Results 21 to 30 of about 7,446,455 (132)

Mechanistic insights into the HPF1/PARP1 complex [PDF]

, 2022
ADP-ribosylation is a vital post-translational modification associated with a large range of processes including DNA damage repair, transcription, replication, mitosis, inflammation and cell death.
Zobel, Florian Franz Henning
core   +1 more source

Recruitment of AP-1 clathrin adaptors to liposomal membranes [PDF]

, 2004
Protein and membrane traffic between organelles within the endocytic and exocytic pathway is mediated most prominently by coated vesicles. These vesicles are formed by the assembly of cytosolic coat proteins onto the donor membrane, which deform it into ...
Meyer, Daniel Markus
core   +1 more source

TARG1 protects against DNA ADP-ribosylation stress [PDF]

, 2021
ADP-ribosylation is a modification that can target a variety of macromolecules and can regulate an array of important cellular processes. ADP-ribosylation is catalysed by ADP-ribosyltransferases that use NAD+ as a cosubstrate to transfer ADP-ribose onto ...
Tromans-Coia, Callum
core   +1 more source

Functions of PARylation in DNA Damage Repair Pathways

Genomics, Proteomics & Bioinformatics, 2016
Protein poly ADP-ribosylation (PARylation) is a widespread post-translational modification at DNA lesions, which is catalyzed by poly(ADP-ribose) polymerases (PARPs).
Huiting Wei, Xiaochun Yu
doaj   +1 more source

Poly(ADP)ribosylation of nuclear proteins in the mouse testis

, 1984
In "Proceedings of the 7th Intern. Symp.
R.,. JONES, QUESADA, PIERINA MARIA, M. MALANGA R. JONES, Enzo Leone, M. MALANGA AND R. JONES, LEONE E, JONES R., E. LEONE, Piera Quesada, Roy Jones, FARINA, BENEDETTA, B. , FARINA, Benedetta Farina, P. QUESADA, B. FARINA, FARINA B, M. , MALANGA, Maria R. Faraone Mennella, E. , LEONE, P. , QUESADA, Maria Malanga, FARAONE MENNELLA, MARIA ROSARIA, MALANGA M   +22 more
core   +1 more source

ADP-Ribosylation of NLRP3 by Mycoplasma pneumoniae CARDS Toxin Regulates Inflammasome Activity

mBio, 2014
The inflammasome is a major regulator of inflammation through its activation of procaspase-1, which cleaves prointerleukin-1β (pro-IL-1β) into its mature form.
Santanu Bose, Jesus A. Segovia, Sudha R. Somarajan, Te-Hung Chang, T. R. Kannan, Joel B. Baseman   +5 more
doaj   +1 more source

ADP-Ribosylation in Antiviral Innate Immune Response

, 2023
Adenosine diphosphate (ADP)-ribosylation is a reversible post-translational modification catalyzed by ADP-ribosyltransferases (ARTs). ARTs transfer one or more ADP-ribose from nicotinamide adenine dinucleotide (NAD+) to the target substrate and release ...
Qian Du, Wei He, Hui Zheng, Ying Miao
core   +1 more source

PARP10 is critical for stress granule initiation

Life Science Alliance
This study identifies PARP10 as a key regulator of stress granule assembly by ADP-ribosylating G3BP1 and modulating eIF2α phosphorylation and translation factor recruitment. Stress granules (SGs) are cytoplasmic biomolecular condensates enriched with RNA
Aravinth Kumar Jayabalan, Krishna Bhambhani, Anthony KL Leung   +2 more
doaj   +1 more source

Cytohesin-2 mediates group I metabotropic glutamate receptor-dependent mechanical allodynia through the activation of ADP ribosylation factor 6 in the spinal cord

Neurobiology of Disease, 2021
Group I metabotropic glutamate receptors (mGluRs), mGluR1 and mGluR5, in the spinal cord are implicated in nociceptive transmission and plasticity through G protein-mediated second messenger cascades leading to the activation of various protein kinases ...
Akiko Ito, Masahiro Fukaya, Takeyuki Sugawara, Yoshinobu Hara, Hirotsugu Okamoto, Junji Yamauchi, Hiroyuki Sakagami   +6 more
doaj   +1 more source

Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP‐ribosylating toxin AB to establish a persistent infection

FEBS Open Bio, EarlyView.
The two catalytic subunits of typhoid toxin dissociate from the holotoxin in the ER of an intoxicated cell, but only CdtB exits the ER to generate immunosuppressive effects. PltA is retained in the ER and sequestered from its cytosolic target, thus allowing the anti‐inflammatory effects of CdtB to promote intestinal colonization.
Maria C. Zabala‐Rodriguez, Juliette K. Tinker, Teresa Frisan, Taj Azarian, Ken Teter   +4 more
wiley   +1 more source