. M., Barbosa, R. M., Belousov, V., Berndt, C., Bernlohr, D., Bertrán, E., Bindoli, A., Bottari, S. P., Brito, P. M., Carrara, G., Casas, A. I., Chatzi, A., Chondrogianni, N., Conrad, M., Cooke, M. S., Costa, J. G., Cuadrado, A., My-Chan Dang, P., De Smet, B., Debelec–Butuner, B., Dias, I. H.K., Dunn, J. D., Edson, A. J., El Assar, M., El-Benna, J., Ferdinandy, P., Fernandes, A. S., Fladmark, K. E., Förstermann, U., Giniatullin, R., Giricz, Z., Görbe, A., Griffiths, H., Hampl, V., Hanf, A., Herget, J., Hernansanz-Agustín, P., Hillion, M., Huang, J., Ilikay, S., Jansen-Dürr, P., Jaquet, V., Joles, J. A., Kalyanaraman, B., Kaminskyy, D., Karbaschi, M., Kleanthous, M., Klotz, L.-O., Korac, B., Korkmaz, K. S., Koziel, R., Kračun, D., Krause, K.-H., Křen, V., Krieg, T., Laranjinha, J., Lazou, A., Li, H., Martínez-Ruiz, A., Matsui, R., McBean, G. J., Meredith, S. P., Messens, J., Miguel, V., Mikhed, Y., Milisav, I., Milković, L., Miranda-Vizuete, A., Mojović, M., Monsalve, M., Mouthuy, P.-A., Mulvey, J., Münzel, T., Muzykantov, V., Nguyen, I. T.N., Oelze, M., Oliveira, N. G., Palmeira, C. M., Papaevgeniou, N., Pavićević, A., Pedre, B., Peyrot, F., Phylactides, M., Pircalabioru, G. G., Pitt, A. R., Poulsen, H. E., Prieto, I., Rigobello, M. P., Robledinos-Antón, N., Rodríguez-Mañas, L., Rolo, A. P., Rousset, F., Ruskovska, T., Saraiva, N., Sasson, S., Schröder, K., Semen, K., Seredenina, T., Shakirzyanova, A., Smith, G. L., Soldati, T., Sousa, B. C., Spickett, C. M., Stancic, A., Stasia, M. J., Steinbrenner, H., Stepanić, V., Steven, S., Tokatlidis, K., Tuncay, E., Turan, B., Ursini, F., Vacek, J., Vajnerova, O., Valentová, K., Van Breusegem, F., Varisli, L., Veal, E. A., Yalçın, A. S., Yelisyeyeva, O., Žarković, N., Zatloukalová, M., Zielonka, J., Touyz, R. M., Papapetropoulos, A., Grune, T., Lamas, S., Schmidt, H. H.H.W., Di Lisa, F., Daiber, A. (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)

Kennedy, S., Salt, I. P. (2017) Molecular mechanisms regulating perivascular adipose tissue - potential pharmacological targets? British Journal of Pharmacology, 174, pp. 3385-3387. (doi: 10.1111/bph.13969)

Magennis, S., Toulmin, A., Baltierra-Jasso, L. E., Morten, M. J., Sabir, T., McGlynn, P., Schröder, G. F., Smith, B. O., Magennis, S. W. (2017) Conformational heterogeneity in a fully-complementary DNA three-way junction with a GC-rich branchpoint Biochemistry, 56, pp. 4985-4991. (doi: 10.1021/acs.biochem.7b00677)

Cardenas-Rodriguez, M., Tokatlidis, K. (2017) Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space FEBS Letters, 591, pp. 2661-2670. (doi: 10.1002/1873-3468.12766)

Spies, M., Smith, B. O. (2017) Protein-nucleic acids interactions: new ways of connecting structure, dynamics and function Biophysical Reviews, 9, pp. 289-291. (doi: 10.1007/s12551-017-0284-4)

MacPherson, L., Tokatlidis, K. (2017) Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease Biochemical Journal, 474, pp. 2533-2545. (doi: 10.1042/BCJ20160627)

Scialò, F., Fernández-Ayala, D. J., Sanz, A. (2017) Role of mitochondrial reverse electron transport in ROS signaling: potential roles in health and disease Frontiers in Physiology, 8, (doi: 10.3389/fphys.2017.00428)

Salt, I. P., Hardie, G. (2017) AMP-activated protein kinase: an ubiquitous signalling pathway with key roles in the cardiovascular system Circulation Research, 120, pp. 1825-1841. (doi: 10.1161/CIRCRESAHA.117.309633)

