High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1

Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481

PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin

Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835

PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL

Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201008084 · Cited by 1,375

Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization

Sarraf, S. A., Raman, M., Guarani-Pereira, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,010

Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy

Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993

Widespread siRNA “off-target” transcript silencing mediated by seed region sequence complementarity

Jackson, A. L., Burchard, J., Schelter, J. M., Chau, B. N., Cleary, M. A., Lim, L. P., & Linsley, P. S. (2006) · RNA · doi:10.1261/rna.25706 · Cited by 979

The actin binding protein profilin 1 localizes inside mitochondria and is critical for their function

Read, T., Cisterna, B. A., Skruber, K., Ahmadieh, S., Liu, T. M., Vitriol, J. A., Shi, Y., Black, J. B., Butler, M. T., Lindamood, H. L., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00209-3 · Cited by 20

Loss of laforin or malin results in increased Drp1 level and concomitant mitochondrial fragmentation in Lafora disease mouse models

Upadhyay, M., Agarwal, S., Bhadauriya, P., & Ganesh, S. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.01.002 · Cited by 20

The Risk G Allele of the Single-Nucleotide Polymorphism rs928413 Creates a CREB1-Binding Site That Activates IL33 Promoter in Lung Epithelial Cells

Gorbacheva, A. M., Korneev, K. V., Kuprash, D. V., & Mitkin, N. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102911 · Cited by 20

Endothelial Mitochondrial Preprotein Translocase Tomm7-Rac1 Signaling Axis Dominates Cerebrovascular Network Homeostasis

Shi, D., Qi, M., Zhou, L., Li, X., Ni, L., Li, C., Yuan, T., Wang, Y., Chen, Y., Hu, C., et al. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311538 · Cited by 20

The Effects of Variants in the Parkin, PINK1, and DJ-1 Genes along with Evidence for their Pathogenicity

Hauser, D. N., Primiani, C. T., & Cookson, M. (2016) · Current Protein and Peptide Science · doi:10.2174/1389203717666160311121954 · Cited by 21

Ubiquitin signaling in PINK1/Parkin-dependent mitophagy

Okatsu, K., & Fukai, S. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf079 · Cited by 20

Mitochondrial proteotoxicity: implications and ubiquitin-dependent quality control mechanisms

Karbowski, M., Oshima, Y., & Verhoeven, N. A. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04604-8 · Cited by 21

MyD88 dimerization inhibitor ST2825 targets the aggressiveness of synovial fibroblasts in rheumatoid arthritis patients

Ramírez-Pérez, S., Vekariya, R., Gautam, S., Reyes‐Pérez, I. V., Drissi, H., & Bhattaram, P. (2023) · Arthritis Research & Therapy · doi:10.1186/s13075-023-03145-0 · Cited by 19

Protective C allele of the single-nucleotide polymorphism rs1335532 is associated with strong binding of Ascl2 transcription factor and elevated CD58 expression in B-cells

Mitkin, N. A., Muratova, A. M., Korneev, K. V., Pavshintsev, V. V., Rumyantsev, K. A., Vagida, M. S., Uvarova, A. N., Afanasyeva, M. A., Schwartz, A. M., & Kuprash, D. V. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.07.008 · Cited by 19

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 17

A hypomorphic variant in the translocase of the outer mitochondrial membrane complex subunit TOMM7 causes short stature and developmental delay

Young, C., Batkovskyte, D., Kitamura, M., Shvedova, M., Mihara, Y., Akiba, J., Zhou, W., Hammarsjö, A., Nishimura, G., Yatsuga, S., et al. (2022) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2022.100148 · Cited by 18

Mitophagy in hypertension-mediated organ damage

Ma, Y., Zhou, X., Gui, M., Yao, L., Li, J., Chen, X., Wang, M., Lu, B., & Fu, D. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1309863 · Cited by 19

