The mitochondrial unfolded protein response–synchronizing genomes

Autophagy and the Integrated Stress Response

Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506 · see citing works

Mitochondria: In Sickness and in Health

Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479 · see citing works

Sirtuins as regulators of metabolism and healthspan

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works

A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology

Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · see citing works

Translocation of Proteins into Mitochondria

Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,486 · see citing works

The NAD+/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works

Rates of Behavior and Aging Specified by Mitochondrial Function During Development

Dillin, A., Hsu, A.-L., Arantes-Oliveira, N., Lehrer-Graiwer, J., Hsin, H., Fraser, A. G., Kamath, R. S., Ahringer, J., & Kenyon, C. (2002) · Science · doi:10.1126/science.1077780 · Cited by 1,121 · see citing works

The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity

Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · see citing works

Mitonuclear protein imbalance as a conserved longevity mechanism

Houtkooper, R. H., Mouchiroud, L., Ryu, D., Moullan, N., Katsyuba, E., Knott, G., Williams, R. W., & Auwerx, J. (2013) · Nature · doi:10.1038/nature12188 · Cited by 1,035 · see citing works

Mitochondrial Import Efficiency of ATFS-1 Regulates Mitochondrial UPR Activation

Nargund, A. M., Pellegrino, M., Fiorese, C. J., Baker, B. M., & Haynes, C. M. (2012) · Science · doi:10.1126/science.1223560 · Cited by 1,027 · see citing works

A mitochondrial specific stress response in mammalian cells

Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · see citing works

Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones

Yoneda, T., Benedetti, C., Urano, F., Clark, S. G., Harding, H. P., & Ron, D. (2004) · Journal of Cell Science · doi:10.1242/jcs.01275 · Cited by 636 · see citing works

ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans

Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., & Ron, D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.016 · Cited by 595 · see citing works

Ceramide targets autophagosomes to mitochondria and induces lethal mitophagy

Sentelle, R. D., Senkal, C. E., Jiang, W., Ponnusamy, S., Gencer, S., Panneer Selvam, S., Ramshesh, V. K., Peterson, Y. K., Lemasters, J. J., Szulc, Z. M., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1059 · Cited by 539 · see citing works

Quality control of mitochondria: protection against neurodegeneration and ageing

Tatsuta, T., & Langer, T. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601972 · Cited by 519 · see citing works

The mitochondrial UPR – protecting organelle protein homeostasis

Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works

The matrix peptide exporter HAF-1 signals a mitochondrial unfolded protein response by activating the transcription factor ZC376.7 in C. elegans

Haynes, C. M., Yang, Y., Blais, S., Neubert, T., & Ron, D. (2010) · Molecules and Cells · doi:10.1016/j.molcel.2010.01.015 · Cited by 480 · see citing works

The origin and early evolution of mitochondria.

Gray, M. W., Burger, G., & Lang, B. F. (2001) · Genome biology · doi:10.1186/gb-2001-2-6-reviews1018 · Cited by 460 · see citing works

Mutations in the clk-1 gene of Caenorhabditis elegans affect developmental and behavioral timing

Wong, A., Boutis, P., & Hekimi, S. (1995) · Genetics · doi:10.1093/genetics/139.3.1247 · Cited by 416 · see citing works

The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria

Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411 · see citing works

Muscle Mitohormesis Promotes Longevity via Systemic Repression of Insulin Signaling

Owusu-Ansah, E., Song, W., & Perrimon, N. (2013) · Cell · doi:10.1016/j.cell.2013.09.021 · Cited by 395 · see citing works

Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3

Khan, N. A., Auranen, M., Paetau, I., Pirinen, E., Euro, L., Forsström, S., Pasila, L., Velagapudi, V., Carroll, C. J., Auwerx, J., et al. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201403943 · Cited by 385 · see citing works

Pharmacological approaches to restore mitochondrial function

Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works

Relationship Between Mitochondrial Electron Transport Chain Dysfunction, Development, and Life Extension in Caenorhabditis elegans

Rea, S. L., Ventura, N., & Johnson, T. E. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050259 · Cited by 383 · see citing works

Ubiquitin-Like Protein 5 Positively Regulates Chaperone Gene Expression in the Mitochondrial Unfolded Protein Response

Benedetti, C., Haynes, C. M., Yang, Y., Harding, H. P., & Ron, D. (2006) · Genetics · doi:10.1534/genetics.106.061580 · Cited by 382 · see citing works

Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection

Pellegrino, M. W., Nargund, A. M., Kirienko, N. V., Gillis, R., Fiorese, C. J., & Haynes, C. M. (2014) · Nature · doi:10.1038/nature13818 · Cited by 369 · see citing works

NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease

Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works

Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome.

