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The FASEB Journal, ISSN 0892-6638, 11/2017, Volume 31, Issue 11, pp. 4720 - 4733
.... Here, we show that both bone morphogenetic protein 2 (BMP2) and BMP6 are proangiogenic in vitro and ex vivo and that the BMP type I receptors, activin receptor‐like kinase 3 (ALK3... 
cell migration | ALK2 | ALK3 | p38 MAPK | SMAD1/5 | MIGRATION | ACTIVATION | TGF-BETA | VEGF | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | NOTCH | ALK1 | CELL BIOLOGY | ENDOTHELIAL-CELLS | BIOLOGY | EXPRESSION | BINDING | MAP Kinase Signaling System - physiology | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Vascular Endothelial Growth Factor A - metabolism | Vascular Endothelial Growth Factor A - genetics | Vascular Endothelial Growth Factor Receptor-2 - genetics | HSP27 Heat-Shock Proteins - genetics | Intercellular Signaling Peptides and Proteins - metabolism | Bone Morphogenetic Protein 6 - genetics | Smad5 Protein - metabolism | Bone Morphogenetic Protein 2 - metabolism | Human Umbilical Vein Endothelial Cells - cytology | Smad1 Protein - genetics | p38 Mitogen-Activated Protein Kinases - metabolism | Smad5 Protein - genetics | Bone Morphogenetic Protein 2 - genetics | Intercellular Signaling Peptides and Proteins - genetics | Bone Morphogenetic Protein Receptors, Type I - genetics | Vascular Endothelial Growth Factor Receptor-2 - metabolism | p38 Mitogen-Activated Protein Kinases - genetics | Activin Receptors, Type I - metabolism | Bone Morphogenetic Protein Receptors, Type I - metabolism | Activin Receptors, Type I - genetics | Neovascularization, Physiologic - physiology | Bone Morphogenetic Protein 6 - metabolism | HSP27 Heat-Shock Proteins - metabolism | Smad1 Protein - metabolism | Complex formation | Genes | Clinical trials | Cell adhesion & migration | Proteins | Angiogenesis | Signal transduction | Receptors | Pathways | Vascular endothelial growth factor | Protein-tyrosine kinase | Enhancer-of-split protein | Bone morphogenetic protein 6 | Tyrosine | Medical research | Bone morphogenetic protein 2 | Heat shock proteins | Gene expression | Spheroids | Endothelial cells | Bone morphogenetic protein receptor type I | Endothelium | Signaling | Antiangiogenics | Hsp27 protein | Activin | Cell migration | Heat shock | SMAD1 | Research
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 8, pp. 2687 - 2700
The microtubule-associated protein tau forms insoluble, amyloid-type aggregates in various dementias, most notably Alzheimer's disease... 
HEAT-SHOCK PROTEINS | NEUROFIBRILLARY TANGLES | OXIDATIVE STRESS | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FRONTOTEMPORAL DEMENTIA | PAIRED HELICAL FILAMENTS | ALPHA-B-CRYSTALLIN | PLASTICITY DEFICITS | BETA-STRUCTURE | AGGREGATION | HSP27 Heat-Shock Proteins - chemistry | HSC70 Heat-Shock Proteins - metabolism | Humans | tau Proteins - metabolism | Amyloid - chemistry | Amyloid - ultrastructure | HSC70 Heat-Shock Proteins - ultrastructure | Recombinant Fusion Proteins - metabolism | tau Proteins - chemistry | HSP27 Heat-Shock Proteins - genetics | HSP27 Heat-Shock Proteins - ultrastructure | Protein Isoforms - metabolism | tau Proteins - genetics | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Protein Isoforms - chemistry | Amyloid - drug effects | Protein Interaction Domains and Motifs | Dimerization | Heparin - pharmacology | tau Proteins - ultrastructure | HSC70 Heat-Shock Proteins - genetics | Solubility | Models, Molecular | Recombinant Fusion Proteins - chemistry | Down-Regulation - drug effects | Amino Acid Motifs | Cryoelectron Microscopy | HSC70 Heat-Shock Proteins - chemistry | Anticoagulants - pharmacology | HSP27 Heat-Shock Proteins - metabolism | Kinetics | Mutation | Protein Aggregation, Pathological - metabolism | Amino Acid Substitution | Protein Structure and Folding | amyloid | chaperone | 70 kilodalton heat shock protein (Hsp70) | tau | aggregation | small heat shock protein (sHsp)
Journal Article
Cell stress & chaperones, ISSN 1355-8145, 9/2010, Volume 15, Issue 5, pp. 567 - 582
A number of missense mutations in the two related small heat shock proteins HspB8 (Hsp22) and HspB1 (Hsp27... 
