# |
PMID |
Sentence |
1 |
1113453
|
There was no loss of glutamic dehydrogenase, glucose-6-phosphate dehydrogenase or acid phosphatase.
|
2 |
24947049
|
Biochemical analysis basically on enzymes of antioxidant-defense system, including glutathione-S-transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase, further supported that diabetes-induced damage in the kidney is mostly dependent on the increased oxidative stress and timolol, having an antioxidant-like action, could protect the kidney against hyperglycemia-induced damage without normalization of high-blood glucose level.
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3 |
30785802
|
Decreased G6PD protein expression was mediated by the ubiquitin proteasome pathway.
|
4 |
30785802
|
We found that the von Hippel-Lindau (VHL) protein, an E3 ubiquitin ligase subunit, directly bound to G6PD and degraded G6PD through ubiquitylating G6PD on K366 and K403.
|
5 |
30785802
|
In summary, our data suggest that high glucose induces ubiquitination of G6PD by VHL E3 ubiquitin ligase, which leads to ROS accumulation and podocyte injury.
|
6 |
30785802
|
Decreased G6PD protein expression was mediated by the ubiquitin proteasome pathway.
|
7 |
30785802
|
We found that the von Hippel-Lindau (VHL) protein, an E3 ubiquitin ligase subunit, directly bound to G6PD and degraded G6PD through ubiquitylating G6PD on K366 and K403.
|
8 |
30785802
|
In summary, our data suggest that high glucose induces ubiquitination of G6PD by VHL E3 ubiquitin ligase, which leads to ROS accumulation and podocyte injury.
|
9 |
30785802
|
Decreased G6PD protein expression was mediated by the ubiquitin proteasome pathway.
|
10 |
30785802
|
We found that the von Hippel-Lindau (VHL) protein, an E3 ubiquitin ligase subunit, directly bound to G6PD and degraded G6PD through ubiquitylating G6PD on K366 and K403.
|
11 |
30785802
|
In summary, our data suggest that high glucose induces ubiquitination of G6PD by VHL E3 ubiquitin ligase, which leads to ROS accumulation and podocyte injury.
|