Results 101 to 110 of about 667,209 (277)

Targeting Renal IGFBP7 With Tetrahedral Framework Nucleic Acid‐Delivered siRNA Alleviates Acute Kidney Injury

open access: yesiNew Medicine, EarlyView.
A tFNA‐based siRNA delivery system targeting IGFBP7 effectively silences IGFBP7 expression and attenuates renal dysfunction, tubular injury, and cell death in both septic (CLP) and ischemic (I/R) murine models of acute kidney injury. ABSTRACT Objective Acute kidney injury (AKI) is a common and serious clinical condition, yet effective targeted ...
Shao‐qi Wu   +11 more
wiley   +1 more source

ATP Citrate Lyase in Metabolic Disease: Mechanistic Insights and Clinical Potential

open access: yesiNew Medicine, EarlyView.
ATP citrate lyase (ACLY) is a central metabolic hub that diverts mitochondrial citrate to fuel de novo lipogenesis, cholesterol biosynthesis, and protein acetylation. Given its robust correlation with pathological changes in multiple human diseases, ACLY inhibitors featuring distinct pharmacological strengths have been developed for therapeutic ...
Wenbiao Wang   +5 more
wiley   +1 more source

A Review on DNA Repair Inhibition by PARP Inhibitors in Cancer Therapy

open access: yesFolia Medica, 2018
The DNA repair process protects the cells from DNA damaging agent by multiple pathways. Majority of the cancer therapy cause DNA damage which leads to apoptosis.
Shah Ashish P.   +3 more
doaj   +1 more source

Bisphenol A and Its Analogs: Toxicity Analysis in Mouse and Rat Liver—A Review

open access: yesJournal of Applied Toxicology, EarlyView.
ABSTRACT Bisphenol A (BPA) and its analogs are widely recognized for their use in industry and plastic manufacturing. Consequently, humans and animals are continually exposed to various substances in their daily lives. This review evaluates the hepatic toxicity of BPA and its analogs in mice and rats, with particular emphasis on molecular mechanisms ...
Sevda Bagdatli   +5 more
wiley   +1 more source

NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains

open access: yesNature Communications, 2018
Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the ...
Marie-France Langelier   +4 more
doaj   +1 more source

Inhibition of poly(ADP-ribose) polymerase interferes with Trypanosoma cruzi infection and proliferation of the parasite.

open access: yesPLoS ONE, 2012
Poly(ADP-ribosylation) is a post-translational covalent modification of proteins catalyzed by a family of enzymes termed poly(ADP-ribose) polymerases (PARPs).
Salomé C Vilchez Larrea   +7 more
doaj   +1 more source

Poly(ADP-ribose) [PDF]

open access: yesNature, 1976
Mark Smulson, Sydney Shall
openaire   +1 more source

Poly(ADP-ribose) modulates the properties of MARCKS proteins.

open access: yes, 1998
In mammalian cells, the formation of DNA strand breaks is accompanied by synthesis of poly(ADP-ribose). This nucleic acid-like homopolymer may modulate protein functions by covalent and/or noncovalent interactions.
Kleczkowska HE   +4 more
core   +1 more source

Anticancer potential of berberine: Molecular pathways and current clinical trial perspectives

open access: yesJSFA reports, EarlyView.
Abstract Cancer is constantly rising mortality rates due to its late prognosis, poor management, and expensive treatment. Multi‐sectoral approaches for cancer management include hygienic practices, synthetic drug exploitation, radiation therapy, and diet modifications.
Muhammad Maaz   +10 more
wiley   +1 more source

Mutations of human DNA topoisomerase I at poly(ADP-ribose) binding sites: modulation of camptothecin activity by ADP-ribose polymers. [PDF]

open access: yes, 2014
Background DNA topoisomerases are key enzymes that modulate the topological state of DNA through the breaking and rejoining of DNA strands. Human topoisomerase I belongs to the family of poly(ADP-ribose)-binding proteins and is the target of camptothecin
Zuccaro, L   +25 more
core   +1 more source

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