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Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 12014 - 12
In eukaryotes, several "hub" proteins integrate signals from different interacting partners that bind through intrinsically disordered regions. The 14-3-3... 
CRYSTALLIZATION | BINDING DOMAINS | INHIBITION | EXOENZYME-S | INTERFACE | STRUCTURAL BASIS | PHOSPHORYLATION | STABILIZATION | MULTIDISCIPLINARY SCIENCES | IDENTIFICATION | 14-3-3-PROTEINS | Protein kinase A | Proteins | 14-3-3 protein | Phosphorylation | Peptides | Synthetic peptides | Chimeras | Biosensors | Kinases | Index Medicus
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 01/2019, Volume 508, Issue 4, p. 1101
Small heat shock proteins (sHsps) are molecular chaperones preventing protein aggregation. Dynamics of quaternary structure plays an important role in the... 
Journal Article
Biochimie, ISSN 0300-9084, 10/2019, Volume 165, pp. 196 - 205
Chemical chaperones are a class of small molecules which enhance folding and prevent aggregation of proteins. Investigation of their effects on the processes... 
2-Hydroxypropyl-β-cyclodextrin | UV-Irradiated muscle glycogen phosphorylase b | Trehalose | Thermal aggregation | Index Medicus
Journal Article
Biochimie, ISSN 0300-9084, 01/2015, Volume 108, p. 68
Effect of trimethylamine N-oxide (TMAO), well-known osmolyte, widely used to imitate crowded intracellular conditions, on the quaternary structure of... 
Oligomers | Crosslinked polymers | Analysis | Heat shock proteins | Chromatography
Journal Article
Biophysical Journal, ISSN 0006-3495, 02/2017, Volume 112, Issue 4, p. 827
(Biophysical Journal 112, 46–56; January 10, 2017) In the published article Andrew Rubin's name was incorrectly spelled Andrei Rubin. Affiliations were... 
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 05/2014, Volume 549, p. 32
Display Omitted 
Journal Article
Biochemical and biophysical research communications, 12/2018
Small heat shock proteins (sHsps) are molecular chaperones preventing protein aggregation. Dynamics of quaternary structure plays an important role in the... 
Journal Article
FEBS Letters, ISSN 0014-5793, 09/2009, Volume 583, Issue 17, pp. 2739 - 2742
Serine residues phosphorylated by protein kinase A (PKA) in the shortest isoform of human tau protein (τ3) were replaced by alanine and interaction of... 
14-3-3 | Phosphorylation | Tau protein | Protein–protein interaction | PKB | PKA | τ3 phosphorylated by protein kinase A | PMSF | the shortest isoform of human tau protein | β-mercaptoethanol | phenylmethane sulfonylfluoride | protein kinase A | pτ3 | protein kinase B | Protein-protein interaction
Journal Article
Biophysical Chemistry, ISSN 0301-4622, 01/2015, Volume 196, p. 77
We applied differential scanning calorimetry (DSC) to investigate the effects of substitutions D137L and G126R (i.e. replacement of conserved non-canonical... 
Muscle proteins
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2017, Volume 12, Issue 6, pp. e0178933 - e0178933
Abundant regulatory 14-3-3 proteins have an extremely wide interactome and coordinate multiple cellular events via interaction with specifically phosphorylated... 
Exoribonucleases - genetics | Phosphorylation | Humans | tau Proteins - metabolism | Protein Interaction Maps | Cyclic AMP-Dependent Protein Kinases - genetics | Protein Isoforms - metabolism | tau Proteins - genetics | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Parkinson Disease - metabolism | Exoribonucleases - analysis | 14-3-3 Proteins - genetics | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Expression | Biomarkers, Tumor - analysis | Protein Isoforms - analysis | 14-3-3 Proteins - metabolism | Cyclic AMP-Dependent Protein Kinases - analysis | 14-3-3 Proteins - analysis | Escherichia coli - genetics | Alzheimer Disease - metabolism | Biomarkers, Tumor - genetics | tau Proteins - analysis | Exoribonucleases - metabolism | Protein Isoforms - genetics | Research | Protein kinases | Protein-protein interactions | Protein kinase A | Stoichiometry | Residues | Identification methods | Escherichia coli | Disorders | Displays | Biochemistry | Biology | Kinases | Proteins | Signal transduction | Functional anatomy | Rodents | Bacteria | Physiology | Binding | Neurodegenerative diseases | Fetuses | Cloning | Diseases | Studies | Neurological diseases | 14-3-3 protein | Tau protein | Protein kinase | Plasmids | Isoforms | Protein expression | Regulation | Alzheimers disease | In vitro methods and tests | Binding sites | Apoptosis | Index Medicus
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 05/2015, Volume 76, p. 86
The main function of small heat shock proteins acting as suppressors of aggregation of non-native proteins is greatly influenced by crowded environment in the... 
Analysis | Myosin | Heat shock proteins | Muscle proteins | Polyols
Journal Article
FEBS Letters, ISSN 0014-5793, 06/2017, Volume 591, Issue 12, pp. 1667 - 1676
Journal Article
Structure, ISSN 0969-2126, 02/2017, Volume 25, Issue 2, pp. 305 - 316
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6,... 
14-3-3 proteins | smooth muscle relaxation | small heat shock proteins | regulatory complex | crystal structure | protein-protein interaction | phosphopeptides | conformational change | small-angle X-ray scattering | intrinsically disordered regions | PHOSPHORYLATION | MOLECULE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-B-CRYSTALLIN | CELL BIOLOGY | DOMAIN DIMERS | BIOPHYSICS | PURIFICATION | AIRWAY SMOOTH-MUSCLE | BINDING | EXPRESSION | WEB SERVER | HSP20 HSPB6 | Exoribonucleases - genetics | Phosphorylation | Humans | Protein Multimerization | Exoribonucleases - chemistry | Substrate Specificity | Crystallography, X-Ray | HSP20 Heat-Shock Proteins - genetics | Phosphoproteins - metabolism | HSP20 Heat-Shock Proteins - metabolism | Phosphoproteins - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Biomarkers, Tumor - metabolism | Protein Interaction Domains and Motifs | Binding Sites | HSP20 Heat-Shock Proteins - chemistry | 14-3-3 Proteins - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Signal Transduction | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Phosphoproteins - genetics | Intrinsically Disordered Proteins - genetics | Amino Acid Motifs | 14-3-3 Proteins - metabolism | Protein Conformation, beta-Strand | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | 14-3-3 Proteins - chemistry | Biomarkers, Tumor - genetics | Biomarkers, Tumor - chemistry | Exoribonucleases - metabolism | Intrinsically Disordered Proteins - metabolism | Proteins | Fluorescence spectroscopy | Proteolysis | Analysis | Crystals | Fluorescence | Atoms | Heat shock proteins | Molecular biology | Structure | Protein-protein interactions | Index Medicus | small angle X-ray scattering
Journal Article