Parkin is dispensable for mitochondrial function, but its ubiquitin ligase activity is critical for macroautophagy and neurotransmitters: therapeutic potential beyond Parkinson's disease

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

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Autophagy fights disease through cellular self-digestion

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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

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

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Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations

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The Beclin 1 network regulates autophagy and apoptosis

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Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

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PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy

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PINK1-dependent recruitment of Parkin to mitochondria in mitophagy

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Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

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Ubiquitin is phosphorylated by PINK1 to activate parkin

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Association between Early-Onset Parkinson's Disease and Mutations in theParkinGene

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PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

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Cargo recognition and trafficking in selective autophagy

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100 years of Lewy pathology

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The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice.

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Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1–phosphatidylinositol-3-kinase complex

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Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with <i>SOD1</i> mutations

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Parkin functions as an E2-dependent ubiquitin– protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

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The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy

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Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

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Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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Parkin Suppresses Unfolded Protein Stress-induced Cell Death through Its E3 Ubiquitin-protein Ligase Activity

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Nilotinib (formerly AMN107), a highly selective BCR-ABL tyrosine kinase inhibitor, is effective in patients with Philadelphia chromosome–positive chronic myelogenous leukemia in chronic phase following imatinib resistance and intolerance

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Divergent roles of ALS-linked proteins FUS/TLS and TDP-43 intersect in processing long pre-mRNAs

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c‐Jun regulates cell cycle progression and apoptosis by distinct mechanisms

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The Beclin 1 interactome

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

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Beclin 1 Gene Transfer Activates Autophagy and Ameliorates the Neurodegenerative Pathology in α-Synuclein Models of Parkinson's and Lewy Body Diseases

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UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids

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Imatinib for Newly Diagnosed Patients With Chronic Myeloid Leukemia: Incidence of Sustained Responses in an Intention-to-Treat Analysis

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Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation

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Huntingtin Expression Stimulates Endosomal–Lysosomal Activity, Endosome Tubulation, and Autophagy

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Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin

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The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo

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Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases

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Somatic mutations of the Parkinson's disease–associated gene PARK2 in glioblastoma and other human malignancies

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Parkin and PINK1: much more than mitophagy

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The role of parkin in familial and sporadic Parkinson's disease

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USP8 regulates mitophagy by removing K6‐linked ubiquitin conjugates from parkin

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Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases

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Neurodegenerative lysosomal disorders: A continuum from development to late age

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Emerging trends in the epidemiology of melanoma

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Autoregulation of Parkin activity through its ubiquitin‐like domain

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The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy

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Structure of the human Parkin ligase domain in an autoinhibited state

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TDP-43 in the Ubiquitin Pathology of Frontotemporal Dementia With VCP Gene Mutations

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Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of α-synuclein in Parkinson's disease models.

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Isolation and characterization of a human p53 cDNA clone: expression of the human p53 gene.

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Molecular pathogenesis of Parkinson disease: insights from genetic studies

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Parkin Interacts with Ambra1 to Induce Mitophagy

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Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function

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PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding

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VCP Is Essential for Mitochondrial Quality Control by PINK1/Parkin and this Function Is Impaired by VCP Mutations

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PARK2 deletions occur frequently in sporadic colorectal cancer and accelerate adenoma development in Apc mutant mice

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Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin–protein ligase with monoubiquitylation capacity

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Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin

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c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease

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Parkin as a tumor suppressor gene for hepatocellular carcinoma

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The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI

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Novel regulation of parkin function through c-Abl-mediated tyrosine phosphorylation: implications for Parkinson’s disease

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Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease

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Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation

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Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function

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Emerging Potential of Therapeutic Targeting of Ubiquitin-Specific Proteases in the Treatment of Cancer

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TDP-43 Proteinopathy in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

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Parkin-mediated K63-linked polyubiquitination: A signal for targeting misfolded proteins to the aggresome-autophagy pathway

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Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated A in AD models

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Point Mutations (Thr240Arg and Ala311Stop) in theParkinGene

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Parkinson's disease: insights from pathways

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Selective escape of proteins from the mitochondria during mitophagy

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Proteomic analysis of parkin knockout mice: alterations in energy metabolism, protein handling and synaptic function

