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SIRT5 gene

Known as: SIR2L5, SIRT5, SIR2, S. CEREVISIAE, HOMOLOG-LIKE 5 
National Institutes of Health

Papers overview

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Highly Cited
2016
Highly Cited
2016
Significance Lysine succinylation is a recently discovered protein posttranslational modification and SIRT5 is an efficient… 
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Highly Cited
2016
Highly Cited
2016
Excess in mitochondrial reactive oxygen species (ROS) is considered as a major cause of cellular oxidative stress. NADPH, the… 
Highly Cited
2015
Highly Cited
2015
In liver the mitochondrial sirtuin, SIRT5, controls ammonia detoxification by regulating CPS1, the first enzyme of the urea cycle… 
Highly Cited
2014
Highly Cited
2014
We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine… 
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Highly Cited
2014
Highly Cited
2014
Lung cancer is one of the leading causes of cancer-related death in developed countries. Despite decades of intensive efforts to… 
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Highly Cited
2012
Highly Cited
2012
Sirtuins are protein deacetylases regulating metabolism, stress responses, and aging processes, and they were suggested to… 
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Highly Cited
2011
Highly Cited
2011
Biological functions of sirtuins may involve lysine desuccinylase and demalonylase activities. Silent information regulator 2… 
Highly Cited
2010
Highly Cited
2010
SIR2 protein, an NAD-dependent deacetylase, is localized to nucleus and is involved in life span extension by calorie restriction… 
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Highly Cited
2008
Highly Cited
2008
The enzymes of the Sirtuin family of nicotinamide-adenine-dinucleotide-dependent protein deacetylases are emerging key players in… 
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Highly Cited
2008
Highly Cited
2008
Background Growing evidence suggests that sirtuins, a family of seven distinct NAD-dependent enzymes, are involved in the… 
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