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Cellular Signalling, ISSN 0898-6568, 2006, Volume 18, Issue 5, pp. 579 - 591
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 10/2018, Volume 19, Issue 10, p. 3282
The protein tyrosine phosphatase interacting protein 51 (PTPIP51) regulates and interconnects signaling pathways, such as the mitogen-activated protein kinase... 
Mitogen-activated protein kinase pathway (MAPK pathway) | Protein-protein interaction (PPI) | Protein tyrosine phosphatase interacting protein 51 (PTPIP51) | Cancer signaling | SIGNALING PATHWAYS | cancer signaling | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACUTE MYELOID-LEUKEMIA | mitogen-activated protein kinase pathway (MAPK pathway) | TRASTUZUMAB RESISTANCE | CHEMISTRY, MULTIDISCIPLINARY | BREAST-CANCER | GROWTH-FACTOR RECEPTOR | METASTATIC MELANOMA | MOLECULAR TARGETS | INSULIN-RESISTANCE | protein tyrosine phosphatase interacting protein 51 (PTPIP51) | THERAPEUTIC TARGET | protein-protein interaction (PPI) | GLIOBLASTOMA CELLS | Protein Binding - genetics | Humans | Protein Tyrosine Phosphatases - metabolism | Mitochondrial Proteins - genetics | Signal Transduction - genetics | Protein Tyrosine Phosphatases - genetics | Animals | Mitochondrial Proteins - metabolism | Mitogen-Activated Protein Kinases - genetics | Signal Transduction - physiology | Gene Expression Regulation, Neoplastic - physiology | Gene Expression Regulation, Neoplastic - genetics | Mitogen-Activated Protein Kinases - metabolism | Protein Binding - physiology | Phosphorylation | Leukemia | Serine | Raf protein | AKT protein | Cell interactions | Kinases | Phosphatase | Cell adhesion & migration | Proteins | Signal transduction | Epidermal growth factor | Growth factors | Tyrosine | NF-κB protein | Epidermal growth factor receptors | MAP kinase | Src protein | Organelles | ErbB-2 protein | Signaling | 14-3-3 protein | Protein kinase | Scaffolding | Medical prognosis | Mutation | Scaffolds | Binding sites | Metabolic disorders | Apoptosis | Protein-tyrosine-phosphatase
Journal Article
PLoS ONE, ISSN 1932-6203, 08/2014, Volume 9, Issue 8, p. e105688
Journal Article
Nature Communications, ISSN 2041-1723, 12/2019, Volume 10, Issue 1, pp. 261 - 17
Bacterial growth and cell division requires precise spatiotemporal regulation of the synthesis and remodelling of the peptidoglycan layer that surrounds the... 
MINICELL LOCUS | STREPTOCOCCUS-PNEUMONIAE | FTSZ | MULTIDISCIPLINARY SCIENCES | GROWTH | PENICILLIN-BINDING PROTEIN | COMPONENT | IDENTIFICATION | PEPTIDOGLYCAN SYNTHESIS | DIVISION | REQUIREMENT | Virulence Factors - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Penicillin-Binding Proteins - genetics | Protein Interaction Maps | Cell Cycle Proteins - chemistry | Recombinant Proteins - isolation & purification | Penicillin-Binding Proteins - chemistry | Streptococcus pneumoniae - metabolism | Cell Division | Cell Cycle Proteins - genetics | Listeria monocytogenes - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Cell Cycle Proteins - isolation & purification | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Recombinant Proteins - chemistry | Virulence Factors - isolation & purification | Recombinant Proteins - genetics | Virulence Factors - chemistry | Penicillin-Binding Proteins - metabolism | Amino Acid Motifs | Peptidoglycan - biosynthesis | Penicillin-Binding Proteins - isolation & purification | Mutagenesis | Cell Wall - metabolism | Bacterial Proteins - metabolism | Cytosol - metabolism | Virulence Factors - metabolism | Bacterial Proteins - isolation & purification | Bacillus subtilis - metabolism | Enzymes | Cell walls | Peptidoglycans | Cell division | Listeria monocytogenes | Membrane proteins | Streptococcus infections | Proteins | Domains | Synthesis | Listeria | Scaffolding | Penicillin | Cell cycle | Bacteria | Viability
Journal Article
Antioxidants & Redox Signaling, ISSN 1523-0864, 03/2017, Volume 26, Issue 9, pp. 432 - 444
Significance: Cellular metabolic activity impacts the production of reactive oxygen species (ROS), both positively through mitochondrial oxidative processes... 
