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FEBS Letters, ISSN 0014-5793, 12/2015, Volume 589, Issue 24, pp. 3760 - 3772
Glial cell line-derived neurotrophic factor (GDNF) and its canonical receptor Ret can signal together or independently to fulfill many important functions in... 
Rearranged during transfection | Parkinson disease | Drug addiction | Mouse model | Dopaminergic system | Glia cell line-derived neurotrophic factor | MAOA/MAOB | orphan nuclear receptor and transcription factor | cytoplasmic SH2 domain containing protein tyrosine phosphatase | Ras | RRF | COMT | PTEN-induced putative kinase 1 | SH3 and multiple ankyrin repeat domains 3, proline-rich synapse-associated protein 2 (ProSAP2) | PI3K | sorting protein-related receptor with A-type repeats, a member of the mammal Vps10p domain receptor | subunits of the Ca2+-sensitive, voltage gated A-type K+ channel | SH2 domain containing transforming protein 1 | Nurr1 | proprotein convertases | protein kinase B, serine/threonine-specific protein kinase | calcium-calmodulin-dependent protein kinase II β isoform | FRS2 | phosphatase and tensin homolog | catecholamine | SHP-2 | growth factor receptor-bound protein 2, 7 and 10, adaptor proteins | fibroblast growth factor receptor substrate 2, adaptor protein | monoamine oxidases A and B | carbonyl cyanide m-chlorophenyl hydrazone | ERK | brain derived neurotrophic factor | deglycase, oxidative stress sensor and redox-sensitive chaperone and protease | VTA | tyrosines, which can be phosphorylated | cAMP | extracellular-signal-regulated kinases, classical MAPKs | CaMKIIβ | Kv4.3 and KChip3 | GRB2/7/10 | Ser/Thr | SNP | endoplasmatic reticulum | nerve growth factor | monoamine, neurotransmitter type including dopamine, epinephrine (adrenaline) and norepinephrine (noradrenaline) | TGF-β | Akt, PKB | phospholipase γ cleaves the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) ppp3R1/ppp3CB, calcineurin subunits | PC5A, PC5B, and PC7 | EGR1 | proprotein convertase subtilisin/kexin type 6 | substantia nigra | phosphotyrosine-interaction domain | BDNF | adaptor protein of the PDZ-LIM family | γ-aminobutyric acid, inhibitory neurotransmitter in mammalian central nervous system | Tyr | FosB/ΔFosB | IRS1/2 | LIM | dopamine transporter | enhanced green fluorescent protein | GDNF | DAT | SOS | 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine | retro-rubal field | transforming growth factor β is a secreted protein that controls proliferation and cellular differentiation | MPTP | GTPase | hypoxia-inducible factor-1alpha | GDNF family of ligands | Ret | GPI | Shank3 | NCAM | Enigma | JNK | (rearranged during transfection) canonical GDNF receptor, a receptor tyrosine kinase | PTEN | 6-OHDA | DJ-1 | (rapidly accelerated fibrosarcoma/rat fibrosarcoma) family of serine/threonine-protein kinase | SHC | NF-κB | (acronym combining the first letters of three proteins – post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) that have this common domain) protein interaction domain | phosphotyrosine-binding domains | insulin receptor substrate 1, adaptor protein, contains a PTB and PH domain | Rac1 | GFRα | nuclear factor ‘kappa-light-chain-enhancer’ of activated B-cells, transcription factor family with Rel homology domain (RHD) | catechol-O-methyltransferase | early growth response protein 1, Zif268 (zinc finger protein 225), NGFI-A (nerve growth factor-induced protein