Brandani, G. B., Vance, S. J., Schor, M., Cooper, A., Kennedy, M. W., Smith, B. O., MacPhee, C. E., Cheung, D. L. (2017) Adsorption of the natural protein surfactant Rsn-2 onto liquid interfaces Physical Chemistry Chemical Physics, 19, pp. 8584-8594. (doi: 10.1039/C6CP07261E)

Parnell, E., McElroy, S. P., Wiejak, J., Baillie, G. L., Porter, A., Adams, D. R., Rehmann, H., Smith, B. O., Yarwood, S. J. (2017) Identification of a novel, small molecule partial agonist for the cyclic AMP sensor, EPAC1 Scientific Reports, 7, (doi: 10.1038/s41598-017-00455-7)

Kritsiligkou, P., Chatzi, A., Charalampous, G., Mironov, A., Grant, C. M., Tokatlidis, K. (2017) Unconventional targeting of a thiol peroxidase to the mitochondrial intermembrane space facilitates oxidative protein folding Cell Reports, 18, pp. 2729-2741. (doi: 10.1016/j.celrep.2017.02.053)

Chen, S.C., Brooks, R., Houskeeper, J., Bremner, S.K., Dunlop, J., Viollet, B., Logan, P.J., Salt, I.P., Ahmed, S.F., Yarwood, S.J. (2017) Corrigendum to "Metformin suppresses adipogenesis through both AMP-activated protein kinase (AMPK)-dependent and AMPK-independent mechanisms" [Mol. Cell. Endocrinol. 440 15 January 2017 57-68] Molecular and Cellular Endocrinology, 443, pp. 176. (doi: 10.1016/j.mce.2017.01.049)

Dobson, A. J., Chaston, J. M., Douglas, A. E. (2017) Erratum to: The Drosophila transcriptional network is structured by microbiota BMC Genomics, 18, (doi: 10.1186/s12864-017-3508-x)

Mancini, S. J., White, A. D., Bijland, S., Rutherford, C., Graham, D., Richter, E. A., Viollet, B., Touyz, R. M., Palmer, T. M., Salt, I. P. (2017) Activation of AMP-activated protein kinase rapidly suppresses multiple pro-inflammatory pathways in adipocytes including IL-1 receptorassociated kinase-4 phosphorylation Molecular and Cellular Endocrinology, 440, pp. 44-56. (doi: 10.1016/j.mce.2016.11.010)

Chen, S. C., Brooks, R., Houskeeper, J., Bremner, S. K., Dunlop, J., Viollet, B., Logan, P. J., Salt, I. P., Ahmed, S. F., Yarwood, S. J. (2017) Metformin suppresses adipogenesis through both AMP-activated protein kinase (AMPK)-dependent and AMPK-independent mechanisms Molecular and Cellular Endocrinology, 440, pp. 57-68. (doi: 10.1016/j.mce.2016.11.011)

Dobson, A. J., Ezcurra, M., Flanagan, C. E., Summerfield, A. C., Piper, M. D.W., Gems, D., Alic, N. (2017) Nutritional programming of lifespan by FOXO inhibition on sugar-rich diets Cell Reports, 18, pp. 299-306. (doi: 10.1016/j.celrep.2016.12.029)

Manganas, P., MacPherson, L., Tokatlidis, K. (2017) Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space Cell and Tissue Research, 367, pp. 43-57. (doi: 10.1007/s00441-016-2488-5)


Malpas, K. R., Jones, M. A. (2016) Natural variation of circadian rhythms in Kalanchoe species Haseltonia, 2016, pp. 35-42. (doi: 10.2985/026.022.0107)

Docherty, C. K., Salt, I. P., Mercer, J. R. (2016) Lin28A induces energetic switching to glycolytic metabolism in human embryonic kidney cells Stem Cell Research and Therapy, 7, (doi: 10.1186/s13287-016-0323-2)

Heathcote, H. R., Mancini, S. J., Strembitska, A., Jamal, K., Reihill, J. A., Palmer, T. M., Gould, G. W., Salt, I. P. (2016) Protein kinase C phosphorylates AMP-activated protein kinase α1 Ser487 Biochemical Journal, 473, pp. 4681-4697. (doi: 10.1042/BCJ20160211)