Engineered Extracellular Vesicles Derived from Juvenile Mice Enhance Mitochondrial Function in the Aging Bone Microenvironment and Achieve Rejuvenation

Zheng, J., Ren, Y., Ke, J., Zhu, G., Wang, Z., Shi, X., & Wang, Y. (2025) · ACS Nano · doi:10.1021/acsnano.4c17989 · Cited by 18

SIAH proteins regulate the degradation and intra‐mitochondrial aggregation of PINK1 : Implications for mitochondrial pathology in Parkinson's disease

Elghani, F. A., Safory, H., Hamza, H., Savyon, M., Farhoud, M., Toren-Hershkoviz, M., Vitic, Z., Ebanks, K., Shani, V., Bisharat, S., et al. (2022) · Aging Cell · doi:10.1111/acel.13731 · Cited by 16

The multifaceted mitochondrion: An attractive candidate for therapeutic strategies

Strappazzon, F., & Cecconi, F. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.007 · Cited by 17

Deep Imaging: the next frontier in microscopy

Roukos, V., & Misteli, T. (2014) · Histochemistry and Cell Biology · doi:10.1007/s00418-014-1239-5 · Cited by 18

Transcriptional alterations in skin fibroblasts from Parkinson's disease patients with parkin mutations

González‐Casacuberta, I., Morén, C., Juárez‐Flores, D. L., Esteve‐Codina, A., Sierra, C., Catalán‐García, M., Guitart‐Mampel, M., Tobías, E., Milisenda, J. C., Pont‐Sunyer, C., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.01.021 · Cited by 17

Role of Mitochondrial Protein Import in Age-Related Neurodegenerative and Cardiovascular Diseases

Bogorodskiy, A. O., Okhrimenko, I. S., Burkatovskii, D., Jakobs, P., Maslov, I., Gordeliy, V., Dencher, N. A., Gensch, T., Voos, W., Altschmied, J., et al. (2021) · Cells · doi:10.3390/cells10123528 · Cited by 19

High-content analysis of α-synuclein aggregation and cell death in a cellular model of Parkinson's disease

Macchi, F., Deleersnijder, A., den Haute, C. V., Munck, S., Pottel, H., Michiels, A., Debyser, Z., Gérard, M., & Baekelandt, V. (2015) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2015.11.009 · Cited by 16

Chaperone complex BAG 2– HSC 70 regulates localization of Caenorhabditis elegans leucine‐rich repeat kinase LRK ‐1 to the Golgi

Fukuzono, T., Pastuhov, S. I., Okinobu, F., Li, C., Hattori, A., Iemura, S., Natsume, T., Shibuyà, H., Hanafusa, H., Matsumoto, K., et al. (2016) · Genes to Cells · doi:10.1111/gtc.12338 · Cited by 17

MitoTimer-based high-content screen identifies two chemically-related benzothiophene derivatives that enhance basal mitophagy

Cerqueira, F. M., Kozer, N., Petcherski, A., Baranovski, B. M., Wolf, D. M., Assali, E. A., Roth, Y., Gazit, R., Barr, H. M., Lewis, E. C., et al. (2020) · Biochemical Journal · doi:10.1042/bcj20190616 · Cited by 18

The A Allele of the Single-Nucleotide Polymorphism rs630923 Creates a Binding Site for MEF2C Resulting in Reduced CXCR5 Promoter Activity in B-Cell Lymphoblastic Cell Lines

Mitkin, N. A., Muratova, A. M., Schwartz, A. M., & Kuprash, D. V. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00515 · Cited by 16

Neuronal Mitophagy: Lessons from a Pathway Linked to Parkinson’s Disease

Corti, O. (2019) · Neurotoxicity Research · doi:10.1007/s12640-019-00060-8 · Cited by 18

The role of mitophagy in the development of chronic kidney disease

Yang, K., Li, T., Geng, Y., Zou, X., Peng, F., & Gao, W. (2024) · PeerJ · doi:10.7717/peerj.17260 · Cited by 16