A), is a zinc finger transcription factor | serine and threonine, which can be phosphorylated | GDNF family receptor α | PKA | protein kinase A, a family of cAMP-dependent protein kinase | MAPK | NGF | SorLA | ventral tegmental area | son of sevenless, family of guanine nucleotide exchange factors that act on Ras | GABA | HIF-1a | Ras-related C3 botulinum toxin substrate 1 (Rho family), a small GTPase, like CDC42 | GAP1/2 | PTB | (Rat sarcoma) family of small membrane-associated GTPase | cycles between an active GTP-bound and an inactive GDP-bound state | glycogen synthase kinase 3β | Src | glia cell line-derived neurotrophic factor | PACE4, PCSK6 | pleckstrin homology domain | co-repressor for element-1-silencing transcription factor, a chromatin-modifying corepressor complex that acts with REST (repressor for element-1 silencing transcription factor) complex | c-Jun N-terminal kinases, members of the MAPK family of proteins | EGFP | cell division control protein 42 homolog, a plasma membrane-associated small GTPase of the Rho family | (acronym combining the first letters of three proteins – Lin11, Isl-1 and Mec-3 – that have this common domain) protein interaction domain of two contiguous zinc finger domains, separated by a two-amino acid residue hydrophobic linker | CCCP | (sarcoma protein) membrane-associated tyrosine kinase with different Src homology (SH) domains characteristic for all 9 members of the Src family kinases | DOK1/4/5/6 | (Ras homolog) family of small GTPases including Cdc42, Rac1, and RhoA | single-nucleotide polymorphism analysis | VPS10P | Rho | MEN2B | phosphatidylinositol-4,5-bisphosphate 3-kinase | 6-hydroxy-dopamine | mitogen-activated protein kinase, can phosphorylate serine, threonine, and tyrosine, e.g. p38MAPK | Cdc42 | docking proteins, have a PH and SH3 domain | GFLs | PDZ | vacuolar protein sorting 10 protein-domain receptors are type 1 transmembrane proteins | PLCγ | GTPase-activating proteins 1 and 2 | 3′,5′-cyclic adenosine monophosphate | neuronal cell adhesion molecule | TIEG | TGF-β-inducible early-response gene, a zinc finger transcription factor Vav2, adaptor protein and guanine nucleotide exchange factor for the Rho family of Ras-related GTPases | PINK1 | Raf | CoREST | multiple endocrine neoplasia 2 type B, mutation in the kinase domain of the Ret leading to constitutive active receptor | dopaminergic | glycosylphosphatidylinositol | FBJ murine osteosarcoma viral oncogene homolog B, a transcription factor with a truncated Δ form | gsk3β | ENTERIC NERVOUS-SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBSTANTIA-NIGRA | CELL BIOLOGY | MICE LACKING GDNF | C-RET | BIOPHYSICS | NEUROTROPHIC FACTOR PROMOTES | MULTIPLE ENDOCRINE NEOPLASIA | SURVIVAL IN-VIVO | RECEPTOR TYROSINE KINASE | CELL-LINE | EARLY-ONSET PARKINSONISM | Glial Cell Line-Derived Neurotrophic Factor - physiology | Parkinson Disease - pathology | Animals | Proto-Oncogene Proteins c-ret - physiology | Dopamine - physiology | Mesencephalon - metabolism | Humans | Dopaminergic Neurons - physiology | Parkinson Disease - metabolism | Synaptic Transmission | Mesencephalon - pathology | Physiological aspects | Neurons | Parkinson's disease
Journal Article
Neuron, ISSN 0896-6273, 2004, Volume 43, Issue 4, pp. 563 - 574
The synapse contains densely localized and interacting proteins that enable it to adapt to changing inputs. We describe a Ca 2+-sensitive protein complex... 