Dobson, A. J., Chaston, J. M., Douglas, A. E. (2016) The Drosophila transcriptional network is structured by microbiota BMC Genomics, 17, (doi: 10.1186/s12864-016-3307-9)

Rutherford, C., Speirs, C., Williams, J. J.L., Ewart, M.-A., Mancini, S. J., Hawley, S. A., Delles, C., Viollet, B., Costa-Pereira, A. P., Baillie, G. S., Salt, I. P., Palmer, T. M. (2016) Phosphorylation of Janus kinase 1 (JAK1) by AMP-activated protein kinase (AMPK) links energy sensing to anti-inflammatory signaling Science Signaling, 9, (doi: 10.1126/scisignal.aaf8566)

Nuebel, E., Manganas, P., Tokatlidis, K. (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, pp. 2613-2623. (doi: 10.1016/j.bbamcr.2016.07.004)

Grinter, R., Josts, I., Mosbahi, K., Roszak, A. W., Cogdell, R. J., Bonvin, A. M.J.J., Milner, J. J., Kelly, S. M., Byron, O., Smith, B. O., Walker, D. (2016) Structure of the bacterial plant-ferredoxin receptor FusA Nature Communications, 7, (doi: 10.1038/ncomms13308)

Heilmann, M., Velanis, C. N., Cloix, C., Smith, B. O., Christie, J. M., Jenkins, G. I. (2016) Dimer/monomer status and in vivo function of salt-bridge mutants of the plant UV-B photoreceptor UVR8 Plant Journal, 88, pp. 71-81. (doi: 10.1111/tpj.13260)

Hawley, S. A., Ford, R. J., Smith, B. K., Gowans, G. J., Mancini, S., Pitt, R. D., Day, E. A., Salt, I. P., Steinberg, G. R., Hardie, D. G. (2016) The Na+ glucose co-transporter inhibitor canagliflozin activates AMP-activated protein kinase by inhibiting mitochondrial function and increasing cellular AMP levels Diabetes, 65, pp. 2784-2794. (doi: 10.2337/db16-0058)

Antoniewski, C., Scialo, F., Sriram, A., Stefanatos, R., Sanz, A. (2016) Practical recommendations for the use of the GeneSwitch Gal4 system to knock-down genes in Drosophila melanogaster PLoS ONE, 11, (doi: 10.1371/journal.pone.0161817)

Morris, R. J., Brandani, G. B., Desai, V., Smith, B. O., Schor, M., MacPhee, C. E. (2016) The conformation of interfacially adsorbed Ranaspumin-2 Is an arrested state on the unfolding pathway Biophysical Journal, 111, pp. 732-742. (doi: 10.1016/j.bpj.2016.06.006)

Dean, A., Nilsen, M., Loughlin, L., Salt, I. P., MacLean, M. R. (2016) Metformin reverses development of pulmonary hypertension via aromatase inhibition Hypertension, 68, pp. 446-454. (doi: 10.1161/HYPERTENSIONAHA.116.07353)

Sanz, A. (2016) Mitochondrial reactive oxygen species: Do they extend or shorten animal lifespan? Biochimica et Biophysica Acta: Bioenergetics, 1857, pp. 1116-1126. (doi: 10.1016/j.bbabio.2016.03.018)

Kalef-Ezra, E., Kotzamani, D., Zaganas, I., Katrakili, N., Plaitakis, A., Tokatlidis, K. (2016) Import of a major mitochondrial enzyme depends on synergy between two distinct helices of its presequence Biochemical Journal, 473, pp. 2813-2829. (doi: 10.1042/BCJ20160535)

Vance, S. J., Desai, V., Smith, B. O., Kennedy, M. W., Cooper, A. (2016) Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2 Biophysical Chemistry, 214-15, pp. 27-32. (doi: 10.1016/j.bpc.2016.05.003)

Johnston, P. R., Dobson, A. J., Rolff, J. (2016) Genomic signatures of experimental adaptation to antimicrobial peptides in Staphylococcus aureus G3: Genes, Genomes, Genetics, 6, pp. 1535-1539. (doi: 10.1534/g3.115.023622)

Chatzi, A., Manganas, P., Tokatlidis, K. (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, pp. 1298-1306. (doi: 10.1016/j.bbamcr.2016.03.023)

Makarova, O., Rodriguez-Rojas, A., Eravci, M., Weise, C., Dobson, A., Johnston, P., Rolff, J. (2016) Antimicrobial defence and persistent infection in insects revisited Philosophical Transactions of the Royal Society B: Biological Sciences, 371, (doi: 10.1098/rstb.2015.0296)