Methods to Monitor Mitophagy and Mitochondrial Quality: Implications in Cancer, Neurodegeneration, and Cardiovascular Diseases

Patergnani, S., Bonora, M., Bouhamida, E., Danese, A., Marchi, S., Morciano, G., Previati, M., Pedriali, G., Rimessi, A., Anania, G., et al. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1433-4_9 · Cited by 15

Mitochondrial entry gate as regulatory hub

den Brave, F., Pfanner, N., & Becker, T. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119529 · Cited by 14

Development and characterization of phospho-ubiquitin antibodies to monitor PINK1-PRKN signaling in cells and tissue

Watzlawik, J. O., Hou, X., Richardson, T., Lewicki, S. L., Siuda, J. S., Wszołek, Z. K., Cook, C. N., Petrucelli, L., Deture, M. A., Dickson, D. W., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2356490 · Cited by 14

p63 and p73 repress CXCR5 chemokine receptor gene expression in p53-deficient MCF-7 breast cancer cells during genotoxic stress

Mitkin, N. A., Muratova, A. M., Sharonov, G. V., Korneev, K. V., Sviriaeva, E. N., Mazurov, D. V., Schwartz, A. M., & Kuprash, D. V. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.10.003 · Cited by 14

E3 ubiquitin ligase-mediated regulation of vertebrate ocular development; new insights into the function of SIAH enzymes

Piedade, W. P., & Famulski, J. K. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200613 · Cited by 19

Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

Alonso-Garrido, M., Manyes, L., Pralea, I.-E., & Iuga, C. A. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111432 · Cited by 14

A dual druggable genome-wide siRNA and compound library screening approach identifies modulators of parkin recruitment to mitochondria

Scott, H. L., Buckner, N., Fernández-Albert, F., Pedone, E., Postiglione, L., Shi, G., Allen, N. D., Wong, L., Magini, L., Marucci, L., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009699 · Cited by 13

Two sides of a coin: Physiological significance and molecular mechanisms for damage-induced mitochondrial localization of PINK1 and Parkin

Matsuda, N., & Yamano, K. (2020) · Neuroscience Research · doi:10.1016/j.neures.2020.03.009 · Cited by 13

Identification of potential blood biomarkers for early diagnosis of schizophrenia through RNA sequencing analysis

Li, Z., Li, X., Jin, M., Liu, Y., He, Y., Jia, N., Cui, X., Liu, Y., Hu, G., & Yu, Q. (2022) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2022.01.003 · Cited by 14

Mitophagy Regulated by the PINK1-Parkin Pathway

Arano, T., & Imai, Y. (2015) · InTech eBooks · doi:10.5772/61284 · Cited by 14

MAPKAP kinase 2–mediated phosphorylation of HspA1L protects male germ cells from heat stress–induced apoptosis

Williams, P. A., Kobilnyk, H. E., McMillan, E. A., & Strochlic, T. I. (2019) · Cell Stress and Chaperones · doi:10.1007/s12192-019-01035-6 · Cited by 13

Deficits in the Skeletal Muscle Transcriptome and Mitochondrial Coupling in Progressive Diabetes-Induced CKD Relate to Functional Decline

Bittel, D. C., Bittel, A. J., Varadhachary, A. S., Pietka, T., & Sinacore, D. R. (2021) · Diabetes · doi:10.2337/db20-0688 · Cited by 12

An interactive web-based application for Comprehensive Analysis of RNAi-screen Data

Dutta, B., Azhir, A., Merino, L.-H., Guo, Y., Revanur, S., Madhamshettiwar, P. B., Germain, R. N., Smith, J. A., Simpson, K. J., Martin, S. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms10578 · Cited by 12

High-Content, Full Genome siRNA Screen for Regulators of Oncogenic HRAS -Driven Macropinocytosis