Martinus, R., Garth, G. P., Webster, T., Cartwright, P., Naylor, D. J., Høj, P., & Hoogenraad, N. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0098h.x · Cited by 340 · see citing works

The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease

Jovaisaite, V., Mouchiroud, L., & Auwerx, J. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.090738 · Cited by 335 · see citing works

Protective Coupling of Mitochondrial Function and Protein Synthesis via the eIF2α Kinase GCN-2

Baker, B. M., Nargund, A. M., Sun, T., & Haynes, C. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002760 · Cited by 326 · see citing works

Caenorhabditis elegans pathways that surveil and defend mitochondria

Liu, Y., Samuel, B. S., Breen, P. C., & Ruvkun, G. (2014) · Nature · doi:10.1038/nature13204 · Cited by 309 · see citing works

Discovery of Genes Activated by the Mitochondrial Unfolded Protein Response (mtUPR) and Cognate Promoter Elements

Aldridge, J. E., Horibe, T., & Hoogenraad, N. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000874 · Cited by 299 · see citing works

SirT3 Regulates the Mitochondrial Unfolded Protein Response

Papa, L., & Germain, D. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01337-13 · Cited by 282 · see citing works

A SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function

Ryu, D., Jo, Y. S., Sasso, G. L., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 258 · see citing works

Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle

Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · see citing works

Multilayered Genetic and Omics Dissection of Mitochondrial Activity in a Mouse Reference Population

Wu, Y., Williams, E. G., Dubuis, S., Mottis, A., Jovaisaite, V., Houten, S. M., Argmann, C. A., Faridi, P., Wolski, W., Kutalik, Z., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.039 · Cited by 244 · see citing works

Extended longevity of Caenorhabditis elegans by knocking in extra copies of hsp70F, a homolog of mot‐2 (mortalin)/mthsp70/Grp75

Yokoyama, K., Fukumoto, K., Murakami, T., Harada, S.-I., Hosono, R., Wadhwa, R., Mitsui, Y., & Ohkuma, S. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02470-5 · Cited by 229 · see citing works

Metabolic networks of longevity

Houtkooper, R. H., Williams, R. W., & Auwerx, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.029 · Cited by 217 · see citing works

Activation of the mitochondrial unfolded protein response does not predict longevity in Caenorhabditis elegans

Bennett, C. F., Wende, H. V., Simko, M., Klum, S., Barfield, S., Choi, H., Pineda, V. V., & Kaeberlein, M. R. (2014) · Nature Communications · doi:10.1038/ncomms4483 · Cited by 215 · see citing works

The Chop Gene Contains an Element for the Positive Regulation of the Mitochondrial Unfolded Protein Response

Horibe, T., & Hoogenraad, N. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000835 · Cited by 208 · see citing works

Stress-Regulated Translational Attenuation Adapts Mitochondrial Protein Import through Tim17A Degradation

Rainbolt, T. K., Atanassova, N., Genereux, J. C., & Wiseman, R. L. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.006 · Cited by 204 · see citing works

Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of γ-glutamylcysteine synthetase heavy subunit gene

Jeyapaul, J., & Jaiswal, A. K. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00256-2 · Cited by 193 · see citing works

Surveillance-Activated Defenses Block the ROS–Induced Mitochondrial Unfolded Protein Response

Runkel, E. D., Liu, S., Baumeister, R., & Schulze, E. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003346 · Cited by 192 · see citing works

Mitochondrial protein quality control during biogenesis and aging

Baker, B. M., & Haynes, C. M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.004 · Cited by 192 · see citing works

Mitochondrial Genome Content Is Regulated during Nematode Development

Tsang, W. Y. W., & Lemire, B. D. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6394 · Cited by 187 · see citing works

Mitonuclear match: Optimizing fitness and fertility over generations drives ageing within generations

Lane, N. J. (2011) · BioEssays · doi:10.1002/bies.201100051 · Cited by 177 · see citing works

Mitochondrial Proteostasis in the Control of Aging and Longevity

Jensen, M. B., & Jasper, H. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.006 · Cited by 162 · see citing works

Molecular mechanisms underlying genotype‐dependent responses to dietary restriction

Schleit, J., Johnson, S. C., Bennett, C. F., Simko, M., Trongtham, N., Castanza, A., Hsieh, E. J., Moller, R. M., Wasko, B. M., Delaney, J. R., et al. (2013) · Aging Cell · doi:10.1111/acel.12130 · Cited by 159 · see citing works

Induction of dsRNA-activated protein kinase links mitochondrial unfolded protein response to the pathogenesis of intestinal inflammation

