Found: 24
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Role of Filamin C in Muscle Cells.
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- Biochemistry (00062979), 2024, v. 89, n. 9, p. 1546, doi. 10.1134/S0006297924090025
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- Article
Universal Adapter Protein Bag3 and Small Heat Shock Proteins.
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- Biochemistry (00062979), 2024, v. 89, n. 9, p. 1535, doi. 10.1134/S0006297924090013
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- Article
Role of Small Heat Shock Proteins in the Remodeling of Actin Microfilaments.
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- Biochemistry (00062979), 2022, v. 87, n. 8, p. 800, doi. 10.1134/S0006297922080119
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- Article
Cardio-Vascular Heat Shock Protein (cvHsp, HspB7), an Unusual Representative of Small Heat Shock Protein Family.
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- Biochemistry (00062979), 2021, v. 86, n. 1, p. S1, doi. 10.1134/S0006297921140017
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- Article
Probable Participation of 14-3-3 in Tau Protein Oligomerization and Aggregation.
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- Journal of Alzheimer's Disease, 2011, v. 27, n. 3, p. 467, doi. 10.3233/JAD-2011-110692
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- Article
α-Crystallin Domains of Five Human Small Heat Shock Proteins (sHsps) Differ in Dimer Stabilities and Ability to Incorporate Themselves into Oligomers of Full-Length sHsps.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 2, p. 1085, doi. 10.3390/ijms24021085
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- Article
Quaternary Structure and Hetero-Oligomerization of Recombinant Human Small Heat Shock Protein HspB7 (cvHsp).
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- International Journal of Molecular Sciences, 2021, v. 22, n. 15, p. 7777, doi. 10.3390/ijms22157777
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- Article
The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 7, p. 3700, doi. 10.3390/ijms22073700
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- Article
The Heterooligomerization of Human Small Heat Shock Proteins Is Controlled by Conserved Motif Located in the N-Terminal Domain.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 12, p. 4248, doi. 10.3390/ijms21124248
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- Article
The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8.
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- International Journal of Molecular Sciences, 2018, v. 19, n. 7, p. 2112, doi. 10.3390/ijms19072112
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- Article
Interaction of Hsp27 with Native Phosphorylase Kinase under Crowding Conditions.
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- Macromolecular Bioscience, 2010, v. 10, n. 7, p. 783, doi. 10.1002/mabi.200900397
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- Article
Characterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron Diseases.
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- PLoS ONE, 2015, v. 10, n. 5, p. 1, doi. 10.1371/journal.pone.0126248
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- Article
Modulation of 14-3-3/Phosphotarget Interaction by Physiological Concentrations of Phosphate and Glycerophosphates.
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- PLoS ONE, 2013, v. 8, n. 8, p. 1, doi. 10.1371/journal.pone.0072597
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- Article
Epitope mapping of anti-troponin I monoclonal antibodies.
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- IUBMB Life, 1998, v. 45, n. 6, p. 1179, doi. 10.1080/15216549800203412
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- Article
Replacement of Arg in the conserved N-terminal RLFDQxFG motif affects physico-chemical properties and chaperone-like activity of human small heat shock protein HspB8 (Hsp22).
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- PLoS ONE, 2021, v. 16, n. 6, p. 1, doi. 10.1371/journal.pone.0253432
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- Article
Moonlighting chaperone-like activity of the universal regulatory 14-3-3 proteins.
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- FEBS Journal, 2017, v. 284, n. 9, p. 1279, doi. 10.1111/febs.13986
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- Article
Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin.
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- FEBS Journal, 2007, v. 274, n. 22, p. 5937, doi. 10.1111/j.1742-4658.2007.06117.x
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- Article
Effect of mutations in the β5–β7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11).
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- FEBS Journal, 2007, v. 274, n. 21, p. 5628, doi. 10.1111/j.1742-4658.2007.06086.x
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- Article
Oligomeric structure of 14-3-3 protein: What do we know about monomers?
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- FEBS Letters, 2012, v. 586, n. 24, p. 4249, doi. 10.1016/j.febslet.2012.10.048
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- Article
Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3ζ
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- FEBS Letters, 2009, v. 583, n. 17, p. 2739, doi. 10.1016/j.febslet.2009.07.043
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- Article
Corrigendum to “Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation” [FEBS Lett. 582 (2008) 1407–1412]
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- 2009
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- Correction Notice
Simultaneous Interaction of Actin With α-Actinin and Calponin.
- Published in:
- IUBMB Life, 2000, v. 49, n. 4, p. 277, doi. 10.1080/15216540050033131
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- Article
Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation
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- FEBS Letters, 2008, v. 582, n. 10, p. 1407, doi. 10.1016/j.febslet.2008.03.035
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- Article
Mechano-chemical effects of Ca<sup>2+</sup> in cross-linked troponin-C films
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- FEBS Letters, 2002, v. 524, n. 1-3, p. 107, doi. 10.1016/S0014-5793(02)03013-2
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- Article