Research ExplorerPublicationsStructure of mouse ADP-ribosylhydrolase 3 (mARH3).

Structure of mouse ADP-ribosylhydrolase 3 (mARH3).

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Structure of mouse ADP-ribosylhydrolase 3 (mARH3). / Mueller-Dieckmann, Christoph; Kernstock, Stefan; Mueller-Dieckmann, Jochen; Weiss, Manfred S; Koch Nolte, Friedrich.

In: ACTA CRYSTALLOGR F, Vol. 64, No. 3, 3, 2008, p. 156-162.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Mueller-Dieckmann, C, Kernstock, S, Mueller-Dieckmann, J, Weiss, MS & Koch Nolte, F 2008, 'Structure of mouse ADP-ribosylhydrolase 3 (mARH3).', ACTA CRYSTALLOGR F, vol. 64, no. 3, 3, pp. 156-162. <http://www.ncbi.nlm.nih.gov/pubmed/18323597?dopt=Citation>

APA

Mueller-Dieckmann, C., Kernstock, S., Mueller-Dieckmann, J., Weiss, M. S., & Koch Nolte, F. (2008). Structure of mouse ADP-ribosylhydrolase 3 (mARH3). ACTA CRYSTALLOGR F, 64(3), 156-162. [3]. http://www.ncbi.nlm.nih.gov/pubmed/18323597?dopt=Citation

Vancouver

Mueller-Dieckmann C, Kernstock S, Mueller-Dieckmann J, Weiss MS, Koch Nolte F. Structure of mouse ADP-ribosylhydrolase 3 (mARH3). ACTA CRYSTALLOGR F. 2008;64(3):156-162. 3.

Bibtex

@article{9286031849b54bbfa5c6dcc682744891,
title = "Structure of mouse ADP-ribosylhydrolase 3 (mARH3).",
abstract = "ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.",
author = "Christoph Mueller-Dieckmann and Stefan Kernstock and Jochen Mueller-Dieckmann and Weiss, {Manfred S} and {Koch Nolte}, Friedrich",
year = "2008",
language = "Deutsch",
volume = "64",
pages = "156--162",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - Structure of mouse ADP-ribosylhydrolase 3 (mARH3).

AU - Mueller-Dieckmann, Christoph

AU - Kernstock, Stefan

AU - Mueller-Dieckmann, Jochen

AU - Weiss, Manfred S

AU - Koch Nolte, Friedrich

PY - 2008

Y1 - 2008

N2 - ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.

AB - ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.

M3 - SCORING: Zeitschriftenaufsatz

VL - 64

SP - 156

EP - 162

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - 3

M1 - 3

ER -