Rath, E., Berger, E., Messlik, A., Nunes, T., Liu, B., Kim, S. C., Hoogenraad, N. J., Sans, M., Sartor, R. B., & Haller, D. (2011) · Gut · doi:10.1136/gutjnl-2011-300767 · Cited by 154 · see citing works

The good and the bad of being connected: the integrons of aging

Dillin, A. G., Gottschling, D. E., & Nyström, T. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.12.003 · Cited by 136 · see citing works

The mitochondrial unfolded protein response activator ATFS-1 protects cells from inhibition of the mevalonate pathway

Rauthan, M., Ranji, P., Pradenas, N. A., Pitot, C., & Pilon, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218778110 · Cited by 129 · see citing works

PINK1-Parkin Pathway Activity Is Regulated by Degradation of PINK1 in the Mitochondrial Matrix

Thomas, R. E., Andrews, L. A., Burman, J. L., Lin, W.-Y., & Pallanck, L. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004279 · Cited by 129 · see citing works

Genetic analysis of mitochondrial protein misfolding in Drosophila melanogaster

Pimenta de Castro, I., Costa, A. C., Lam, D., Tufi, R., Fedele, V, Moisoi, N., Dinsdale, D., Deas, E., Loh, S. H. Y., & Martins, L. M. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.5 · Cited by 128 · see citing works

Complex IV-deficient Surf1−/− mice initiate mitochondrial stress responses

Pulliam, D. A., Deepa, S. S., Liu, Y., Hill, S., Lin, A., Bhattacharya, A., Shi, Y., Sloane, L. B., Viscomi, C. F., Zeviani, M., et al. (2014) · Biochemical Journal · doi:10.1042/bj20140291 · Cited by 108 · see citing works

The Paradox of Mitochondrial Dysfunction and Extended Longevity

Munkácsy, E., & Rea, S. L. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.016 · Cited by 101 · see citing works

Mitochondrial proteolytic stress induced by loss of mortalin function is rescued by Parkin and PINK1

Burbulla, L. F., Fitzgerald, J. C., Stegen, K., Westermeier, J., Thost, A.-K., Kato, H., Mokranjac, D., Sauerwald, J., Martins, L. M., Woitalla, D., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.103 · Cited by 97 · see citing works

TOR Signaling Couples Oxygen Sensing to Lifespan in C. elegans

Schieber, M., & Chandel, N. S. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.075 · Cited by 79 · see citing works

Genome‐wide screen identifies signaling pathways that regulate autophagy during Caenorhabditis elegans development

Guo, B., Huang, X., Zhang, P., Qi, L., Liang, Q., Zhang, X., Huang, J. S., Fang, B., Hou, W., Han, J., et al. (2014) · EMBO Reports · doi:10.1002/embr.201338310 · Cited by 63 · see citing works

Caenorhabditis elegans mitochondrial mutants as an investigative tool to study human neurodegenerative diseases associated with mitochondrial dysfunction

Ventura, N., & Rea, S. L. (2007) · Biotechnology Journal · doi:10.1002/biot.200600248 · Cited by 54 · see citing works

Mitochondrial Dysfunction in Aging and Longevity: A Causal or Protective Role?

Pulliam, D. A., Bhattacharya, A., & Remmen, H. V. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4950 · Cited by 33 · see citing works

Proteostasis and aging

Kaushik, S., & Cuervo, A. M. (2015) · Nature Medicine · doi:10.1038/nm.4001 · Cited by 899 · see citing works

Mitochondrial quality control and muscle mass maintenance.

Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works

The Mitochondrial Basis of Aging and Age-Related Disorders

Srivastava, S. (2017) · Genes · doi:10.3390/genes8120398 · Cited by 428 · see citing works

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works

The metabolic regulation of aging

Finkel, T. (2015) · Nature Medicine · doi:10.1038/nm.3998 · Cited by 325 · see citing works

The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress

Kim, K. H., Son, J. M., Benayoun, B. A., & Lee, C. D. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.06.008 · Cited by 311 · see citing works

NAD+ homeostasis in renal health and disease

Ralto, K. M., Rhee, E. P., & Parikh, S. M. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0216-6 · Cited by 288 · see citing works

The role of mitochondria in stem cell fate and aging

Zhang, H., Menzies, K. J., & Auwerx, J. H. (2018) · Development · doi:10.1242/dev.143420 · Cited by 285 · see citing works

The NAD-booster nicotinamide riboside potently stimulates hematopoiesis through increased mitochondrial clearance

Vannini, N., Campos, V., Girotra, M., Trachsel, V., Rojas-Sutterlin, S., Tratwal, J., Ragusa, S., Stefanidis, E., Ryu, D., Rainer, P. Y., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2019.02.012 · Cited by 218 · see citing works

