Pages that link to "Q27646902"
Jump to navigation
Jump to search
The following pages link to Biophysical Properties of γC-Crystallin in Human and Mouse Eye Lens: The Role of Molecular Dipoles (Q27646902):
Displaying 19 items.
- A nonsense mutation in CRYGC associated with autosomal dominant congenital nuclear cataract in a Chinese family (Q24312191) (← links)
- Structure and Dynamics of the Fish Eye Lens Protein, γM7-Crystallin (Q27677446) (← links)
- Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human γC-Crystallin: Role of the Dipole Moment in Protein Solubility (Q27704882) (← links)
- Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells (Q28655525) (← links)
- NEIBank: genomics and bioinformatics resources for vision research (Q33354091) (← links)
- Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin (Q33845392) (← links)
- A single destabilizing mutation (F9S) promotes concerted unfolding of an entire globular domain in gammaS-crystallin (Q33999026) (← links)
- Mutation screening and genotype phenotype correlation of α-crystallin, γ-crystallin and GJA8 gene in congenital cataract. (Q34693091) (← links)
- The molecular refractive function of lens γ-Crystallins. (Q35136629) (← links)
- The role of macromolecular crowding in the evolution of lens crystallins with high molecular refractive index. (Q35150467) (← links)
- γ-Crystallins of the chicken lens: remnants of an ancient vertebrate gene family in birds. (Q35935292) (← links)
- Evolution of crystallins for a role in the vertebrate eye lens. (Q36722216) (← links)
- Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins. (Q37480798) (← links)
- Primary sequence contribution to the optical function of the eye lens. (Q40375255) (← links)
- Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate (Q42086016) (← links)
- A novel mutation impairing the tertiary structure and stability of γC-crystallin (CRYGC) leads to cataract formation in humans and zebrafish lens. (Q44692060) (← links)
- Crystal Structure of Chicken γS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the βγ-Crystallins. (Q47993461) (← links)
- Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity (Q64269917) (← links)
- Crystallins and Their Complexes (Q92651148) (← links)