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Large potentials of small heat shock proteins.
All small heat shock proteins play important "housekeeping" roles and regulate many vital processes; therefore, they are considered as attractive therapeutic targets. Expand
Troponin: structure, properties, and mechanism of functioning.
This review discusses the structure and properties of the isolated components of troponin, their interaction, and the mechanisms of regulation of contractile activity of skeletal and cardiac muscle.Expand
Structure and Properties of Small Heat Shock Proteins (sHsp) and Their Interaction with Cytoskeleton Proteins
The modern classification of small heat shock proteins (sHsp) is presented and peculiarities of their primary structure and the mechanism of formation of oligomeric complexes are described. Data onExpand
Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex.
It is demonstrated that the main part of cTnI in serum collected from acute myocardial infarction patients is presented in the complex from CTnC, which results in a significant decrease of the interaction of mAbs with TnI. Expand
Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20).
In heterooligomeric complexes HspB6 and HSpB1 mutually affect the structure of each other and formation of heterooligenic complexes might influence diverse processes depending on small heat shock proteins. Expand
Three-dimensional structure of α-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6.
Using SAXS, it is shown that it is possible to discriminate between different putative registers of the β7/β7 interface, with the results indicating that, under physiological conditions, there is only a single register of the strands for both proteins. Expand
Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.
This structure provides the first atomic resolution snapshot of a human small HSP in functional state, explains how 14-3-3 proteins sequester their regulatory partners, and can inform the design of small-molecule interaction modifiers to be used as myorelaxants. Expand
Some properties of human small heat shock protein Hsp22 (H11 or HspB8).
Untagged recombinant human small heat shock protein with apparent molecular mass 22 kDa (Hsp22) was obtained in homogeneous state. Size exclusion chromatography and chemical crosslinking withExpand
Oligomeric structure of 14‐3‐3 protein: What do we know about monomers?
A recently characterized monomeric 14‐3‐3 contains few mutations and retains the original secondary structure and interacts with phosphorylated target proteins and has higher chaperone‐like activity than dimeric 14‐ 3‐3. Expand
Phosphorylation of aorta caldesmon by endogeneous proteolytic fragments of protein kinase C
Phosphorylation of both intact caldesmon and of its C-terminal fragment (658C), containing residues 658–756, significantly decreased their ability to inhibit acto-heavy meromyosin ATPase. Expand