Comparative structural analysis of the putative mono-ADP-ribosyltransferases of the ARTD/PARP family
Pinto, Ana Filipa and Schüler, Herwig LU
(2015)
In Current Topics in Microbiology and Immunology
384.
p.66-153
- Abstract
The existence and significance of endogenous cytosolic and nuclear mono-ADP-ribosylation has been a matter of debate. Today, evidence suggests that the human enzymes that catalyze the reaction have been rounded up. Moreover, substrate proteins and specific functions for mono-ADP-ribosyltransferases are beginning to be defined. Reader domains that specifically recognize mono-ADP-ribosylated target proteins and erasers that remove the mono-ADP-ribosyl mark have been identified. Here, we review the contribution of crystal structures to our understanding of the putative mono-ADP-ribosyltransferases with Diphtheria toxin and ARTD1/PARP1 homology.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/fb5ec2ca-1e27-4860-bb77-795e39cab54d
- author
- Pinto, Ana Filipa
and Schüler, Herwig
LU
- publishing date
- 2015
- type
- Chapter in Book/Report/Conference proceeding
- publication status
- published
- keywords
- ADP Ribose Transferases/chemistry, Amino Acid Sequence, Animals, Humans, Models, Molecular, Molecular Sequence Data, Multigene Family, Sequence Alignment, Structural Homology, Protein
- host publication
- Endogenous ADP-Ribosylation
- series title
- Current Topics in Microbiology and Immunology
- editor
- Koch-Nolte, Friedrich
- volume
- 384
- edition
- 1
- pages
- 14 pages
- publisher
- Springer
- external identifiers
-
- scopus:84921887114
- pmid:25015788
- ISSN
- 0070-217X
- ISBN
- 978-3-319-10771-4
- 978-3-319-10770-7
- 978-3-319-34597-0
- DOI
- 10.1007/82_2014_417
- language
- English
- LU publication?
- no
- id
- fb5ec2ca-1e27-4860-bb77-795e39cab54d
- date added to LUP
- 2024-11-21 17:55:14
- date last changed
- 2025-01-09 14:37:02
@inbook{fb5ec2ca-1e27-4860-bb77-795e39cab54d,
abstract = {{<p>The existence and significance of endogenous cytosolic and nuclear mono-ADP-ribosylation has been a matter of debate. Today, evidence suggests that the human enzymes that catalyze the reaction have been rounded up. Moreover, substrate proteins and specific functions for mono-ADP-ribosyltransferases are beginning to be defined. Reader domains that specifically recognize mono-ADP-ribosylated target proteins and erasers that remove the mono-ADP-ribosyl mark have been identified. Here, we review the contribution of crystal structures to our understanding of the putative mono-ADP-ribosyltransferases with Diphtheria toxin and ARTD1/PARP1 homology.</p>}},
author = {{Pinto, Ana Filipa and Schüler, Herwig}},
booktitle = {{Endogenous ADP-Ribosylation}},
editor = {{Koch-Nolte, Friedrich}},
isbn = {{978-3-319-10771-4}},
issn = {{0070-217X}},
keywords = {{ADP Ribose Transferases/chemistry; Amino Acid Sequence; Animals; Humans; Models, Molecular; Molecular Sequence Data; Multigene Family; Sequence Alignment; Structural Homology, Protein}},
language = {{eng}},
pages = {{66--153}},
publisher = {{Springer}},
series = {{Current Topics in Microbiology and Immunology}},
title = {{Comparative structural analysis of the putative mono-ADP-ribosyltransferases of the ARTD/PARP family}},
url = {{http://dx.doi.org/10.1007/82_2014_417}},
doi = {{10.1007/82_2014_417}},
volume = {{384}},
year = {{2015}},
}