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Biochemical Journal, ISSN 0264-6021, 01/2012, Volume 441, Issue 2, pp. 523 - 540
Reactive oxygen and nitrogen species change cellular responses through diverse mechanisms that are now being defined. At low levels, they are signalling... 
Mitochondrion | Oxidative stress | Redox signalling | Neurodegeneration | Autophagy | Nitrative stress | autophagy | CHAPERONE-MEDIATED AUTOPHAGY | ANTIOXIDANT RESPONSIVE ELEMENTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIPOFUSCINOSES BATTEN-DISEASE | neurodegeneration | AMYOTROPHIC-LATERAL-SCLEROSIS | mitochondrion | redox signalling | MOTOR-NEURON DEGENERATION | MANGANESE SUPEROXIDE-DISMUTASE | nitrative stress | SMOOTH-MUSCLE-CELLS | PATHOGENIC DJ-1 MUTATIONS | HYPOXIA-INDUCED AUTOPHAGY | oxidative stress | COMPLEX-I DEFICIENCY | Protein Kinases - metabolism | Transcription, Genetic - drug effects | Cardiovascular Diseases - physiopathology | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Reactive Nitrogen Species - metabolism | Humans | Oxidative Stress - physiology | Hydrogen Peroxide - pharmacology | Oncogene Proteins - metabolism | Nitric Oxide - physiology | Autophagy - physiology | Intracellular Signaling Peptides and Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Parkinson Disease - physiopathology | Lysosomes - physiology | Protein Deglycase DJ-1 | Animals | Signal Transduction - physiology | TOR Serine-Threonine Kinases - physiology | Neoplasms - physiopathology | AMPK, 5′-AMP-activated protein kinase | NBR1, neighbour of BRCA1 (breast cancer early-onset 1) | NGF, nerve growth factor | LC3, light chain 3 | NOX, NADPH oxidase | EM, electron microscopy | TOR, target of rapamycin | ULK, unc (unco-ordinated family member)-51-like kinase | mtDNA, mitochondrial DNA | mTOR, mammalian target of rapamycin | IKKβ, IκB kinase β | LRRK2, leucine-rich repeat kinase 2 | NAC, N-acetyl-L-cysteine | Nrf2, nuclear factor-erythroid 2-related factor 2 | PI3P, phosphatidylinositol 3-phosphate | ECH, enoyl-CoA hydratase | BNIP3L, BNIP3-like | Drp1, dynamin-related protein 1 | tfLC3, tandem fluorescently tagged LC3 | NF-κB, nuclear factor κB | BAG, Bcl-2-associated athanogene | Keap1, Kelch-like ECH-associated protein 1 | PE, phosphatidylethanolamine | 3-MA, 3-methyladenine | UCP, uncoupling protein | IκB, inhibitor of nuclear factor κB | FIP200, focal adhesion kinase family-interacting protein of 200 kDa | PI3K, phosphoinositide 3-kinase | HNE, 4-hydroxynonenal | Review | ALS, amyotrophic lateral sclerosis | ATG, AuTophaGy-related | adenovirus E18 19-kDa-interacting protein | Tzb, trastuzumab | mETC, mitochondrial electron-transport chain | Rubicon, RUN domain- and cysteine-rich domain-containing beclin-1-interacting protein | VDAC, voltage-dependent anion channel | IP3, inositol 1,4,5-trisphosphate | RFP, red fluorescent protein | ROS, reactive oxygen species | TNFα, tumour necrosis factor α | PINK1, PTEN (phosphatase and tensin homologue deleted on chromosome 10)-induced kinase 1 | GFP, green fluorescent protein | LAMP, lysosome-associated membrane protein | JNK1, c-Jun N-terminal kinase 1 | TAC, transverse aortic constriction | GABARAP, GABAA (γ-aminobutyric acid type A)-receptor-associated protein | HIF-1, hypoxia-inducible factor 1 | NOS, nitric oxide synthase | siRNA, small interfering RNA | SOD, superoxide dismutase | RLS, reactive lipid species | RNS, reactive nitrogen species | ER, endoplasmic reticulum | TIGAR, TP53 (tumour protein 53)-induced glycolysis and apoptosis regulator | Vps34, vacuolar protein sorting 34 | BNIP, Bcl-2
Journal Article
Biochemical Journal, ISSN 0264-6021, 07/2007, Volume 405, Issue 2, pp. 307 - 317
Mutations in the LRRK2 (leucine-rich repeat kinase-2) gene cause late-onset PD (Parkinson's disease). LRRK2 contains leucine-rich repeats, a GTPase domain, a... 
