Purification of Recombinant Human PARG and Activity Assays.

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Purification of Recombinant Human PARG and Activity Assays.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Purification of Recombinant Human PARG and Activity Assays.

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Purification of Recombinant Human PARG and Activity Assays.

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Item

label

Purification of Recombinant Human PARG and Activity Assays.

@en

Purification of Recombinant Human PARG and Activity Assays.

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Purification of Recombinant Human PARG and Activity Assays.

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Purification of Recombinant Human PARG and Activity Assays.

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P1476

Purification of Recombinant Human PARG and Activity Assays

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P2093

Barbara Camuzeaux

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Jean-Christophe Amé

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Valérie Schreiber

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Éléa Héberlé

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P2860

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element

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

Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase

Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments.

Poly(ADP-ribose) (PAR) polymer is a death signal

Roles of poly(ADP-ribose) glycohydrolase in DNA damage and apoptosis.

A high-throughput screening-compatible homogeneous time-resolved fluorescence assay measuring the glycohydrolase activity of human poly(ADP-ribose) glycohydrolase.

Molecular heterogeneity and regulation of poly(ADP-ribose) glycohydrolase.

Radiation-induced mitotic catastrophe in PARG-deficient cells.

P304

395-413

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P31

scholarly article

P356

10.1007/978-1-4939-6993-7_25

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P407

English

P478

1608

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P50

Françoise Dantzer

P577

2017-01-01T00:00:00Z

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P698

28695523

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