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Actin interacts with CCT via discrete binding sites: A binding transition-release model for CCT-mediated actin folding
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The folding pathways of actin and tubulins, mechanism of and recognition by the eukaryotic chaperones prefoldin and CCT
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Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding
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Structural plasticity of functional actin: Pictures of actin binding protein and polymer interfaces (vol 11, pg 1279, 2004)
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Myopathy mutations in alpha-skeletal-muscle actin cause a range of molecular defects
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Structural plasticity of functional actin: Pictures of actin binding protein and polymer interfaces
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The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
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Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors.
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Cofactor A is a molecular chaperone required for β-tubulin folding : functional and structural characterization
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Pathway leading to correctly folded beta-tubulin.