The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Parkin Interacts with Ambra1 to Induce Mitophagy
Open accessAbstract
Mutations in the gene encoding Parkin are a major cause of recessive Parkinson's disease. Recent work has shown that Parkin translocates from the cytosol to depolarized mitochondria and induces their autophagic removal (mitophagy). However, the molecular mechanisms underlying Parkin-mediated mitophagy are poorly understood. Here, we investigated whether Parkin interacts with autophagy-regulating proteins. We purified Parkin and associated proteins from HEK293 cells using tandem affinity purification and identified the Parkin interactors using mass spectrometry. We identified the autophagy-promoting protein Ambra1 (activating molecule in Beclin1-regulated autophagy) as a Parkin interactor. Ambra1 activates autophagy in the CNS by stimulating the activity of the class III phosphatidylinositol 3-kinase (PI3K) complex that is essential for the formation of new phagophores. We found Ambra1, like Parkin, to be widely expressed in adult mouse brain, including midbrain dopaminergic neurons. Endogenous Parkin and Ambra1 coimmunoprecipitated from HEK293 cells, SH-SY5Y cells, and adult mouse brain. We found no evidence for ubiquitination of Ambra1 by Parkin. The interaction of endogenous Parkin and Ambra1 strongly increased during prolonged mitochondrial depolarization. Ambra1 was not required for Parkin translocation to depolarized mitochondria but was critically important for subsequent mitochondrial clearance. In particular, Ambra1 was recruited to perinuclear clusters of depolarized mitochondria and activated class III PI3K in their immediate vicinity. These data identify interaction of Parkin with Ambra1 as a key mechanism for induction of the final clearance step of Parkin-mediated mitophagy.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Although the role of ATG4A in mitophagy is unclear, AMBRA1 and ATG12 positively regulate mitophagy [56–58].”
From miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1) (2016) · cites this paper as [56]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
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
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
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
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · cited 2×
“Because Parkin is an E3 ubiquitin ligase (Shimura et al., 2000), we asked whether Ambra1 might be a substrate for Parkinmediated ubiquitination.”
BackgroundMatsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705
Network organization of the human autophagy system
Behrends, C., Sowa, M. E., Gygi, S. P., & Harper, J. W. (2010) · Nature · doi:10.1038/nature09204 · Cited by 1,554
Research works printed but not linked: 1
- Hailey DW, Rambold AS, Satpute-Krishnan P, Mitra K, Sougrat R, Kim PK, Lippincott-Schwartz J (2010) Mitochondria supply membranes for au- tophagosome biogenesis during starvation. Cell 141:656 -667.
Cited by
Sorted by citations
Items 201–260 of 260
AMBRA1 phosphorylation by CDK1 and PLK1 regulates mitotic spindle orientation
Faienza, F., Polverino, F., Rajendraprasad, G., Milletti, G., Hu, Z.-H., Colella, B., Gargano, D., Strappazzon, F., Rizza, S., Vistesen, M., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04878-6 · Cited by 11
Baek, S.-H., & Jang, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222112079 · Cited by 11
“AMBRA1 is involved in the induction of autophagy via interactions with ULK1 [3] and elongin B [4] and in the induction of mitophagy via interactions with PARKIN [5] and LC3 [6].”
BackgroundLijie, G., Yueyue, Z., Zhu, N., Ling, W., Xuan, W., & Weijie, Y. (2019) · Cell Biology International · doi:10.1002/cbin.11097 · Cited by 12
Demine, S., Michel, S., Vannuvel, K., Wanet, A., Renard, P., & Arnould, T. (2012) · Cells · doi:10.3390/cells1020168 · Cited by 11
“Interestingly, it has also been shown that Ambra1 is recruited to perinuclear depolarized mitochondria, interacts with endogenous Parkin and is critical for clearance of damaged organelles after prolonged mitochondrial depolarization [79].”