Ashraf, K. U., Josts, I., Mosbahi, K., Kelly, S. M., Byron, O., Smith, B. O., Walker, D. (2016) The potassium binding protein Kbp is a cytoplasmic potassium sensor Structure, 24, pp. 741-749. (doi: 10.1016/j.str.2016.03.017)

Scialò, F., Sriram, A., Fernández-Ayala, D., Gubina, N., Lõhmus, M., Nelson, G., Logan, A., Cooper, H. M., Navas, P., Enríquez, J. A., Murphy, M. P., Sanz, A. (2016) Mitochondrial ROS produced via reverse electron transport extend animal lifespan Cell Metabolism, 23, pp. 725-734. (doi: 10.1016/j.cmet.2016.03.009)

Modjtahedi, N., Tokatlidis, K., Dessen, P., Kroemer, G. (2016) Mitochondrial proteins containing coiled-coil-helix-coiled-coil-helix (CHCH) domains in health and disease Trends in Biochemical Sciences, 41, pp. 245-260. (doi: 10.1016/j.tibs.2015.12.004)

Regan, J. C., Khericha, M., Dobson, A. J., Bolukbasi, E., Rattanavirotkul, N., Partridge, L. (2016) Sex difference in pathology of the ageing gut mediates the greater response of female lifespan to dietary restriction eLife, 5, (doi: 10.7554/eLife.10956)

Chaston, J. M., Dobson, A. J., Newell, P. D., Douglas, A. E. (2016) Host genetic control of the microbiota mediates the Drosophila nutritional phenotype Applied and Environmental Microbiology, 82, pp. 671-679. (doi: 10.1128/AEM.03301-15)

Litthauer, S., Battle, M. W., Jones, M. A. (2016) Phototropins do not alter accumulation of evening-phased circadian transcripts under blue light Plant Signaling and Behavior, 11, (doi: 10.1080/15592324.2015.1126029)


Rey, B. M.F., Ibáñez, S. M., Gabrielsen, M., Franchini, G. R., Roe, A. J., Griffiths, K., Zhan, B., Cooper, A., Kennedy, M. W., Córsico, B., Smith, B. O. (2015) Diversity in the structures and ligand binding sites of nematode fatty acid and retinol binding proteins revealed by Na-FAR-1 from Necator americanus Biochemical Journal, 471, pp. 403-414. (doi: 10.1042/BJ20150068)

Thomson, R., Smith, B. O. (2015) Solution structure of human MBD1 CXXC1 Journal of Biomolecular NMR, 63, pp. 309-314. (doi: 10.1007/s10858-015-9986-8)

Gerhold, J. M., Cansiz-Arda, Ş., Lõhmus, M., Engberg, O., Reyes, A., van Rennes, H., Sanz, A., Holt, I. J., Cooper, H. M., Spelbrink, J. N. (2015) Human mitochondrial DNA-protein complexes attach to a cholesterol-rich membrane structure Scientific Reports, 5, (doi: 10.1038/srep15292)

Jones, M. A., Hu, W., Litthauer, S., Lagarias, J. C., Harmer, S. L. (2015) A constitutively active allele of phytochrome B maintains circadian robustness in the absence of light. Plant Physiology, 169, pp. 814-825. (doi: 10.1104/pp.15.00782)

Litthauer, S., Battle, M. W., Lawson, T., Jones, M. A. (2015) Phototropins maintain robust circadian oscillation of PSII operating efficiency under blue light Plant Journal, 83, pp. 1034-1045. (doi: 10.1111/tpj.12947)

Rovenko, B. M., Kubrak, O. I., Gospodaryov, D. V., Yurkevych, I. S., Sanz, A., Lushchak, O. V., Lushchak, V. I. (2015) Restriction of glucose and fructose causes mild oxidative stress independently of mitochondrial activity and reactive oxygen species in Drosophila melanogaster Comparative Biochemistry and Physiology. Part A: Molecular and Integrative Physiology, 187, pp. 27-39. (doi: 10.1016/j.cbpa.2015.04.012)

Syrjänen, L., Valanne, S., Kuuslahti, M., Tuomela, T., Sriram, A., Sanz, A., Jacobs, H. T., Rämet, M., Parkkila, S. (2015) β carbonic anhydrase is required for female fertility in Drosophila melanogaster Frontiers in Zoology, 12, (doi: 10.1186/s12983-015-0111-3)

