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Literature summary for 5.2.1.8 extracted from

  • Rudrabhatla, P.; Zheng, Y.L.; Amin, N.D.; Kesavapany, S.; Albers, W.; Pant, H.C.
    Pin1-dependent prolyl isomerization modulates the stress-induced phosphorylation of high molecular weight neurofilament protein (2008), J. Biol. Chem., 283, 26737-26747.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information both hydrogen peroxide and heat stresses induce phosphorylation of neurofilament protein NF-H in transfected HEK-293 cells and primary cortical cultures. Knockdown of Pin1 by transfected Pin1 short interference RNA and dominant negative-Pin1 rescues the effect of stress-induced NF-H phosphorylation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13526 isoform Pin1
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Source Tissue

Source Tissue Comment Organism Textmining
cell culture primary cortical culture Homo sapiens
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HEK-293 cell
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform Pin1 modulates oxidative stress-induced neurofilament NF-H phosphorylation. In vitro, the addition of Pin1 substantially increases phosphorylation of NF-H KSP repeats by proline-directed kinases, Erk1/2, Cdk5/p35, and JNK3 in a concentration-dependent manner. In vivo, dominant-negative Pin1 and Pin1 small interfering RNA inhibit epidermal growth factor-induced NF-H phosphorylation Homo sapiens ?
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