SMYD3 Modulates AMPK-mTOR Signaling Balance in Cancer Cell Response to DNA Damage
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
Unraveling the epigenetic code in cancer cell–tumor microenvironment crosstalk
Epigenetic regulation is a key driver of cancer development and progression. Diverse epigenetic alterations in cancer cells and components of the tumor microenvironment (TME) orchestrate their communication through multiple mechanisms. We discuss how the epigenetic code coordinates bidirectional cancer cell–TME crosstalk to promote cancer progression ...
Ji Hoon Park, Mi‐Young Kim
wiley +1 more source
Protein Posttranslational Modifications in Immunity: Molecular Mechanisms and Therapeutic Targets
Protein posttranslational modifications, including phosphorylation, ubiquitination, SUMOylation, acetylation, methylation, glycosylation, and other new types, dynamically regulate antigen presentation and recognition, immune signal transduction, antibody production and class switching, immune contraction, immune memory establishment, as well as immune ...
Yuxing Yao +10 more
wiley +1 more source
Overexpression of SMYD3 Is Predictive of Unfavorable Prognosis in Hepatocellular Carcinoma
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
SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer [PDF]
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
SMYD3 Modulates the HGF/MET Signaling Pathway in Gastric Cancer
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
Conservation Status of Two Italian Local Poultry Breeds: Faraona Camosciata and Oca Padovana
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
Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3
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
A SMYD3 Small‐Molecule Inhibitor Impairing Cancer Cell Growth [PDF]
SMYD3 is a histone lysine methyltransferase that plays an important role in transcriptional activation as a member of an RNA polymerase complex, and its oncogenic role has been described in different cancer types. We studied the expression and activity of SMYD3 in a preclinical model of colorectal cancer (CRC) and found that it is strongly upregulated ...
Peserico +25 more
openaire +6 more sources
SMYD3–PARP16 axis accelerates unfolded protein response and mediates neointima formation
Neointimal hyperplasia after vascular injury is a representative complication of restenosis. Endoplasmic reticulum (ER) stress-induced unfolded protein response (UPR) is involved in the pathogenesis of vascular intimal hyperplasia.
Fen Long +7 more
doaj +1 more source