BackgroundAkatsuka, H., Kuga, S., Masuhara, K., Davaadorj, O., Okada, C., Iida, Y., Okada, Y., Fukunishi, N., Suzuki, T., Hosomichi, K., et al. (2017) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2017.08.019 · Cited by 9
“, AMBRA1 is involve ATG7-independent pathway, Biochemical and Biophysical Research Com Since Ambra1 is reported to be involved in “mitophagy” [15,16,31], it is assumed that Ambra1-deficiency resulted in perturbed mitochondrial homeostasis, leading to diminished MitoTracker staining.”
BackgroundMechanisms 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
Mitophagy in gynecological malignancies: roles, advances, and therapeutic potential
Wang, J., & Wang, D. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02259-x · Cited by 9
“Among them, the pro-autophagic molecule AMBRA1 has been de fi ned as a regulator of mitophagy in both canonical PINK1/Parkin-dependent and -inde- pendent systems [59 – 62].”
Ma, L., Li, J., Zhang, X., Zhang, W., Chen, J., Yang, B. W., & Yang, H. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1360179 · Cited by 7
Molecular Biology Digest of Cell Mitophagy
Matić, I., Strobbe, D., Guglielmo, F. D., & Campanella, M. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2016.12.003 · Cited by 7
The Intersection of Mitophagy and Autism Spectrum Disorder: A Systematic Review
Kovacheva, E., Gevezova, M., Mehterov, N. H., Kazakova, M., & Sarafian, V. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052217 · Cited by 8
“AMBRA1 deficiency severely disrupts neuronal mitophagy [89].”
Selective autophagy: a therapeutic target for healthy aging?
Manastireanu, D. M., Salazar, N. A., Bejarano, E., & Nieto-Torres, J. L. (2024) · Aging advances. · doi:10.4103/agingadv.agingadv-d-24-00002 · Cited by 10
García‐Prat, L., Martínez‐Vicente, M., & Muñoz‐Cánoves, P. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3810-0_16 · Cited by 9
Mitochondrial dynamics, biogenesis, mitophagy and oxidative stress in gestational obesity: A review
Rodríguez-Córdoba, K. M., Agreda-Soto, S., Garzón, J. A. C., & Pustovrh, M. C. (2024) · Endocrine and Metabolic Science · doi:10.1016/j.endmts.2024.100205 · Cited by 7
Zhang, J., Yan, H., Wang, Y., Yue, X., Wang, M., Liu, L., Qiao, P., Zhu, Y., & Li, Z. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05096-9 · Cited by 7
“Recent studies have elucidated that both PINK1 and Parkin have the direct interaction with PI3K and Beclin-1 [61].”
Targeting mitophagy for neurological disorders treatment: advances in drugs and non-drug approaches
Yang, X., Zhang, Y., Luo, J.-X., Zhu, T., Zhao, R., Mu, B., & Lu, M. (2023) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-023-02636-w · Cited by 9
“Additionally, other studies have identified a number of mitophagy receptors that respond to different stressors, including BCL2L13, DISC1, MCL1, AMBRA1, FKBP8, ATAD3B, and SPATA3 (Cen et al. 2021; Otsu et al. 2015; Shu et al. 2021; Van Humbeeck et al. 2011; Wang et al. 2019; Xu et al. n.d.).”
BackgroundMitophagy could fight Parkinson’s disease through antioxidant action
Rita, A. D., & Strappazzon, F. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0095 · Cited by 7
Mueller, S., Bialas, J., Ryu, S., Catone, N., & Aichem, A. (2023) · PLoS ONE · doi:10.1371/journal.pone.0290002 · Cited by 5
Liu, F., Koepp, D. M., & Walters, K. J. (2015) · Scientific Reports · doi:10.1038/srep12088 · Cited by 5
Rasmussen, L. K., Moreira, D. G., Okarmus, J., Simonsen, A., & Meyer, M. (2026) · Autophagy · doi:10.1080/15548627.2026.2711596 · Cited by 4
Hara, E., Ohshima, K., Takimoto, M., Bai, Y., Hirata, M., Zeng, W., Uomoto, S., Todoroki, M., Kobayashi, M., Kozono, T., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062709 · Cited by 5
“In the Parkin-dependent mitophagy, activated Parkin interacts with AMBRA1 expressed on the outer mitochondrial membrane, which, in turn, promotes mitophagy by activating the class III phosphatidylinositol 3-kinase (PI3K) complex, an essential contributor to autophagosome formation [15,16].”
