Browse our anti-PKC gamma (PRKCG) Antibodies

Human Protein Kinase C, gamma (PRKCG) interaction partners

1. This review showed that the PKC Gamma signaling related genes and calcium signaling related genes then discuss their role for both Purkinje cell dendritic development and cerebellar ataxia.

2. SUMOylation of EphB1 (show EPHB1 Antibodies) repressed activation of its downstream signaling molecule PKC-gamma, and consequently inhibited neuroblastoma (show ARHGEF16 Antibodies) tumorigenesis.

3. two out of three known mutations in the catalytic domain of PKCgamma did indeed show increased biological activity.

4. Lysophosphatidylcholines prime polymorphonuclear neutrophil through Hck (show HCK Antibodies)-dependent activation of PKCdelta (show PKCd Antibodies), which stimulates PKCgamma, resulting in translocation of phosphorylated p47(phox).

5. The gene-environment combination of PRKCG rs3745406 C allele, BDNF (show BDNF Antibodies) rs6265 G allele and high level of negative life events was significantly associated with major depressive disorder.

6. Data suggest that PRKCG (protein kinase C gamma) phosphorylates TA isoforms of p63 (tumor protein p63 (show TP63 Antibodies)) at Thr157 to stabilize them and promote cell apoptosis in tumor cells.

7. PKCgamma,mutated in the neurodegenerative disease spinocerebellar ataxia type 14 is a novel amyloidogenic protein.

8. The rs454006 polymorphism of the PRKCG gene correlated to osteosarcoma susceptibility and might increase the risk of osteosarcoma.

9. findings provide evidence for both an increased PKCgamma activity in Purkinje cells in vivo and for pathological changes typical for cerebellar disease thus linking increased and dysregulated activity of PKCgamma to development of cerebellar disease

10. we show that the mutation V138E of the protein kinase C gamma (PKCgamma) C1B domain, which is implicated in spinocerebellar ataxia type 14, exhibits a partially unfolded C-terminus

Mouse (Murine) Protein Kinase C, gamma (PRKCG) interaction partners

1. cPKC&-gamma modulated sequential reactivation of mTOR (show FRAP1 Antibodies) inhibited autophagic flux in neurons exposed to OGD (show FGFR1 Antibodies)/R, which may provide endogenous interventional strategies for stroke, especially ischemia/reperfusion injury

2. PKCgamma-mediated down-regulation of UCHL1 (show UCHL1 Antibodies) alleviates ischemic neuronal injuries by decreasing autophagy via ERK (show EPHB2 Antibodies)-mTOR (show FRAP1 Antibodies) pathway.

3. SUMOylation of EphB1 (show EPHB1 Antibodies) repressed activation of its downstream signaling molecule PKC-gamma, and consequently inhibited neuroblastoma (show ARHGEF16 Antibodies) tumorigenesis.

4. CA8 (show CA8 Antibodies) is a novel important regulator of Purkinje cell dendritic development and that its expression is controlled by PKCgamma activity.

5. These results suggested that cPKCgamma-modulated neuron-specific autophagy improves the neurological outcome of mice following ischemic stroke through the Akt (show AKT1 Antibodies)-mTOR (show FRAP1 Antibodies) pathway, providing a potential therapeutic target for ischemic stroke.

6. Lysophosphatidylcholines prime polymorphonuclear neutrophil through Hck (show HCK Antibodies)-dependent activation of PKCdelta (show PKCd Antibodies), which stimulates PKCgamma, resulting in translocation of phosphorylated p47(phox).

7. Immunoblotting and RT-PCR results showed that NIHL increased the expression of PKCgamma but decreased that of GABABR1 (show GABBR1 Antibodies) and GABABR2 (show GABBR2 Antibodies) at both protein and mRNA levels in the CNC

8. Therefore, we propose that PKCgamma positively modulates dopamine release through beta2PIX phosphorylation.

9. These findings indicate that the identity of the calcium-dependent PKCgamma that mediates PTP controls the mechanism and functional consequences of Posttetanic potentiation.

10. This study provided new evidence to support the possibility of the involvement of PKC-gamma in the actions of volatile anesthetics in mice brain.

Rabbit Protein Kinase C, gamma (PRKCG) interaction partners

1. Here, substitution studies on peptides correlating to the C1B domain in PKC gamma show that a flexible structure and ability to be phosphorylated on serine 109 are critical for this purpose.