Results 201 to 210 of about 43,499 (244)

Poster Sessions

open access: yes
HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

Publication Only

open access: yes
HemaSphere, Volume 10, Issue S1, June 2026.
wiley   +1 more source

Novel alkoxybenzamide inhibitors of poly(ADP-ribose) polymerase

Bioorganic and Medicinal Chemistry Letters, 2008
We have previously described poly(ADP-ribose) polymerase-1 (PARP-1) inhibitors based on a substituted benzyl-phthalazinone scaffold. As an alternative chemical template, a novel series of alkoxybenzamides were developed with restricted conformation through intramolecular hydrogen bond formation; the compounds exhibit low nM enzyme and cellular activity
Niall M B Martin
exaly   +3 more sources

New inhibitors of poly(ADP-ribose) polymerase (PARP)

Expert Opinion on Therapeutic Patents, 2004
Poly(ADP-ribose) polymerase-1 (PARP-1), the most prominent member of the PARP family, is a DNA-binding protein that is activated by nicks in DNA occurring during inflammation, ischaemia, neurodegeneration or cancer therapy. Activated PARP-1 consumes NAD+ that is cleaved into nicotinamide and ADP-ribose and polymerises the latter onto nuclear acceptor ...
Stefan Peukert
exaly   +2 more sources

Comparative Analyses of Poly(ADP-Ribose) Polymerase Inhibitors

International Journal of Toxicology, 2022
Poly(ADP-ribose) polymerase inhibitors (PARPi) are approved as monotherapies in BRCA1/2-mutated (m BRCA1/2) metastatic breast and ovarian cancers, and in advanced pancreatic and metastatic castration-resistant prostate cancers. Differential safety profiles across PARPi necessitate improved mechanistic understanding of inhibitor ...
Mausumee Guha   +9 more
openaire   +2 more sources

Poly(ADP-Ribose) Polymerase Inhibitors

Current Medicinal Chemistry, 2003
Poly(ADP-ribose) polymerase-1 (PARP-1) is the principal member of the PARP enzyme family consisting of PARP-1 and several recently identified novel poly(ADP-ribosyl)ating enzymes. PARP-1 functions as a DNA damage sensor and signalling molecule. Upon binding to DNA breaks, activated PARP cleaves NAD(+) into nicotinamide and ADP-ribose and polymerizes ...
Garry J, Southan, Csaba, Szabó
openaire   +2 more sources

Current role of poly(ADP-ribose) polymerase inhibitors: which poly(ADP-ribose) polymerase inhibitor and when?

Current Opinion in Oncology, 2019
Purpose of review In the past few years, the advent of PARP inhibitors has been a revolution in the management of ovarian cancer. Patients harboring somatic or germ line BRCA1/2 mutations exhibit different clinical and treatment response behavior.
Hélène, Vanacker   +2 more
openaire   +2 more sources

Natural Inhibitors of Poly(ADP-ribose) Polymerase-1

Molecular Neurobiology, 2012
Poly(ADP-ribose) polymerases (PARPs) are enzymes that catalyze the transfer of ADP-ribose units from β-nicotinamide adenine dinucleotide (NAD(+)) to acceptor proteins. PARP-1 is responsible for more than 90 % of protein poly-ADP-ribosylation in the brain and may play a role as a molecular switch for cell survival and death. The functional roles of PARP-
Marek, Banasik   +2 more
openaire   +2 more sources

Poly (ADP-ribose) Polymerase Inhibitors in Cancer Treatment

American Journal of Clinical Oncology, 2014
Recent research on inhibitors of poly (ADP-ribose) polymerase (PARP) has demonstrated their potential for improving cancer therapy. They inhibit protein poly (ADP-ribosyl)ation and thus affect numerous molecular and cellular functions, including DNA repair and cell survival, that are critical for such physiological and patho-physiological states as ...
Kathryn A, Mason   +5 more
openaire   +2 more sources

The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors

Pharmacological Reviews, 2002
Poly(ADP-ribose) polymerase-1 (PARP-1) is a member of the PARP enzyme family consisting of PARP-1 and several recently identified novel poly(ADP-ribosylating) enzymes. PARP-1 is an abundant nuclear protein functioning as a DNA nick-sensor enzyme. Upon binding to DNA breaks, activated PARP cleaves NAD(+) into nicotinamide and ADP-ribose and polymerizes ...
László, Virág, Csaba, Szabó
openaire   +2 more sources

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