Fennell, M., Commisso, C., Ramírez, C., Garippa, R. J., & Bar‐Sagi, D. (2015) · Assay and Drug Development Technologies · doi:10.1089/adt.2015.660 · Cited by 12

TOM7 silencing exacerbates focal cerebral ischemia injury in rat by targeting PINK1/Beclin1-mediated autophagy

Ning, J., Tan, J., Chang, M., Wang, Y., Zhang, J., Zhu, J., Zhao, J., & Zhao, Y. (2018) · Behavioural Brain Research · doi:10.1016/j.bbr.2018.11.031 · Cited by 12

The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q

Che, X., Tang, B., Wang, H., Yan, X., Jiang, H. N., Shen, L., Xu, Q., Wang, G., Zhang, H., Wang, C.-Y., et al. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2014.940585 · Cited by 12

Mechanisms of mitophagy: putting the powerhouse into the doghouse

Riley, J. S., & Tait, S. W. G. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0137 · Cited by 13

A method for the detection of virus infectivity in single cells and real time: Towards an automated fluorescence neutralization test

Maistriau, M., Carletti, T., Zakaria, M. K., Braga, L., Faoro, V., Vasileiadis, V., & Marcello, A. (2017) · Virus Research · doi:10.1016/j.virusres.2017.05.004 · Cited by 12

Potential Markers of Autoimmune Diseases, Alleles rs115662534(T) and rs548231435(C), Disrupt the Binding of Transcription Factors STAT1 and EBF1 to the Regulatory Elements of Human CD40 Gene

Putlyaeva, L. V., Демин, Д. Э., Korneev, K. V., Kasyanov, A. S., Tatosyan, K. A., Kulakovskiy, I. V., Kuprash, D. V., & Schwartz, A. M. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918120118 · Cited by 12

Φ-score: A cell-to-cell phenotypic scoring method for sensitive and selective hit discovery in cell-based assays

Guyon, L., Lajaunie, C., Fer, F., Bhajun, R., Sulpice, E., Pinna, G., Campalans, A., Radicella, J. P., Rouillier, P., Mary, M., et al. (2015) · Scientific Reports · doi:10.1038/srep14221 · Cited by 11

Crosstalk between Autophagy and Obesity: Potential Use of Avian Model

Piekarski, A., Greene, E., Anthony, N. B., Bottje, W. G., & Dridi, S. (2015) · Advanced in Food Technology and Nutritional Sciences - Open Journal · doi:10.17140/aftnsoj-1-106 · Cited by 12

Glucocorticoid Receptor Binding Inhibits an Intronic IL33 Enhancer and is Disrupted by rs4742170 (T) Allele Associated with Specific Wheezing Phenotype in Early Childhood

Gorbacheva, A. M., Kuprash, D. V., & Mitkin, N. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123956 · Cited by 11

Maintaining mitochondria in beige adipose tissue

Lü, X. (2019) · Adipocyte · doi:10.1080/21623945.2019.1574194 · Cited by 11

Autophagy and mitophagy as potential therapeutic targets in diabetic heart condition: Harnessing the power of nanotheranostics

Nag, S., Mitra, O., Maturi, B., Kaur, S. P., Saini, A., Nama, M., Roy, S., Samanta, S., Chacko, L., Dutta, R., et al. (2024) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2024.100927 · Cited by 12

Fast and quantitative mitophagy assessment by flow cytometry using the mito-QC reporter

Jiménez‐Loygorri, J. I., Jiménez-García, C., Viedma-Poyatos, Á., & Boya, P. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1460061 · Cited by 10

Elucidation of ubiquitin-conjugating enzymes that interact with RBR-type ubiquitin ligases using a liquid–liquid phase separation–based method

Hayashida, R., Kikuchi, R., Imai, K., Kojima, W., Yamada, T., Iijima, M., Sesaki, H., Tanaka, K., Matsuda, N., & Yamano, K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102822 · Cited by 10

