COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.
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Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approachInteraction of extracellular domain 2 of the human retina-specific ATP-binding cassette transporter (ABCA4) with all-trans-retinalThe small heat shock protein p26 aids development of encysting Artemia embryos, prevents spontaneous diapause termination and protects against stress.Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lensesStage-specific excretory-secretory small heat shock proteins from the parasitic nematode Strongyloides ratti--putative links to host's intestinal mucosal defense system.Changes in function but not oligomeric size are associated with αB-crystallin lysine substitution.
P2860
COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 28 July 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
@en
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
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type
label
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
@en
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
@nl
prefLabel
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
@en
COOH-terminal truncations and ...... of porcine alphaB-crystallin.
@nl
P2093
P2860
P1433
P1476
COOH-terminal truncations and ...... y of porcine alphaB-crystallin
@en
P2093
Jiahn-Haur Liao
Jiahn-Shing Lee
Shih-Hsiung Wu
Shyh-Horng Chiou
P2860
P304
P577
2009-07-28T00:00:00Z