Skip to Content
MilliporeSigma
Search Within

43420

Applied Filters:
Keyword:'43420'
Showing 1-9 of 9 results for "43420" within Papers
Michael Maurer et al.
Cell chemical biology, 26(8), 1169-1179 (2019-06-18)
ATP-driven bacterial AAA+ proteases have been recognized as drug targets. They possess an AAA+ protein (e.g., ClpC), which threads substrate proteins into an associated peptidase (e.g., ClpP). ATPase activity and substrate selection of AAA+ proteins are regulated by adapter proteins
Mahmoud Hajj Chehade et al.
Cell chemical biology, 26(4), 482-492 (2019-01-29)
Ubiquinone (UQ) is a polyprenylated lipid that is conserved from bacteria to humans and is crucial to cellular respiration. How the cell orchestrates the efficient synthesis of UQ, which involves the modification of extremely hydrophobic substrates by multiple sequential enzymes
V A Soldatenkov et al.
Current drug targets, 5(4), 357-365 (2004-05-12)
Poly(ADP-ribose) polymerization is a unique post-translation protein modification that utilizes an ADP-ribose moiety from NAD+ to form long and branched polymers attached via glutamic acid residues to nuclear acceptor proteins. The corresponding enzyme, poly(ADP-ribose) polymerase (PARP-1), is a zinc finger-containing
Mi Young Kim et al.
Genes & development, 19(17), 1951-1967 (2005-09-06)
Poly(ADP-ribose) (PAR) and the PAR polymerases (PARPs) that catalyze its synthesis from donor nicotinamide adenine dinucleotide (NAD+) molecules have received considerable attention in the recent literature. Poly(ADP-ribosyl)ation (PARylation) plays diverse roles in many molecular and cellular processes, including DNA damage
Chemical, Biochemical and Medical Aspects, 776-776 null
Célia Deville et al.
Cell reports, 27(12), 3433-3446 (2019-06-20)
AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined is key to understanding the AAA+ protein mechanism.
D.Dolphin, R.Poulson, O.Avramovic, eds.
Chemical, Biochemical and Medical Aspects, 759-759 (1987)
Paul J Derry et al.
Nanoscale, 11(22), 10791-10807 (2019-05-28)
Previously, our group reported on the promising efficacy of poly(ethylene glycol)-hydrophilic carbon clusters (PEG-HCCs) to work as broadly active and high capacity antioxidants in brain ischemia and injury models including stroke and traumatic brain injury coupled with hemorrhagic shock. PEG-HCCs
D D'Amours et al.
The Biochemical journal, 342 ( Pt 2), 249-268 (1999-08-24)
Poly(ADP-ribosyl)ation is a post-translational modification of proteins. During this process, molecules of ADP-ribose are added successively on to acceptor proteins to form branched polymers. This modification is transient but very extensive in vivo, as polymer chains can reach more than
Page 1 of 1