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Showing 1 to 7 of 7 for “"UNC-45"”.
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The Role of UNC-45 in Heart Development and Human Breast Cancer
The C. elegans UNC-45 has been demonstrated as a molecular chaperone of body-wall muscle myosins. In human and other vertebrates, two UNC-45 genes code two UNC-45 protein isoforms: UNC-45A/a and UNC-45B/b. UNC-45A/a is expressed in all cell types, whereas UNC-45B/b only exists in heart and skeletal …
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The UNC-45 molecular chaperone: Its interactions with myosin and its thermosensing properties
In order to perform their biological functions, proteins must fold into a defined structure which is termed the “native state”. In some cases proteins can acquire the native structure spontaneously; however for others additional assistance of molecular chaperones is needed. The molecular chaperones …
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Simulation of the Interaction Between Striated Muscle UNC-45 and Transcription Factor GATA-4
<p> Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large …
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GENERATION OF FULL-LENGTH WILD-TYPE GATA4 PROTEIN AND CHARACTERIZATION OF ITS BINDING TO UNC-45 DOMAINS
<p>Striated muscle UNC-45 (SM UNC-45) protein acts as a chaperone for cardiac and skeletal muscle myosins; regulating their folding, assembly into thick filaments, interaction with other sarcomeric proteins, and degradation. GATA4 is an important transcription factor that regulates the expression …
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The Myosin-Binding UCS Domain but not the Hsp90-Binding TPR Domain of the UNC-45 Chaperone is Essential for Myosin Accumulation and Assembly in Caenorhabditis elegans
The UNC-45 family of molecular chaperones is expressed in metazoan organisms from C. elegans to humans. The UNC-45 protein is essential in C. elegans for early body-wall muscle cell development and A band assembly. We show that the myosin-binding UCS domain of UNC-45 alone is sufficient to rescue …
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Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer
The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two …
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Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer
The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two …