Noncovalent PAR Binding Guides Proteins to PARP1-Mediated PARylation. [PDF]
Fischbach A +3 more
europepmc +1 more source
Investigating strategies to modify PARP14 function through macrodomain inhibition
Macrodomains are conserved protein interaction modules that are present in all domains of life and mediate recognition of sequence motifs harbouring adenosine diphosphate ribose (ADPR) modifications. In addition, some of them are able to control the turnover of ADPR signalling through their catalytic activity removing these modifications.
openaire +1 more source
Primary electron transfer kinetics in bacterial reaction centers with modified bacteriochlorophylls at tghe monomeric sites Ba, B [PDF]
Finkele, Ulrich +5 more
core +1 more source
Family-wide analysis of human macrodomains reveals novel activities
Abstract ADP-ribosylation is well-known as protein posttranslational modification and was recently also identified as RNA posttranscriptional modification. ADP-ribose is added onto substrates by PARP enzymes and removed by the structurally distinct ADP-ribosylhydrolases (ARH) or macrodomain-containing proteins.
Lisa Weixler* +8 more
openaire +1 more source
Efficient Binding Affinity Estimation for Fragment-Based Compounds Using a Separated Topologies Approach. [PDF]
Caldaruse AM, Baumann HM, Mobley DL.
europepmc +1 more source
Excited state properties of modified pigment of bacterial photosynthesis [PDF]
Leupold, D. +4 more
core +1 more source
Poly(ADP-ribose) polymerases as modulators of mitochondrial activity [PDF]
Bai, Péter +4 more
core +1 more source
Rv1899c, an HDAC1-ZBTB25-Interacting Protein of <i>Mycobacterium tuberculosis</i>, Promotes Stress Resistance and Immune Evasion in Infected Macrophages. [PDF]
Menon AM +9 more
europepmc +1 more source
Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15. [PDF]
Ebenwaldner C +7 more
europepmc +1 more source
AcrIF11 is a potent CRISPR-specific ADP-ribosyltransferase encoded by phage and plasmid. [PDF]
Chen DF +15 more
europepmc +1 more source

