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Journal of Molecular Biology, ISSN 0022-2836, 08/2019, Volume 431, Issue 17, pp. 3157 - 3178
Journal Article
2000, Frontiers in molecular biology, ISBN 9780199637614, Volume 31, xix, 314
Book
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 21, pp. 7942 - 7968
In aortic vascular smooth muscle (VSM), the canonical Wnt receptor LRP6 inhibits protein arginine (Arg) methylation, a new component of noncanonical Wnt... 
atherosclerosis | Type 2 diabetes | BONE BIOLOGY | cardiovascular disease | TRANSCRIPTION FACTOR RUNX2 | SINGLETON-MERTEN SYNDROME | CARDIOVASCULAR CALCIFICATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | INHIBITS VASCULAR CALCIFICATION | vascular biology | metabolic syndrome | DIABETES-MELLITUS | Wnt signaling | arteriosclerosis | protein methylation | ATHEROSCLEROTIC CALCIFICATION | IN-VIVO | calcification | ARGININE METHYLATION | vascular smooth muscle cells | CORONARY-ARTERY-DISEASE | Calcinosis - genetics | RNA Helicases - metabolism | Poly-ADP-Ribose Binding Proteins - metabolism | Calcium - metabolism | Humans | Myocytes, Smooth Muscle - pathology | Antiviral Agents - metabolism | Aorta - metabolism | Arteriosclerosis - genetics | Wnt Proteins - metabolism | Wnt Proteins - genetics | RNA Helicases - genetics | Calcinosis - metabolism | RNA Recognition Motif Proteins - metabolism | DNA Helicases - genetics | Myocytes, Smooth Muscle - metabolism | Low Density Lipoprotein Receptor-Related Protein-6 | Signal Transduction | Mice, Inbred C57BL | Cells, Cultured | Poly-ADP-Ribose Binding Proteins - genetics | beta Catenin - metabolism | beta Catenin - genetics | Mice, Knockout | Aorta - pathology | DNA Helicases - metabolism | Adaptor Proteins, Signal Transducing - physiology | Animals | Arteriosclerosis - metabolism | Mice | RNA Recognition Motif Proteins - genetics | Receptors, LDL - physiology | Calcinosis - pathology | Arteriosclerosis - pathology | Molecular Bases of Disease
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 6689 - 6695
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions... 
signaling | residual structure | electrostatics | coupled folding and binding | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein electrostatics | C-MYB | TRANSITION-STATE | INDUCED FIT | protein-protein interactions | INTRINSICALLY DISORDERED PROTEINS | LINEAGE LEUKEMIA PROTEIN | IDP | MOLECULAR RECOGNITION | KIX DOMAIN | SEQUENCE | protein folding | phi-value | TRANSACTIVATION DOMAIN | kinetics | biophysics | protein dynamic | CONFORMATIONAL SELECTION | Cyclic AMP Response Element-Binding Protein - chemistry | Humans | Myeloid Cell Leukemia Sequence 1 Protein - metabolism | CREB-Binding Protein - chemistry | Proto-Oncogene Proteins - chemistry | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Thermodynamics | Apoptosis Regulatory Proteins - genetics | Myeloid Cell Leukemia Sequence 1 Protein - chemistry | Protein Interaction Domains and Motifs | Proto-Oncogene Proteins - metabolism | Signal Transduction | Apoptosis Regulatory Proteins - chemistry | Proto-Oncogene Proteins - genetics | Static Electricity | Intrinsically Disordered Proteins - genetics | Molecular Dynamics Simulation | Myeloid Cell Leukemia Sequence 1 Protein - genetics | Protein Folding | Apoptosis Regulatory Proteins - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Intrinsically Disordered Proteins - chemistry | Cyclic AMP Response Element-Binding Protein - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Kinetics | Intrinsically Disordered Proteins - metabolism | Minireviews
Journal Article