Results 41 to 50 of about 160,489 (252)

Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase. [PDF]

open access: yesPLoS ONE, 2014
Protein poly(ADP-ribosyl)ation (PARylation) regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase (PARG) is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) (PAR) polymer in vivo.
Zhizhi Wang   +3 more
doaj   +1 more source

Molecular characterization of novel ADP-ribosyl cyclases from the sea urchin [PDF]

open access: yes, 2010
Calcium signalling is ubiquitous and regulates diverse cellular processes. Cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) are second messengers that are involved in calcium release from the intracellular organelles ...
Ramakrishnan, L.
core  

Membrane composition and thermodynamic identity as boundaries of life for synthetic cell research

open access: yesFEBS Letters, EarlyView.
What makes a cell a cell? The boundary of a living cell is not just a wall. Read as a Markov blanket, the membrane separates internal from external states, generating identity and non‐equilibrium order. Can this identity be rebuilt from scratch in a synthetic cell?
Caterina Presutti, Bert Poolman
wiley   +1 more source

ADP-ribose polymer - a novel and general biomarker of human cancers of head & neck, breast, and cervix

open access: yesMolecular Cancer, 2010
Background Poly-ADP-ribosylation, a reversible post-translational modification of primarily chromosomal proteins, is involved in various cellular and molecular processes including carcinogenesis.
Sharan Rajeshwar N   +2 more
doaj   +1 more source

Mechanisms of poly(ADP-ribose) polymerase catalysis; mono-ADP-ribosylation of poly(ADP-ribose) polymerase at nanomolar concentrations of NAD [PDF]

open access: yes, 1986
Calf thymus and rat liver poly(ADP-ribose) polymerase enzymes, and the polymerase present in extracts of rat liver nuclei synthesize unstable mono-ADP-ribose protein adducts at 100 nM or lower NAD concentrations.
Kun, Ernest   +5 more
core   +1 more source

Loss of IGF‐1R impairs DNA‐PKcs recruitment to chromatin leading to defective end‐joining

open access: yesMolecular Oncology, EarlyView.
IGF‐1R promotes radioresistance by facilitating DNA‐PKcs recruitment to chromatin, enabling non‐homologous end‐joining (NHEJ) repair of double‐strand breaks. Inhibition or loss of IGF‐1R disrupts this recruitment to damage sites, driving compensatory reliance on microhomology‐mediated end‐joining (MMEJ) repair.
Matthew O. Ellis   +3 more
wiley   +1 more source

Recruitment of ubiquitin-activating enzyme UBA1 to DNA by poly(ADP-ribose) promotes ATR signalling

open access: yesLife Science Alliance, 2018
Human but not yeast UBA1 binds poly(ADP-ribose) polymers via a solvent-exposed and positively charged patch. Poly(ADP-ribose) polymerase 1–dependent recruitment of UBA1 to DNA ensures ataxia-telangiectasia and RAD3-related activation.
Ramhari Kumbhar   +8 more
doaj   +1 more source

Inhibition of Poly(ADP-ribose)polymerase impairs Epstein Barr Virus lytic cycle progression-8

open access: yes, 2011
Copyright information:Taken from "Inhibition of Poly(ADP-ribose)polymerase impairs Epstein Barr Virus lytic cycle progression"http://www.infectagentscancer.com/content/2/1/18Infectious Agents and Cancer 2007;2():18-18.Published online 11 Oct 2007PMCID ...
Giulia Matusali (83277)   +8 more
core   +1 more source

Inhibition of cyclin‐dependent kinases 12/13 using CT7439 as a treatment for colorectal cancer with CDK12 upregulation

open access: yesMolecular Oncology, EarlyView.
The proposed mechanism of action for the CDK12/13 inhibitor and cyclin K degrader, CT7439. CDK12/13 inhibition interrupts transcription elongation, leading to increased DNA damage that results in cell death. This agent is a potentially novel treatment option for patients with colorectal cancer. Created in BioRender. Cyclin‐dependent kinase (CDK) 12 and
Wylie K. Watlington   +10 more
wiley   +1 more source

Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives. [PDF]

open access: yesPLoS ONE, 2012
Poly(ADP-ribose) glycohydrolase (PARG) is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, thereby reversing the effects of poly(ADP-ribose) polymerases.
Julie A Tucker   +9 more
doaj   +1 more source

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