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Biochemical Journal, ISSN 0264-6021, 03/2011, Volume 434, Issue 3, pp. 365 - 381
Iron is an essential but potentially hazardous biometal. Mammalian cells require sufficient amounts of iron to satisfy metabolic needs or to accomplish... 
Ferroportin | Iron-sulfur cluster (ISC) | Transferrin receptor (TfR) | Iron-regulatory protein 2 (IRP2) | Ferritin | Iron-regulatory protein 1 (IRP1) | ferritin | iron-sulfur cluster (ISC) | transferrin receptor (TfR) | OXIDATIVE STRESS | MAMMALIAN IRON | FE-S CLUSTER | iron-regulatory protein 2 (IRP2) | HEME-SYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | iron-regulatory protein 1 (IRP1) | ferroportin | AMYLOID PRECURSOR PROTEIN | RESPONSIVE ELEMENT | TRANSFERRIN-BOUND IRON | SULFUR CLUSTER BIOGENESIS | HEPCIDIN EXPRESSION | UBIQUITIN-PROTEASOME PATHWAY | Neoplasms - metabolism | Oxidation-Reduction | Response Elements | Humans | RNA, Messenger - genetics | RNA, Messenger - physiology | Mitochondria - metabolism | Iron - metabolism | Iron-Regulatory Proteins - genetics | Animals | Ferritins - metabolism | Biological Transport | Iron-Regulatory Proteins - physiology | Transferrin - metabolism | DHBA, dihydroxybenzoic acid | IRP, iron-regulatory protein | UTR, untranslated region | SLC, solute carrier | iron–sulfur cluster (ISC) | MRCKα, myotonic dystrophy kinase-related Cdc42 (cell division cycle 42)-binding kinase α | LIP, labile iron pool | Lcn2, lipocalin 2 | FLVCR, feline leukaemia virus, subgroup C, receptor | CIA, cytosolic ISC assembly | Cfd1, cytosolic Fe–S cluster-deficient protein 1 | BMP, bone morphogenetic protein | PCBP1, poly(rC)-binding protein 1 | Abcb, ATP-binding cassette, subfamily B | STAT3, signal transducer and activator of transcription 3 | SDH, succinate dehydrogenase | TfR, Tf receptor | c-aconitase, cytosolic aconitase | HIF, hypoxia-inducible factor | HO-1, haem oxygenase 1 | IRIDA, iron-refractory iron deficiency anaemia | ISC, iron–sulfur cluster | m-aconitase, mitochondrial aconitase | DMT1, divalent metal transporter 1 | Review | EBPα, CCAAT | IRE, iron-responsive element | IOP1, iron-only hydrogenase-like protein 1 | Nbp35, nucleotide-binding protein 35 | Skp1, S-phase kinase-associated protein 1 | Nfs, nitrogen fixation homologue | FBXL5, F-box and leucine-rich repeat protein 5 | ROS, reactive oxygen species | Tf, transferrin | enhancer-binding protein α | H, heavy | Isu, iron–sulfur cluster scaffold homologue | Rbx1, Ring-box 1 | β-APP, β-amyloid precursor protein | Dcytb, duodenal cytochrome b | Nar1, nuclear architecture-related protein 1 | ALAS, ALA synthase | NTBI, non-transferrin-bound iron | ALA, 5-aminolevulinic acid | Hpx, haemopexin | Cul1, Cullin 1 | Grx, glutaredoxin | ER, endoplasmic reticulum | L, light
Journal Article
Science, ISSN 0036-8075, 1/2009, Volume 323, Issue 5911, pp. 269 - 272
The Vibrio parahaemolyticus type III effector VopS is implicated in cell rounding and the collapse of the actin cytoskeleton by inhibiting Rho guanosine... 
Proteins | Phosphates | Enzymes | HeLa cells | Amino acids | Ions | Mass spectroscopy | Reports | Infections | Biochemistry | Post translational modification | ACTIVATION | PROTEIN | PARAHAEMOLYTICUS | MULTIDISCIPLINARY SCIENCES | III SECRETION SYSTEM | Phosphorylation | Threonine - chemistry | rho GTP-Binding Proteins - antagonists & inhibitors | Humans | Bacterial Proteins - chemistry | Molecular Sequence Data | rac GTP-Binding Proteins - metabolism | Vibrio parahaemolyticus - metabolism | cdc42 GTP-Binding Protein - metabolism | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | rac GTP-Binding Proteins - antagonists & inhibitors | Cell Shape | cdc42 GTP-Binding Protein - antagonists & inhibitors | rho GTP-Binding Proteins - chemistry | Binding Sites | Protein Structure, Tertiary | Amino Acid Sequence | Signal Transduction | Adenosine Monophosphate - metabolism | Bacterial Proteins - genetics | Mutant Proteins - metabolism | Vibrio parahaemolyticus - pathogenicity | Amino Acid Motifs | Mutant Proteins - chemistry | rho GTP-Binding Proteins - metabolism | rac GTP-Binding Proteins - chemistry | Bacterial Proteins - metabolism | cdc42 GTP-Binding Protein - chemistry | Protein Processing, Post-Translational | HeLa Cells | Genetic aspects | Chemical properties | Guanosine triphosphatase | Vibrio | Signal transduction | Eukaryotes | Cellular biology | Molecular biology | Binding sites
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2016, Volume 291, Issue 9, pp. 4323 - 4333
Invadosomes are actin-rich membrane protrusions that degrade the extracellular matrix to drive tumor cell invasion. Key players in invadosome formation are... 