Rovenko, B. M., Kubrak, O. I., Gospodaryov, D. V., Perkhulyn, N. V., Yurkevych, I. S., Sanz, A., Lushchak, O. V., Lushchak, V. I. (2015) High sucrose consumption promotes obesity whereas its low consumption induces oxidative stress in Drosophila melanogaster Journal of Insect Physiology, 79, pp. 42-54. (doi: 10.1016/j.jinsphys.2015.05.007)

Dutta, D., Dobson, A. J., Houtz, P. L., Gläßer, C., Revah, J., Korzelius, J., Patel, P. H., Edgar, B. A., Buchon, N. (2015) Regional cell-specific transcriptome mapping reveals regulatory complexity in the adult Drosophila midgut Cell Reports, 12, pp. 346-358. (doi: 10.1016/j.celrep.2015.06.009)

Hangen, E., Féraud, O., Lachkar, S., Mou, H., Doti, N., Fimia, G.M., Lam, N.v., Zhu, C., Godin, I., Muller, K., Chatzi, A., Nuebel, E., Ciccosanti, F., Flamant, S., Bénit, P., Perfettini, J.-L., Sauvat, A., Bennaceur-Griscelli, A., Ser-Le Roux, K., Gonin, P., Tokatlidis, K., Rustin, P., Piacentini, M., Ruvo, M., Blomgren, K., Kroemer, G., Modjtahedi, N. (2015) Interaction between AIF and CHCHD4 regulates respiratory chain biogenesis Molecular Cell, 58, pp. 1001-1014. (doi: 10.1016/j.molcel.2015.04.020)

Dobson, A. J., Chaston, J. M., Newell, P. D., Donahue, L., Hermann, S. L., Sannino, D. R., Westmiller, S., Wong, A. C.-N., Clark, A. G., Lazzaro, B. P., Douglas, A. E. (2015) Corrigendum: Host genetic determinants of microbiota-dependent nutrition revealed by genome-wide analysis of Drosophila melanogaster Nature Communications, 6, (doi: 10.1038/ncomms8296)

Parnell, E., Smith, B. O., Yarwood, S. J. (2015) The cAMP sensors, EPAC1 and EPAC2, display distinct subcellular distributions despite sharing a common nuclear pore localisation signal Cellular Signalling, 27, pp. 989-996. (doi: 10.1016/j.cellsig.2015.02.009)

Buetow, L., Gabrielsen, M., Anthony, N. G., Dou, H., Patel, A., Aitkenhead, H., Sibbet, G. J., Smith, B. O., Huang, D. T. (2015) Activation of a primed RING E3-E2–ubiquitin complex by non-covalent ubiquitin Molecular Cell, 58, pp. 297-310. (doi: 10.1016/j.molcel.2015.02.017)

Dobson, A. J., Chaston, J. M., Newell, P. D., Donahue, L., Hermann, S. L., Sannino, D. R., Westmiller, S., Wong, A. C.-N., Clark, A. G., Lazzaro, B. P., Douglas, A. E. (2015) Host genetic determinants of microbiota-dependent nutrition revealed by genome-wide analysis of Drosophila melanogaster Nature Communications, 6, (doi: 10.1038/ncomms7312)

Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Güntert, P., Ito, Y. (2015) Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins Biochemical and Biophysical Research Communications, 457, pp. 200-205. (doi: 10.1016/j.bbrc.2014.12.088)

Rovenko, B. M., Perkhulyn, N. V., Gospodaryov, D. V., Sanz, A., Lushchak, O. V., Lushchak, V. I. (2015) High consumption of fructose rather than glucose promotes a diet-induced obese phenotype in Drosophila melanogaster Comparative Biochemistry and Physiology. Part A: Molecular and Integrative Physiology, 180, pp. 75-85. (doi: 10.1016/j.cbpa.2014.11.008)

Franchini, G. R., Pórfido, J. L., Ibáñez Shimabukuro, M., Rey Burusco, M. F., Bélgamo, J. A., Smith, B. O., Kennedy, M. W., Córsico, B. (2015) The unusual lipid binding proteins of parasitic helminths and their potential roles in parasitism and as therapeutic targets Prostaglandins, Leukotrienes and Essential Fatty Acids (PLEFA), 93, pp. 31-36. (doi: 10.1016/j.plefa.2014.08.003)

