Results 81 to 90 of about 6,651 (207)

Involvement of PARP1 in the regulation of alternative splicing [PDF]

Cell Discovery, 2016
AbstractSpecialized chromatin structures such as nucleosomes with specific histone modifications decorate exons in eukaryotic genomes, suggesting a functional connection between chromatin organization and the regulation of pre-mRNA splicing. Through profiling the functional location of Poly (ADP) ribose polymerase, we observed that it is associated ...
Elena Matveeva, John Maiorano, Qingyang Zhang, Abdallah M Eteleeb, Paolo Convertini, Jing Chen, Vittoria Infantino, Stefan Stamm, Jiping Wang, Eric C Rouchka, Yvonne N Fondufe-Mittendorf   +10 more
openaire   +3 more sources

Nuclear IDH3A Drives Transcriptional Programs in Melanoma via the YBX1–JUN/FOS Axis

Advanced Science, EarlyView.
Genomic amplification drives aberrant nuclear localization of IDH3A in melanoma. Independent of its canonical metabolic activity, nuclear IDH3A cooperates with YBX1 to activate the c‐JUN/c‐FOS transcriptional program, while NONO facilitates its nuclear localization.
Juan Ran, Yanchun Fang, Shengming Ruan, Juling Wang, Songbai Liu, Yuan Mao, Dongsheng Hou, Yanping Wang, Zi Ye, Qiong Li, Daoxiang Zhang   +10 more
wiley   +1 more source

MDL‐800‐induced SIRT6 activation decreases age‐associated osteoarthritis in mice

Arthritis &Rheumatology, Accepted Article.
Objective SIRT6 is a nuclear‐localized histone deacetylase that regulates multiple pathways associated with aging. This study aimed to determine whether systemic administration of a small molecule activator of SIRT6, MDL‐800, decreases the severity of age‐associated osteoarthritis (OA) in mice.
Matheus Moreira Perez, Pranay Ramteke, Bahiyah Watson, Owen Haslam, Eirene Choi, Susan Chubinskaya, Mandy J. Peffers, William R. Davis, Jacqueline Shine, Brian O. Diekman, Richard F. Loeser, Theresa A. Freeman, Makarand V. Risbud, John A. Collins   +13 more
wiley   +1 more source

The effect of dimeric bisbenzimidazoles on the activity of DNA repair enzymes TDP1, TDP2, PARP1 and PARP2

Вавиловский журнал генетики и селекции
Oncological diseases remain a leading cause of pathological mortality worldwide, making the development of anticancer drugs a critical focus in medicinal chemistry.
N. S. Dyrkheeva, I. A. Chernyshova, A. F. Arutyunyan, A. L. Zakharenko, M. M. Kutuzov, K. N. Naumenko, A. S. Venzel, V. A. Ivanisenko, S. M. Deyev, A. L. Zhuze, O. I. Lavrik   +10 more
doaj   +1 more source

Monitoring pharmacodynamic and molecular drug targets in liquid biopsy: Exploratory study in liver cancer with modelling of EGFR Receptor engagement

British Journal of Clinical Pharmacology, EarlyView.
Abstract Aim Liquid biopsy is minimally invasive (compared with tissue biopsy) and has previously been used to generate systems data regarding drug elimination via hepatic enzymes and transporters. This study extends quantitative assessment of systems parameters in liquid biopsy to pharmacodynamic (PD) and disease markers relevant to cancer development
Zubida M. Al‐Majdoub, Armin Sepp, Amin Rostami‐Hodjegan, Brahim Achour   +3 more
wiley   +1 more source

Nucleosome unwrapping and PARP1 allostery drive affinities for chromatin and DNA breaks

Nature Communications
Poly(ADP-ribose) polymerase 1 (PARP1) detects DNA strand breaks that occur in duplex DNA and chromatin. Here, correlative optical tweezers and fluorescence microscopy reveal how single molecules of PARP1 identify single-strand breaks (i.e., nicks ...
Matthew A. Schaich, Tyler M. Weaver, Jennifer A. Rakowski, Vera Roginskaya, Liam P. Leary, Aafke A. Van den Berg, Janet H. Iwasa, Bret D. Freudenthal, Bennett Van Houten   +8 more
doaj   +1 more source

The Histone Methyltransferase SMYD2 Methylates PARP1 and Promotes Poly(ADP-ribosyl)ation Activity in Cancer Cells

Neoplasia: An International Journal for Oncology Research, 2014
Poly(ADP-ribose) polymerase-1 (PARP1) catalyzes the poly(ADP-ribosyl)ation of protein acceptors using NAD+ as the substrate is now considered as an important target for development of anticancer therapy. PARP1 is known to be post-translationally modified
Lianhua Piao, Daechun Kang, Takehiro Suzuki, Akiko Masuda, Naoshi Dohmae, Yusuke Nakamura, Ryuji Hamamoto   +6 more
doaj   +1 more source

Vacancy defect‐induced electron homing breaks phosphodiester bonds for RNA depletion‐driven cancer therapy

BMEMat, EarlyView.
Illustration of 5% S‐vacancy Bi2S3 mediated phosphodiester bonds cleavage in RNA of hepatocellular carcinoma cells, which suppressing ERI3 expression, inhibiting cell proliferation and promoting apoptosis. Abstract Genome‐wide hypertranscription is a hallmark of malignant progression.
Chuncheng Yang, Zehao Shen, Guangming Xiang, Zhe Liu, Huaxin Liu, Jiabei Li, Ao Wang, Yelin Wu, Peiran Zhao, Xingwu Jiang, Jinghan Wang, Xiaoqing Jiang, Wenbo Bu   +12 more
wiley   +1 more source

PAX3 Loads onto Pericentromeric Heterochromatin During S Phase Through PARP1

, 2014
[[abstract]]BACKGROUND: Proper re-establishment of heterochromatin after each round of DNA replication is critical to the preservation of cell identity. Paired box 3 (PAX3), a transcription factor important in embryonic development, was found to mediate ...
Wu TF; Yao YL ;Lai IL; Lee TH; Underhill DA; Yang WM.
core   +1 more source

Targeting the Shared PARP1-HPF1 Active Site [PDF]

, 2023
DNA holds all genetic material but is also under constant threat of damage. DNA damage can occur through external insults, for example UV radiation, and internal mishaps, including dNTP misincorporation during DNA replication.
Noor, Rida
core   +1 more source