The Role and Mechanism of Ambra1-Mediated Mitophagy in TDCPP-Exposed Mouse Hippocampal Neurons
Zhang, X., Lin, C., Hu, H., Zhao, W., Li, G., Xia, Y., & Chen, N. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04160-6 · Cited by 4
King, L., & Plun‐Favreau, H. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803783-6.00005-5 · Cited by 6
Mitophagy in breast cancer: Regulatory mechanisms and therapeutic potential
Chang, Y., Zhou, Y., Yang, L., Gao, L., Zhang, Y., Feng, M., Shen, M., Wei, B., Bu, H., & Zhang, Z. (2025) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003949 · Cited by 2
Mitophagy in kidney transplantation ischemia–reperfusion injury
Wang, X., Li, R., Zhu, B., Zhu, X., & Lou, B. (2025) · International Urology and Nephrology · doi:10.1007/s11255-025-04761-2 · Cited by 3
“During mitochondrial depolarization, AMBRA1 is rapidly recruited to the outer mitochondrial membrane, where it interacts with the ATAD3A complex to stabilize PINK1, thereby promoting Parkin-dependent mitophagy [86, 87].”
Vieira, J., Barros, M., López-Fernández, H., Glez‐Peña, D., Nogueira-Rodríguez, A., & Vieira, C. P. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031325 · Cited by 5
Zhong, K., Du, X., Niu, Y., Li, Z., Tao, Y., Wu, Y., Zhang, R., Guo, L., Bi, Y., Tang, L., et al. (2024) · Frontiers in Medicine · doi:10.3389/fmed.2024.1491009 · Cited by 2
Nedelsky, N. B., Kuballa, P., Castoreno, A. B., & Xavier, R. J. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8256-7_12 · Cited by 1
“In addition, activating molecule in beclin 1-regulated autophagy (Ambra1), an autophagy-regulating protein initially identifi ed in neuronal cells [ 84 ] , is recruited to damaged mitochondria in a Parkin1-dependent fashion [ 85 ] and knockdown of Ambra1 expression results in impairment of mitophagy.”
BackgroundMitochondrial Proteins in the Development of Parkinson’s Disease
Zilocchi, M., Fasano, M., & Alberio, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8367-0_2 · Cited by 5
Targeting mitophagy for neuroprotection: mechanisms and therapeutic opportunities
Yang, J., Li, J., Hou, X., Zheng, Y., Zhao, Z., Zhou, T., Jing, T., Kong, J., Zhang, G., & Guo, Y. (2026) · npj Aging · doi:10.1038/s41514-026-00424-3 · Cited by 3
“These fi ndings support the concept that targeting AMBRA1-mediated mitophagy could be a promising therapeutic approach 148,149 .”
Dai, Y., Li, F., Tang, Y., Sun, L.-L., Liu, Y.-P., Zhan, J., Zhou, C.-Y., & Li, A. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119997 · Cited by 2
Functional Role of Hepatitis C Virus NS5A in the Regulation of Autophagy
Ke, P., & Yeh, C. (2024) · Pathogens · doi:10.3390/pathogens13110980 · Cited by 3
Tang, Y., Zhu, B.-Y., Shi, J., Liu, Q.-H., Chen, L.-H., Peng, Q.-H., Peng, J., & Yao, X.-L. (2022) · Digital Chinese Medicine · doi:10.1016/j.dcmed.2022.10.006 · Cited by 2
Phosphorylation Events in Selective Mitophagy: Possible Biochemical Markers?
