Ignet

Gene Information

Gene symbol: SLC9A3R2

Gene name: solute carrier family 9, subfamily A (NHE3, cation proton antiporter 3), member 3 regulator 2

HGNC ID: 11076

Synonyms: SIP-1, TKA-1, NHERF-2, E3KARP

Related Genes

#	Gene Symbol	Number of hits
1	DLG4	1 hits
2	EFNB1	1 hits
3	NPHS1	1 hits
4	SCHIP1	1 hits

Related Sentences

#	PMID	Sentence
1	25807495	Schip1 is a novel podocyte foot process protein that mediates actin cytoskeleton rearrangements and forms a complex with Nherf2 and ezrin.
2	25965062	Correction: Schip1 Is a Novel Podocyte Foot Process Protein that Mediates Actin Cytoskeleton Rearrangements and Forms a Complex with Nherf2 and Ezrin.
3	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
4	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
5	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
6	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
7	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
8	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
9	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
10	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
11	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
12	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
13	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
14	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
15	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
16	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
17	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
18	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
19	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
20	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
21	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
22	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
23	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
24	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
25	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
26	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
27	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
28	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
29	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
30	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
31	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
32	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
33	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
34	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
35	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
36	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
37	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
38	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
39	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
40	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
41	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
42	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
43	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
44	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
45	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
46	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
47	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
48	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
49	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
50	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
51	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
52	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
53	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
54	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
55	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
56	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
57	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
58	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
59	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
60	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
61	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
62	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
63	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
64	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
65	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.
66	33887216	Nephrin-Ephrin-B1-Na⁺/H⁺ Exchanger Regulatory Factor 2-Ezrin-Actin Axis Is Critical in Podocyte Injury.
67	33887216	RNA-sequencing analysis suggested that Na⁺/H⁺ exchanger regulatory factor 2 (NHERF2), a scaffolding protein, is associated with ephrin-B1.
68	33887216	NHERF2 was expressed at the apical area and the slit diaphragm, and interacted with the nephrin-ephrin-B1 complex at the slit diaphragm.
69	33887216	The nephrin-ephrin-B1-NHERF2 complex interacted with ezrin bound to F-actin.
70	33887216	NHERF2 bound ephrin-B1 via its first postsynaptic density protein-95/disks large/zonula occludens-1 domain, and podocalyxin via its second postsynaptic density protein-95/disks large/zonula occludens-1 domain.
71	33887216	Both in vitro analyses with human embryonic kidney 293 cells and in vivo study with rat nephrotic model showed that stimulaiton of the slit diaphragm, phosphorylation of nephrin and ephrin-B1, and dephosphorylation of NHERF2 and ezrin, disrupted the linkages of ephrin-B1-NHERF2 and NHERF2-ezrin.
72	33887216	It is conceivable that the linkage of nephrin-ephrin-B1-NHERF2-ezrin-actin is a novel critical axis in the podocytes.
73	33887216	Ephrin-B1 phosphorylation also disrupted the linkage of an apical transmembrane protein, podocalyxin, with NHERF2-ezrin-actin.
74	33887216	The phosphorylation of ephrin-B1 and the consequent dephosphorylation of NHERF2 are critical initiation events leading to podocyte injury.