Transcriptome Highlights Cannabinol Modulation of Mitophagy in a Parkinson’s Disease In Vitro Model

Gugliandolo, A., Blando, S., Salamone, S., Pollastro, F., Mazzon, E., & D’Angiolini, S. (2023) · Biomolecules · doi:10.3390/biom13081163 · Cited by 10

Stressful situations: Molecular insights on mitochondrial quality control pathways

Romanelli, S., & Trempe, J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110483 · Cited by 11

Mitochondrial protein TOMM7 alleviates diabetic kidney disease by regulating mitophagy via intracellular redistribution of phospholipase PLA2G6

Wang, Y.-H., Chang, D., Zhao, Y.-Y., Tang, S. C. W., Zhao, M., & Chen, M. (2025) · Kidney International · doi:10.1016/j.kint.2025.10.009 · Cited by 9

Cell Biology of Parkin: Clues to the Development of New Therapeutics for Parkinson’s Disease

Patel, J., Panicker, N., Dawson, V. L., & Dawson, T. M. (2022) · CNS Drugs · doi:10.1007/s40263-022-00973-7 · Cited by 9

Loss of HIPK2 Protects Neurons from Mitochondrial Toxins by Regulating Parkin Protein Turnover

Zhang, J., Shang, Y., Kamiya, S., Kotowski, S. J., Nakamura, K., & Huang, E. J. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2017-19.2019 · Cited by 12

Molecular targets and approaches to restore autophagy and lysosomal capacity in neurodegenerative disorders

Bastien, J., Menon, S., Messa, M., & Nyfeler, B. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101018 · Cited by 9

Carrying Excess Baggage Can Slowdown Life: Protein Clearance Machineries That Go Awry During Aging and the Relevance of Maintaining Them

Sarkar, A., & Nazir, A. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02640-2 · Cited by 10

A Genome-wide Functional Signature Ontology Map and Applications to Natural Product Mechanism of Action Discovery

McMillan, E. A., Kwon, G., Clemenceau, J. R. V., Fisher, K. W., Vaden, R. M., Shaikh, A. F., Neilsen, B. K., Kelly, D., Potts, M. B., Sung, Y.-J., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.07.008 · Cited by 9

Classical and Innovative Evidence for Therapeutic Strategies in Retinal Dysfunctions

Caruso, L., Fields, M., Rimondi, E., Zauli, G., Longo, G., Marcuzzi, A., Previati, M., Gonelli, A., Zauli, E., & Milani, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042124 · Cited by 8

Regulation of Parkin-dependent mitophagy by Bcl-2-associated athanogene (BAG) family members

Kalia, S. K., Kapadia, M., de Snoo, M. L., & Kalia, L. V. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.295330 · Cited by 8

A genome on shaky ground: exploring the impact of mitochondrial DNA integrity on Parkinson’s disease by highlighting the use of cybrid models

Lang, M., Grünewald, A., Pramstaller, P. P., Hicks, A. A., & Pichler, I. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04304-3 · Cited by 8

VEGFR3 MITIGATES HYPERTENSIVE NEPHROPATHY BY ENHANCING MITOPHAGY VIA REGULATING CROTONYLATION OF HSPA1L

Wu, Q., Fu, J., Zhu, B., Meng, W., Ma, J., Lv, Y., Zhao, W., Wang, F., Liu, J., Wang, Y., et al. (2025) · Journal of Hypertension · doi:10.1097/01.hjh.0001197376.28877.a0 · Cited by 9

Genome-wide association study identifies SIAH3 locus influencing the rate of ventricular enlargement in non-demented elders

Li, X., Initiative, O. B. O. A. D. N., Chu, S.-G., Shen, X.-N., Hou, X.-H., Xu, W., Ou, Y.-N., Dong, Q., Tan, L., & Yu, J.-T. (2019) · Aging · doi:10.18632/aging.102435 · Cited by 7