CAMKII | DOMAIN-CONTAINING PROTEINS | SYNGAP | RAS-GTPASE | PDZ DOMAINS | GTPASE-ACTIVATING PROTEIN | MOLECULAR-BASIS | NEUROSCIENCES | CULTURED HIPPOCAMPAL-NEURONS | CEREBRAL-CORTEX | PLASTICITY | Synaptic Transmission - physiology | Humans | Receptors, N-Methyl-D-Aspartate - metabolism | Molecular Sequence Data | Synapses - genetics | Receptors, N-Methyl-D-Aspartate - genetics | Transfection | Hippocampus - enzymology | Calcium-Calmodulin-Dependent Protein Kinase Type 2 | p38 Mitogen-Activated Protein Kinases | GTPase-Activating Proteins - physiology | Calcium-Calmodulin-Dependent Protein Kinases - physiology | Carrier Proteins - physiology | Amino Acid Sequence | Cell Line | Nerve Tissue Proteins - physiology | Calcium-Calmodulin-Dependent Protein Kinases - genetics | Synapses - physiology | ras GTPase-Activating Proteins | Rats | Synapses - enzymology | Receptors, N-Methyl-D-Aspartate - physiology | Carrier Proteins - genetics | Hippocampus - metabolism | Animals | Mitogen-Activated Protein Kinases - genetics | GTPase-Activating Proteins - genetics | Hippocampus - physiology | Mitogen-Activated Protein Kinases - metabolism | Proteins | Software | Kinases | Rodents | Mitogen-Activated Protein Kinases | GTPase-Activating Proteins | Receptors, N-Methyl-D-Aspartate | Nerve Tissue Proteins | Calcium-Calmodulin-Dependent Protein Kinases | Cellular Biology | Synaptic Transmission | Life Sciences | Synapses | Hippocampus | Carrier Proteins
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2015, Volume 10, Issue 2, p. e0117668
PDZ domains in general, and those of PSD-95 in particular, are emerging as promising drug targets for diseases such as ischemic stroke. We have previously... 
GLUTAMATE RECEPTORS | FLUORESCENCE POLARIZATION | RECEPTOR INTERACTION | DIMERIC INHIBITOR | PDZ DOMAIN | MULTIDISCIPLINARY SCIENCES | GUANYLATE KINASE PROTEINS | SUPERTERTIARY STRUCTURE | BINDING SELECTIVITY | ISCHEMIC BRAIN-DAMAGE | POSTSYNAPTIC DENSITY | Disks Large Homolog 4 Protein | Guanylate Kinases - genetics | Tumor Suppressor Proteins - antagonists & inhibitors | Guanylate Kinases - antagonists & inhibitors | Protein Multimerization | Intracellular Signaling Peptides and Proteins - metabolism | Peptides - metabolism | Adaptor Proteins, Signal Transducing - antagonists & inhibitors | Tumor Suppressor Proteins - genetics | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Binding, Competitive | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Peptides - chemistry | Membrane Proteins - genetics | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Nuclear Proteins - metabolism | Transcription Factors - antagonists & inhibitors | Binding Sites - genetics | Transcription Factors - genetics | Peptides - pharmacology | Transcription Factors - metabolism | Membrane Proteins - antagonists & inhibitors | Mutagenesis | Nuclear Proteins - antagonists & inhibitors | Adaptor Proteins, Signal Transducing - genetics | Guanylate Kinases - metabolism | PDZ Domains | Protein Binding | Ligands | Kinetics | Adaptor Proteins, Signal Transducing - metabolism | Fluorescence Polarization | Stroke (Disease) | Proteins | Cysteine | Chemical properties | Ischemia | Protein-protein interactions | Binding | Fluorescence polarization | Stroke | Disease | Peptides | Fluorescence | Biochemistry | Pharmacology | Kinases | Studies | Spectrometry | Inhibitors | Guanylate kinase | Rodents | Brain damage | Affinity | Postsynaptic density proteins | Protein interaction | Basic Medicine | Medical Biotechnology | Medical and Health Sciences | Microbiology in the medical area | Medicin och hälsovetenskap | Medicinska och farmaceutiska grundvetenskaper | Medicinsk bioteknologi | Mikrobiologi inom det medicinska området | Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) | Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2011, Volume 6, Issue 10, p. e25519
Background: Ankrd2 (also known as Arpp) together with Ankrd1/CARP and DARP are members of the MARP mechanosensing proteins that form a complex with titin... 
