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1. Full Text Heterozygous PINK1 p.G411S increases risk of Parkinson's disease via a dominant-negative mechanism
by Puschmann, Andreas and Fiesel, Fabienne C and Caulfield, Thomas R and Hudec, Roman and Ando, Maya and Truban, Dominika and Hou, Xu and Ogaki, Kotaro and Heckman, Michael G and James, Elle D and Swanberg, Maria and Jimenez-Ferrer, Itzia and Hansson, Oskar and Opala, Grzegorz and Siuda, Joanna and Boczarska-Jedynak, Magdalena and Friedman, Andrzej and Koziorowski, Dariusz and Rudzińska-Bar, Monika and Aasly, Jan O and Lynch, Timothy and Mellick, George D and Mohan, Megha and Silburn, Peter A and Sanotsky, Yanosh and Vilariño-Güell, Carles and Farrer, Matthew J and Chen, Li and Dawson, Valina L and Dawson, Ted M and Wszolek, Zbigniew K and Ross, Owen A and Springer, Wolfdieter and Klinisk minnesforskning and Lund University and Neurologi, Lund and MultiPark: Multidisciplinary research focused on Parkinson´s disease and Translational Neurogenetics and Translationell Neurogenetik and Clinical Memory Research and Lunds universitet and Neurology, Lund
Brain, ISSN 0006-8950, 2017, Volume 140, Issue 1, pp. 98 - 117
It has been postulated that heterozygous mutations in recessive Parkinson's genes may increase the risk of developing the disease. In particular, the... 
Ubiquitin | PINK1 | Parkinson's disease | Heterozygous mutation | Mitophagy | TRANSLOCATION | SUBSTITUTION | ACTIVATION | PHOSPHORYLATION | LRRK2 | MITOCHONDRIA | heterozygous mutation | UBIQUITIN CHAIN | NEUROSCIENCES | ubiquitin | PROTEIN-STRUCTURE PREDICTION | CLINICAL NEUROLOGY | mitophagy | PINK1/PARKIN-MEDIATED MITOPHAGY | MUTATIONS | Genetic Predisposition to Disease - genetics | Protein Kinases - genetics | Genetic Association Studies | Humans | Middle Aged | Models, Molecular | Male | Risk | Parkinson Disease - genetics | Case-Control Studies | Young Adult | Pedigree | Adolescent | Aged, 80 and over | Fibroblasts | Adult | Female | Heterozygote | Aged | Neurologi | Clinical Medicine | Neurology | Basic Medicine | Neurosciences | Medical and Health Sciences | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Klinisk medicin | Journal Article | Neurovetenskaper
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2. Full Text The AMPK-Parkin axis negatively regulates necroptosis and tumorigenesis by inhibiting the necrosome
by Lee, SB and Kim, JJ and Han, SA and Fan, YF and Guo, LS and Aziz, K and Nowsheen, S and Kim, SS and Park, SY and Lue, QF and Chung, JO and Choi, SI and Aziz, A and Yin, P and Tong, SY and Fiesel, FC and Springer, W and Zhang, JS and Lou, ZK
NATURE CELL BIOLOGY, ISSN 1465-7392, 08/2019, Volume 21, Issue 8, pp. 940 - 940
The receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 play important roles in necroptosis that are closely linked to the inflammatory... 
APOPTOSIS | ACTIVATED PROTEIN-KINASE | PHOSPHORYLATION | COLORECTAL-CANCER | UBIQUITIN | INFLAMMATION | DISEASE | TUMOR-SUPPRESSOR GENE | COLON CARCINOGENESIS | CROSSTALK | CELL BIOLOGY | Medical research | Ligases | Cell death | Physiological aspects | Medicine, Experimental | Development and progression | Cyclic adenylic acid | Inflammation | Research | Health aspects | Protein kinases | Carcinogenesis | Ubiquitin | Phosphorylation | Complex formation | AMP | Threonine | Serine | Inflammatory response | Protein deficiency | Kinases | AMP-activated protein kinase | Proteins | Tumorigenesis | Parkin protein | Inhibition | Ubiquitin-protein ligase | Tumors
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3. PINK1, Parkin, and Mitochondrial Quality Control: What can we Learn about Parkinson's Disease Pathobiology?
by Truban, Dominika and Hou, Xu and Caulfield, Thomas R and Fiesel, Fabienne C and Springer, Wolfdieter
Journal of Parkinson's Disease, ISSN 1877-7171, 2017, Volume 7, Issue 1, pp. 13 - 29
The first clinical description of Parkinson's disease (PD) will embrace its two century anniversary in 2017. For the past 30 years, mitochondrial dysfunction... 