Receptors, Lysophosphatidic Acid - metabolism | Lysophospholipids - metabolism | Receptors, G-Protein-Coupled - metabolism | Humans | Extracellular Matrix - metabolism | Melanoma - enzymology | Podosomes - enzymology | Neoplasm Proteins - antagonists & inhibitors | Receptors, Lysophosphatidic Acid - agonists | Receptors, Lysophosphatidic Acid - genetics | cdc42 GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - metabolism | rhoA GTP-Binding Protein - genetics | Endothelins - metabolism | Neoplasm Proteins - metabolism | Time-Lapse Imaging | Podosomes - metabolism | RNA Interference | cdc42 GTP-Binding Protein - antagonists & inhibitors | Fluorescence Resonance Energy Transfer | Receptors, Lysophosphatidic Acid - antagonists & inhibitors | Neoplasm Proteins - genetics | Biomarkers - metabolism | Melanoma - metabolism | Recombinant Proteins - metabolism | rac1 GTP-Binding Protein - agonists | rhoA GTP-Binding Protein - antagonists & inhibitors | Recombinant Proteins - genetics | Melanoma - pathology | cdc42 GTP-Binding Protein - agonists | Hydrolysis | Podosomes - pathology | Microscopy, Confocal | Neoplasm Proteins - agonists | cdc42 GTP-Binding Protein - genetics | Receptors, G-Protein-Coupled - antagonists & inhibitors | rac1 GTP-Binding Protein - antagonists & inhibitors | Cell Line, Tumor | Luminescent Proteins - genetics | Receptors, G-Protein-Coupled - genetics | Extracellular Matrix - pathology | Microscopy, Fluorescence | rac1 GTP-Binding Protein - metabolism | Luminescent Proteins - metabolism | rac1 GTP-Binding Protein - genetics | CDC42 | invadopodia | biosensor | fluorescence resonance energy transfer (FRET) | calcium intracellular release | G protein-coupled receptor (GPCR) | Rho (Rho GTPase) | phosphatidylinositide 3-kinase (PI 3-kinase) | imaging | Rac (Rac GTPase) | Cell Biology
Journal Article
The New England Journal of Medicine, ISSN 0028-4793, 12/2011, Volume 365, Issue 25, pp. 2377 - 2388
The authors report that INF2 mutations are present in patients with focal segmental glomerulosclerosis (FSGS) associated with Charcot–Marie–Tooth neuropathy.... 
GLOMERULOSCLEROSIS | MEDICINE, GENERAL & INTERNAL | MYELIN | PROTEIN | NEUROPATHY | EPITHELIAL-CELLS | GENE | RHO | MEDIATED TRANSPORT | FORMIN | NEPHROPATHY | Humans | Middle Aged | Proteolipids - metabolism | Actins - metabolism | Male | Charcot-Marie-Tooth Disease - genetics | Young Adult | Kidney - metabolism | Glomerulosclerosis, Focal Segmental - etiology | Myelin and Lymphocyte-Associated Proteolipid Proteins | Adult | Female | Membrane Transport Proteins - metabolism | Microfilament Proteins - metabolism | Child | Microfilament Proteins - genetics | Charcot-Marie-Tooth Disease - complications | Schwann Cells - metabolism | Phenotype | Animals | Adolescent | Age of Onset | Heterozygote | Mice | Mutation | Myelin Proteins - metabolism | Glomerulonephritis | Gene mutations | Charcot-Marie-Tooth disease | Causes of | Genetic aspects | Research | Myelin proteins | Cdc42 protein | Disease | Exons | Genes | Amino acids | Nervous system | Neuropathy | Guanine nucleotide-binding protein | Proteins | Myelin P0 protein | Localization | Peripheral myelin protein 22 | Deoxyribonucleic acid--DNA | Kidneys | Schwann cells | Polymerization | Myelination | Genotyping | Biopsy | Glomerulus | Cytoskeleton | Genetic testing | Cytoplasm | Guanosinetriphosphatase | Schwann Cells | Genomics | Kidney | Charcot-Marie-Tooth Disease | Life Sciences | Proteolipids | Biochemistry, Molecular Biology | Actins | Microfilament Proteins | Membrane Transport Proteins | Myelin Proteins | Glomerulosclerosis, Focal Segmental
Journal Article
Science, ISSN 0036-8075, 7/2009, Volume 325, Issue 5936, pp. 83 - 87
Type IV pili mediate the initial interaction of many bacterial pathogens with their host cells. In Neisseria meningitidis, the causative agent of cerebrospinal... 
