Pages that link to "Q73827885"
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The following pages link to Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin (Q73827885):
Displaying 26 items.
- Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins (Q24303942) (← links)
- Analysis of betaB1-crystallin unfolding equilibrium by spin and fluorescence labeling: evidence of a dimeric intermediate (Q24650937) (← links)
- Structural origin of weakly ordered nitroxide motion in spin-labeled proteins (Q27655050) (← links)
- Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5 (Q27679512) (← links)
- Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens (Q28513843) (← links)
- The specificity of the interaction between αB-crystallin and desmin filaments and its impact on filament aggregation and cell viability (Q30539278) (← links)
- Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation (Q33302904) (← links)
- Free-solution label-free detection of alpha-crystallin chaperone interactions by back-scattering interferometry (Q33403849) (← links)
- Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol (Q33799786) (← links)
- Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates. (Q34065998) (← links)
- Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain (Q35801033) (← links)
- A conserved role of αA-crystallin in the development of the zebrafish embryonic lens. (Q36264038) (← links)
- Specificity of alphaA-crystallin binding to destabilized mutants of betaB1-crystallin (Q36415638) (← links)
- Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-crystallin (Q36512835) (← links)
- Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding (Q36620780) (← links)
- Alternating access of the putative substrate-binding chamber in the ABC transporter MsbA. (Q37384273) (← links)
- Conformational cycle of the ABC transporter MsbA in liposomes: detailed analysis using double electron-electron resonance spectroscopy. (Q37384297) (← links)
- Substrate binding site flexibility of the small heat shock protein molecular chaperones (Q37412434) (← links)
- Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins (Q37424170) (← links)
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones (Q37589738) (← links)
- An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis. (Q37677565) (← links)
- Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity (Q41084011) (← links)
- Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins. (Q41960429) (← links)
- Distance mapping in proteins using fluorescence spectroscopy: tyrosine, like tryptophan, quenches bimane fluorescence in a distance-dependent manner (Q42943969) (← links)
- Binding of destabilized betaB2-crystallin mutants to alpha-crystallin: the role of a folding intermediate (Q75411064) (← links)
- Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity (Q89462234) (← links)