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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.3.1.286
739727
Amberlyst-15 catalyzed Povarov reaction of N-arylidene-1H-indazol-6-amines and indoles: a greener approach to the synthesis of exo-1,6,7,7a,12,12a-hexahydroindolo[3,2-c]pyrazolo[3,4-f]quinolines as potential sirtuin inhibitors
Tetrahedron Lett.
56
2289-2292
2015
Homo sapiens
-
2.3.1.286
752068
The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
Proc. Natl. Acad. Sci. USA
97
5807-5811
2000
Saccharomyces cerevisiae
10811920
2.3.1.286
750253
Crystal structure of a SIR2 homolog-NAD complex
Cell
105
269-279
2001
Archaeoglobus fulgidus
11336676
2.3.1.286
729560
hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
Cell
107
149-159
2001
Homo sapiens
11672523
2.3.1.286
749874
Chemistry of gene silencing the mechanism of NAD+-dependent deacetylation reactions
Biochemistry
40
15456-15463
2001
Thermotoga maritima
11747420
2.3.1.286
729638
Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
EMBO J.
21
2383-2396
2002
Homo sapiens
12006491
2.3.1.286
730840
SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria
Proc. Natl. Acad. Sci. USA
99
13653-13658
2002
Homo sapiens
12374852
2.3.1.286
752253
Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
Science
298
2390-2392
2002
Salmonella enterica
12493915
2.3.1.286
752023
Histone deacetylation by Sir2 generates a transcriptionally repressed nucleoprotein complex
Proc. Natl. Acad. Sci. USA
100
1609-1614
2003
Drosophila melanogaster
12571358
2.3.1.286
749878
Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
Biochemistry
42
9249-9256
2003
Archaeoglobus fulgidus
12899610
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