Ignet

Gene Information

Gene symbol: AKT2

Gene name: v-akt murine thymoma viral oncogene homolog 2

HGNC ID: 392

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	CD8A	1 hits
3	GZMB	1 hits
4	PIK3CA	1 hits
5	SREBF1	1 hits

Related Sentences

#	PMID	Sentence
1	20130133	Hepatitis C virus genotype-3a core protein enhances sterol regulatory element-binding protein-1 activity through the phosphoinositide 3-kinase-Akt-2 pathway.
2	20130133	We previously showed that, through sterol regulatory element binding protein-1 (SREBP-1), HCV-3a core protein upregulates the promoter activity of fatty acid synthase, a major enzyme involved in de novo lipid synthesis.
3	20130133	In this study, we investigated whether HCV-3a core can activate SREBP-1 and studied the role of phosphoinositide 3-kinase (PI3K)-Akt-2 pathway in modulating SREBP-1 activity by HCV-3a core.
4	20130133	To investigate the role of the PI3K-Akt-2 pathway in SREBP-1 activation by HCV-3a core, PI3K and Akt-2 activity was inhibited by using the chemical inhibitor LY294002, a dominant-negative Akt-2 plasmid, or knockdown of Akt-2 by small hairpin RNA.
5	20130133	Our results showed that inhibition of PI3K and Akt-2 was associated with reduced SREBP-1 activation by HCV-3a core.
6	20130133	These results indicate a role for PI3K and Akt-2 in increasing SREBP-1 activity by HCV-3a core protein and provide a mechanism of steatosis caused by HCV.
7	20130133	Hepatitis C virus genotype-3a core protein enhances sterol regulatory element-binding protein-1 activity through the phosphoinositide 3-kinase-Akt-2 pathway.
8	20130133	We previously showed that, through sterol regulatory element binding protein-1 (SREBP-1), HCV-3a core protein upregulates the promoter activity of fatty acid synthase, a major enzyme involved in de novo lipid synthesis.
9	20130133	In this study, we investigated whether HCV-3a core can activate SREBP-1 and studied the role of phosphoinositide 3-kinase (PI3K)-Akt-2 pathway in modulating SREBP-1 activity by HCV-3a core.
10	20130133	To investigate the role of the PI3K-Akt-2 pathway in SREBP-1 activation by HCV-3a core, PI3K and Akt-2 activity was inhibited by using the chemical inhibitor LY294002, a dominant-negative Akt-2 plasmid, or knockdown of Akt-2 by small hairpin RNA.
11	20130133	Our results showed that inhibition of PI3K and Akt-2 was associated with reduced SREBP-1 activation by HCV-3a core.
12	20130133	These results indicate a role for PI3K and Akt-2 in increasing SREBP-1 activity by HCV-3a core protein and provide a mechanism of steatosis caused by HCV.
13	20130133	Hepatitis C virus genotype-3a core protein enhances sterol regulatory element-binding protein-1 activity through the phosphoinositide 3-kinase-Akt-2 pathway.
14	20130133	We previously showed that, through sterol regulatory element binding protein-1 (SREBP-1), HCV-3a core protein upregulates the promoter activity of fatty acid synthase, a major enzyme involved in de novo lipid synthesis.
15	20130133	In this study, we investigated whether HCV-3a core can activate SREBP-1 and studied the role of phosphoinositide 3-kinase (PI3K)-Akt-2 pathway in modulating SREBP-1 activity by HCV-3a core.
16	20130133	To investigate the role of the PI3K-Akt-2 pathway in SREBP-1 activation by HCV-3a core, PI3K and Akt-2 activity was inhibited by using the chemical inhibitor LY294002, a dominant-negative Akt-2 plasmid, or knockdown of Akt-2 by small hairpin RNA.
17	20130133	Our results showed that inhibition of PI3K and Akt-2 was associated with reduced SREBP-1 activation by HCV-3a core.
18	20130133	These results indicate a role for PI3K and Akt-2 in increasing SREBP-1 activity by HCV-3a core protein and provide a mechanism of steatosis caused by HCV.
19	20130133	Hepatitis C virus genotype-3a core protein enhances sterol regulatory element-binding protein-1 activity through the phosphoinositide 3-kinase-Akt-2 pathway.
20	20130133	We previously showed that, through sterol regulatory element binding protein-1 (SREBP-1), HCV-3a core protein upregulates the promoter activity of fatty acid synthase, a major enzyme involved in de novo lipid synthesis.
21	20130133	In this study, we investigated whether HCV-3a core can activate SREBP-1 and studied the role of phosphoinositide 3-kinase (PI3K)-Akt-2 pathway in modulating SREBP-1 activity by HCV-3a core.
22	20130133	To investigate the role of the PI3K-Akt-2 pathway in SREBP-1 activation by HCV-3a core, PI3K and Akt-2 activity was inhibited by using the chemical inhibitor LY294002, a dominant-negative Akt-2 plasmid, or knockdown of Akt-2 by small hairpin RNA.