Choudhury, Y., Salt, I., Leung, H. (2015) AMPK—friend or foe for targeted therapy? Cell Cycle, 14, pp. 1761-1762. (doi: 10.1080/15384101.2015.1022066)

Mathes, T., Heilmann, M., Pandit, A., Zhu, J., Ravensbergen, J., Kloz, M., Fu, Y., Smith, B.O., Christie, J.M., Jenkins, G.I., Kennis, J.T.M. (2015) Proton-coupled electron transfer constitutes the photoactivation mechanism of the plant photoreceptor UVR8 Journal of the American Chemical Society, 137, pp. 8113-8120. (doi: 10.1021/jacs.5b01177)

Scialò, F., Sriram, A., Naudí, A., Ayala, V., Jové, M., Pamplona, R., Sanz, A. (2015) Target of rapamycin activation predicts lifespan in fruit flies Cell Cycle, 14, pp. 2949-2958. (doi: 10.1080/15384101.2015.1071745)

Mordas, A., Tokatlidis, K. (2015) The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis Accounts of Chemical Research, 48, pp. 2191-2199. (doi: 10.1021/acs.accounts.5b00150)


Newell, P. D., Chaston, J. M., Wang, Y., Winans, N. J., Sannino, D. R., Wong, A. C.N., Dobson, A. J., Kagle, J., Douglas, A. E. (2014) In vivo function and comparative genomic analyses of the Drosophila gut microbiota identify candidate symbiosis factors. Frontiers in Microbiology, 5, (doi: 10.3389/fmicb.2014.00576)

Dobson, A. J., Purves, J., Rolff, J. (2014) Increased survival of experimentally evolved antimicrobial peptide-resistant Staphylococcus aureus in an animal host. Evolutionary Applications, 7, pp. 905-912. (doi: 10.1111/eva.12184)

Mallikarjun, V., Sriram, A., Scialo, F., Sanz, A. (2014) The interplay between mitochondrial protein and iron homeostasis and its possible role in ageing Experimental Gerontology, 56, pp. 123-134. (doi: 10.1016/j.exger.2013.12.015)

Beckham, K. S.H., Connolly, J. P.R., Ritchie, J. M., Wang, D., Gawthorne, J. A., Tahoun, A., Gally, D. L., Burgess, K., Burchmore, R. J., Smith, B. O., Beatson, S. A., Byron, O., Wolfe, A. J., Douce, G., Roe, A. J. (2014) The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7 Molecular Microbiology, 93, pp. 199-211. (doi: 10.1111/mmi.12651)

Cameron, R. T., Quinn, S. D., Cairns, L. S., MacLeod, R., Samuel, I. D.W., Smith, B. O., Penedo, J. C., Baillie, G. S. (2014) The phosphorylation of Hsp20 enhances its association with amyloid-β to increase protection against neuronal cell death Molecular and Cellular Neuroscience, 61, pp. 46-55. (doi: 10.1016/j.mcn.2014.05.002)

Choudhury, Y., Yang, Z., Ahmad, I., Nixon, C., Salt, I. P., Leung, H. Y. (2014) AMP-activated protein kinase (AMPK) as a potential therapeutic target independent of PI3K/Akt signaling in prostate cancer Oncoscience, 1, pp. 446-456. (doi: 10.18632/oncoscience.49)

Wong, A. C.-N., Dobson, A. J., Douglas, A. E. (2014) Gut microbiota dictates the metabolic response of Drosophila to diet Journal of Experimental Biology, 217, pp. 1894-1901. (doi: 10.1242/jeb.101725)

Ibáñez-Shimabukuro, M., Rey-Burusco, M.F., Cooper, A., Kennedy, M. W., Córsico, B., Smith, B. O. (2014) Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum Biomolecular NMR Assignments, 8, pp. 33-36. (doi: 10.1007/s12104-012-9447-1)

Vance, S. J., McDonald, R. E., Cooper, A., Kennedy, M. W., Smith, B. O. (2014) Resonance assignments for latherin, a natural surfactant protein from horse sweat Biomolecular NMR Assignments, 8, pp. 213-216. (doi: 10.1007/s12104-013-9485-3)

Yvon, C., Surman, A. J., Hutin, M., Alex, J., Smith, B. O., Long, D. L., Cronin, L. (2014) Polyoxometalate clusters integrated into peptide chains and as inorganic amino acids: solution- and solid-phase approaches Angewandte Chemie (International Edition), 53, pp. 3336-3341. (doi: 10.1002/anie.201311135)