Recent Advances in Mitochondrial Aminoacyl-tRNA Synthetases and Disease

Sissler, M., González-Serrano, L. E., & Westhof, É. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.06.002 · Cited by 197 · see citing works

Mitohormesis in exercise training

Merry, T. L., & Ristow, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.032 · Cited by 176 · see citing works

Antibiotic use and abuse: A threat to mitochondria and chloroplasts with impact on research, health, and environment

Wang, X., Ryu, D., Houtkooper, R., & Auwerx, J. (2015) · Bioessays · doi:10.1002/bies.201500071 · Cited by 146 · see citing works

Mitochondrial NAD + /NADH Redox State and Diabetic Cardiomyopathy

Berthiaume, J. M., Kurdys, J., Muntean, D. M., & Rosca, M. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7415 · Cited by 168 · see citing works

Mitochondrial ClpP serine protease-biological function and emerging target for cancer therapy

Nouri, K., Feng, Y., & Schimmer, A. D. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03062-z · Cited by 156 · see citing works

Placental Ageing in Adverse Pregnancy Outcomes: Telomere Shortening, Cell Senescence, and Mitochondrial Dysfunction

Manna, S., McCarthy, C., & McCarthy, F. P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3095383 · Cited by 141 · see citing works

Mitochondria Retrograde Signaling and the UPRmt: Where Are We in Mammals?

Arnould, T., Michel, S., & Renard, P. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160818224 · Cited by 134 · see citing works

A Conserved Mito-Cytosolic Translational Balance Links Two Longevity Pathways

Molenaars, M., Janssens, G. E., Williams, E. G., Jongejan, A., Lan, J., Rabot, S., Joly, F., Moerland, P. D., Schomakers, B. V., Lezzerini, M., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.01.011 · Cited by 120 · see citing works

Metabolism and the UPR mt

Lin, Y., & Haynes, C. M. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.004 · Cited by 123 · see citing works

Mitochondrial dysfunction in cancer: Potential roles of ATF5 and the mitochondrial UPR

Deng, P., & Haynes, C. M. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.002 · Cited by 119 · see citing works

Defective Mitochondrial tRNA Taurine Modification Activates Global Proteostress and Leads to Mitochondrial Disease

Fakruddin, M., Wei, F., Suzuki, T., Asano, K., Kaieda, T., Omori, A., Izumi, R., Fujimura, A., Kaitsuka, T., Miyata, K., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.051 · Cited by 121 · see citing works

Mechanisms and rejuvenation strategies for aged hematopoietic stem cells

Li, X., Zeng, X., Xu, Y., Wang, B., Zhao, Y., Lai, X., Qian, P., & Huang, H. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00864-8 · Cited by 118 · see citing works

Defending the mitochondria: The pathways of mitophagy and mitochondrial-derived vesicles

Roberts, R. F., Tang, M. Y. H., Fon, E. A., & Durcan, T. M. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.020 · Cited by 120 · see citing works

UPRmt-mediated cytoprotection and organismal aging

Schulz, A. M., & Haynes, C. M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.008 · Cited by 110 · see citing works

Cytosolic Proteostasis Networks of the Mitochondrial Stress Response

D'Amico, D. F., Sorrentino, V., & Auwerx, J. H. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.05.002 · Cited by 106 · see citing works

Mitochondrial Proteins Moonlighting in the Nucleus

Monaghan, R. M., & Whitmarsh, A. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.10.003 · Cited by 104 · see citing works

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95 · see citing works

The role of mitophagy in innate immune responses triggered by mitochondrial stress

Song, Y., Zhou, Y., & Zhou, X. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00659-x · Cited by 87 · see citing works

Protein trafficking at the crossroads to mitochondria

Wasilewski, M., Chojnacka, K., & Chacińska, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.019 · Cited by 89 · see citing works

Mitochondrial Quality Control Mechanisms and the PHB (Prohibitin) Complex

Hernando‐Rodríguez, B., & Artal‐Sanz, M. (2018) · Cells · doi:10.3390/cells7120238 · Cited by 83 · see citing works

Mitochondrial Dysfunction in Obesity and Reproduction

Das, M., Sauceda, C., & Webster, N. J. G. (2020) · Endocrinology · doi:10.1210/endocr/bqaa158 · Cited by 83 · see citing works

The transcriptional coactivator CBP/p300 is an evolutionarily conserved node that promotes longevity in response to mitochondrial stress