The role of mitophagy in female reproductive system diseases: from molecular mechanisms to therapeutic strategies

Zhao, H., Wang, Y., Han, H., Jiang, Y., Ji, X., & Zhang, Y. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1645711 · Cited by 7

Recent insights into HSP70: proteostasis and beyond

Pustovaya, K., Venediktov, A. A., Soldatov, V. O., Александрович, К. Е., Pokidova, K., Gartzeva, V. A., Payushina, O. V., Tsytsarev, V., Meglinski, I. V., & Piavchenko, G. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1791536 · Cited by 7

Mitochondrial Dysfunction-Molecular Mechanisms and Potential Treatment approaches of Hepatocellular Carcinoma

Zeng, L., Zhu, L., Fu, S., Li, Y., & Hu, K. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05144-4 · Cited by 10

Parkinson’s Disease: Insights from Drosophila Model

Ayajuddin, M., Das, A., Phom, L., Modi, P., Chaurasia, R., Koza, Z., Thepa, A., Jamir, N., Singh, P. R., Longkumer, S., et al. (2018) · InTech eBooks · doi:10.5772/intechopen.72021 · Cited by 7

Reconstructing regulatory pathways by systematically mapping protein localization interdependency networksPreprint

Dodgson, J., Chessel, A., Vaggi, F., Giordan, M., Yamamoto, M. L., Arai, K., Madrid, M., Geymonat, M., Abenza, J. F., Cansado, J., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/116749 · Cited by 7

miRNA family miR-29 inhibits PINK1-PRKN dependent mitophagy via ATG9APreprint

Markham, B. N., Ramnarine, C., Kim, S., Grever, W. E., Soto‐Beasley, A. I., Heckman, M. G., Ren, Y., Osborne, A. C., Bhagwate, A. V., Liu, Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.17.576122 · Cited by 7

From Diabetes to Dementia: Identifying Key Genes in the Progression of Cognitive Impairment

Cao, Z., Du, Y., Xu, G., Zhu, H., Ma, Y., Wang, Z., Wang, S., & Lu, Y. (2024) · Brain Sciences · doi:10.3390/brainsci14101035 · Cited by 7

3D-Suspension culture platform for high throughput screening of neurotoxic chemicals using LUHMES dopaminergic neurons

Tong, Z., Huang, R., Braisted, J. C., Chu, P., Simeonov, A. M., & Gerhold, D. L. (2024) · SLAS DISCOVERY · doi:10.1016/j.slasd.2024.01.004 · Cited by 6

A gender geography of intentional homicide within and outside of the family: Male and female murders in Europe, the US and Canada (2003–15)

Minello, A., & Dalla‐Zuanna, G. (2019) · European Journal of Criminology · doi:10.1177/1477370819884251 · Cited by 6

Regulation of IL33 Gene Expression by SP1 and Foxa1 in Breast and Lung Cancer Cells

Gorbacheva, A. M., Kuprash, D. V., & Mitkin, N. A. (2021) · Molecular Biology · doi:10.1134/s0026893321010064 · Cited by 6

Use of Chemical Genomics to Investigate the Mechanism of Action for Inhibitory Bioactive Natural Compounds

Burnside, D. J., Moteshareie, H., Márquez, I. G., Hooshyar, M., Samanfar, B., Shostak, K., Omidi, K., Peery, H. E., Smith, M. L., & Golshani, A. (2014) · Wiley eBooks · doi:10.1002/9783527684403.ch2 · Cited by 6

Chaperone client proteins evolve slower than non-client proteins

Victor, M. P., Acharya, D., Chakraborty, S., & Ghosh, T. C. (2020) · Functional & Integrative Genomics · doi:10.1007/s10142-020-00740-1 · Cited by 5

Relative Efficiency of Transcription Factor Binding to Allelic Variants of Regulatory Regions of Human Genes in Immunoprecipitation and Real-Time PCR

