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The protein encoded by NHLRC1 is a single subunit E3 ubiquitin ligase. Zusätzlich bieten wir Ihnen NHLRC1 Antikörper (67) und NHLRC1 Kits (3) und viele weitere Produktgruppen zu diesem Protein an.
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Malin promotes its own degradation via auto-ubiquitination.Malin preferentially degrades the phosphatase-inactive laforin (zeige EPM2A Proteine) monomer.
laforin/malin complex is able to interact with and ubiquitinate both PKM1 and PKM2
Lafora disease proteins laforin (zeige EPM2A Proteine) and malin negatively regulate the HIPK2 (zeige HIPK2 Proteine)-p53 (zeige TP53 Proteine) cell death pathway.
This study demonistrated that NHLRC1 mutations were detected in some case of Mild Lafora disease patients.
Without functional laforin (zeige EPM2A Proteine)-malin complex assembled on polyglucosan bodies, polyglucosan is not degraded.
Malin regulates the recruitment of mRNA-decapping enzyme 1A (Dcp1a (zeige DCP1A Proteine)) to processing bodies.
Malin forms a functional complex with laforin (zeige EPM2A Proteine). This complex promotes the ubiquitination of proteins involved in glycogen (zeige GYS1 Proteine) metabolism and misregulation of pathways involved in this process results in Lafora body formation. (Review)
This study identified that NHLRC1 gene mutations leading to Lafora disease in six Turkish families.
Our results indicate that malin regulates Wnt (zeige WNT2 Proteine) signaling pathway through the degradation of dishevelled2 and suggest possible deregulation of Wnt (zeige WNT2 Proteine) signaling in Lafora disease.
Mutations in the NHL repeat containing 1 (NHLRC1) gene are described in association with a more benign clinical course and later age of death in an adolescent patient.
Loss of malin leads to reduced proteasomal activity in the heat-shocked cells.
This study also suggests a malin function independent of laforin (zeige EPM2A Proteine), possibly in lysosomal biogenesis and/or lysosomal glycogen (zeige GYS1 Proteine) disposal.
Results indicate that malin has no effect on whole-body glucose metabolism and insulin (zeige INS Proteine) sensitivity.
Dysfunction of autophagy is a common feature of both laforin (zeige EPM2A Proteine)- and malin-deficient mice.
malin functions to regulate laforin (zeige EPM2A Proteine) and that malin deficiency at least in part causes LB and LD through increased laforin (zeige EPM2A Proteine) binding to glycogen (zeige GYS1 Proteine).
Results show that a functional laforin (zeige EPM2A Proteine)-malin complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres.
Motor coordination, activity impairment, and memory deficits progressively increase with age in Epm2b deficient mice.
Data conclude that EPM2B functions to maintain laforin (zeige EPM2A Proteine) associated with soluble glycogen (zeige GYS1 Proteine) and that its absence causes sequestration of laforin (zeige EPM2A Proteine) to an insoluble polysaccharide fraction where it is functionally inert.
laforin (zeige EPM2A Proteine) and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins
The protein encoded by this gene is a single subunit E3 ubiquitin ligase. Laforin is polyubiquitinated by the encoded protein. Defects in this intronless gene lead to an accumulation of laforin and onset of Lafora disease, also known as progressive myoclonic epilepsy type 2 (EPM2).
NHL repeat containing 1
, thiopurine methyltransferase
, NHL repeat-containing protein 1
, E3 ubiquitin-protein ligase NHLRC1
, NHL repeat-containing protein 1-like