Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients
Highlights • Total soluble lens proteins and α-crystallin were extensively glycated. • The protein glycation was confirmed by different methods. • Glycated crystallins indicate higher conformational stability than non-glycated protein counterparts. • Glycation causes crystallins to resist against st...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yousefi, Reza [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Schlagwörter: |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor - Penchovsky, Robert ELSEVIER, 2019, structure, function and interactions, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:82 ; year:2016 ; pages:328-338 ; extent:11 |
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| DOI / URN: |
10.1016/j.ijbiomac.2015.10.036 |
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assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: the pathomechanisms underlying cataract development in diabetic patients |
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Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients |
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Highlights • Total soluble lens proteins and α-crystallin were extensively glycated. • The protein glycation was confirmed by different methods. • Glycated crystallins indicate higher conformational stability than non-glycated protein counterparts. • Glycation causes crystallins to resist against stress-induced unfolding and aggregation. |
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Highlights • Total soluble lens proteins and α-crystallin were extensively glycated. • The protein glycation was confirmed by different methods. • Glycated crystallins indicate higher conformational stability than non-glycated protein counterparts. • Glycation causes crystallins to resist against stress-induced unfolding and aggregation. |
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Highlights • Total soluble lens proteins and α-crystallin were extensively glycated. • The protein glycation was confirmed by different methods. • Glycated crystallins indicate higher conformational stability than non-glycated protein counterparts. • Glycation causes crystallins to resist against stress-induced unfolding and aggregation. |
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Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients |
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10.1016/j.ijbiomac.2015.10.036 |
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2024-07-06T19:31:27.718Z |
| _version_ |
1803859303039238144 |
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