Rey-Burusco, M.F., Ibañez-Shimabukuro, M., Cooper, A., Kennedy, M. W., Córsico, B., Smith, B. O. (2014) 1H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus Biomolecular NMR Assignments, 8, pp. 19-21. (doi: 10.1007/s12104-012-9444-4)

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

Almabrouk, T.A.M., Ewart, M.-A., Salt, I.P., Kennedy, S. (2014) Perivascular fat, AMP-activated protein kinase and vascular diseases British Journal of Pharmacology, 171, pp. 595-617. (doi: 10.1111/bph.12479)

McCaughey, L. C., Grinter, R., Josts, I., Roszak, A. W., Waløen, K., Cogdell, R. J., Milner, J., Evans, T., Kelly, S., Tucker, N. P., Byron, O., Smith, B., Walker, D. (2014) Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor PLoS Pathogens, 10, pp. e1003898. (doi: 10.1371/journal.ppat.1003898)

Caldwell, S.T., Maclean, C., Riehle, M., Cooper, A., Nutley, M., Rabani, G., Fitzpatrick, B., Rotello, V.M., Smith, B.O., Khaled, B., Woisel, P., Cooke, G. (2014) Protein-mediated dethreading of a biotin-functionalised pseudorotaxane Organic and Biomolecular Chemistry, 12, pp. 511-516. (doi: 10.1039/C3OB41612G)

Salt, I.P., Harnett, M.M., Goodridge, H.S. (2014) Membrane receptors and signal transduction Saunders Elsevier

Josts, I., Grinter, R., Kelly, S. M., Mosbahi, K., Roszak, A., Cogdell, R., Smith, B. O., Byron, O., Walker, D. (2014) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963–1138 domain of TamB from Escherichia coli Acta Crystallographica. Section F: Structural Biology Communications, 70, pp. 1272-1275. (doi: 10.1107/S2053230X14017403)


Laird, J., McInally, C., Carr, C., Doddiah, S., Yates, G., Chrysanthou, E., Khattab, A., Love, A.J., Geri, C., Sadanandom, A., Smith, B.O., Kobayashi, K., Milner, J.J. (2013) Identification of the domains of cauliflower mosaic virus protein P6 responsible for suppression of RNA silencing and salicylic acid signalling Journal of General Virology, 94, pp. 2777-2789. (doi: 10.1099/vir.0.057729-0)

Kemppainen, K. K., Rinne, J., Sriram, A., Lakanmaa, M., Zeb, A., Tuomela, T., Popplestone, A., Singh, S., Sanz, A., Rustin, P., Jacobs, H. T. (2013) Expression of alternative oxidase in Drosophila ameliorates diverse phenotypes due to cytochrome oxidase deficiency Human Molecular Genetics, 23, pp. 2078-2093. (doi: 10.1093/hmg/ddt601)

Scialo, F., Mallikarjun, V., Stefanatos, R., Sanz, A. (2013) Regulation of lifespan by the mitochondrial electron transport chain: reactive oxygen species-dependent and reactive oxygen species-independent mechanisms Antioxidants and Redox Signaling, 19, pp. 1953-1969. (doi: 10.1089/ars.2012.4900)

Dobson, A. J., Purves, J., Kamysz, W., Rolff, J. (2013) Comparing selection on S. aureus between antimicrobial peptides and common antibiotics PLoS ONE, 8, (doi: 10.1371/journal.pone.0076521)

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

Tokatlidis, K., Brown, G.C. (2013) Introduction: focus on mitochondria FEBS Journal, 280, pp. 4932. (doi: 10.1111/febs.12504)

Douglas, A. E., Dobson, A. J. (2013) New synthesis: animal communication mediated by microbes: fact or fantasy? Journal of Chemical Ecology, 39, pp. 1149. (doi: 10.1007/s10886-013-0343-7)

Chatzi, A., Tokatlidis, K. (2013) The mitochondrial intermembrane space: a hub for oxidative folding linked to protein biogenesis Antioxidants and Redox Signaling, 19, pp. 54-62. (doi: 10.1089/ars.2012.4855)

MacKenzie, R.M., Salt, I.P., Miller, W.H., Logan, A., Ibrahim, H.A., Degasperi, A., Dymott, J.A., Hamilton, C.A., Murphy, M.P., Delles, C., Dominiczak, A.F. (2013) Mitochondrial reactive oxygen species enhance AMP-activated protein kinase activation in the endothelium of patients with coronary artery disease and diabetes Clinical Science, 124, pp. 403-411. (doi: 10.1042/CS20120239)

