Ignet

Gene Information

Gene symbol: PHB2

Gene name: prohibitin 2

HGNC ID: 30306

Synonyms: REA, BCAP37, Bap37, p22

Related Genes

#	Gene Symbol	Number of hits
1	INS	1 hits
2	INSR	1 hits
3	NPHS2	1 hits
4	PHB	1 hits
5	STOM	1 hits
6	TP53	1 hits

Related Sentences

#	PMID	Sentence
1	25643582	Here, we provide a link between PHB2 deficiency and hyperactive insulin/IGF-1 signaling.
2	25643582	Inhibition of the insulin/IGF-1 signaling system through genetic deletion of the insulin receptor alone or in combination with the IGF-1 receptor or treatment with rapamycin prevented hyperphosphorylation of S6RP without affecting the mitochondrial structural defect, alleviated renal disease, and delayed the onset of kidney failure in PHB2-deficient animals.
3	25643582	Here, we provide a link between PHB2 deficiency and hyperactive insulin/IGF-1 signaling.
4	25643582	Inhibition of the insulin/IGF-1 signaling system through genetic deletion of the insulin receptor alone or in combination with the IGF-1 receptor or treatment with rapamycin prevented hyperphosphorylation of S6RP without affecting the mitochondrial structural defect, alleviated renal disease, and delayed the onset of kidney failure in PHB2-deficient animals.
5	27105734	Loss of the stomatin/PHB/flotillin/HflK/C (SPFH) domain containing protein PHB2 causes mitochondrial dysfunction and defective mitochondria-mediated signaling, which is implicated in a variety of human diseases, including progressive renal disease.
6	27105734	PHB2 coprecipitated with podocin, another SPFH domain-containing protein, essential for the assembly of the slit diaphragm protein-lipid supercomplex.
7	27105734	Consistent with an evolutionarily conserved extra-mitochondrial function, the ortholog of PHB2 in Caenorhabditis elegans was also not restricted to mitochondria but colocalized with the mechanosensory complex that requires the podocin ortholog MEC2 for assembly.
8	27105734	Loss of the stomatin/PHB/flotillin/HflK/C (SPFH) domain containing protein PHB2 causes mitochondrial dysfunction and defective mitochondria-mediated signaling, which is implicated in a variety of human diseases, including progressive renal disease.
9	27105734	PHB2 coprecipitated with podocin, another SPFH domain-containing protein, essential for the assembly of the slit diaphragm protein-lipid supercomplex.
10	27105734	Consistent with an evolutionarily conserved extra-mitochondrial function, the ortholog of PHB2 in Caenorhabditis elegans was also not restricted to mitochondria but colocalized with the mechanosensory complex that requires the podocin ortholog MEC2 for assembly.
11	27105734	Loss of the stomatin/PHB/flotillin/HflK/C (SPFH) domain containing protein PHB2 causes mitochondrial dysfunction and defective mitochondria-mediated signaling, which is implicated in a variety of human diseases, including progressive renal disease.
12	27105734	PHB2 coprecipitated with podocin, another SPFH domain-containing protein, essential for the assembly of the slit diaphragm protein-lipid supercomplex.
13	27105734	Consistent with an evolutionarily conserved extra-mitochondrial function, the ortholog of PHB2 in Caenorhabditis elegans was also not restricted to mitochondria but colocalized with the mechanosensory complex that requires the podocin ortholog MEC2 for assembly.
14	28187984	Last, we compared Cre efficiency in a disease model by mating Nphs2^{pod.T2A.ciCre.T2A.mTomato/wild-type} and hNphs2.Cre mice to Phb2^fl/fl mice.
15	28187984	The podocyte-specific Phb2 knockout by Nphs2^{pod.T2A.ciCre.T2A.mTomato/wild-type} mice resulted in an aggravated glomerular injury as compared to a podocyte-specific Phb2 gene deletion triggered by hNphs2.Cre.
16	28187984	Last, we compared Cre efficiency in a disease model by mating Nphs2^{pod.T2A.ciCre.T2A.mTomato/wild-type} and hNphs2.Cre mice to Phb2^fl/fl mice.
17	28187984	The podocyte-specific Phb2 knockout by Nphs2^{pod.T2A.ciCre.T2A.mTomato/wild-type} mice resulted in an aggravated glomerular injury as compared to a podocyte-specific Phb2 gene deletion triggered by hNphs2.Cre.
18	31883607	Among the differentially expressed proteins, prohibitin 1 (PHB1) and prohibitin 2 (PHB2) were upregulated in the kidneys of mice with MN, as demonstrated by immunohistochemistry (IHC), and this upregulation was observed in both the tubular cells and glomeruli.
19	31883607	Both shRNA-mediated knockdown of PHB1 or PHB2 inhibited tumor suppressor p53 expression and significantly promoted podocyte proliferation.
20	31883607	In addition, both PHB1 and PHB2 were responsible for cBSA-induced cytotoxicity.
21	31883607	Microarray analysis further revealed that the upregulation of PHB1 and PHB2 may be due to a blockage of proteasome activity.
22	31883607	Among the differentially expressed proteins, prohibitin 1 (PHB1) and prohibitin 2 (PHB2) were upregulated in the kidneys of mice with MN, as demonstrated by immunohistochemistry (IHC), and this upregulation was observed in both the tubular cells and glomeruli.
23	31883607	Both shRNA-mediated knockdown of PHB1 or PHB2 inhibited tumor suppressor p53 expression and significantly promoted podocyte proliferation.
24	31883607	In addition, both PHB1 and PHB2 were responsible for cBSA-induced cytotoxicity.
25	31883607	Microarray analysis further revealed that the upregulation of PHB1 and PHB2 may be due to a blockage of proteasome activity.
26	31883607	Among the differentially expressed proteins, prohibitin 1 (PHB1) and prohibitin 2 (PHB2) were upregulated in the kidneys of mice with MN, as demonstrated by immunohistochemistry (IHC), and this upregulation was observed in both the tubular cells and glomeruli.
27	31883607	Both shRNA-mediated knockdown of PHB1 or PHB2 inhibited tumor suppressor p53 expression and significantly promoted podocyte proliferation.
28	31883607	In addition, both PHB1 and PHB2 were responsible for cBSA-induced cytotoxicity.
29	31883607	Microarray analysis further revealed that the upregulation of PHB1 and PHB2 may be due to a blockage of proteasome activity.
30	31883607	Among the differentially expressed proteins, prohibitin 1 (PHB1) and prohibitin 2 (PHB2) were upregulated in the kidneys of mice with MN, as demonstrated by immunohistochemistry (IHC), and this upregulation was observed in both the tubular cells and glomeruli.
31	31883607	Both shRNA-mediated knockdown of PHB1 or PHB2 inhibited tumor suppressor p53 expression and significantly promoted podocyte proliferation.
32	31883607	In addition, both PHB1 and PHB2 were responsible for cBSA-induced cytotoxicity.
33	31883607	Microarray analysis further revealed that the upregulation of PHB1 and PHB2 may be due to a blockage of proteasome activity.