Results 51 to 60 of about 1,974 (156)

SMYD3 Modulates AMPK-mTOR Signaling Balance in Cancer Cell Response to DNA Damage

open access: yesCells, 2023
Cells respond to DNA damage by activating a complex array of signaling networks, which include the AMPK and mTOR pathways. After DNA double-strand breakage, ATM, a core component of the DNA repair system, activates the AMPK-TSC2 pathway, leading to the ...
Martina Lepore Signorile   +12 more
doaj   +1 more source

SMYD3 (SET and MYND domain containing 3) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on SMYD3 (SET and MYND domain containing 3), with data on DNA, on the protein encoded, and where the gene is implicated.
Luo, XG, Guo, S, Zhang, TC
openaire   +2 more sources

Discovery of Isoxazole Amides as Potent and Selective SMYD3 Inhibitors

open access: yesACS Medicinal Chemistry Letters, 2019
We report herein the discovery of isoxazole amides as potent and selective SET and MYND Domain-Containing Protein 3 (SMYD3) inhibitors. Elucidation of the structure-activity relationship of the high-throughput screening (HTS) lead compound 1 provided potent and selective SMYD3 inhibitors.
Dai-Shi Su   +23 more
openaire   +3 more sources

SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer [PDF]

open access: yesNature, 2014
Deregulation of lysine methylation signalling has emerged as a common aetiological factor in cancer pathogenesis, with inhibitors of several histone lysine methyltransferases (KMTs) being developed as chemotherapeutics. The largely cytoplasmic KMT SMYD3 (SET and MYND domain containing protein 3) is overexpressed in numerous human tumours.
Mazur, Pawel   +16 more
openaire   +5 more sources

Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3

open access: yesPLoS ONE, 2011
The SET and MYND Domain (SMYD) proteins comprise a unique family of multi-domain SET histone methyltransferases that are implicated in human cancer progression. Here we report an analysis of the crystal structure of the full length human SMYD3 in a complex with an analog of the S-adenosyl methionine (SAM) methyl donor cofactor.
Kenneth W Foreman   +10 more
openaire   +4 more sources

Conservation Status of Two Italian Local Poultry Breeds: Faraona Camosciata and Oca Padovana

open access: yesAnimal Genetics, Volume 57, Issue 3, June 2026.
ABSTRACT The present study aimed to assess the conservation status and characterize the phenotypic and genomic diversity of two endangered Italian poultry genetic resources to guide their conservation plans. Blood samples and morphometric data were collected on 50 Faraona Camosciata (FAC, Numida meleagris) and 50 Oca Padovana (OPD, Anser anser) adult ...
Filippo Cendron   +7 more
wiley   +1 more source

SMYD3 Modulates the HGF/MET Signaling Pathway in Gastric Cancer

open access: yesCells, 2023
Gastric cancer (GC) is the third most deadly cancer worldwide. Considerable efforts have been made to find targetable drivers in order to improve patient outcomes.
Katia De Marco   +11 more
doaj   +1 more source

Chitooligosaccharides Modulate Glucose-Lipid Metabolism by Suppressing SMYD3 Pathways and Regulating Gut Microflora

open access: yesMarine Drugs, 2020
Chitooligosaccharides (COS) have a variety of biological activities due to their positively charged amino groups. Studies have shown that COS have antidiabetic effects, but their molecular mechanism has not been fully elucidated.
Qiutong Wang   +7 more
doaj   +1 more source

Overexpression of SMYD3 Is Predictive of Unfavorable Prognosis in Hepatocellular Carcinoma

open access: yesThe Tohoku Journal of Experimental Medicine, 2017
SET and MYND domain-containing protein 3 (SMYD3) is a kind of histone lysine methyltransferase, responsible for transcriptional activation as a member of an RNA polymerase complex. The ectopic expression of SMYD3 is proved to promote the progress of many kinds of cancers.
Fei, Xiao   +3 more
openaire   +3 more sources

RNA‐Binding Proteins and Ferroptosis in Cancer: Mechanism and Therapeutic Implications

open access: yesMedComm – Oncology, Volume 5, Issue 1, March 2026.
Ferroptosis critically influences cancer cell fate and represents a promising therapeutic strategy. Emerging evidence identifies RNA‐binding proteins (RBPs) as key post‐transcriptional regulators of ferroptosis. The figure summarizes ferroptosis‐related RBPs across cancers: blue RBPs act as tumor suppressors by promoting ferroptosis, whereas red RBPs ...
Linlin Chang   +6 more
wiley   +1 more source

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