Li, T. Y., Sleiman, M. B., Li, H., Gao, A. W., Mottis, A., Bachmann, A. M., Alam, G. E., Li, X., Goeminne, L. J. E., Schoonjans, K., et al. (2021) · Nature Aging · doi:10.1038/s43587-020-00025-z · Cited by 78 · see citing works

Ground control to major TOM: mitochondria–nucleus communication

Eisenberg‐Bord, M., & Schuldiner, M. (2016) · FEBS Journal · doi:10.1111/febs.13778 · Cited by 80 · see citing works

Oxidized nicotinamide adenine dinucleotide-dependent mitochondrial deacetylase sirtuin-3 as a potential therapeutic target of Parkinson’s disease

Zhou, Z., & Tan, E. K. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101107 · Cited by 76 · see citing works

The Endoplasmic Reticulum Stress Response in Neuroprogressive Diseases: Emerging Pathophysiological Role and Translational Implications

Morris, G., Puri, B. K., Walder, K. R., Berk, M., Stubbs, B., Maes, M. H. J., & Carvalho, A. F. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1028-6 · Cited by 78 · see citing works

Chatty Mitochondria: Keeping Balance in Cellular Protein Homeostasis

Topf, U., Wróbel, L., & Chacińska, A. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.002 · Cited by 75 · see citing works

Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration

Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7145 · Cited by 77 · see citing works

Abnormal Mitochondrial Quality Control in Neurodegenerative Diseases

Yan, X., Wang, B., Hu, Y., Wang, S., & Zhang, X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00138 · Cited by 74 · see citing works

Mitochondrial determinants of cancer health disparities

Choudhury, A. R., & Singh, K. K. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.001 · Cited by 74 · see citing works

ClpX stimulates the mitochondrial unfolded protein response (UPRmt) in mammalian cells

Al-Furoukh, N., Ianni, A., Nolte, H., Hölper, S., Krüger, M., Wanrooij, S., & Braun, T. W. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.06.016 · Cited by 71 · see citing works

Mitochondrial pathways in human health and aging

Bornstein, R., González, B., & Johnson, S. C. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.07.007 · Cited by 70 · see citing works

Unveiling “Musica Universalis” of the Cell: A Brief History of Biological 12-Hour Rhythms

Zhu, B., Dacso, C. C., & O’Malley, B. W. (2018) · Journal of the Endocrine Society · doi:10.1210/js.2018-00113 · Cited by 63 · see citing works

Mitochondrially-targeted treatment strategies

Bozi, L. H. M., Campos, J. C., Zambelli, V. O., Ferreira, N. D., & Ferreira, J. C. B. (2019) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100836 · Cited by 65 · see citing works

Mitochondrial Quality Control in Cardiac Diseases

Campos, J. C., Bozi, L. H. M., Bechara, L. R. G., Lima, V. M., & Ferreira, J. C. B. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00479 · Cited by 64 · see citing works

Role of eIF5A in Mitochondrial Function

Barba‐Aliaga, M., & Alepuz, P. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031284 · Cited by 60 · see citing works

Analysis of heat-induced protein aggregation in human mitochondria

Wilkening, A., Rüb, C., Sylvester, M., & Voos, W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002122 · Cited by 59 · see citing works

Decoding the Rosetta stone of mitonuclear communication

English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55 · see citing works

Mitochondria and mitochondria-induced signalling molecules as longevity determinants

Rose, G., Santoro, A., & Salvioli, S. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.002 · Cited by 56 · see citing works

Protein aggregation, cardiovascular diseases, and exercise training: Where do we stand?

Gouveia, M., Xia, K., Colón, W., Vieira, S. I., & Ribeiro, F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.07.005 · Cited by 54 · see citing works

From mitochondria to sarcopenia: role of 17β-estradiol and testosterone

Tian, X., Lou, S., & Shi, R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1156583 · Cited by 54 · see citing works

Local and long-range activation of innate immunity by infection and damage in C. elegans

Ewbank, J. J., & Pujol, N. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.09.005 · Cited by 53 · see citing works

A New Vision of Mitochondrial Unfolded Protein Response to the Sirtuin Family

Weng, H., Ma, Y., Chen, L., Cai, G., Chen, Z., Zhang, S., & Ye, Q. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200123165002 · Cited by 50 · see citing works

Mitochondrial protease ClpP supplementation ameliorates diet-induced NASH in mice

Choi, S., Hwang, Y., Lee, S., Jung, H.-K., Shin, T. H., Son, Y., Park, S., Han, S. J., Kim, H. J., Lee, K. W., et al. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2022.03.034 · Cited by 48 · see citing works

Differential Protein Distribution between the Nucleus and Mitochondria: Implications in Aging