Zhang, W., Wu, H., Liu, L., Zhu, Y., & Chen, Q. (2013) · Current Pathobiology Reports · doi:10.1007/s40139-013-0033-8 · Cited by 2
Control of Autophagy in Parkinson’s Disease
González‐Polo, R. A., Gómez‐Sánchez, R., Pizarro‐Estrella, E., Yakhine-Diop, S. M. S., Rodríguez‐Arribas, M., & Fuentes, J. M. (2015) · Current topics in neurotoxicity · doi:10.1007/978-3-319-13939-5_6 · Cited by 1
Coomar, S., Gasser, J. A., Slabicki, M. M., Donovan, K. A., Fischer, E. S., Ebert, B. L., Gillingham, D. G., & Thomä, N. H. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00054h · Cited by 1
Nedelsky, N. B., Kuballa, P., Castoreno, A. B., & Xavier, R. J. (2019) · Springer eBooks · doi:10.1007/978-3-030-28703-0_14 · Cited by 3
“In addition, activating molecule in Beclin 1-regulated autophagy (Ambra1), an autophagy-regulating protein initially identified in neuronal cells [84], is recruited to damaged mitochondria in a Parkin1-dependent fashion [85] and knockdown of Ambra1 expression results in impairment of mitophagy.”
BackgroundMitochondrial Biology in Hepatobiliary Tumors: Changes of the Cellular Energy Factory
Zimmermann, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-26587-2_171-1 · Cited by 1
Mitochondrial Dynamics, Mitophagy and Mitochondrial Spheroids in Drug-Induced Liver Injury
Williams, J. A., Ni, H.-M., & Ding, W.-X. (2015) · doi:10.1201/b19420-13 · Cited by 1
Wang, S.-H. (2012) · doi:10.17077/etd.bbjshj2n · Cited by 1
“Parkin then interacts with Ambra1, and a class III PI3K is activated in a compartmentalized manner [132].”
Mitophagy in neuronal health and disease: from mechanisms to neurodegeneration
Basak, B., Riley, J. F., Nataraj, N. M., & Holzbaur, E. L. F. (2026) · Journal of Clinical Investigation · doi:10.1172/jci199847 · Cited by 1
“Upon mitochondrial insult, AMBRA1 localizes around juxtanuclear clusters of the damaged organelles, where it stimulates phagophore formation by activating class III PI3K (42).”
Suri, P., Daartey, A. B., Khan, D. M. I. O., Rayana, N. P., Chilamakuri, R., Godugu, D., Azad, M. G., Reeb, K. L., & Richardson, D. R. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100158
Liu, Z., Zhang, S., & Zeng, T. (2026) · Inflammation · doi:10.1007/s10753-026-02548-w · Cited by 1
“Following mitochondrial damage, it also locally acti - vates the class III Phosphoinositide 3-kinase(PI3K) complex to facilitate autophagosome formation and expansion [61 ].”
Zou, X., Zhang, T., Wang, N., Li, Y., Jiang, X., & zhong, X. (2026) · Biomolecules · doi:10.3390/biom16070941
“AMBRA1 functions both as a regulator of autophagy and as a mitophagy receptor [150].”