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Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance

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The Machado–Joseph disease-associated mutant form of ataxin-3 regulates parkin ubiquitination and stability

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A molecular explanation for the recessive nature of parkin-linked Parkinson’s disease

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Tyrosine kinase inhibition increases functional parkin‐Beclin‐1 interaction and enhances amyloid clearance and cognitive performance

Lonskaya, I., Hebron, M. L., Desforges, N. M., Franjie, A., & Moussa, C. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302771 · Cited by 139 · see citing works

Parkin Ubiquitinates Tar-DNA Binding Protein-43 (TDP-43) and Promotes Its Cytosolic Accumulation via Interaction with Histone Deacetylase 6 (HDAC6)

Hebron, M. L., Lonskaya, I., Sharpe, K., Weerasinghe, P. P. K., Algarzae, N. K., Shekoyan, A. R., & Moussa, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419945 · Cited by 138 · see citing works

Pruning and loss of excitatory synapses by the parkin ubiquitin ligase

Helton, T. D., Otsuka, T., Lee, M.-C., Mu, Y., & Ehlers, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802280105 · Cited by 127 · see citing works

Autophagy in neurodegeneration and development

Winslow, A. R., & Rubinsztein, D. C. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.06.010 · Cited by 126 · see citing works

Parkin Enhances the Expression of Cyclin-dependent Kinase 6 and Negatively Regulates the Proliferation of Breast Cancer Cells*

Tay, S.-P., Yeo, C. W. S., Chai, C., Chua, P., Tan, H.-M., Ang, A. X. Y., Yip, D. L. H., Sung, J.-X., Tan, P. H., Bay, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.108241 · Cited by 114 · see citing works

Induction of autophagy in neurite degeneration of mouse superior cervical ganglion neurons

Yang, Y., Fukui, K., Koike, T., & Zheng, X. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05914.x · Cited by 109 · see citing works

Parkin mutations reduce the complexity of neuronal processes in iPSC-derived human neurons

Ren, Y., Jiang, H., Hu, Z., Fan, K., Wang, J., Janoschka, S., Wang, X., Ge, S., & Feng, J. (2015) · Stem Cells · doi:10.1002/stem.1854 · Cited by 109 · see citing works

Pathogenic mutations inactivate parkin by distinct mechanisms

Henn, I. H., Gostner, J. M., Lackner, P., Tatzelt, J., & Winklhofer, K. F. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02854.x · Cited by 108 · see citing works

Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin

Caulfield, T. R., Fiesel, F. C., Moussaud-Lamodière, E. L., Dourado, D. F. A. R., Flores, S. C., & Springer, W. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003935 · Cited by 108 · see citing works

PINK 1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease

Kazlauskaite, A., & Muqit, M. M. K. (2014) · FEBS Journal · doi:10.1111/febs.13127 · Cited by 106 · see citing works

PINK1 Triggers Autocatalytic Activation of Parkin to Specify Cell Fate Decisions

Zhang, C., Lee, S., Peng, Y., Bunker, E. N., Giaime, E., Shen, J., Zhou, Z., & Liu, X. (2014) · Current Biology · doi:10.1016/j.cub.2014.07.014 · Cited by 101 · see citing works

Parkin promotes intracellular A 1-42 clearance

Burns, M. P., Zhang, L., Rebeck, G. W., Querfurth, H. W., & Moussa, C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp258 · Cited by 98 · see citing works

Parkin Pathway Activation Mitigates Glioma Cell Proliferation and Predicts Patient Survival

Yeo, C. W. S., Ng, F., Chai, C., Tan, J. M. M., Koh, G. R. H., Chong, Y. K., Koh, L., Foong, C. S. F., Sandanaraj, E., Holbrook, J. D., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3060 · Cited by 97 · see citing works

Parkin reverses intracellular β‐amyloid accumulation and its negative effects on proteasome function

Rosen, K. M., Moussa, C., Lee, H., Kumar, P., Kitada, T., Qin, G., Fu, Q., & Querfurth, H. W. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22178 · Cited by 95 · see citing works

Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism

Zheng, X., & Hunter, T. R. (2013) · Cell Research · doi:10.1038/cr.2013.66 · Cited by 94 · see citing works

Diminished Parkin Solubility and Co-Localization with Intraneuronal Amyloid-β are Associated with Autophagic Defects in Alzheimer's Disease

Lonskaya, I., Shekoyan, A. R., Hebron, M. L., Desforges, N. M., Algarzae, N. K., & Moussa, C. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121141 · Cited by 91 · see citing works

ER-stress-associated functional link between Parkin and DJ-1 via a transcriptional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1

Duplan, E., Giaime, E., Viotti, J., Sévalle, J., Corti, O., Brice, A., Ariga, H., Qi, L., Checler, F., & da Costa, C. A. (2013) · Journal of Cell Science · doi:10.1242/jcs.127340 · Cited by 90 · see citing works

Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model

Khandelwal, P. J., Dumanis, S. B., Feng, L., Maguire‐Zeiss, K. A., Rebeck, G. W., Lashuel, H. A., & Moussa, C. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-47 · Cited by 89 · see citing works

S-Nitrosylation of parkin as a novel regulator of p53-mediated neuronal cell death in sporadic Parkinson’s disease

Sunico, C. R., Nakamura, T., Rockenstein, E. M., Mante, M., Adame, A., Chan, S. F., Newmeyer, T. F., Masliah, E., Nakanishi, N., & Lipton, S. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-29 · Cited by 83 · see citing works

Differential Effects of UCHL1 Modulation on Alpha-Synuclein in PD-Like Models of Alpha-Synucleinopathy

Cartier, A. E., Ubhi, K. K., Spencer, B. J., Vázquez‐Roque, R. A., Kosberg, K. A., Fourgeaud, L., Kanayson, P., Patrick, C., Rockenstein, E. M., Patrick, G. N., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034713 · Cited by 70 · see citing works

Glioma tumor grade correlates with parkin depletion in mutant p53-linked tumors and results from loss of function of p53 transcriptional activity

Viotti, J., Duplan, E., Caillava, C., Condat, J., Goiran, T., Giordano, C., Marie, Y., Idbaïh, A., Delattre, J.-Y., Honnorat, J., et al. (2013) · Oncogene · doi:10.1038/onc.2013.124 · Cited by 69 · see citing works

Decreased parkin solubility is associated with impairment of autophagy in the nigrostriatum of sporadic Parkinson’s disease

Lonskaya, I., Hebron, M. L., Algarzae, N. K., Desforges, N. M., & Moussa, C. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.12.018 · Cited by 68 · see citing works

Regulation of Parkin E3 ubiquitin ligase activity

Walden, H., & Martinez-Torres, R. J. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0978-5 · Cited by 68 · see citing works

Tumorigenesis and neurodegeneration: two sides of the same coin?

Staropoli, J. F. (2008) · BioEssays · doi:10.1002/bies.20784 · Cited by 67 · see citing works

α-Synuclein Aggregates Interfere with Parkin Solubility and Distribution

Kawahara, K., Hashimoto, M., Bar‐On, P., Ho, G. J., Crews, L. A., Mizuno, H., Rockenstein, E. M., Imam, S. Z., & Masliah, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710418200 · Cited by 64 · see citing works

Mitochondria directly donate their membrane to form autophagosomes during a novel mechanism of parkin-associated mitophagy

Cook, K. L., Soto‐Pantoja, D. R., Abu-Asab, M. S., Clarke, P. A. G., Roberts, D. D., & Clarke, R. C. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-16 · Cited by 64 · see citing works

Mitochondrial dysfunction and Parkinson’s disease genes: insights from Drosophila

Park, J., Kim, Y., & Chung, J. (2009) · Disease Models & Mechanisms · doi:10.1242/dmm.003178 · Cited by 63 · see citing works

Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation

Sun, X., Liu, M., Hao, J., Li, D., Luo, Y., Wang, X., Yang, Y., Li, F., Shui, W., Chen, Q., et al. (2013) · Cell Cycle · doi:10.4161/cc.24215 · Cited by 62 · see citing works