SKELETAL-MUSCLE | CARP | PDZ DOMAINS | MULTIDISCIPLINARY SCIENCES | GENE-EXPRESSION | ANKYRIN-REPEAT PROTEIN | NUCLEAR-PROTEIN | TIGHT JUNCTION | CELL | BINDING | FAMILY | Homeodomain Proteins - metabolism | Humans | Transcriptome | Muscle Proteins - deficiency | Muscle Fibers, Skeletal - metabolism | Promoter Regions, Genetic - genetics | RNA Interference | Repressor Proteins - deficiency | Nuclear Proteins - deficiency | Muscle Proteins - metabolism | Transcription, Genetic | Nuclear Proteins - genetics | Muscle, Striated - cytology | Repressor Proteins - metabolism | Cell Line | Tumor Suppressor Protein p53 - metabolism | Repressor Proteins - genetics | Nuclear Proteins - metabolism | MyoD Protein - metabolism | src Homology Domains | Muscle Proteins - genetics | Transcription Factors - metabolism | Homeobox Protein Nkx-2.5 | Mechanotransduction, Cellular | Animals | PDZ Domains | Muscle Fibers, Skeletal - cytology | Muscle, Striated - metabolism | Actin | Genes | Calpain | Bone morphogenetic proteins | Cellular signal transduction | DNA binding proteins | Genetic transcription | Transforming growth factors | Tumor proteins | Muscle proteins | Protein binding | Heart | Biotechnology | Transcription factors | Intercellular signalling | Connectin | Wnt protein | Calcium | Cardiomyopathy | p53 Protein | Homeostasis | Intracellular signalling | Feedback loops | Nuclei | Proteins | Signal transduction | Endocytosis | Pathways | Methyl-CpG binding protein | Rodents | DNA methylation | Localization | Nkx2.5 protein | Deoxyribonucleic acid--DNA | MyoD protein | Myotubes | Calcium (intracellular) | Carp | MAP kinase | Cardiomyocytes | Gene expression | Insulin | Skeletal muscle | Myoblasts | Pax6 protein | Musculoskeletal system | MeCP2 protein | Cytoskeleton | Genetic engineering | Mutation | Molecular biology | Cytoplasm | Apoptosis | Deoxyribonucleic acid | DNA
Journal Article
PLoS ONE, ISSN 1932-6203, 03/2014, Volume 9, Issue 3, p. e92259
ZASP is a cytoskeletal PDZ-LIM protein predominantly expressed in striated muscle. It forms multiprotein complexes and plays a pivotal role in the structural... 
SKELETAL-MUSCLE | SEVERE FORM | SARCOMERIC Z-DISC | MYOGENIC DIFFERENTIATION | MULTIDISCIPLINARY SCIENCES | PDZ | TRANSCRIPTIONAL REPRESSION | LIM-DOMAIN | DILATED CARDIOMYOPATHY | BINDING | ALPHA-ACTININ | Adaptor Proteins, Signal Transducing - chemistry | Proto-Oncogene Proteins c-mdm2 - genetics | Fluorescence Recovery After Photobleaching | Humans | Transcriptional Activation | LIM Domain Proteins - metabolism | Promoter Regions, Genetic - genetics | Protein Isoforms - metabolism | Muscle Proteins - metabolism | Binding Sites | Proto-Oncogene Proteins c-mdm2 - metabolism | LIM Domain Proteins - chemistry | Repressor Proteins - metabolism | bcl-2-Associated X Protein - genetics | Actinin - metabolism | Cell Line | Repressor Proteins - chemistry | Signal Transduction | Tumor Suppressor Protein p53 - metabolism | bcl-2-Associated X Protein - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Ankyrin Repeat | Nuclear Proteins - chemistry | Protein Transport | Animals | Intracellular Space - metabolism | Protein Binding | Mice | Muscle Proteins - chemistry | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Muscle, Striated - metabolism | Tumor proteins | Gene expression | Structural integrity | Competition | Heart | Neonates | Biotechnology | Alternative splicing | Bax protein | Cardiomyopathy | p53 Protein | Homology | Lethality | Compaction | Protein turnover | Proteins | SUMO protein | Signal transduction | Rodents | Cell cycle | Cardiology | Bioinformatics | MDM2 protein | Nomenclature | Muscles | Cell division | Muscle contraction | Ablation | Skeletal muscle | Mutants | Musculoskeletal system | Signaling | Dilated cardiomyopathy | Insects | LIM protein | Isoforms | Cytoskeleton | Genetic engineering | Ventricle | Sarcomeres | Binding sites | Tumors | Myopathy
Journal Article