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PMID |
Sentence |
1 |
18054327
|
Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5.
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2 |
18054327
|
Yeast silent information regulator 2 (SIR2) is involved in extension of yeast longevity by calorie restriction, and SIRT3, SIRT4, and SIRT5 are mammalian homologs of SIR2 localized in mitochondria.
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3 |
18054327
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SIRT3, SIRT4, and SIRT5 proteins were localized in different compartments of the mitochondria.
|
4 |
18054327
|
When SIRT3 and SIRT5 were co-expressed in the cell, localization of SIRT3 protein changed from mitochondria to nucleus.
|
5 |
18054327
|
These results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria.
|
6 |
18054327
|
Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5.
|
7 |
18054327
|
Yeast silent information regulator 2 (SIR2) is involved in extension of yeast longevity by calorie restriction, and SIRT3, SIRT4, and SIRT5 are mammalian homologs of SIR2 localized in mitochondria.
|
8 |
18054327
|
SIRT3, SIRT4, and SIRT5 proteins were localized in different compartments of the mitochondria.
|
9 |
18054327
|
When SIRT3 and SIRT5 were co-expressed in the cell, localization of SIRT3 protein changed from mitochondria to nucleus.
|
10 |
18054327
|
These results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria.
|
11 |
18054327
|
Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5.
|
12 |
18054327
|
Yeast silent information regulator 2 (SIR2) is involved in extension of yeast longevity by calorie restriction, and SIRT3, SIRT4, and SIRT5 are mammalian homologs of SIR2 localized in mitochondria.
|
13 |
18054327
|
SIRT3, SIRT4, and SIRT5 proteins were localized in different compartments of the mitochondria.
|
14 |
18054327
|
When SIRT3 and SIRT5 were co-expressed in the cell, localization of SIRT3 protein changed from mitochondria to nucleus.
|
15 |
18054327
|
These results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria.
|
16 |
18054327
|
Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5.
|
17 |
18054327
|
Yeast silent information regulator 2 (SIR2) is involved in extension of yeast longevity by calorie restriction, and SIRT3, SIRT4, and SIRT5 are mammalian homologs of SIR2 localized in mitochondria.
|
18 |
18054327
|
SIRT3, SIRT4, and SIRT5 proteins were localized in different compartments of the mitochondria.
|
19 |
18054327
|
When SIRT3 and SIRT5 were co-expressed in the cell, localization of SIRT3 protein changed from mitochondria to nucleus.
|
20 |
18054327
|
These results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria.
|
21 |
18054327
|
Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5.
|
22 |
18054327
|
Yeast silent information regulator 2 (SIR2) is involved in extension of yeast longevity by calorie restriction, and SIRT3, SIRT4, and SIRT5 are mammalian homologs of SIR2 localized in mitochondria.
|
23 |
18054327
|
SIRT3, SIRT4, and SIRT5 proteins were localized in different compartments of the mitochondria.
|
24 |
18054327
|
When SIRT3 and SIRT5 were co-expressed in the cell, localization of SIRT3 protein changed from mitochondria to nucleus.
|
25 |
18054327
|
These results suggest that the SIRT3, SIRT4, and SIRT5 proteins exert distinct functions in mitochondria.
|
26 |
20097174
|
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1.
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27 |
20097174
|
We identified carbamoyl phosphate synthetase 1 (CPS1), a key enzyme of the urea cycle that catalyzes condensation of ammonia with bicarbonate to form carbamoyl phosphate, as a target of SIRT5 by two-dimensional electrophoresis comparing mitochondrial proteins in livers of SIRT5 Tg and wild-type mice.
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28 |
20097174
|
CPS1 protein was more deacetylated and activated in liver of SIRT5 Tg mice than in wild-type.
|
29 |
20097174
|
Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1.
|
30 |
20097174
|
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1.
|
31 |
20097174
|
We identified carbamoyl phosphate synthetase 1 (CPS1), a key enzyme of the urea cycle that catalyzes condensation of ammonia with bicarbonate to form carbamoyl phosphate, as a target of SIRT5 by two-dimensional electrophoresis comparing mitochondrial proteins in livers of SIRT5 Tg and wild-type mice.
|
32 |
20097174
|
CPS1 protein was more deacetylated and activated in liver of SIRT5 Tg mice than in wild-type.
|
33 |
20097174
|
Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1.
|
34 |
20097174
|
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1.
|
35 |
20097174
|
We identified carbamoyl phosphate synthetase 1 (CPS1), a key enzyme of the urea cycle that catalyzes condensation of ammonia with bicarbonate to form carbamoyl phosphate, as a target of SIRT5 by two-dimensional electrophoresis comparing mitochondrial proteins in livers of SIRT5 Tg and wild-type mice.
|
36 |
20097174
|
CPS1 protein was more deacetylated and activated in liver of SIRT5 Tg mice than in wild-type.
|
37 |
20097174
|
Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1.
|
38 |
20097174
|
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1.
|
39 |
20097174
|
We identified carbamoyl phosphate synthetase 1 (CPS1), a key enzyme of the urea cycle that catalyzes condensation of ammonia with bicarbonate to form carbamoyl phosphate, as a target of SIRT5 by two-dimensional electrophoresis comparing mitochondrial proteins in livers of SIRT5 Tg and wild-type mice.
|
40 |
20097174
|
CPS1 protein was more deacetylated and activated in liver of SIRT5 Tg mice than in wild-type.
|
41 |
20097174
|
Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1.
|
42 |
22249520
|
The nuclear sirtuins, SIRT1, SIRT6 and SIRT7, regulate the activity of key transcription factors and cofactors of numerous metabolic pathways in almost all tissues by linking nutrient signals with the cellular responses to energy demands.
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43 |
22249520
|
The mitochondrial sirtuins, SIRT3, SIRT4 and SIRT5, regulate the activity of important mitochondrial enzymes and drive metabolic cycles in response to fasting and calorie restriction.
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44 |
23085393
|
These results suggest that SIRT5 activates UOX through deacetylation in mouse liver mitochondria.
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45 |
23908846
|
The sirtuins are highly conserved enzyme homologues of the yeast Sir2, with activities of NAD+ dependent deacetylase and/or mono ADP ribosyltransferase.
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46 |
23908846
|
In addition, until recently, the role of the seven mammalian sirtuins, SIRT1 to SIRT7, in regulating lifespan was unclear.
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47 |
24014411
|
Of the seven mammalian sirtuins, three localize to the mitochondria: SIRT3, SIRT4, and SIRT5.
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