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biochemistry & molecular biology (33) 33
animals (26) 26
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s100 proteins (5) 5
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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2012, Volume 109, Issue 16, pp. 6048 - 6053
S100A4 is a member of the S100 family of calcium-binding proteins that is directly involved in tumor metastasis. It binds to the nonmuscle myosin IIA (NMIIA)... 
Proteins | Stoichiometry | Atomic interactions | Ligands | Dimers | Biochemistry | Titration | Metastasis | Binding sites | Crystal structure | binding | Myosin filaments | Cell migration | Protein-protein interactions | MTS1 | TERMINAL DOMAIN | MULTIDISCIPLINARY SCIENCES | ANNEXIN-II | KINASE-C | FILAMENT FORMATION | METASTASIS-ASSOCIATED PROTEIN | S100 PROTEINS | myosin filaments | protein-protein interactions | NONMUSCLE MYOSIN | Ca2+-binding | CIRCULAR-DICHROISM | cell migration | HEAVY-CHAIN PHOSPHORYLATION | Protein Structure, Tertiary | Protein Structure, Secondary | S100 Calcium-Binding Protein A4 | Humans | Protein Multimerization | Models, Molecular | Crystallography, X-Ray | S100 Proteins - metabolism | S100 Proteins - chemistry | Nonmuscle Myosin Type IIA - metabolism | S100 Proteins - genetics | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Protein Binding | Calorimetry | Mutation | Nonmuscle Myosin Type IIA - chemistry | Binding Sites | Circular Dichroism | Physiological aspects | Research | Structure | Myosin | Crystals | Protein binding | protein–protein interactions | Biological Sciences | calcium | Biokemi och molekylärbiologi | metastasis | motor protein | Strukturbiologi | Structural Biology | Cell and Molecular Biology | Biochemistry and Molecular Biology | cancer | protein binding | Cell- och molekylärbiologi
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2017, Volume 12, Issue 5, pp. e0177489 - e0177489
Journal Article
Journal Article
The FEBS Journal, ISSN 1742-464X, 01/2018, Volume 285, Issue 1, pp. 46 - 71
Assembly and disassembly of protein–protein complexes needs to be dynamically controlled and phosphoswitches based on linear motifs are crucial in this... 
mitogen‐activated kinases | PDZ domain | protein phosphorylation | extracellular signal–regulated kinase | linear‐binding motif | signal transduction | mitogen-activated kinases | linear-binding motif | LOCALIZATION | extracellular signal-regulated kinase | DOMAIN | ACTIVATION | PROTEIN | SPECIFICITY | PHOSPHORYLATION | MAP KINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | MAGI-1 PDZ1 | BINDING | Phosphorylation | Mitogen-Activated Protein Kinase 3 - genetics | Signal Transduction | Humans | Serine - genetics | Substrate Specificity | Crystallography, X-Ray | Binding Sites - genetics | Ribosomal Protein S6 Kinases, 90-kDa - chemistry | Serine - chemistry | Serine - metabolism | Molecular Dynamics Simulation | Mitogen-Activated Protein Kinase 1 - chemistry | Ribosomal Protein S6 Kinases, 90-kDa - metabolism | Mitogen-Activated Protein Kinase 3 - metabolism | Mitogen-Activated Protein Kinase 1 - genetics | Ribosomal Protein S6 Kinases, 90-kDa - genetics | HEK293 Cells | Protein Binding | Protein Conformation | Enzyme Activation | Mitogen-Activated Protein Kinase 3 - chemistry | Mitogen-Activated Protein Kinase 1 - metabolism | Cellular signal transduction | Epidermal growth factor | Mitogens | Protein kinases | Protein-protein interactions | Protein binding | Binding | Residues | Nuclear magnetic resonance--NMR | Switches | Extracellular signal-regulated kinase | Kinases | Masks | Substrates | Data bases | MAGI-1 protein | Proteins | Dynamic control | Cores | Ribosomal protein S6 kinase | Signaling | Allosteric properties | Databases | Signal processing | Protein interaction | Dismantling
Journal Article
ISSN 1742-4658, 2017
Assembly and disassembly of protein–protein complexes needs to be dynamically controlled and phosphoswitches based on linear motifs are crucial in this... 
Journal Article
Structure, ISSN 0969-2126, 08/2017, Volume 25, Issue 8, pp. 1195 - 1207.e5
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 4, p. e18818
Journal Article
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 8110 - 11
Sodium channel inhibitor drugs decrease pathological hyperactivity in various diseases including pain syndromes, myotonia, arrhythmias, nerve injuries and... 
Channel opening | Pain | Sodium | Channel gating | Hyperactivity | Myotonia | Drug development | Gating | Conformation
Journal Article