Lionaki, E., Gkikas, I., & Tavernarakis, N. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00162 · Cited by 50 · see citing works

Linking mitochondrial dynamics to mitochondrial protein quality control

Haroon, S., & Vermulst, M. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.04.004 · Cited by 46 · see citing works

Role of FOXO transcription factors in crosstalk between mitochondria and the nucleus

Kim, S., & Koh, H. (2017) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-017-9705-0 · Cited by 46 · see citing works

Mitochondrial dynamics, quality control and miRNA regulation in skeletal muscle: implications for obesity and related metabolic disease

Dahlmans, D., Houzelle, A., Schrauwen, P., & Joris Hoeks, J. (2016) · Clinical Science · doi:10.1042/cs20150780 · Cited by 44 · see citing works

Molecular hydrogen modulates gene expression via histone modification and induces the mitochondrial unfolded protein response

Sobue, S., Inoue, C., Hori, F., Qiao, S., Murate, T., & Ichihara, M. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.09.024 · Cited by 44 · see citing works

Mitochondrial regulation of cardiac aging

Wang, Y., Li, Y., He, C., Gou, B., & Song, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.12.008 · Cited by 42 · see citing works

Mutant huntingtin inhibits the mitochondrial unfolded protein response by impairing ABCB10 mRNA stability

Fu, Z., Liu, F., Liu, C., Jin, B., Jiang, Y., Tang, M., Qi, X., & Guo, X. L. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.02.015 · Cited by 41 · see citing works

The intersection of exercise and aging on mitochondrial protein quality control

Zhang, Y., Oliveira, A. N., & Hood, D. A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110824 · Cited by 37 · see citing works

Matrix Metalloproteinase-11 Promotes Early Mouse Mammary Gland Tumor Growth through Metabolic Reprogramming and Increased IGF1/AKT/FoxO1 Signaling Pathway, Enhanced ER Stress and Alteration in Mitochondrial UPR

Tan, B., Jaulin, A., Bund, C., Outilaft, H., Wendling, C., Chenard, M., Alpy, F., Çiçek, A. E., Namer, I. J., Tomasetto, C., et al. (2020) · Cancers · doi:10.3390/cancers12092357 · Cited by 35 · see citing works

Activation of mitochondrial unfolded protein response is associated with Her2-overexpression breast cancer

Chen, F.-M., Huang, L., Ou‐Yang, F., Kan, J., Kao, L.-C., & Hou, M. (2020) · Breast Cancer Research and Treatment · doi:10.1007/s10549-020-05729-9 · Cited by 34 · see citing works

Mitochondrial Caseinolytic Protease P: A Possible Novel Prognostic Marker and Therapeutic Target in Cancer

Cormio, A., Sanguedolce, F., Pesce, V., & Musicco, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126228 · Cited by 34 · see citing works

ATF5 is a regulator of exercise-induced mitochondrial quality control in skeletal muscle

Slavin, M. B., Kumari, R., & Hood, D. A. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101623 · Cited by 33 · see citing works

Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration

Amanullah, A., Upadhyay, A., Joshi, V., Mishra, R., Jana, N. R., & Mishra, A. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.08.005 · Cited by 33 · see citing works

Sesn2 Serves as a Regulator between Mitochondrial Unfolded Protein Response and Mitophagy in Intervertebral Disc Degeneration

Xu, W., Liu, C., Zheng, H., Xu, H., Yang, R., Jiang, S., & Zhu, L.-X. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.70211 · Cited by 33 · see citing works

Proteostasis and ageing: insights from long‐lived mutant mice

Sands, W. A., Page, M. M., & Selman, C. (2017) · The Journal of Physiology · doi:10.1113/jp274334 · Cited by 32 · see citing works

Mitochondrial quality control in the cardiac system: An integrative view

Cadete, V. J. J., Vasam, G., Menzies, K. J., & Burelle, Y. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.11.018 · Cited by 32 · see citing works

The compensatory antioxidant response system with a focus on neuroprogressive disorders

Morris, G., Puri, B. K., Walker, A. J., Berk, M., Walder, K. R., Bortolasci, C. C., Marx, W., Carvalho, A. F., & Maes, M. H. J. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109708 · Cited by 31 · see citing works

Rosmarinic Acid Inhibits Mitochondrial Damage by Alleviating Unfolded Protein Response

Cai, G., Lin, F., Wu, D., Lin, C., Chen, H., Wei, Y., Weng, H., Chen, Z., Wu, M., Huang, E., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.859978 · Cited by 30 · see citing works

Double-edged alliance: mitochondrial surveillance by the UPS and autophagy

Franz, A., Kevei, É., & Hoppe, T. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.08.004 · Cited by 28 · see citing works

