Visualisation of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.

E* Barkauskaite; A* Brassington; ES Tan; J Warwicker; MS Dunstan; B Banos; P Lafite; M Ahel; TJ Mitchison; I Ahel; D Leys

Visualisation of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.

E* Barkauskaite, A* Brassington, ES Tan, J Warwicker, MS Dunstan, B Banos, P Lafite, M Ahel, TJ Mitchison, I Ahel, D Leys

The University of Manchester

Research output: Contribution to journal › Article › peer-review

Original language	English
Journal	Nature Communications
Publication status	Published - 6 Aug 2013

Cite this

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title = "Visualisation of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.",

author = "E* Barkauskaite and A* Brassington and ES Tan and J Warwicker and MS Dunstan and B Banos and P Lafite and M Ahel and TJ Mitchison and I Ahel and D Leys",

year = "2013",

month = aug,

day = "6",

language = "English",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Research",

}

TY - JOUR

T1 - Visualisation of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.

AU - Barkauskaite, E

AU - Brassington, A

AU - Tan, ES

AU - Warwicker, J

AU - Dunstan, MS

AU - Banos, B

AU - Lafite, P

AU - Ahel, M

AU - Mitchison, TJ

AU - Ahel, I

AU - Leys, D

PY - 2013/8/6

Y1 - 2013/8/6

M3 - Article

SN - 2041-1723

JO - Nature Communications

JF - Nature Communications

ER -