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Analysis of interaction surfaces between NEPH1 and MYO1c (zeige MYO1C Proteine) led to the identification of a critical residue in Neph1 involved in binding to Myo1c (zeige MYO1C Proteine). Indeed, a point mutant from this site abolished interaction between Neph1 and Myo1c (zeige MYO1C Proteine).
maintaining high levels of Neph1 at the membrane using a podocyte cell line overexpressing chimeric Neph1 increased the ability of podocytes to resist PAN-induced injury and PAN-induced albumin (zeige ALB Proteine) leakage
Neph1-CD adopts a global shape in solution, and its interaction with ZO-1 (zeige TJP1 Proteine) involves multiple sites.
Localization of Neph1 to the podocyte cell membrane is altered in the presence of mutant Myo1c (zeige MYO1C Proteine), and is actin dependent. Knockdown of Myo1c (zeige MYO1C Proteine) inhibits Neph1 membrane localization. Neph1 is critical for the maintenance of glomerular function.
A striking finding in this study is the lack of contribution of NEPH1, NPHS1, and NPHS2 genes in 15 Asian families with steroid-resistant nephrotic syndrome.
common variants in LRRC7, KIRREL, NPHS2 and ACTN4 (zeige ACTN4 Proteine) do not appeear to contribute to susceptibility to diabetic nephropathy in Finnish patients with type 1 diabetes
Neph1 but not nephrin (zeige NPHS1 Proteine) specifically binds to adaptor protein Grb2 (zeige GRB2 Proteine) and tyrosine kinase (zeige TXK Proteine) Csk (zeige CSK Proteine) in a phosphorylation-dependent manner.
Neph1-Nephrin (zeige NPHS1 Proteine) proteins bind the Par3 (zeige F2RL2 Proteine)-Par6 (zeige PARD6A Proteine)-atypical protein kinase C (zeige PRKCZ Proteine) (aPKC) complex to regulate podocyte cell polarity
tyrosine phosphorylation of Neph1 mediated by Fyn (zeige FYN Proteine) results in significantly increased Neph1 and ZO-1 (zeige TJP1 Proteine) binding, suggesting a critical role for Neph1 tyrosine phosphorylation in reorganizing the Neph1-ZO-1 (zeige TJP1 Proteine) complex.
Here we demonstrate that Neph1, Neph2, and Neph3 are expressed differentially in various tissues during ontogenesis in mouse and chicken.
Fyn (zeige FYN Proteine) catalyzes Nephrin (zeige NPHS1 Proteine) phosphorylation in podocyte detergent-resistant membrane fractions.
nephrin (zeige NPHS1 Proteine) and Neph1 interact and have roles in glomerular permeability
In the adult brain, Neph1 is seen in the olfactory nerve layer and the glomerular layer of the olfactory bulb, in the hippocampus, and in cerebellar Purkinje cells. At the ultrastructural level, Neph1 is seen in dendritic shafts of pyramidal neurons.
Nephrin-Neph1 complex transduces phosphorylation-mediated signals that assemble an actin polymerization complex at the podocyte intercellular junction.
NEPH1 is a member of the nephrin-like protein family, which includes NEPH2 (MIM 607761) and NEPH3 (MIM 607762). The cytoplasmic domains of these proteins interact with the C terminus of podocin (NPHS2\; MIM 604766), and the genes are expressed in kidney podocytes, cells involved in ensuring size- and charge-selective ultrafiltration (Sellin et al., 2003
, kin of IRRE-like protein 1
, kin of irregular chiasm-like protein 1
, nephrin-like protein 1
, kin of IRRE like 1
, nephrin 1