Aperçu des produits pour anti-PDPK1 (PDPK1) Anticorps

Pig (Porcine) 3-phosphoinositide Dependent Protein Kinase-1 (PDPK1) interaction partners

1. miR-375 directly targeted PDK1 in porcine pancreatic stem cells suppressing cell proliferation and differentiation into islet-like cells.

Human 3-phosphoinositide Dependent Protein Kinase-1 (PDPK1) interaction partners

1. Studied role of 3-phosphoinositide dependent protein kinase (PDPK1) in gemcitabine resistance in pancreatic cancer stem-like cells.

2. The present study strongly suggests that miR-718 inhibits papillary thyroid cancer cell proliferation, metastasis, and glucose metabolism...through PDPK1

3. the combination of BX-912 and ABT-263, a BH3 mimetic, resulted in the enhancement of the induction of apoptosis. In conclusion, our results suggest that PDPK1 is a potential novel therapeutic target in Mantle cell lymphoma (MCL) and indicate that clinical development of PDPK1-targeted therapy for MCL is desirable.

4. Our experimental results suggested that PDK1 may promote chondrocyte apoptosis in osteoarthritis via p38 MAPK signaling pathway

5. our results offer significant insight into how PIK3CA overexpression drives squamous cell carcinoma (HNSCC) invasion and metastasis, providing a rationale for targeting PI3K/PDK1 and TGFb signaling in advanced HNSCC patients with PIK3CA amplification

6. Ribociclib, in combination with GSK2334470 or the PI3Kalpha inhibitor alpelisib, decreased xenograft tumor growth more potently than each drug alone. Taken together, our results highlight a role for the PI3K-PDK1 signaling pathway in mediating acquired resistance to CDK4/6 inhibitors.

7. Decreased PDK1 protein expression in A2058 cells.

8. Together these results indicate a strong potential regulatory role for PDK1 in OC stimulatory pathways (Akt, ERK) and autophagy induction (via mTORC1), which may contribute to the OC phenotype in Paget's disease of bone.

9. It targeted the 3-phosphoinositide-dependent protein kinase 1 gene that appeared to be a potent regulator of AKT.

10. Highly expressed PDK1 could promote cell invasion and secretion of IL-1beta and IL-6 in human rheumatoid arthritis synovial MH7A cells. Inhibition of RSK2 reduced the PDK1-induced cell invasion and cytokines secretion in MH7A cells. In response to TNF-alpha, PDK1 could phosphorylate RSK2 and activated RSK2, then promoting the activation of NF-kappaB.

11. In cancer cells resistant to PI3Kalpha inhibition, PDK1 blockade restores sensitivity to these therapies. SGK1, which is activated by PDK1, contributes to the maintenance of residual mTORC1 activity through direct phosphorylation and inhibition of TSC2.

12. Results suggest that Ser-64 is an important phosphorylation site that is part of a positive feedback loop for human PDK1-PKCtheta;-mediated T cell activation.

13. Elevated expression of PDK1 was an independent negative prognostic factor of gastric carcinoma.

14. miR-138-1* played a critical role in aflatoxin B1-induced malignant transformation of B-2A13 cells by targeting PDK1.

15. miR-454 functions as a tumor suppressor in glioblastoma, inhibiting proliferation of human glioblastoma cells by suppressing PDK1 expression.

16. Decreased PDK1 level is closely associated with reduced Akt/cyclin D1 activity.

17. MiR-138 regulation of PI3K signaling in ASMCs by altering the expression of PDK1.

18. Dephosphorylation of PDK-1 and the resulting changes to Akt phosphorylation is one of the mechanisms by which infection with Helicobacter pylori alter the balance between apoptosis and cell proliferation.

19. Data suggest that claudin-18 suppresses the abnormal proliferation and motility of lung epithelial cells mediated by inhibition of phosphorylation of phosphoinositide-dependent protein kinase-1 and proto-oncogene protein c-akt (Akt).

20. DK1 inhibits the formation of the TAK1-TAB2-TRAF6 complex and leads to the inhibition of TRAF6 ubiquitination.

Mouse (Murine) 3-phosphoinositide Dependent Protein Kinase-1 (PDPK1) interaction partners

1. our results offer significant insight into how PIK3CA overexpression drives squamous cell carcinoma (HNSCC) invasion and metastasis, providing a rationale for targeting PI3K/PDK1 and TGFb signaling in advanced HNSCC patients with PIK3CA amplification

2. PDK1 signaling regulates the basal-to-suprabasal switch in developing epidermis by acting as both an activator and organizer of asymmetric cell division and the Notch-dependent differentiation program.