mitophagy | PINK1 | Parkinson's disease | mitochondria | ubiquitin | Parkin | RESPIRATORY-CHAIN | LOSS-OF-FUNCTION | OXIDATIVE STRESS | DAMAGED MITOCHONDRIA | PINK1-DEPENDENT PHOSPHORYLATION | PHOSPHORYLATED UBIQUITIN | ALPHA-SYNUCLEIN | NEUROSCIENCES | DOPAMINE NEURONS | COMPLEX-I | E3 LIGASE PARKIN
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4. Full Text PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
by Geisler, Sven and Holmström, Kira M and Skujat, Diana and Fiesel, Fabienne C and Rothfuss, Oliver C and Kahle, Philipp J and Springer, Wolfdieter
Nature Cell Biology, ISSN 1465-7392, 2010, Volume 12, Issue 2, pp. 119 - 131
Parkinson's disease is the most common neurodegenerative movement disorder. Mutations in PINK1 and PARKIN are the most frequent causes of recessive Parkinson's... 
PINK1 | DOMAIN | GENE | UBIQUITIN-PROTEIN LIGASE | DEGRADATION | MUTATIONS | AUTOPHAGY | NEURODEGENERATIVE DISEASES | PARKINSONS-DISEASE | CELL-DEATH | CELL BIOLOGY | Protein Kinases - metabolism | Protein Kinases - genetics | Immunoprecipitation | Sequestosome-1 Protein | Humans | Ubiquitin-Protein Ligases - metabolism | Voltage-Dependent Anion Channel 1 - metabolism | Immunoblotting | Autophagy - physiology | Mitochondria - metabolism | Parkinson Disease - genetics | RNA Interference | Adaptor Proteins, Signal Transducing - genetics | Fluorescent Antibody Technique | Cell Line, Tumor | Biological Transport - genetics | Biological Transport - physiology | Parkinson Disease - metabolism | Autophagy - genetics | HeLa Cells | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitin-Protein Ligases - genetics | Voltage-Dependent Anion Channel 1 - genetics
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5. Full Text Age- and disease-dependent increase of the mitophagy marker phospho-ubiquitin in normal aging and Lewy body disease
by Hou, Xu and Fiesel, Fabienne C and Truban, Dominika and Castanedes Casey, Monica and Lin, Wen-lang and Soto, Alexandra I and Tacik, Pawel and Rousseau, Linda G and Diehl, Nancy N and Heckman, Michael G and Lorenzo-Betancor, Oswaldo and Ferrer, Isidre and Arbelo, José M and Steele, John C and Farrer, Matthew J and Cornejo-Olivas, Mario and Torres, Luis and Mata, Ignacio F and Graff-Radford, Neill R and Wszolek, Zbigniew K and Ross, Owen A and Murray, Melissa E and Dickson, Dennis W and Springer, Wolfdieter
Autophagy, ISSN 1554-8627, 08/2018, Volume 14, Issue 8, pp. 1404 - 1418
Although exact causes of Parkinson disease (PD) remain enigmatic, mitochondrial dysfunction is increasingly appreciated as a key determinant of dopaminergic... 
lewy body disease | autophagy | parkin | mitochondria | tau | alpha-synuclein | parkinson disease | PARK2 | ubiquitin | mitophagy | PINK1 | Aging | phospho-ubiquitin | MAPT | SNCA | DEMENTIA | GRANULOVACUOLAR DEGENERATION | ALZHEIMERS-DISEASE | DAMAGED MITOCHONDRIA | CELL BIOLOGY | DOPAMINE NEURONS | IN-VIVO | DIAGNOSTIC-CRITERIA | SPORADIC PARKINSONS-DISEASE | Ubiquitin | Mitochondria | Parkinson's disease | Envelliment | Ubiqüitina | Malaltia de Parkinson | Autofàgia | Mitocondris | Autophagy
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6. Full Text Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin
: e1003935
by Thomas R Caulfield and Fabienne C Fiesel and Elisabeth L Moussaud-Lamodière and F A R Dourado and Samuel C Flores and Wolfdieter Springer
PLoS Computational Biology, ISSN 1553-734X, 11/2014, Volume 10, Issue 11
  Loss-of-function mutations in PINK1 or PARKIN are the most common causes of autosomal recessive Parkinson's disease. Both gene products, the Ser/Thr kinase... 
Proteins | Enzymes | Phosphorylation | Mitochondria | Quality control | Animation | Mutation | Kinases
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7. TDP-43 and FUS/TLS: cellular functions and implications for neurodegeneration
by Fabienne C. Fiesel and Philipp J. Kahle
The FEBS Journal, ISSN 1742-464X, 10/2011, Volume 278, Issue 19, p. 3550
TDP-43 (transactive response binding protein of 43kDa) and FUS (fused in sarcoma) comprise the neuropathological protein aggregates of distinct subtypes of the... 