Forum Review Articles | oxidative stress | INITIATING CELLS | fatty acid metabolism | BIOCHEMISTRY & MOLECULAR BIOLOGY | PML NUCLEAR-BODIES | CYTOPLASMIC PML | DNA-DAMAGE | PML nuclear bodies | RAR-ALPHA | ARSENIC TRIOXIDE | BREAST-CANCER | FATTY-ACID OXIDATION | HEMATOPOIETIC STEM-CELLS | ENDOCRINOLOGY & METABOLISM | TUMOR-SUPPRESSOR PROTEIN | cancer | Intranuclear Inclusion Bodies - chemistry | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Oxidative Stress | Signal Transduction | Humans | Intranuclear Inclusion Bodies - genetics | Tumor Suppressor Protein p53 - metabolism | Nuclear Proteins - metabolism | Promyelocytic Leukemia Protein - chemistry | Nuclear Proteins - chemistry | Autophagy | Protein Transport | Animals | Energy Metabolism | Promyelocytic Leukemia Protein - metabolism | Protein Binding | Sumoylation | Protein Interaction Domains and Motifs | Protein Processing, Post-Translational | Nuclear Proteins - genetics | Intranuclear Inclusion Bodies - metabolism | Promyelocytic Leukemia Protein - genetics | Care and treatment | Reactive oxygen species | Myelocytic leukemia | Cancer cells | Nonlymphoid leukemia | Rapamycin | Dosage and administration | Research | TOR protein | Oxidative stress | Regulators | Senescence | Oxidative metabolism | Leukemia | p53 Protein | AKT protein | Proteins | SUMO protein | Promyeloid leukemia | Mitochondria | Cell fate | Post-translation | Oxidation | NADP | Glutathione | Cellular manufacture | Cell survival | Stability | Reducing agents | Metabolism | SIRT1 protein | Fatty acids | Biological activity | Promyelocytic leukemia protein | Scaffolding | Cell death | Tumor suppressor genes | Cancer
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 12/2017, Volume 493, Issue 4, pp. 1384 - 1389
Scaffold proteins play a pivotal role in making protein complexes, and organize binding partners into a functional unit to enhance specific signaling pathways.... 
VCP | Proteomics | IQGAP1 | TARGET | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PAGET-DISEASE | CDC42 | EFFECTOR | BIOPHYSICS | RAC1 | BINDING | SCAFFOLDING PROTEINS | Immunohistochemistry | ras GTPase-Activating Proteins - chemistry | Humans | Valosin Containing Protein | Osteitis Deformans - metabolism | Osteitis Deformans - genetics | Cell Cycle Proteins - chemistry | Frontotemporal Dementia - metabolism | ras GTPase-Activating Proteins - genetics | Muscular Dystrophies, Limb-Girdle - genetics | HEK293 Cells | Cell Cycle Proteins - genetics | Neurons - metabolism | Protein Interaction Domains and Motifs | Frontotemporal Dementia - genetics | Recombinant Proteins - metabolism | ras GTPase-Activating Proteins - metabolism | Mutagenesis, Site-Directed | Cell Cycle Proteins - metabolism | Mutant Proteins - genetics | Adenosine Triphosphatases - metabolism | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Myositis, Inclusion Body - genetics | Hippocampus - metabolism | Muscular Dystrophies, Limb-Girdle - metabolism | Mutant Proteins - chemistry | Adenosine Triphosphatases - chemistry | Myositis, Inclusion Body - metabolism | Adenosine Triphosphatases - genetics | HeLa Cells | Amino Acid Substitution | Proteins | Physiological aspects | Protein binding | Medical colleges | Neurons | Index Medicus
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 8/2015, Volume 72, Issue 16, pp. 3009 - 3035
Transglutaminase 2 (TG2) is a ubiquitously expressed member of an enzyme family catalyzing Ca2+-dependent transamidation of proteins. It is a multifunctional... 
Life Sciences | Biochemistry, general | Anti-TG2 antibodies | Life Sciences, general | Scaffolding | Intrinsically disordered regions | Non-enzymatic interactions | Transglutaminase 2 | Biomedicine general | Cell Biology | TRANSDAB database | GTP-BINDING PROTEIN | SWISS 3T3 FIBROBLASTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | COAGULATION FACTOR-XIII | HUMAN-ERYTHROCYTE TRANSGLUTAMINASE | CEREBELLAR GRANULE CELLS | CELL BIOLOGY | CELL-SURFACE TRANSGLUTAMINASE | GUANINE-NUCLEOTIDE-BINDING | HEPARAN-SULFATE PROTEOGLYCANS | CATALYZED CROSS-LINKING | TISSUE-TYPE TRANSGLUTAMINASE | GTP-Binding Proteins - physiology | GTP-Binding Proteins - immunology | Gene Expression Regulation - genetics | Syndecan-4 - metabolism | Humans | Gene Expression Regulation - physiology | Models, Molecular | Receptors, LDL - metabolism | Integrins - metabolism | Cell Movement - physiology | Fibronectins - metabolism | Transglutaminases - immunology | Protein Interaction Mapping | Cell Adhesion - physiology | Transglutaminases - metabolism | Antibodies - immunology | Transglutaminases - physiology | Protein Conformation | GTP-Binding Proteins - metabolism | Receptors, Growth Factor - metabolism | Viral antibodies | Enzymes | Crosslinked polymers | Analysis | Stem cells | Physiological aspects | Antibodies | Protein kinases | Protein binding | Proteins | Extracellular matrix | Catalysts | Cellular biology | Kinases
Journal Article
Science Signaling, ISSN 1945-0877, 01/2017, Volume 10, Issue 463, p. eaai9219
Journal Article