Results 21 to 30 of about 20,190 (223)

The interplay of TARG1 and PARG protects against genomic instability

Cell Reports, 2023
Summary: The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspartate/
Joséphine Groslambert, Evgeniia Prokhorova, Anne R. Wondisford, Callum Tromans-Coia, Celeste Giansanti, Jennifer Jansen, Gyula Timinszky, Matthias Dobbelstein, Dragana Ahel, Roderick J. O’Sullivan, Ivan Ahel   +10 more
doaj  

Altered cytoplasmic and nuclear ADP‐ribosylation levels analyzed with an improved ADP‐ribose binder are a prognostic factor in renal cell carcinoma

The Journal of Pathology: Clinical Research, 2023
ADP‐ribosylation (ADPR) of proteins is catalyzed by ADP‐ribosyltransferases, which are targeted by inhibitors (i.e. poly(ADP‐ribose) polymerase inhibitors [PARPi]). Although renal cell carcinoma (RCC) cells are sensitive in vitro to PARPi, studies on the
Peter Schraml, Fabio Aimi, Martin Zoche, Domingo Aguilera‐Garcia, Fabian Arnold, Holger Moch, Michael O Hottiger   +6 more
doaj   +1 more source

Elongation factor 2-diphthamide is critical for translation of two IRES-dependent protein targets, XIAP and FGF2, under oxidative stress conditions [PDF]

, 2013
Elongation factor-2 (eEF2) catalyzes the movement of the ribosome along the mRNA. A single histidine residue in eEF2 (H715) is modified to form diphthamide. A role for eEF2 in cellular stress responses is highlighted by the fact that eEF2 is sensitive to
Argüelles Castilla, Sandro, Ayala Gómez, Antonio, Camandola, Simonetta, Cutler, Roy G.   +3 more
core   +1 more source

Characterization of ERp29 and ADP-Ribosylation Factor 5 Interaction [PDF]

Journal of Life Science, 2011
ERp29 is a endoplasmic reticulum (ER) lumenal resident protein that shows sequence similarity to the protein disulfide isomerase family. Its biological function is thought to play a role in the processing of secretory proteins within the ER, possibly by participating in the folding of proteins in the ER.
Kweon Yu, O-Yu Kwon, Seung Whan Kim, Kisang Kwon, Dae-Hyun Seog   +4 more
openaire   +2 more sources

PARP-3 and APLF function together to accelerate nonhomologous end joining [PDF]

, 2010
PARP-3 is a member of the ADP-ribosyl transferase superfamily of unknown function. We show that PARP-3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the poly (ADP-ribose)-binding protein APLF to accelerate
Ahel, Ame, Anna E.O. Fisher, Audebert, Bekker-Jensen, Benjamin, Bernardo Reina-San-Martin, Boulton, Brown, Bryant, Bryant, Caldecott, Caldecott, Critchlow, Ding, Drouet, El-Khamisy, Farmer, Fisher, Grawunder, Guy Poirier, Hochegger, Hottiger, Iles, Isabelle Robert, Kanno, Keith W. Caldecott, Kickhoefer, Kleine, Le Page, Lehtio, Limei Ju, Lobrich, Loseva, Macrae, Mahaney, Maria C. Zuma, Mehrotra, Michele Rouleau, Morrison, Okano, Otto, Poirier, Robert, Roberts, Rogakou, Rogakou, Rouleau, Rulten, Smith, Soulas-Sprauel, Stevnsner, Stuart L. Rulten, Sugimura, Trucco, Wang, Yan, Yang, Yano, Yano   +59 more
core   +1 more source

To translate, or not to translate: viral and host mRNA regulation by interferon-stimulated genes. [PDF]

, 2015
Type I interferon (IFN) is one of the first lines of cellular defense against viral pathogens. As a result of IFN signaling, a wide array of IFN-stimulated gene (ISG) products is upregulated to target different stages of the viral life cycle.
Li, Melody MH, MacDonald, Margaret R, Rice, Charles M   +2 more
core   +1 more source

ADP‐ribosylated elongation factor 2 (ADP‐ribosyl‐EF‐2) is unable to promote translocation within the ribosome [PDF]

FEBS Letters, 1990
Elongation factor 2 (EF‐2), ADP‐ribosylated in vitro by the A‐fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable corn plexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe‐tRNA in the A‐site.
E.K. Davydova, Lev P. Ovchinnikov
openaire   +3 more sources

ADP-Ribosylation Factor Family of Small GTP-Binding Proteins: Their Membrane Recruitment, Activation, Crosstalk and Functions

Frontiers in Cell and Developmental Biology, 2022
Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide binding proteins play critical roles in various cellular processes, especially in regulating the secretory, and endocytic pathways.
Tiantian Li, Yusong Guo, Yusong Guo, Yusong Guo   +3 more
doaj   +1 more source

Filling in the GAPs in the ADP-ribosylation factor story [PDF]

Proceedings of the National Academy of Sciences, 2000
The GTP-binding proteins known as ADP-ribosylation factors (ARFs) function in cells to regulate membrane traffic and structure. Like all GTPases, ARFs cycle between a GDP-bound, inactive and a GTP-bound, active form. When GTP-bound, ARFs alter membrane lipid composition, assemble cytosolic coat proteins, and remodel actin associated with various ...
openaire   +3 more sources

ADP ribosylation factor regulates spectrin binding to the Golgi complex [PDF]

Proceedings of the National Academy of Sciences, 1998
Homologues of two major components of the well-characterized erythrocyte plasma-membrane-skeleton, spectrin (a not-yet-cloned isoform, βIΣ* spectrin) and ankyrin (Ank G119 and an ≈195-kDa ankyrin), associate with the Golgi complex. ADP ribosylation factor (ARF) is a small G protein that controls the architecture and
Godi, A, Santone, I, Pertile, P, Devarajan, P, Stabach, P. R, Morrow, J. S, Di Tullio, G, Polishchuk, R, Petrucci, T. C, Luini, A, DE MATTEIS, Maria Antonietta   +10 more
openaire   +4 more sources