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Items: 1 to 20 of 120

1.

The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5).

Zhou Y, Zhang H, He B, Du J, Lin H, Cerione RA, Hao Q.

J Biol Chem. 2012 Aug 17;287(34):28307-14. doi: 10.1074/jbc.M112.384511.

2.

Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.

Du J, Zhou Y, Su X, Yu JJ, Khan S, Jiang H, Kim J, Woo J, Kim JH, Choi BH, He B, Chen W, Zhang S, Cerione RA, Auwerx J, Hao Q, Lin H.

Science. 2011 Nov 11;334(6057):806-9. doi: 10.1126/science.1207861.

3.

Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin.

Schuetz A, Min J, Antoshenko T, Wang CL, Allali-Hassani A, Dong A, Loppnau P, Vedadi M, Bochkarev A, Sternglanz R, Plotnikov AN.

Structure. 2007 Mar;15(3):377-89.

4.

Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition.

Fischer F, Gertz M, Suenkel B, Lakshminarasimhan M, Schutkowski M, Steegborn C.

PLoS One. 2012;7(9):e45098. doi: 10.1371/journal.pone.0045098.

5.

Chemical probing of the human sirtuin 5 active site reveals its substrate acyl specificity and peptide-based inhibitors.

Roessler C, Nowak T, Pannek M, Gertz M, Nguyen GT, Scharfe M, Born I, Sippl W, Steegborn C, Schutkowski M.

Angew Chem Int Ed Engl. 2014 Sep 26;53(40):10728-32. doi: 10.1002/anie.201402679.

PMID:
25111069
6.

Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5.

Szczepankiewicz BG, Dai H, Koppetsch KJ, Qian D, Jiang F, Mao C, Perni RB.

J Org Chem. 2012 Sep 7;77(17):7319-29. doi: 10.1021/jo301067e.

PMID:
22849721
7.

Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins).

Trapp J, Meier R, Hongwiset D, Kassack MU, Sippl W, Jung M.

ChemMedChem. 2007 Oct;2(10):1419-31.

PMID:
17628866
8.

Inhibitors of the NAD(+)-Dependent Protein Desuccinylase and Demalonylase Sirt5.

Maurer B, Rumpf T, Scharfe M, Stolfa DA, Schmitt ML, He W, Verdin E, Sippl W, Jung M.

ACS Med Chem Lett. 2012 Oct 6;3(12):1050-3. doi: 10.1021/ml3002709.

9.

Structure and biochemical functions of SIRT6.

Pan PW, Feldman JL, Devries MK, Dong A, Edwards AM, Denu JM.

J Biol Chem. 2011 Apr 22;286(16):14575-87. doi: 10.1074/jbc.M111.218990.

10.

Thiosuccinyl peptides as Sirt5-specific inhibitors.

He B, Du J, Lin H.

J Am Chem Soc. 2012 Feb 1;134(4):1922-5. doi: 10.1021/ja2090417.

11.

Role of the Substrate Specificity-Defining Residues of Human SIRT5 in Modulating the Structural Stability and Inhibitory Features of the Enzyme.

Yu J, Haldar M, Mallik S, Srivastava DK.

PLoS One. 2016 Mar 29;11(3):e0152467. doi: 10.1371/journal.pone.0152467.

12.

Structural insights into intermediate steps in the Sir2 deacetylation reaction.

Hawse WF, Hoff KG, Fatkins DG, Daines A, Zubkova OV, Schramm VL, Zheng W, Wolberger C.

Structure. 2008 Sep 10;16(9):1368-77. doi: 10.1016/j.str.2008.05.015.

13.

Crystal structures of human SIRT3 displaying substrate-induced conformational changes.

Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB.

J Biol Chem. 2009 Sep 4;284(36):24394-405. doi: 10.1074/jbc.M109.014928.

14.

Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases.

Borra MT, Langer MR, Slama JT, Denu JM.

Biochemistry. 2004 Aug 3;43(30):9877-87.

PMID:
15274642
15.

Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide.

Hoff KG, Avalos JL, Sens K, Wolberger C.

Structure. 2006 Aug;14(8):1231-40.

16.

Inhibition of the human deacylase Sirtuin 5 by the indole GW5074.

Suenkel B, Fischer F, Steegborn C.

Bioorg Med Chem Lett. 2013 Jan 1;23(1):143-6. doi: 10.1016/j.bmcl.2012.10.136.

PMID:
23195732
17.

Inhibitors of NAD+ dependent histone deacetylases (sirtuins).

Neugebauer RC, Sippl W, Jung M.

Curr Pharm Des. 2008;14(6):562-73. Review.

PMID:
18336301
18.

Structural basis for the NAD-dependent deacetylase mechanism of Sir2.

Chang JH, Kim HC, Hwang KY, Lee JW, Jackson SP, Bell SD, Cho Y.

J Biol Chem. 2002 Sep 13;277(37):34489-98.

19.
20.

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases.

Zhao K, Harshaw R, Chai X, Marmorstein R.

Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8563-8.

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