Intercellular junctions | Cell lines | Actins | Small interfering RNA | Bacteria | Cadherins | Reports | Bacterial adhesion | Infections | Blood brain barrier | Endothelial cells | CDC42 | ADHESION | HUMAN EPITHELIAL-CELLS | PATHOGENIC NEISSERIA | TWITCHING MOTILITY | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | BARRIER | PAR3 | RECEPTOR | ADHERENS | Cell Polarity | Brain - microbiology | Cadherins - metabolism | Humans | cdc42 GTP-Binding Protein - metabolism | Intercellular Junctions - microbiology | Phosphoproteins - metabolism | Blood-Brain Barrier - microbiology | Antigens, CD - metabolism | Catenins | Endothelial Cells - microbiology | Endothelium, Vascular - ultrastructure | Brain - blood supply | Protein Kinase C - metabolism | Membrane Proteins - metabolism | Neisseria meningitidis - physiology | Neisseria meningitidis - pathogenicity | Cell Line | Brain - cytology | Endothelial Cells - metabolism | Cell Cycle Proteins - metabolism | Intercellular Junctions - metabolism | Cell Adhesion Molecules - metabolism | Blood-Brain Barrier - metabolism | Endothelium, Vascular - microbiology | Bacterial Adhesion | Endothelium, Vascular - metabolism | Fimbriae, Bacterial - physiology | Adaptor Proteins, Signal Transducing - metabolism | Intercellular Junctions - ultrastructure | Measurement | Polarity (Biology) | Neisseria meningitidis | Properties | Health aspects | Endothelium | Brain | Meningitis | Eukaryotes | Cell adhesion & migration | Fimbriae, Bacterial | Endothelial Cells | Cell Adhesion Molecules | Intercellular Junctions | Membrane Proteins | Life Sciences | Microbiology and Parasitology | Adaptor Proteins, Signal Transducing | Phosphoproteins | cdc42 GTP-Binding Protein | Endothelium, Vascular | Cell Cycle Proteins | Antigens, CD | Protein Kinase C | Blood-Brain Barrier | cytology | meningitis | microbiology | physiology | ultrastructure | blood brain barrier | pathogenicity | blood supply | metabolism
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 1/2005, Volume 168, Issue 3, pp. 441 - 452
Invadopodia are actin-rich membrane protrusions with a matrix degradation activity formed by invasive cancer cells. We have studied the molecular mechanisms of... 
Receptors | Microfilaments | Actin depolymerizing factors | Small interfering RNA | Actins | Antibodies | Polymerization | Cultured cells | Cell membranes | Cells | CARCINOMA-CELLS | GROWTH-FACTOR RECEPTOR | MAMMARY ADENOCARCINOMA | ACTIN POLYMERIZATION | LAMELLIPOD EXTENSION | N-WASP | EXTRACELLULAR-MATRIX | SPECIALIZED SURFACE PROTRUSIONS | ALDRICH-SYNDROME PROTEIN | INVASIVE CELLS | CELL BIOLOGY | Oncogene Proteins - genetics | RNA, Small Interfering - genetics | Epidermal Growth Factor - physiology | Cytoskeletal Proteins - genetics | Actins - metabolism | Microfilament Proteins - physiology | Extracellular Matrix - metabolism | cdc42 GTP-Binding Protein - metabolism | Quinazolines | Oncogene Proteins - physiology | Cell Movement - physiology | Transfection | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Cytoskeletal Proteins - physiology | Wiskott-Aldrich Syndrome Protein Family | Microfilament Proteins - genetics | Carrier Proteins - physiology | Nerve Tissue Proteins - physiology | Wiskott-Aldrich Syndrome Protein, Neuronal | Cell Surface Extensions - metabolism | Neoplasm Invasiveness | RNA, Small Interfering - pharmacology | Enzyme Inhibitors - pharmacology | Oncogene Proteins - metabolism | Rats | Tyrphostins - pharmacology | Actin Depolymerizing Factors | cdc42 GTP-Binding Protein - physiology | Nerve Tissue Proteins - genetics | Fibronectins - metabolism | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Adaptor Proteins, Signal Transducing - physiology | Animals | Carrier Proteins - metabolism | GRB2 Adaptor Protein | Models, Biological | cdc42 GTP-Binding Protein - genetics | Cell Surface Extensions - drug effects | Adaptor Proteins, Signal Transducing - genetics | Actin-Related Protein 2 | Cell Line, Tumor | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Actin-Related Protein 3 | Adaptor Proteins, Signal Transducing - metabolism | Microscopy, Fluorescence | Cell Surface Extensions - physiology | Epidermal growth factor | Metastasis | Cancer invasiveness | Cancer cells
Journal Article
Structure, ISSN 0969-2126, 09/2016, Volume 24, Issue 9, pp. 1499 - 1508
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 27, pp. 11361 - 11373
Journal Article
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 | 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 | sensitive, voltage gated A-type K+ channel | 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 | subunits of the Ca | (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 | proprotein convertase subtilisin | 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 | exin type 6 | 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