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Nature reviews. Molecular cell biology, ISSN 1471-0080, 01/2010, Volume 11, Issue 1, pp. 9 - 22
The AGC kinase subfamily of protein kinases contains 60 members, including PKA, PKG and PKC. The family comprises some intensely examined protein kinases (such... 
Life Sciences & Biomedicine | Science & Technology | Cell Biology | Diabetes Mellitus - enzymology | Animals | Protein-Serine-Threonine Kinases - physiology | Humans | Neoplasms - enzymology | Protein-Serine-Threonine Kinases - chemistry | Enzyme Activation | Physiological aspects | Research | Enzyme kinetics | Properties | Protein kinases | Index Medicus
Journal Article
ACS chemical biology, ISSN 1554-8929, 01/2013, Volume 8, Issue 1, pp. 96 - 104
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 05/2012, Volume 109, Issue 20, pp. 7929 - 7934
Journal Article
Biochemical journal, ISSN 0264-6021, 03/2000, Volume 346, Issue 3, pp. 561 - 576
Journal Article
Biochemical journal, ISSN 1470-8728, 06/2007, 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) | Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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 | Index Medicus | LRRKtide, RLGRDKYKTLRQIRQ | BUBR1, Bub (budding uninhibited by benomyl)-related 1 | ezrin | GbpC, cGMP-binding protein C | protein kinase | moesin family of proteins (ERM proteins) | CRMP2, collapsin response mediator protein 2 | WD40, Trp-Asp 40 | kinase substrate tracking and elucidation screening (KESTREL screening) | 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 | leucine-rich repeat kinase 2 (LRRK2) | 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 | mass spectrometry (MS)
Journal Article
Nature (London), ISSN 1476-4687, 10/2017, Volume 550, Issue 7677, pp. 534 - 538
The ubiquitin system regulates essential cellular processes in eukaryotes. Ubiquitin is ligated to substrate proteins as monomers or chains and the topology of... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Pyridines - chemistry | Ubiquitin-Specific Peptidase 7 - chemistry | Humans | Ubiquitin - metabolism | Substrate Specificity | Tumor Suppressor Protein p53 - genetics | Aminopyridines - chemistry | Ubiquitin-Specific Peptidase 7 - deficiency | Proto-Oncogene Proteins c-pim-1 - antagonists & inhibitors | Female | Proto-Oncogene Proteins c-mdm2 - metabolism | Phenols - pharmacology | Binding, Competitive | Indazoles - chemistry | Tumor Suppressor Protein p53 - metabolism | Ubiquitin - chemistry | Models, Molecular | Neoplasms - enzymology | Ubiquitin-Specific Peptidase 7 - antagonists & inhibitors | Ubiquitin-Specific Peptidase 7 - metabolism | Mice, SCID | Tumor Suppressor Protein p53 - deficiency | Neoplasms - drug therapy | Drug Synergism | Indazoles - pharmacology | Animals | Aminopyridines - pharmacology | Cell Line, Tumor | Protein Binding | Phenols - chemistry | Mice | Pyridines - pharmacology | Neoplasms - pathology | Biological research | Physiological aspects | Chemical inhibitors | Research | Ubiquitin-proteasome system | Biology, Experimental | Ubiquitin | Nuclear magnetic resonance--NMR | Toxicity | Hydrogen | p53 Protein | Cytotoxicity | Chains | Kinases | Monomers | Proteins | Depolymerization | Eukaryotes | Ubiquitination | Cell cycle | Reaction kinetics | Catalysis | Crystal structure | Binding | Enzymes | Magnetic resonance | Topology | Substrates | Chemotherapy | Inhibitors | Cell death | Proteasomes | Resonance | Mutation | Kinetics | Cancer | Tumors | Index Medicus
Journal Article