Pterostilbene in Combination With Mitochondrial Cofactors Improve Mitochondrial Function in Cellular Models of Mitochondrial Diseases

Suarez-Rivero, J. M., Pastor‐Maldonado, C. J., Romero-González, A., Gómez-Fernández, D., Povea-Cabello, S., Álvarez-Córdoba, M., Villalón-García, I., Talaverón-Rey, M., Suárez-Carrillo, A., Munuera-Cabeza, M., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.862085 · Cited by 28 · see citing works

Effect of Tim23 knockdown in vivo on mitochondrial protein import and retrograde signaling to the UPRmt in muscle

Oliveira, A. N., & Hood, D. A. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00275.2017 · Cited by 28 · see citing works

FANCD2 modulates the mitochondrial stress response to prevent common fragile site instability

Fernandes, P., Miotto, B., Saint‐Ruf, C., Said, M., Barra, V., Nähse, V., Ravera, S., Cappelli, E., & Naim, V. (2021) · Communications Biology · doi:10.1038/s42003-021-01647-8 · Cited by 27 · see citing works

MicroRNA‐382 silencing induces a mitonuclear protein imbalance and activates the mitochondrial unfolded protein response in muscle cells

Dahlmans, D., Houzelle, A., Andreux, P. A., Wang, X., Jörgensen, J. A., Moullan, N., Daemen, S., Kersten, S., Auwerx, J. H., & Joris Hoeks, J. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27401 · Cited by 26 · see citing works

Overexpression of PGC-1α influences the mitochondrial unfolded protein response (mtUPR) induced by MPP+ in human SH-SY5Y neuroblastoma cells

Cai, Y., Shen, H., Weng, H., Wang, Y.-Q., Cai, G., Chen, X., & Ye, Q. (2020) · Scientific Reports · doi:10.1038/s41598-020-67229-6 · Cited by 26 · see citing works

Mammalian RNA switches: Molecular rheostats in gene regulation, disease, and medicine

Subbaiah, K. C. V., Hedaya, O. M., Wu, J., Jiang, F., & Yao, P. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.10.001 · Cited by 23 · see citing works

Interplay between the Ubiquitin Proteasome System and Mitochondria for Protein Homeostasis

Escobar‐Henriques, M., Altin, S., & den Brave, F. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.035 · Cited by 23 · see citing works

The mitochondrial UPR induced by ATF5 attenuates intervertebral disc degeneration via cooperating with mitophagy

Xu, W., Zheng, H., Yang, R., Sun, Y.-F., Peng, B., Liu, C., Song, J., Jiang, S., & Zhu, L. (2024) · Cell Biology and Toxicology · doi:10.1007/s10565-024-09854-9 · Cited by 22 · see citing works

ATF5, a putative therapeutic target for the mitochondrial DNA 3243A > G mutation-related disease

Gao, X., Jiang, Z., Yan, X., Liu, J., Li, F., Liu, P., Li, J., Wei, Y., Sun, Y. E., Zhang, Y., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03993-1 · Cited by 22 · see citing works

ATF5 Attenuates the Secretion of Pro-Inflammatory Cytokines in Activated Microglia

Zhu, J., Lee, M. J., An, J. H., Oh, E., Chung, W., & Heo, J. Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043322 · Cited by 24 · see citing works

Cell-Nonautonomous Mechanisms Underlying Cellular and Organismal Aging

Medkour, Y., Svistkova, V., & Titorenko, V. I. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.09.003 · Cited by 22 · see citing works

Is the liver resilient to the process of ageing?

Chatterjee, N., Sharma, R., Kale, P. R., Trehanpati, N., & Ramakrishna, G. (2024) · Annals of Hepatology · doi:10.1016/j.aohep.2024.101580 · Cited by 20 · see citing works

Epicatechin Reduces Spatial Memory Deficit Caused by Amyloid-β25–35 Toxicity Modifying the Heat Shock Proteins in the CA1 Region in the Hippocampus of Rats

Díaz, A., Treviño, S., Pulido, G., Martínez-Muñoz, E., Cervantes, N., Espinosa, B., Rojas, K., Pérez‐Severiano, F., Montes, S., Rubio‐Osornio, M., et al. (2019) · Antioxidants · doi:10.3390/antiox8050113 · Cited by 19 · see citing works

UPR mt coordinates immunity to maintain mitochondrial homeostasis and animal fitness

Wang, S., Gao, K., & Liu, Y. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.11.004 · Cited by 19 · see citing works