Mitkin, N. A., Korneev, K. V., Gorbacheva, A. M., & Kuprash, D. V. (2019) · Molecular Biology · doi:10.1134/s0026893319030117 · Cited by 5

High-Content Functional Genomic Screening to Identify Novel Regulators of the PINK1–Parkin Pathway

Ng, A. C., Baird, S. D., & Screaton, R. A. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00001-1 · Cited by 5

Cellular Imaging in Drug Discovery: Imaging and Informatics for Complex Cell Biology

Li, Z., Cvijic, M. E., & Zhang, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12328-5 · Cited by 5

A long-lived pool of PINK1 imparts a molecular memory of depolarisation-induced activityPreprint

Pollock, L., Georgiou, I. C., Rusilowicz-Jones, E. V., Clague, M. J., & Urbé, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.03.601901 · Cited by 5

Vexed mutations promote degeneration of dopaminergic neurons through excessive activation of the innate immune response

Davis, J., Kolaski, E., & Babcock, D. T. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00417-5 · Cited by 5

Genome-Wide RNAi Screen Identifies Regulators of Cardiomyocyte Necrosis

Cheng, Z., Combs, M., Zhu, Q., Xia, P., Opheim, Z., Parker, J. S., Mack, C. P., & Taylor, J. M. (2019) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.9b00052 · Cited by 5

ZetaSuite: computational analysis of two-dimensional high-throughput data from multi-target screens and single-cell transcriptomics

Hao, Y., Zhang, S., Shao, C., Li, J., Zhao, G., Zhang, D., & Fu, X. (2022) · Genome biology · doi:10.1186/s13059-022-02729-4 · Cited by 4

Inhibition of PTEN-induced kinase 1 autophosphorylation may assist in preventing epileptogenesis induced by pentylenetetrazol

Cui, Y., Zhai, Y., Yuan, Y., Wang, X., Xu, Q., Xu, L., Xu, L., Ren, T., Wang, Q., & Sun, H. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105644 · Cited by 4

Mitochondrial dysfunction in breast cancer

Germain, D., Papa, L., Kenny, T. C., Takabatake, Y., & Riar, A. K. (2015) · Research and Reports in Biology · doi:10.2147/rrb.s62507 · Cited by 4

A long-lived pool of PINK1 imparts a molecular memory of depolarization-induced activity

Pollock, L., Georgiou, I. C., Rusilowicz-Jones, E. V., Clague, M. J., & Urbé, S. (2025) · Science Advances · doi:10.1126/sciadv.adr1938 · Cited by 8

Food-derived bioactive compounds targeting mitophagy: Emerging nutritional strategies against sarcopenia

Zhang, H., Zhang, L., Liu, D., Ye, X., & Chen, S. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105314 · Cited by 4

The Metabolic Role of Mitochondria in the Perinatal Cardiac Development and Cardiovascular Diseases

Li, M., Zhang, R., Li, X., & Huang, H. (2026) · Exploration · doi:10.1002/exp.20240414 · Cited by 3

Mitophagy

Sica, V., Izzo, V., Pedro, J. M. B., Zamzami, N., & Maiuri, M. C. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802936-7.00003-9 · Cited by 4

Efficient Cloning and Sequence Validation of Repetitive and High GC-Content Short Hairpin RNAs

Chilamkurthy, R., White, A. A., Pater, A. A., Jensik, P. J., & Gagnon, K. T. (2022) · Human Gene Therapy · doi:10.1089/hum.2021.273 · Cited by 3

Ectopic BH3-Only Protein Bim Associates with Hsp70 to Regulate Yeast Mitophagy

Yuan, L., Wang, Y., Margulis, B. A., Song, T., Wang, Z., & Zhang, Z. (2023) · Doklady Biochemistry and Biophysics · doi:10.1134/s1607672923700485 · Cited by 3