Tissue- and Cell-Specific Mitochondrial Defect in Parkin-Deficient Mice

Damiano, M. G., Gautier, C., Bulteau, A., Ferrando-Miguel, R., Gouarné, C., Giraudon‐Paoli, M., Pruss, R. M., Auchère, F., L'Hermitte-Stead, C., Bouillaud, F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099898 · Cited by 57 · see citing works

Direct Binding with Histone Deacetylase 6 Mediates the Reversible Recruitment of Parkin to the Centrosome

Jiang, Q., Ren, Y., & Feng, J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2860-08.2008 · Cited by 57 · see citing works

Parkin regulates kainate receptors by interacting with the GluK2 subunit

Maraschi, A., Ciammola, A., Folci, A., Sassone, F., Ronzitti, G., Cappelletti, G., Silani, V., Sato, S., Hattori, N., Mazzanti, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms6182 · Cited by 55 · see citing works

Parkin differently regulates presenilin-1 and presenilin-2 functions by direct control of their promoter transcription

Duplan, E., Sévalle, J., Viotti, J., Goiran, T., Bauer, C., Renbaum, P., Levy‐Lahad, E., Gautier, C., Corti, O., Leroudier, N., et al. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt003 · Cited by 45 · see citing works

Enhanced sensitivity to group II mGlu receptor activation at corticostriatal synapses in mice lacking the familial parkinsonism-linked genes PINK1 or Parkin

Martella, G., Platania, P., Vita, D., Sciamanna, G., Cuomo, D., Tassone, A., Tscherter, A., Kitada, T., Bonsi, P., Shen, J., et al. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.11.001 · Cited by 44 · see citing works

Parkin-mediated reduction of nuclear and soluble TDP-43 reverses behavioral decline in symptomatic mice

Chen, W., Lonskaya, I., Hebron, M. L., Ibrahim, Z., Olszewski, R. T., Neale, J. H., & Moussa, C. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu211 · Cited by 44 · see citing works

Mutant ataxin-3 promotes the autophagic degradation of parkin

Durcan, T. M., & Fon, E. A. (2011) · Autophagy · doi:10.4161/auto.7.2.14224 · Cited by 41 · see citing works

Parkin reverses TDP ‐43‐induced cell death and failure of amino acid homeostasis

Hebron, M. L., Chen, W., Miessau, M., Lonskaya, I., & Moussa, C. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12630 · Cited by 38 · see citing works

Parkin deletion causes cerebral and systemic amyloidosis in human mutated tau over-expressing mice

Rodríguez‐Navarro, J. A., Gómez, A., Rodal, I., Perucho, J., Martínez, A., Furió, V., Ampuero, I., Casarejos, M. J., Solano, R. M., de Yébenes, J. G., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn210 · Cited by 36 · see citing works

Parkin prevents cortical atrophy and Aβ-induced alterations of brain metabolism: 13C NMR and magnetic resonance imaging studies in AD models

Algarzae, N. K., Hebron, M. L., Miessau, M., & Moussa, C. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.08.057 · Cited by 27 · see citing works

Parkin Induces Upregulation of 40S Ribosomal Protein SA and Posttranslational Modification of Cytokeratins 8 and 18 in Human Cervical Cancer Cells

Song, D., Kim, Y. S., Jung, B. C., Rhee, K., & Pan, C. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0443-4 · Cited by 24 · see citing works

Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase

Byrd, R. A., & Weissman, A. M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.158 · Cited by 23 · see citing works

The ubiquitin ligase parkin modulates the execution of autophagy

Herman, A. M., & Moussa, C. (2011) · Autophagy · doi:10.4161/auto.7.8.15814 · Cited by 17 · see citing works

Contribution of germline mutations to PARK2 gene inactivation in lung adenocarcinoma

Iwakawa, R., Okayama, H., Kohno, T., Sato‐Otsubo, A., Ogawa, S., & Yokota, J. (2012) · Genes Chromosomes and Cancer · doi:10.1002/gcc.21933 · Cited by 16 · see citing works

Mitochondria initiate and regulate sarcopenia

Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153 · see citing works

Pharmacokinetics and pharmacodynamics of a single dose Nilotinib in individuals with Parkinson's disease

