Free and bound water in normal and cataractous human lenses.
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Summary
As the human lens ages, bound water is progressively changed to free water.
- Type
- article
- Published
- 2008-05-01
- Cited by
- 68
- References
- 40
- Access
- Open access
- OpenAlex
- https://openalex.org/W1967429157
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:893649
Keywords
Bound water, Free water, Chemistry, Lens (geology), Nucleus
References
- Normal human lens - the distribution of protein.
- Age-related nuclear cataract-oxidation is the key.
- Age-dependent changes in the molecular size of human lens proteins and their relationship to light scatter.
- Freezable and non-freezable water content of cataractous human lenses.
- Color and solubility of the proteins of human cataracts.
- Nuclear magnetic resonance study of free and bound water fractions in normal lenses.
- Age dependence of freezable and nonfreezable water content of normal human lenses.
- Morphology of the normal human lens.
- Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, α‐crystallin, in maintaining lens flexibility
- An ultrastructural analysis of the epithelial-fiber interface (EFI) in primate lenses.
- Dynamic mechanical properties of human lenses.
- Changes in Weight and in Protein – Water Ratio of the Lens in Human Senile Cataracts
- The interrelationship of lens anatomy and optical quality. I. Non-primate lenses.
- Age-related changes in the kinetics of water transport in normal human lenses.
- Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?
- The state of water in normal human, bird and fish eye lenses.
- Changes in proteins of the human lens in development and aging.
- The ageing lens
- Epithelial organization of the mammalian lens.
- Changes in the distribution of proteins in the aging human lens.
Cited by
- Investigation into the extent of lipid turnover in the mammalian lens
- New capabilities and applications of ambient ionization mass spectrometry for the surface analysis and imaging of lipids
- Information processing for mass spectrometry imaging
- Investigating human lens lipids using tandem mass spectrometric techniques
- Investigations into the biochemical basis for the formation of the barrier in the aging human lens.
- Hydration, fluid regulation and the eye: in health and disease
- Aqueous Humor Ferritin in Hereditary Hyperferritinemia Cataract Syndrome
- α- and β-crystallins modulate the head group order of human lens membranes during aging.
- The ageing lens and cataract: a model of normal and pathological ageing
- Instability of the cellular lipidome with age
- Estimation of mechanical properties of a viscoelastic medium using a laser-induced microbubble interrogated by an acoustic radiation force.
- Hydration water/interfacial water in crystalline lens.
- Presbyopia and cataract: a question of heat and time.
- Effect of acid whey concentrate on thermophysical properties of milk-based ice-cream
- Enhanced Water Retention by Using Polymeric Microcapsules to Confer High Proton Conductivity on Membranes at Low Humidity
- Imaging of human lens lipids by desorption electrospray ionization mass spectrometry
- Tight binding of proteins to membranes from older human cells
- Crystalline lens power and refractive error.
- Racemisation and human cataract. d-Ser, d-Asp/Asn and d-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses
- The gradient index lens of the eye: an opto-biological synchrony.
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