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ProteomicsAge-related cleavages of crystallins in human lens cortical fibre cells generate a plethora of low molecular weight peptides and cross-linked crystallin complexes
A large variety of low molecular weight (LMW) peptides, derived from the breakdown of crystallins, have been reported in middle to old age human lenses. The proliferation of these LMW peptides coincides with the earliest stages of cataract formation, suggesting that the protein cleavages involved ma...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000081536 | MassIVE
UnknownSolution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.
Not available
S-EPMC3892302 | biostudies-literature
UnknownSolution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.
Not available
S-EPMC3892301 | biostudies-literature
UnknownThe molecular refractive function of lens γ-Crystallins.
Not available
S-EPMC3146585 | biostudies-literature
UnknownCa2+-binding motif of βγ-crystallins.
Not available
S-EPMC4036236 | biostudies-literature
UnknownFunction and Aggregation in Structural Eye Lens Crystallins.
Not available
S-EPMC7486140 | biostudies-literature
ProteomicsAge-related cleavages of crystallins in human lens cortical fibre cells generate a plethora of low molecular weight peptides and cross-linked crystallin complexes
A large variety of low molecular weight (LMW) peptides, derived from the breakdown of crystallins, have been reported in middle to old age human lenses. The proliferation of these LMW peptides coincides with the earliest stages of cataract formation, suggesting that the protein cleavages involved ma...
ORGANISM(S): Homo sapiens (Human) 
2016-09-29 | PXD001593 | Pride
Human lens Crystallin Endogeneuous peptideslens aging  crystallin  cataract  mass spectrometry  endogenous peptides  2-d gel electrophoresis  nanolc-esi-ms/ms  trypsin-like cleavage 
UnknownZinc and Copper Ions Induce Aggregation of Human β-Crystallins.
Not available
S-EPMC9105653 | biostudies-literature
UnknownAssociation properties of betaB1- and betaA3-crystallins: ability to form heterotetramers.
Not available
S-EPMC2752815 | biostudies-literature
ProteomicsAbsolute abundance of human crystallins in lens
Purpose: Measurement of crystallin abundances in human lens has previous relied on poorly reproducible electrophoretic separations or only semi-quantitative mass spectrometry. Therefore, isotope labeled standards were created for all major human lens crystallins so that their absolute abundances cou...
ORGANISM(S): Homo Sapiens Mus Musculus 
PXD053890 | panorama
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