Structural basis and prediction of substrate specificity in protein serine/threonine kinases
Ross I. Brinkworth+2 more
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C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1 [PDF]
Chou Hung Sim+6 more
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This review highlights the complex roles of cellular senescence in cancer progression and suppression, discusses the mechanisms and regulatory pathways involved, and evaluates the efficacy of the “One‐Two punch” sequential treatment approach while addressing emerging challenges in this novel therapeutic strategy.
Qiuming Pan+12 more
wiley +1 more source
Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution. [PDF]
Li H, Li R, Yu H, Zhang Y, Feng H.
europepmc +1 more source
EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis [PDF]
Kirti Sharma+4 more
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Abstract Background Intrahepatic cholangiocarcinoma (ICC) is a challenging cancer with an increasing incidence. The Phase III TOPAZ‐1/KEYNOTE‐966 study demonstrated chemo‐immunotherapy (CIT) as a significant advancement, potentially replacing traditional chemotherapy for advanced biliary tract cancer.
Jinghan Zhu+12 more
wiley +1 more source
The Role of Protein Kinases in the Suppressive Phenotype of Myeloid-Derived Suppressor Cells. [PDF]
Kali A+4 more
europepmc +1 more source
Ubiquitination in cancer: mechanisms and therapeutic opportunities
Abstract Ubiquitination, a key post‐translational modification, plays an essential role in tumor biology by regulating fundamental cellular processes, such as metabolism and cell death. Additionally, it interacts with other post‐translational modifications, which are closely linked to tumorigenesis, tumor progression, the tumor microenvironment, and ...
Susi Zhu+7 more
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The Membrane-Associated Protein-Serine/Threonine Kinase fromSulfolobus solfataricusIs a Glycoprotein
Brian H. Lower, Peter J. Kennelly
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Abstract Post‐translational modifications (PTMs) play a pivotal role in epigenetic regulation and are key pathways for modulating protein functionality. PTMs involve the covalent attachment of distinct chemical groups, such as succinyl, crotonyl, and lactyl, at specific protein sites, which alter protein structure, function, stability, and activity ...
Ting Wu+16 more
wiley +1 more source