Proteins | Motor neurons | RNA | Complementary DNA | Neurons | Antibodies | Small heat shock proteins | Genetic mutation | SMN complex proteins | Cell extracts | Motor neuropathy | DEAD-BOX PROTEIN | MARIE-TOOTH-DISEASE | Protein-protein interaction | SMALL HEAT-SHOCK-PROTEIN-22 | ALPHA-B-CRYSTALLIN | NEURON SMN PROTEIN | UMCG Approved | HEAT-SHOCK-PROTEIN | Survival-of-motor-neurons protein | CHAPERONE ACTIVITY | BREAST-CANCER CELLS | SPINAL MUSCULAR-ATROPHY | Charcot-Marie-Tooth disease | Ddx20 | Heat shock protein B8 | HUMAN NEUROMUSCULAR DISORDERS | CELL BIOLOGY | HSP27 Heat-Shock Proteins - chemistry | Immunoprecipitation | Humans | Isoelectric Focusing | Molecular Sequence Data | Survival of Motor Neuron 1 Protein - chemistry | HSP27 Heat-Shock Proteins - genetics | Heat-Shock Proteins - genetics | DEAD Box Protein 20 - genetics | Survival of Motor Neuron 1 Protein - genetics | DEAD Box Protein 20 - metabolism | Fluorescence Resonance Energy Transfer | Charcot-Marie-Tooth Disease - metabolism | Protein-Serine-Threonine Kinases - metabolism | Amino Acid Sequence | Cell Line | Heat-Shock Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Survival of Motor Neuron 1 Protein - metabolism | DEAD Box Protein 20 - chemistry | Two-Hybrid System Techniques | Fluorescent Antibody Technique | HSP27 Heat-Shock Proteins - metabolism | Protein-Serine-Threonine Kinases - chemistry | Heat-Shock Proteins - chemistry | Mortality | SMN protein | Motor neuron disease | Ribonucleoproteins | fluorescence resonance energy transfer | Data processing | Infants | Chaperones | Neuropathy | Ribonuclease | small heat shock proteins | Missense mutation | Hsp27 protein | DEAD box protein | spinal muscular atrophy | Protein interaction | Spliceosomes | RNA helicase | Original Paper | Protein–protein interaction
Journal Article
Acta neuropathologica communications, ISSN 2051-5960, 2017, Volume 5, Issue 1, p. 5
Journal Article
Cell stress & chaperones, ISSN 1355-8145, 7/2017, Volume 22, Issue 4, pp. 503 - 515
Small heat shock proteins (sHsps) are a ubiquitous part of the machinery that maintains cellular protein homeostasis by acting as molecular chaperones... 
SMALL HEAT SHOCK PROTEINS | Protein aggregation | Protein-protein interaction | Chaperone | Small heat shock protein (sHSP) | Light scattering assay | Fusion protein | Glutathione-S-transferase (GST) | DOMAIN | MALATE-DEHYDROGENASE | PHOSPHORYLATION | DETERMINANTS | ALPHA-B-CRYSTALLIN | HSPB1 | CELL BIOLOGY | DISSOCIATION | IN-VIVO | N-TERMINAL ARM | BINDING | Malate Dehydrogenase - metabolism | Protein Aggregates | Amino Acid Sequence | HSP27 Heat-Shock Proteins - chemistry | Humans | Protein Multimerization | Glutathione Transferase - metabolism | Substrate Specificity | alpha-Crystallin B Chain - metabolism | Recombinant Fusion Proteins - chemistry | Glutathione Transferase - chemistry | Recombinant Fusion Proteins - metabolism | Protein Interaction Maps | alpha-Crystallin B Chain - chemistry | HSP27 Heat-Shock Proteins - metabolism | Protein Domains | Protein Conformation | Malate Dehydrogenase - chemistry | Oligomers | Heat shock proteins | Glutathione transferase | Analysis | Protein-protein interactions | Molecular structure | Homeostasis | Agglomeration | Chaperones | Small heat shock proteins | Dehydrogenase | Tissues | Machinery | Monomers | Complexity | Machinery and equipment | Proteins | Substrate specificity | Mathematical models | Monitoring | Crystal structure | Glutathione | Forming | Malate dehydrogenase | Equilibrium | Substrates | Heat | Crystallin | Storage | Mutagenesis | Malate | Hsp27 protein | N-Terminus | Dimers | ATP | Heat shock | Index Medicus | Small Heat Shock Proteins
Journal Article
Journal Article
Journal of cellular and molecular medicine, ISSN 1582-4934, 2008, Volume 12, Issue 3, pp. 829 - 875
... •  Role of lipids in cell functions •  Lipid influence in transmembrane protein function... 
transmembrane protein | PKC | lipid composition‐structure | membrane lipid organization | membrane ion channel | heat‐shock protein | cell signalling | peripheral protein | lipid bilayer | GPCR | membrane receptor | protein‐lipid interactions | G protein | MEDICINE, RESEARCH & EXPERIMENTAL | lipid composition-structure | heat-shock protein | PLASMA-MEMBRANE | CELL BIOLOGY | HEAT-SHOCK PROTEINS | CYTOCHROME-C INTERACTION | NICOTINIC ACETYLCHOLINE-RECEPTOR | PHOSPHATIDIC-ACID | KINASE-C | protein-lipid interactions | SIGNAL-TRANSDUCTION | COLI ALPHA-HEMOLYSIN | GATED K+ CHANNELS | POTASSIUM CHANNEL | Animals | Membrane Proteins - chemistry | Models, Biological | Humans | Drug Therapy | Membrane Lipids - metabolism | Membrane Proteins - metabolism | Molecular Structure | Membrane Lipids - chemistry | Hsp90 protein | Regulators | Protein kinase C | Lipid composition | Membranes | Physiological effects | Demixing | Lipids | Lipid rafts | Hydrophobicity | Drug development | Kinases | Hydrogen bonding | Lipid structure | Lipid bilayers | Proteins | Signal transduction | Receptors | Physiology | Potassium channels (voltage-gated) | Bonding | Neurodegenerative diseases | Mechanosensitive channels | Van der Waals forces | Diabetes mellitus | Hsp70 protein | Cell membranes | Potassium channels | Electrostatic properties | Organelles | Membrane proteins | Diseases | Signaling | Lateral pressure | Hsp27 protein | Transduction | Potassium | Electrostatics | Cellular stress response | Cancer | Reviews
Journal Article