Banci, L., Bertini, I., Cefaro, C., Ciofi-Baffoni, S., Gajda, K., Felli, I.C., Gallo, A., Pavelkova, A., Kallergi, E., Andreadaki, M., Katrakili, N., Pozidis, C., Tokatlidis, K. (2013) An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control Journal of Molecular Biology, 425, pp. 594-608. (doi: 10.1016/j.jmb.2012.11.032)

Hamatsu, J., O’Donovan, D., Tanaka, T., Shirai, T., Hourai, Y., Mikawa, T., Ikeya, T., Mishima, M., Boucher, W., Smith, B.O., Laue, E.D., Shirakawa, M., Ito, Y. (2013) High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system Journal of the American Chemical Society, 135, pp. 1688-1691. (doi: 10.1021/ja310928u)

Hu, W., Franklin, K. A., Sharrock, R. A., Jones, M. A., Harmer, S. L., Lagarais, J. C. (2013) Unanticipated regulatory roles for Arabidopsis phytochromes revealed by null mutant analysis Proceedings of the National Academy of Sciences of the United States of America, 110, pp. 1542-1547. (doi: 10.1073/pnas.1221738110)

Salt, I. P. (2013) Examining the role of insulin in the regulation of cardiovascular health Future Cardiology, 9, pp. 39-52. (doi: 10.2217/fca.12.77)

Bijland, S., Mancini, S.J., Salt, I.P. (2013) Role of AMP-activated protein kinase in adipose tissue metabolism and inflammation Clinical Science, 124, pp. 491-507. (doi: 10.1042/CS20120536)

Vance, S.J., McDonald, R.E., Cooper, A., Smith, B.O., Kennedy, M.W. (2013) The structure of latherin, a surfactant allergen protein from horse sweat and saliva Journal of the Royal Society: Interface, 10, pp. Art. 20130453. (doi: 10.1098/rsif.2013.0453)

Kennedy, M.W., Córsico, B., Cooper, A., Smith, B.O. (2013) The unusual lipid-binding proteins of nematodes: NPAs, nemFABPs and FARs CABI; Wallingford; UK

Mitochondria control life and death in cells as they are central hubs for metabolism, protein cell homeostasis and cellular stress responses. We are interested in how mitochondria are made, how they function to sustain life and control death, how they are selectively cleared when they get damaged and how they exert a key role in ageing.

We use a variety of model systems including yeast, Drosophila and human cells and a combination of approaches ranging from chemical and structural biology to biochemistry, omics and cell biology at different levels of complexity working with isolated proteins and their complexes (in vitro), isolated mitochondria (in organello) and intact cells and organisms (in vivo).

Our work also links redox control and stress responses in the oxidative protein folding mechanisms in the two central hubs for protein folding in eukaryotic cells ie the mitochondria and the ER.

Specific areas

  • Protein import, folding and assembly mechanisms of mitochondria biogenesis. Emphasis on oxidative protein folding in the mitochondrial intermembrane space (IMS), biogenesis of mitochondria metabolite transporter proteins, and novel unconventional mitochondrial import pathways.
  • Pink1 signaling mechanisms underpinning selective clearance of damaged mitochondria (mitophagy)
  • The role of complex I, mitochondria reactive oxygen species (mtROS) and senescence in ageing
  • Oxidative Protein folding, redox stress regulation and unfolded protein responses in the ER

Wider impact of research

The work of this theme is mainly based on curiosity-driven discovery research, but we have a strong interest in translating our mechanistic molecular research findings to applications in human health and societal problems by ttackling important, yet unresolved challenges that require a strong inter-disciplinary approach.

Areas where our research has a wider impact include:

  • Development of a platform technology for therapeutic delivery of useful cargo to mitochondria, an unmet and critical need of the Pharma Industry for several of the most common human diseases (cancer, neurodegeneration and diabetes) as well as rare human mitochondrial diseases
  • Exploit the mechanistic knowledge of the Pink1 signalling pathway that mediates mitophagy in developing new models and designing more targeted approaches for Parkinsons’ disease
  • Develop a rational framework and tractable fly models for establishing the role of mitochondrial function and senescence in healthy ageing
  • Establish new unfolded protein and stress pathways in the ER as potential therapeutic targets for protein misfolding and aggregation diseases