Results 41 to 50 of about 40,918 (202)

The Critical Role of PARPs in Regulating Innate Immune Responses

Frontiers in Immunology, 2021
Poly (adenosine diphosphate-ribose) polymerases (PARPs) are a family of proteins responsible for transferring ADP-ribose groups to target proteins to initiate the ADP-ribosylation, a highly conserved and fundamental post-translational modification in all
Huifang Zhu, Yan-Dong Tang, Guoqing Zhan, Chenhe Su, Chunfu Zheng   +4 more
doaj   +1 more source

Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG

Nature Communications
Ester-linked post-translational modifications, including serine and threonine ubiquitination, have gained recognition as important cellular signals. However, their detection remains a significant challenge due to the chemical lability of the ester bond ...
Edoardo José Longarini, Ivan Matić
doaj   +1 more source

In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation

eLife, 2016
PARP catalysed ADP-ribosylation is a post-translational modification involved in several physiological and pathological processes, including cellular stress.
Angelica Aguilera-Gomez, Marinke M van Oorschot, Tineke Veenendaal, Catherine Rabouille   +3 more
doaj   +1 more source

Reversible ADP-ribosylation of RNA [PDF]

Nucleic Acids Research, 2019
AbstractADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA.
Munnur, D, Bartlett, E, Mikolcevic, P, Kirby, I, Rack, J, Mikoc, A, Cohen, M, Ahel, I   +7 more
openaire   +3 more sources

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

FEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho, Shin Morioka, Junko Sasaki, Takehiko Sasaki   +3 more
wiley   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source

Plecstatin inhibits hepatocellular carcinoma tumorigenesis and invasion through cytolinker plectin

Molecular Oncology, EarlyView.
The ruthenium‐based metallodrug plecstatin exerts its anticancer effect in hepatocellular carcinoma (HCC) primarily through selective targeting of plectin. By disrupting plectin‐mediated cytoskeletal organization, plecstatin inhibits anchorage‐dependent growth, cell polarization, and tumor cell dissemination.
Zuzana Outla, Jan Kosla, Magdalena Prechova, Lukas Frick, Patricia Bortel, Yasmin Borutzki, Andrea Bileck, Christopher Gerner, Samuel M. Meier‐Menches, Selma Osmanagic‐Myers, Martin Gregor   +10 more
wiley   +1 more source

Proteasome Regulation by ADP-Ribosylation [PDF]

Cell, 2013
Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome is a large protease complex that degrades ubiquitinated proteins. Here, we show that ADP-ribosylation promotes 26S proteasome activity
Cho-Park, Park F., Steller, Hermann
openaire   +2 more sources

SIRT4 positively regulates autophagy via ULK1, but independently of HDAC6 and OPA1

FEBS Open Bio, EarlyView.
Cells expressing SIRT4 (H161Y), a catalytically inactive mutant of the sirtuin SIRT4, fail to upregulate LC3B‐II and exhibit a reduced autophagic flux under stress conditions. Interestingly, SIRT4(H161Y) promotes phosphorylation of ULK1 at S638 and S758 that are associated with inhibition of autophagy initiation.
Isabell Lehmkuhl, Khawar Amin, Lydia Gabriel, Nils Hampel, Afshin Iram, Julia Hesse, Constanze Wiek, Jasmin Thuy Vy Nguyen, Helmut Hanenberg, Jürgen Scheller, M. Reza Ahmadian, Björn Stork, Doreen M. Floss, Roland P. Piekorz   +13 more
wiley   +1 more source

Interplay of Histone Marks with Serine ADP-Ribosylation

Cell Reports, 2018
Summary: Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1).
Edward Bartlett, Juan José Bonfiglio, Evgeniia Prokhorova, Thomas Colby, Florian Zobel, Ivan Ahel, Ivan Matic   +6 more
doaj   +1 more source