Proteins | Brain | Neurodegeneration | Ribonucleic acid--RNA | Molecular biology | Neurological disorders | Binding sites
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8. Full Text Structural and Functional Impact of Parkinson Disease-Associated Mutations in the E3 Ubiquitin Ligase Parkin
: HUMAN MUTATION
by Fiesel, Fabienne C and Caulfield, Thomas R and Moussaud-Lamodière, Elisabeth L and Ogaki, Kotaro and Dourado, Daniel F.A.R and Flores, Samuel C and Ross, Owen A and Springer, Wolfdieter
Human Mutation, ISSN 1059-7794, 08/2015, Volume 36, Issue 8, pp. 774 - 786
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9. Full Text (Patho‐)physiological relevance of PINK 1‐dependent ubiquitin phosphorylation
by Fiesel, Fabienne C and Ando, Maya and Hudec, Roman and Hill, Anneliese R and Castanedes‐Casey, Monica and Caulfield, Thomas R and Moussaud‐Lamodière, Elisabeth L and Stankowski, Jeannette N and Bauer, Peter O and Lorenzo‐Betancor, Oswaldo and Ferrer, Isidre and Arbelo, José M and Siuda, Joanna and Chen, Li and Dawson, Valina L and Dawson, Ted M and Wszolek, Zbigniew K and Ross, Owen A and Dickson, Dennis W and Springer, Wolfdieter
EMBO reports, ISSN 1469-221X, 09/2015, Volume 16, Issue 9, pp. 1114 - 1130
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10. Full Text TDP-43 and FUS/TLS: cellular functions and implications for neurodegeneration
: Pathophysiology of TDP-43 and FUS
by Fiesel, Fabienne C and Kahle, Philipp J
FEBS Journal, ISSN 1742-464X, 10/2011, Volume 278, Issue 19, pp. 3550 - 3568
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11. Full Text Activation of the E3 ubiquitin ligase Parkin
by Caulfield, Thomas R and Fiesel, Fabienne C and Springer, Wolfdieter
Biochemical Society Transactions, ISSN 0300-5127, 04/2015, Volume 43, Issue 2, pp. 269 - 274
The PINK1 (phosphatase and tensin homologue-induced putative kinase 1)/Parkin-dependent mitochondrial quality control pathway mediates the clearance of damaged... 
Phosphatase and tensin homologue-induced putative kinase 1 (PINK1) | Molecular dynamics | Simulations | Ubiquitin (Ub) | Parkinson's disease (PD) | Parkin | DOMAIN | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOPHAGY | MECHANISMS | molecular dynamics | simulations | phosphatase and tensin homologue-induced putative kinase 1 (PINK1) | MITOCHONDRIAL TRANSLOCATION | PINK1 | RING | PROTEASOME | ubiquitin (Ub) | Protein Kinases - metabolism | Protein Structure, Tertiary | Parkinson Disease - pathology | Phosphorylation | Protein Kinases - genetics | Humans | Ubiquitin-Protein Ligases - metabolism | Protein Kinases - chemistry | Crystallography, X-Ray | Parkinson Disease - drug therapy | Structure-Activity Relationship | Parkinson Disease - genetics | Ubiquitin-Protein Ligases - chemistry | Autophagy - genetics | Mutation | Ubiquitin-Protein Ligases - genetics | Parkinson’s disease | ubiquitin
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12. Full Text TDP‐43 and FUS/TLS: cellular functions and implications for neurodegeneration
by Fiesel, Fabienne C and Kahle, Philipp J
The FEBS Journal, ISSN 1742-464X, 10/2011, Volume 278, Issue 19, pp. 3550 - 3568
TDP‐43 (transactive response binding protein of 43 kDa) and FUS (fused in sarcoma) comprise the neuropathological protein aggregates of distinct subtypes of... 