Mechanisms and Therapeutic Potential of Targeting Mitophagy in Neurodegenerative Diseases
Wang, Y.-N., Wang, X., Huang, Q., Yang, Y., Wang, T., Qu, X.-H., & Han, X. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06104-3
Ploumi, C., & Palikaras, K. (2025) · Brain Organoid and Systems Neuroscience Journal · doi:10.1016/j.bosn.2025.06.001
Chowdhury, R. M. (2022) · National Journal of Maxillofacial Surgery · doi:10.4103/njms.njms_123_20
“where it interacts with Beclin1 protein causing activation of Parkin independently of PINK.[20,21] According to other data,”
BackgroundResultHaddad, D., & Verstreken, P. (2016) · Wiley eBooks · doi:10.1002/9781118978320.ch4 · Cited by 1
Mitochondria in Parkinson's Disease
Arena, G., & Valente, E. M. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch16
Bertolin, G. (2013) · theses.fr (ABES) · doi:10.70675/85cf9b94z9680z40bfzaabezd31446437e10
“This program relies, in the end, on the fusion between autophagosomes and lysosomes, and pharmacological treatments blocking this step, as for example bafilomycin A1 (which dissipates the acidic pH of lysosomes) or 3-methyladenine (which inhibits the formation of autophagosomes), were shown to abolish PINK1/Parkin-dep…”
BackgroundAdvances in Relationship Between Class Ⅲ PI3K Complex and Autophagy*
Wu, P., & Xu, C. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00387
Prospective Advances in Exercise-Induced Autophagy on Health
Liang, J., Kirberger, M., & Chen, N. (2021) · Springer eBooks · doi:10.1007/978-981-16-4525-9_11
Parkin Protein: The Missing Link Between Cardiovascular and Parkinson’s Disease
Bagchi, A. (2019) · Modulation of Oxidative Stress in Heart Disease · doi:10.1007/978-981-13-8946-7_20
The Evolving Concept of Mitochondrial Dynamics in Heart: Interventional Opportunities
Ashok, S., Ganjoo, M., Panicker, V. T., Pillai, V. V., & Gopala, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-8946-7_25
AMBRA1-Mediated Regulation of C-MYC and Its Relevance to Cancer
Cianfanelli, V., & Cecconi, F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-812146-7.00018-4
Necrobiology of Liver Cancer: Autophagy and Cellular Senescence
Zimmermann, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-26587-2_179-1
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
Mount, M. P. (2015) · uO Research (University of Ottawa) · doi:10.20381/ruor-2755
“PINK1 is believed to recruit Parkin to damaged mitochondria, where Parkin can target these defective organelles for a specific degradation by autophagy, a process termed mitophagy (McBride, 2008; Geisler et al., 2010; Narendra et al., 2010; Sha:2010bv Van Humbeeck et al., 2011).”
BackgroundThe Role of Parkin and PINK1 in Mitochondrial Quality Control
Tang, M. Y., & Durcan, T. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801032-7.00018-6
Aging, Nutrition and Lifestyle
Wohlgemuth, S. E. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-385101-7.00012-7
Metadata
- Authors
- Van Humbeeck, C., Cornelissen, T., Hofkens, H., Mandemakers, W., Gevaert, K., De Strooper, B., & Vandenberghe, W.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Universitair Ziekenhuis Leuven (BE)
- Corresponding author
- Vandenberghe, W.
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2011-07-13
- Volume
- 31
- Issue
- 28
- Pages
- 10249-10261
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6623066
- OpenAlex
- W2069519643
- Cited by
- 287
- References
- 0
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 23 · 2023: 15 · 2022: 11 · 2021: 22 · 2020: 19 · 2019: 20 · 2018: 11 · 2017: 21 · 2016: 22 · 2015: 33 · 2014: 26 · 2013: 21 · 2012: 22
- FWCI
- 16.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- UCL Discovery (University College London) (submittedVersion)
- Lirias (KU Leuven) (submittedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- Funders
- Fonds Wetenschappelijk Onderzoek
- KU Leuven (P6/28)
- Universiteit Gent
- Vlaamse regering
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- Parkin, AMBRA1, mitophagy, Parkinson's disease, mitochondrial depolarization, class III PI3K, Beclin-1, autophagy, dopaminergic neurons, protein-protein interaction, mitochondrial clearance, ubiquitination
- MeSH terms
- Animals, Autophagy, Brain, Cells, Cultured, Humans, Mitochondria, Neurons, Ubiquitin-Protein Ligases, Adaptor Proteins, Signal Transducing, Mice, Ubiquitination, HEK293 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