23	20130133	Our results showed that inhibition of PI3K and Akt-2 was associated with reduced SREBP-1 activation by HCV-3a core.
24	20130133	These results indicate a role for PI3K and Akt-2 in increasing SREBP-1 activity by HCV-3a core protein and provide a mechanism of steatosis caused by HCV.
25	26155399	Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8⁺ T-cell proliferation and survival.
26	26155399	The differentiation of CD8 ⁺ memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway.
27	26155399	We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 ⁺ T cells.
28	26155399	We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 ⁺ T cells, and their inhibition enhances the therapeutically superior T_CM phenotype.
29	26155399	Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 ⁺ T-cell exhaustion and preserves naïve and T_CM CD8 ⁺ T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability.
30	26155399	Here, we define a mechanism in which proliferative potential, function, and survival of CD8 ⁺ T cells are enhanced by maintaining a reservoir of T_CM and naïve cells using only Akt1 and Akt2 inhibition.
31	26155399	Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 ⁺ T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies.
32	26155399	Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8⁺ T-cell proliferation and survival.
33	26155399	The differentiation of CD8 ⁺ memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway.
34	26155399	We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 ⁺ T cells.
35	26155399	We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 ⁺ T cells, and their inhibition enhances the therapeutically superior T_CM phenotype.
36	26155399	Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 ⁺ T-cell exhaustion and preserves naïve and T_CM CD8 ⁺ T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability.
37	26155399	Here, we define a mechanism in which proliferative potential, function, and survival of CD8 ⁺ T cells are enhanced by maintaining a reservoir of T_CM and naïve cells using only Akt1 and Akt2 inhibition.
38	26155399	Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 ⁺ T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies.
39	26155399	Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8⁺ T-cell proliferation and survival.
40	26155399	The differentiation of CD8 ⁺ memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway.
41	26155399	We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 ⁺ T cells.
42	26155399	We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 ⁺ T cells, and their inhibition enhances the therapeutically superior T_CM phenotype.
43	26155399	Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 ⁺ T-cell exhaustion and preserves naïve and T_CM CD8 ⁺ T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability.
44	26155399	Here, we define a mechanism in which proliferative potential, function, and survival of CD8 ⁺ T cells are enhanced by maintaining a reservoir of T_CM and naïve cells using only Akt1 and Akt2 inhibition.
45	26155399	Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 ⁺ T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies.
46	26155399	Akt1 and -2 inhibition diminishes terminal differentiation and enhances central memory CD8⁺ T-cell proliferation and survival.
47	26155399	The differentiation of CD8 ⁺ memory T cells is thought to be coordinated by the phosphoinositide 3-kinase (PI3K)/Akt pathway.
48	26155399	We, therefore, investigated the role of Akt isoforms in the differentiation and proliferation of memory CD8 ⁺ T cells.
49	26155399	We found that Akt1 and Akt2, but not Akt3, drive the terminal differentiation of CD8 ⁺ T cells, and their inhibition enhances the therapeutically superior T_CM phenotype.
50	26155399	Furthermore, the inhibition of Akt1 and Akt2, but not Akt 3, delays CD8 ⁺ T-cell exhaustion and preserves naïve and T_CM CD8 ⁺ T cells, thus enhancing their proliferative ability and survival and prolonging their cytokine and Granzyme B production ability.
51	26155399	Here, we define a mechanism in which proliferative potential, function, and survival of CD8 ⁺ T cells are enhanced by maintaining a reservoir of T_CM and naïve cells using only Akt1 and Akt2 inhibition.
52	26155399	Therefore, our findings strongly suggest the utility of using Akt1 and Akt2 inhibitors to modulate CD8 ⁺ T cells, both for adoptive cell transfer and vaccine-based cancer immune therapies.