autophagy | RNA | transcription | FUS | FTLD | ALS | splicing | TDP‐43 | HDAC6 | RNA metabolism | TDP-43 | VALOSIN-CONTAINING PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYOTROPHIC-LATERAL-SCLEROSIS | MOTOR-NEURON DISEASE | FRONTOTEMPORAL LOBAR DEGENERATION | RNA-BINDING PROTEIN | SPLICING FACTOR TLS | MESSENGER-RNA | NUCLEAR FACTOR TDP-43 | GENE-EXPRESSION | HUMAN MYXOID LIPOSARCOMA | Frontotemporal Lobar Degeneration - pathology | Amyotrophic Lateral Sclerosis - physiopathology | Humans | Gene Expression Regulation | Nerve Degeneration - physiopathology | RNA-Binding Protein FUS - genetics | Autophagy - physiology | RNA-Binding Protein FUS - metabolism | Frontotemporal Lobar Degeneration - physiopathology | Cytoplasmic Granules - chemistry | DNA-Binding Proteins - genetics | RNA Stability | Nerve Degeneration - pathology | DNA-Binding Proteins - metabolism | Amyotrophic Lateral Sclerosis - pathology | Animals | Cytoplasmic Granules - metabolism | RNA - metabolism | Proteins | Messenger RNA | Sarcoma | Physiological aspects | Amyotrophic lateral sclerosis | Disease susceptibility | Protein binding
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13. Full Text The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations
by Geisler, Sven and Holmström, Kira M and Treis, Angela and Skujat, Diana and Weber, Stephanie S and Fiesel, Fabienne C and Kahle, Philipp J and Springer, Wolfdieter
Autophagy, ISSN 1554-8627, 10/2010, Volume 6, Issue 7, pp. 871 - 878
Mitochondrial dysfunction is an early sign of many neurodegenerative diseases. Very recently, two Parkinson disease (PD) associated genes, PINK1 and Parkin,... 
Binding | Proteins | Landes | Calcium | Bioscience | Biology | Cell | Cycle | Cancer | Organogenesis | Ubiquitin | Mitochondria | PINK1 | Parkinson disease | p62/SQSTM1 | VDAC1 | Mitophagy | Autophagy | Parkin | LOCALIZATION | OXIDATIVE STRESS | autophagy | parkin | PHOSPHORYLATION | mitochondria | STABILITY | parkinson disease | RECESSIVE PARKINSONISM | ubiquitin | CELL BIOLOGY | mitophagy | DISEASE | MITOCHONDRIAL DYSFUNCTION | DROSOPHILA-PINK1 | PROMOTES | Protein Kinases - metabolism | RNA, Small Interfering - genetics | Parkinson Disease - pathology | Protein Kinases - genetics | Humans | Ubiquitin-Protein Ligases - metabolism | Mitochondria - pathology | Parkinson Disease - genetics | Parkinson Disease - physiopathology | Animals | HEK293 Cells | Autophagy - genetics | HeLa Cells | Mutation | Mitochondria - physiology | Ubiquitin-Protein Ligases - genetics | RNA, Small Interfering - metabolism
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14. Full Text Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin
by Caulfield, Thomas R and Fiesel, Fabienne C and Moussaud-Lamodière, Elisabeth L and Dourado, Daniel F. A. R and Flores, Samuel C and Springer, Wolfdieter and Teknisk-naturvetenskapliga vetenskapsområdet and Biologiska sektionen and Uppsala universitet and Institutionen för cell- och molekylärbiologi and Beräknings- och systembiologi
PLoS Computational Biology, ISSN 1553-734X, 11/2014, Volume 10, Issue 11, p. e1003935
Loss-of-function mutations in PINK1 or PARKIN are the most common causes of autosomal recessive Parkinson's disease. Both gene products, the Ser/Thr kinase... 
MITOCHONDRIAL TRANSLOCATION | MOLECULAR-DYNAMICS | ACTIVATION | MODELS | RNA | RING | INFORMATION | BIOCHEMICAL RESEARCH METHODS | MATHEMATICAL & COMPUTATIONAL BIOLOGY | MITOPHAGY | PROTEIN-STRUCTURE PREDICTION | INSIGHTS | Protein Kinases - metabolism | Protein Structure, Tertiary | Phosphorylation | Humans | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Protein Kinases - chemistry | Ubiquitin-Protein Ligases - chemistry | Molecular Dynamics Simulation | Parkinson Disease | Protein Binding | Protein Conformation | HeLa Cells | Protein research | Research | Ligases | Phosphotransferases | Health aspects | Biological Sciences | Biochemistry and Molecular Biology | Naturvetenskap | Natural Sciences | Biokemi och molekylärbiologi | Biologiska vetenskaper | Proteins | Enzymes | Mitochondria | Quality control | Animation | Mutation | Kinases
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15. Full Text Parkinson's disease-associated DJ-1 modulates innate immunity signaling in Caenorhabditis elegans
by Cornejo Castro, Elena M and Waak, Jens and Weber, Stephanie S and Fiesel, Fabienne C and Oberhettinger, Philipp and Schütz, Monika and Autenrieth, Ingo B and Springer, Wolfdieter and Kahle, Philipp J
Journal of Neural Transmission, ISSN 0300-9564, 2010, Volume 117, Issue 5, pp. 599 - 604
DJ-1 is a neuroprot