Kinase substrate tracking and elucidation screening (KESTREL screening) | Ezrin/radixin/moesin family of proteins (ERM proteins) | Protein kinase | Leucine-rich repeat kinase 2 (LRRK2) | Mass spectrometry (MS) | Parkinson's disease (PD) | SITE | GENE LRRK2 | DOMAIN | ERM PROTEINS | ezrin/radixin/moesin family of proteins (ERM proteins) | F-ACTIN BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | leucine-rich repeat kinase 2 (LRRK2) | protein kinase | kinase substrate tracking and elucidation screening (KESTREL screening) | IN-VITRO | EZRIN | MUTATIONS | ASSOCIATION | mass spectrometry (MS) | Amino Acid Sequence | Humans | Protein-Serine-Threonine Kinases - genetics | Rats | Parkinson Disease - genetics | Threonine - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Animals | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Microfilament Proteins - metabolism | Parkinson Disease - metabolism | Protein-Serine-Threonine Kinases - metabolism | LRRKtide, RLGRDKYKTLRQIRQ | BUBR1, Bub (budding uninhibited by benomyl)-related 1 | ezrin | GbpC, cGMP-binding protein C | moesin family of proteins (ERM proteins) | CRMP2, collapsin response mediator protein 2 | WD40, Trp-Asp 40 | MALDI-TOF, matrix-assisted laser-desorption ionization–time-of-flight | NCBI, National Center for Biotechnology Information | radixin | TSSK1, testis-specific serine kinase 1 | LRRK2, leucine-rich repeat kinase 2 | RIPK, Rho-interacting protein kinase | GST, glutathione S-transferase | LDS, lithium dodecyl sulfate | ROCK-II, Rho-associated kinase-2 | ERM, ezrin | PD, Parkinson's disease | MBP, myelin basic protein | moesin | COR, C-terminal of Roc (Ras of complex) | FERM, four-point-one | KESTREL, kinase substrate tracking and elucidation
Journal Article
Biochemical Journal, ISSN 0264-6021, 09/2010, Volume 430, Issue 3, pp. 393 - 404
LRRK2 (leucine-rich repeat protein kinase 2) is mutated in a significant number of Parkinson's disease patients, but still little is understood about how it is... 
Pathogenic mutation | 14-3-3 protein | Phosphorylation | Cytoplasmic localization | Parkinson's disease | Leucine-rich repeat protein kinase 2 (LRRK2) | KINASE-ACTIVITY | leucine-rich repeat protein kinase 2 (LRRK2) | cytoplasmic localization | pathogenic mutation | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEPHOSPHORYLATION | PROTEINS | phosphorylation | 14-3-3-PROTEINS | Immunoprecipitation | Humans | Swiss 3T3 Cells | Molecular Sequence Data | Cytoplasm - metabolism | Green Fluorescent Proteins - genetics | Brain - metabolism | Kidney - metabolism | Protein-Serine-Threonine Kinases - metabolism | 14-3-3 Proteins - genetics | Amino Acid Sequence | Cell Line | Green Fluorescent Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Serine - genetics | Binding Sites - genetics | Parkinson Disease - genetics | Serine - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Mice, Knockout | 14-3-3 Proteins - metabolism | Sequence Homology, Amino Acid | Animals | Spleen - metabolism | Protein Binding | Mice | Mutation | Microscopy, Fluorescence | DIG, digoxigenin | GFP, green fluorescent protein | COR, C-terminal of ROC | FBS, fetal bovine serum | SILAC, stable isotope labelling of amino acids | TBST, Tris-buffered saline with Tween 20 | DTT, dithiothreitol | HEK-293, human embryonic kidney | Hsp90, heat-shock protein 90 | PD, Parkinson's disease | DMEM, Dulbecco's modified Eagle's medium | IPI, International Protein Index | MARK3, microtubule affinity-regulating kinase 3 | CDC, cell division cycle | LRRK2, leucine-rich repeat protein kinase 2 | ROC, Ras of complex GTPase domain | KLH, keyhole-limpet haemocyanin
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 3, p. e17153
Background: Recent studies show that mutations in Leucine Rich Repeat Kinase 2 (LRRK2) are the cause of the most common inherited and some sporadic forms of... 