SIAH3 is frequently epigenetically silenced in cancer and regulates mitochondrial metabolism

Deutschmeyer, V. E., Schlaudraff, N. A., Walesch, S. K., Moyer, J., Sokòl, A. M., Graumann, J., Meißner, W., Schneider, M. A., Muley, T., Helmbold, P., et al. (2024) · International Journal of Cancer · doi:10.1002/ijc.35202 · Cited by 3

Potential association between TSGA13 variants and risk of total colonic aganglionosis in Hirschsprung disease

Jung, S., Namgoong, S., Seo, J.-M., Kim, D. Y., Oh, J.-T., Kim, H., & Kim, J. (2019) · Gene · doi:10.1016/j.gene.2019.06.007 · Cited by 3

AxGxE

Burke, C., Trinh, K., Nadar, V., & Sanyal, S. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.007 · Cited by 3

Mitochondrial Genomics and Targeted Toxicities

Copeland, W. C., & Wallace, K. B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.64219-8 · Cited by 3

Mitophagy

King, L., & Plun‐Favreau, H. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00005-5 · Cited by 6

Transcriptome-wide association study identifies novel susceptibility genes contributing to hearing impairmentPreprint

Xie, C., Niu, Y., Ping, J., Zhang, Q. Y., Zhang, Z., Wang, Y., Yang, C., Zhou, G., & Li, Y. (2021) · Research Square · doi:10.21203/rs.3.rs-465737/v1 · Cited by 3

Targeting TOMM40 and TOMM22 to Rescue Statin-Impaired Mitochondrial Function, Dynamics, and Mitophagy in Skeletal Myotubes

Yang, N. V., Rogers, S. W., Guerra, R. M., Chao, J. Y., Pagliarini, D. J., Theusch, E., & Krauss, R. M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210977 · Cited by 2

Multi-omics Mendelian randomization and machine learning identify candidate therapeutic targets for Alzheimer’s and Parkinson’s diseases

Li, X., Zhang, L., Xia, J., Zheng, M., Zhou, Z., & Cai, J. (2026) · Mammalian Genome · doi:10.1007/s00335-025-10191-3 · Cited by 2

Mastering cardiomyocyte mitophagy: molecular governance, pathological derailment and therapeutics

Liu, P., Wu, H., Ren, H., Wang, J., & Yang, F. (2026) · PeerJ · doi:10.7717/peerj.20700 · Cited by 2

Awakening endogenous repair: salidroside boosts mitophagy in NPMSCs via SIRT1/FOXO3 to combat intervertebral disc degeneration

Li, Z., Wu, Y., Hua, B., Sun, H., 武火峰, Zai, S., Liu, C., Zhang, Y., Li, Z., You, X., et al. (2026) · Stem Cell Research & Therapy · doi:10.1186/s13287-026-05051-z · Cited by 2

Genome-wide CRISPR screen for PARKIN regulators reveals transcriptional repression as a determinant of mitophagy

Potting, C., Crochemore, C., Moretti, F., Nigsch, F., Schmidt, I., Manneville, C., Carbone, W., Knehr, J., DeJesus, R., Lindeman, A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711023115 · Cited by 93

High-Content Functional Genomic Screening to Identify Novel Regulators of the PINK1–Parkin Pathway

Ng, A. C., Baird, S. D., & Screaton, R. A. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00001-1 · Cited by 5

Identification of Novel Parkinson’s Disease Genes Involved in Parkin Mediated Mitophagy

Lefebvre, V. (2013) · uO Research (University of Ottawa) · doi:10.20381/ruor-3402

Mitophagy Controlled by the PINK1-Parkin Pathway Is Associated with Parkinson’s Disease Pathogenesis

Imai, Y., & Hattori, N. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405528-5.00015-8 · Cited by 2

The function of PINK1 and parkin in mitochondrial quality control (234.2)

Fon, E. A. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.234.2