Roles of mitochondrial unfolded protein response in mammalian stem cells

Gu, L., Chen, J., Lin, Q., & Yang, Y. (2021) · World Journal of Stem Cells · doi:10.4252/wjsc.v13.i7.737 · Cited by 18 · see citing works

Mitochondrial protein import and UPRmt in skeletal muscle remodeling and adaptation

Richards, B. J., Slavin, M. B., Oliveira, A. N., Sanfrancesco, V. C., & Hood, D. A. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.01.002 · Cited by 18 · see citing works

Harnessing Mitochondrial Stress for Health and Disease: Opportunities and Challenges

Sun, Y., Jin, L., Qin, Y., Ouyang, Z., Zhong, J., & Zeng, Y. (2024) · Biology · doi:10.3390/biology13060394 · Cited by 17 · see citing works

The Endoplasmic Reticulum and the Cellular Reticular Network

Agellon, L. B., & Michalak, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55858-5_4 · Cited by 17 · see citing works

Nutritional control of postembryonic development progression and arrest in Caenorhabditis elegans.

Mata-Cabana, A., Pérez-Nieto, C., & Olmedo, M. (2021) · Advances in Genetics · doi:10.1016/bs.adgen.2020.11.002 · Cited by 11 · see citing works

Sirt1 promotes tissue regeneration in zebrafish through regulating the mitochondrial unfolded protein response

Lin, Y., Sam, J., & Evans, T. (2021) · iScience · doi:10.1016/j.isci.2021.103118 · Cited by 17 · see citing works

TLR22-Induced Pro-Apoptotic mtROS Abets UPRmt-Mediated Mitochondrial Fission in Aeromonas hydrophila-Infected Headkidney Macrophages of Clarias gariepinus

Kumar, M., Sharma, S., Haque, M., Kumar, J., Hathi, U. P. S., & Mazumder, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.931021 · Cited by 16 · see citing works

Study of ATF4/CHOP axis-mediated mitochondrial unfolded protein response in neuronal apoptosis induced by methylmercury

Xu, S., Liu, H., Wang, C., Deng, Y., Xu, B., Yang, T., & Liu, W. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.114190 · Cited by 16 · see citing works

Mitochondrial Unfolded Protein Response and Its Roles in Stem Cells

Shen, G., Liu, W., Xu, L., & Wang, L. (2020) · Stem Cells and Development · doi:10.1089/scd.2019.0278 · Cited by 16 · see citing works

MOTS-c attenuates lung ischemia-reperfusion injury via MYH9-Dependent nuclear translocation and transcriptional activation of antioxidant genes

Li, X., Zhan, F., Qiu, G., Lu, P., Shen, Z., Qi, Y., Wu, M., Chu, M., Feng, J., Wen, Z., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103681 · Cited by 14 · see citing works

Transcription Factor Nrf2 and Mitochondria – Friends or Foes in the Regulation of Aging Rate

Shilovsky, G. A., & Ashapkin, V. V. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922120057 · Cited by 13 · see citing works

Aerobic Exercise Delays Alzheimer’s Disease by Regulating Mitochondrial Proteostasis in the Cerebral Cortex and Hippocampus

Cui, K., Li, C., & Fang, G. (2023) · Life · doi:10.3390/life13051204 · Cited by 14 · see citing works

“…Rewritten in the Skin”: Clues to Skin Biology and Aging from Inherited Disease

Monnat, R. J. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.88 · Cited by 13 · see citing works

ONC201 Suppresses Neuroblastoma Growth by Interrupting Mitochondrial Function and Reactivating Nuclear ATRX Expression While Decreasing MYCN

Wu, J., Huang, C., Wang, P., Chen, T., Hsu, W., Chuang, J., & Chuang, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021649 · Cited by 13 · see citing works

Unfolded proteins in the mitochondria activate HRI and inhibit mitochondrial protein translation

Wu, Y., Yang, Y., Qin, X., Zhang, Z., Ullah, M., Li, Y., & Zhang, Z. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111353 · Cited by 10 · see citing works

Signaling the mitochondrial unfolded protein response

Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359 · see citing works

Integrating the UPRmtinto the mitochondrial maintenance network

Fiorese, C. J., & Haynes, C. M. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291577 · Cited by 66 · see citing works

Mitochondrial unfolded protein response (UPRmt): what we know thus far

Torres, A. K., Fleischhart, V., & Inestrosa, N. C. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1405393 · Cited by 65 · see citing works

The mitochondrial unfolded protein response in health and disease

Safakli, R. N., & Smyrnias, I. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15260-3.00015-6 · Cited by 2 · see citing works

Methods to analyze the mitochondrial unfolded protein response (UPRmt)

Mallick, A., & Haynes, C. M. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.07.029 · Cited by 3 · see citing works