Pagán, F., Hebron, M. L., Wilmarth, B., Torres-Yaghi, Y. A., Lawler, A., Mundel, E. E., Yusuf, N., Starr, N. J., Arellano, J., Howard, H. H., et al. (2019) · Pharmacology Research & Perspectives · doi:10.1002/prp2.470 · Cited by 117 · see citing works

Multikinase Abl/DDR/Src Inhibition Produces Optimal Effects for Tyrosine Kinase Inhibition in Neurodegeneration

Fowler, A. J., Hebron, M. L., Missner, A. A., Wang, R., Gao, X., Kurd-Misto, B. T., Liu, X., & Moussa, C. (2019) · Drugs in R&D · doi:10.1007/s40268-019-0266-z · Cited by 68 · see citing works

Discoidin domain receptor inhibition reduces neuropathology and attenuates inflammation in neurodegeneration models

Hebron, M. L., Peyton, M. A., Liu, X., Gao, X., Wang, R., Lonskaya, I., & Moussa, C. (2017) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2017.07.009 · Cited by 65 · see citing works

Activating Autophagy as a Therapeutic Strategy for Parkinson’s Disease

Fowler, A. J., & Moussa, C. (2018) · CNS Drugs · doi:10.1007/s40263-018-0497-5 · Cited by 52 · see citing works

Post-translational modifications of Parkinson's disease-related proteins: Phosphorylation, SUMOylation and Ubiquitination

Junqueira, S. C., Centeno, E. G. Z., Wilkinson, K. A., & Cimarosti, H. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.025 · Cited by 50 · see citing works

Novel Ubiquitin Specific Protease-13 Inhibitors Alleviate Neurodegenerative Pathology

Liu, X., Balaraman, K., Lynch, C. C., Hebron, M. L., Wolf, C., & Moussa, C. (2021) · Metabolites · doi:10.3390/metabo11090622 · Cited by 26 · see citing works

Regulatory Role of Ubiquitin Specific Protease-13 (USP13) in Misfolded Protein Clearance in Neurodegenerative Diseases

Liu, X., & Moussa, C. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.02.004 · Cited by 24 · see citing works

Safety, target engagement, and biomarker effects of bosutinib in dementia with Lewy bodies

Pagán, F., Torres-Yaghi, Y. A., Hebron, M. L., Wilmarth, B., Turner, R. S., Matar, S., Ferrante, D., Ahn, J., & Moussa, C. (2022) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12296 · Cited by 21 · see citing works

Two sides of the same coin: tyrosine kinase inhibition in cancer and neurodegeneration

Moussa, C., & Hebron, M. L. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.165320 · Cited by 9 · see citing works

Antioxidants and Polyphenols Mediate Mitochondrial Mediated Muscle Death Signaling in Sarcopenia

Alway, S. E. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-810422-4.00026-9 · Cited by 6 · see citing works

Could cancer drugs be repurposed for use in Parkinson’s and Alzheimer’s?

Moussa, C. (2016) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2016.1248411

The Role of Parkin in Rat Pancreatic Beta Cells Fate

Verdi, H., Çebi, H. P. B., Yalçın, Y., Özkan, T., Ok, M. A., Sunguroğlu, A., & Ataç, F. B. (2023) · Cellular and Molecular Biology · doi:10.14715/cmb/2023.69.8.9 · Cited by 1 · see citing works

Correspondence

Seirafi, M., Kozlov, G., & Gehring, K. (2014)

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 · see citing works

Parkin structure and function

Seirafi, M., Kozlov, G., & Gehring, K. (2015) · The FEBS Journal · doi:10.1111/febs.13249 · Cited by 256 · see citing works

PARK2 Induces Autophagy Removal of Impaired Mitochondria via Ubiquitination

Lim, K., Chua, D. S. K., Gallart‐Palau, X., & Yao, T. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405528-5.00011-0 · Cited by 1 · see citing works

PTEN-induced kinase 1 (PINK1) and Parkin: Unlocking a mitochondrial quality control pathway linked to Parkinson's disease

Agarwal, S., & Muqit, M. M. K. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.09.005 · Cited by 103 · see citing works