PROTEIN-KINASE-A | NEUROTRANSMISSION | GENE | LEUCINE-RICH-REPEAT-KINASE-2 LRRK2 | IN-VIVO | BIOLOGY | RECEPTOR | RIM1-ALPHA | GTPASE | 14-3-3-PROTEINS | PLASTICITY | Cyclic AMP-Dependent Protein Kinases - metabolism | Phosphorylation | Protein Multimerization | Cells, Cultured | Brain - enzymology | Mice, Transgenic | Parkinson Disease - genetics | Mutation - genetics | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | 14-3-3 Proteins - metabolism | Animals | Protein Isoforms - metabolism | Parkinson Disease - enzymology | Brain - pathology | Protein Binding | Family | Mice | Phosphoserine | Protein-Serine-Threonine Kinases - metabolism | Amino Acid Substitution | Viral antibodies | Analysis | Physiological aspects | Antibodies | Genetic aspects | Binding proteins | Mass spectrometry | Protein kinases | Protein binding | Protein kinase A | Brain | Cell culture | Neurosciences | Parkinson's disease | Peptides | Laboratories | Protein purification | Parkinsons disease | Identification | Leucine | Kinases | Autophagy | Proteins | Spectrometry | Transgenic animals | Rodents | Animal tissues | LRRK2 protein | Age | Movement disorders | Binding | Medical research | Dopamine | Neurodegenerative diseases | Upstream | Medicine | Neurology | 14-3-3 protein | Brain research | N-Terminus | Isoforms | Proteomics | Scientific imaging | In vivo methods and tests | Mutation
Journal Article
Journal of Neurochemistry, ISSN 0022-3042, 11/2009, Volume 111, Issue 3, pp. 703 - 715
Mutations in the gene encoding leucine‐rich repeat kinase 2 (LRRK2) are the most common cause of autosomal‐dominant familial and late‐onset sporadic... 
dimerization | leucine‐rich repeat kinase 1 | kinase inhibition | leucine‐rich repeat kinase 2 | Parkinson’s disease | death‐associated protein kinase 1 | Leucine-rich repeat kinase 1 | Death-associated protein kinase 1 | Leucine-rich repeat kinase 2 | Parkinson's disease | Kinase inhibition | Dimerization | leucine-rich repeat kinase 2 | DISEASE-ASSOCIATED MUTATIONS | GENE LRRK2 | ACTIVATION | DOMAIN | leucine-rich repeat kinase 1 | AUTOSOMAL-DOMINANT PARKINSONISM | LEUCINE-RICH-REPEAT-KINASE-2 LRRK2 | PROTEIN-KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEURONAL TOXICITY | GTP-BINDING | NEUROSCIENCES | death-associated protein kinase 1 | Lipids - genetics | Calcium-Calmodulin-Dependent Protein Kinases - genetics | Apoptosis Regulatory Proteins - chemistry | Humans | Protein-Serine-Threonine Kinases - genetics | Protein Structure, Tertiary - genetics | Signal Transduction - genetics | Mutation - genetics | Apoptosis Regulatory Proteins - metabolism | Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 | Calcium-Calmodulin-Dependent Protein Kinases - chemistry | Two-Hybrid System Techniques | Transfection - methods | Protein Multimerization - genetics | Apoptosis Regulatory Proteins - genetics | Protein Conformation | Protein-Serine-Threonine Kinases - chemistry | Death-Associated Protein Kinases | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Cell Line, Transformed | Protein-Serine-Threonine Kinases - metabolism | Proteins | Protein kinases | Neurology | Biochemistry | Mutation | Kinases | Parkinsons disease
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2014, Volume 9, Issue 10, p. e111632
Journal Article
Human Molecular Genetics, ISSN 0964-6906, 05/2012, Volume 21, Issue 9, pp. 1931 - 1944
Journal Article