3. Data indicate that mammary-specific ablation of 3-phosphoinositide dependent protein kinase 1 (PDK1) could delay tumor initiation, progression and metastasis in a spontaneous mouse tumor model.

4. PDK1 was highly expressed in synovia of collagen-induced-arthritis mice compared to control. The expressions of PDK1, p-PDK1, RSK2 and p-RSK2 were all up-regulated in CIA compared with normal. This indicated that PDK1/RSK2 may participate in inflammatory progress of RA.

5. PDK1 is required for Ca(2+)-dependent platelet activation on stimulation of collagen receptor glycoprotein VI, arterial thrombotic occlusion, and ischemic stroke in vivo.

6. In conclusion, we have identified that ARL15 acts as an insulin-sensitizing effector molecule to upregulate the phosphorylation of members of the canonical IR/IRS1/PDPK1/AKT insulin pathway by interacting with its GAP ASAP2 and activating PDPK1. This research may provide new insights into GTPase-mediated insulin signalling regulation and facilitate the development of new pharmacotherapeutic targets for insulin sensitizati

7. Only when suboptimal doses of Akt-Pdpk1 interaction inhibitor NSC156529 were used an additive effect with Notch inhibition was seen. We conclude that the Akt pathway inhibitor NSC156529 is potentially useful as single treatment for liver tumors with hyperactivated Akt signaling.

8. Xanthium strumarium methanolic extract exerts anti-inflammatory activity in vitro and in vivo by inhibiting PDK1 kinase activity and blocking signaling to its downstream transcription factor, NF-kappaB.

9. PDPK1 is required for exercise-induced cardiac hypertrophy but does not contribute to exercise-induced increases in mitochondrial function.

10. The PDK1 knock-in mice displayed a reduced brain size due to a reduction in neuronal cell size rather than cell number.

11. PDK1 is an important regulator in arterial thrombosis formation.

12. PDK1 is essential for BCR-induced signal transduction to Foxo and NF-kappaB and is indispensable for both resting and activated B cell survival.

13. Results suggest that heat shock protein 90 inhibitor radicicol inhibited 3T3-L1 preadipocyte differentiation through affecting the PDK1/Akt pathway.

14. Inhibition of PDK1 promotes localization of TACE to the plasma membrane, restores TACE-dependent alpha-secretase activity and cleavage of APP, PrP(C) and TNFR1, and attenuates PrP(Sc)- and Abeta-induced neurotoxicity.

15. Data show that insulin stimulates GLUT4 translocation to the cell surface and iglucose uptake in an Akt1/2-dependent manner; PI3K phosphorylates Thr308 and Ser473 for Akt1 and Ser474 alone for Akt2; and PDK1 phosphorylates Thr308 for Akt1 and Akt2.

16. Direct genetic evidence for the importance of PDK1, in part through FOXO3a-dependent pathway, in melanoma development and progression.

17. These results indicate that PDK1 participates in the dysregulation of electrophysiological basis by regulating the PDK1-Foxo1 pathway

18. T34 phosphorylation by PDK1 promotes the membrane dissociation of activated Akt for its downstream action through attenuating membrane binding affinity.

19. PDK1 ablation promotes epidermal and T-cell mediated dysfunction leading to dermatitis.

20. PDK1 plays a significant role in the progression and growth of vascular tumors and targeting PDK1 may thus be considered in their treatment

Caenorhabditis elegans (C. elegans) 3-phosphoinositide Dependent Protein Kinase-1 (PDPK1) interaction partners

1. at least three C. elegans MTMs play essential roles in coelomocyte endocytosis, a process that also requires VPS34 (PI3K)

Arabidopsis thaliana 3-phosphoinositide Dependent Protein Kinase-1 (PDPK1) interaction partners

1. Piriformospora indica-stimulated growth response is mediated by a pathway consisting of the PLD-PDK1-OXI1 cascade.

2. PDK1 undergoes autophosphorylation at several sites; mutation of Ser-276 to Ala resulted in enzyme with no detectable autophosphorylation; other sites important for autophosphorylation &/or activity were Asp-167, Thr-176, & Thr-211

3. PDK1 is a potent enhancer of PID activity.

4. specific lipid signaling pathways converge on PTI1-2 via the PDK1-OXI1 axis