Medical research

Novel therapeutic target for acute myeloid leukemia

Northwestern Medicine investigators have discovered the mechanisms by which a particular protein promotes cancer cell proliferation and survival in acute myeloid leukemia (AML), according to a Northwestern Medicine study ...

Oncology & Cancer

Radiation segmentectomy efficacious for unresectable liver cancer

For patients with unresectable very early to early-stage hepatocellular carcinoma with suboptimal location for ablation, radiation segmentectomy is efficacious with few high-grade adverse events, according to a study published ...

Medical research

Optimized vitamin K2 helps to treat osteoporosis

Osteoporosis is a common debilitating bone disease, which is characterized by bone loss and degeneration of bone structure, primarily caused by an imbalance between bone formation by osteoblasts and bone resorption by osteoclasts. ...

Biomedical technology

A 'sugar' coating for bone implants

Osteoporosis is a leading global health challenge. Besides its own adverse effects, it also impairs the function of bone implants—normally made of a metal called titanium (Ti). Because there is less bone than normal at ...

Oncology & Cancer

Scientists identify new target for wide array of cancers

Many types of human cancers exhibit changes in kinase and phosphatase balances. Drugs that inhibit kinase activity have shown success in the clinic as cancer therapeutics, but the phosphatases still remain a largely underexploited ...

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Phosphatase

A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase.

Protein phosphorylation is the most common and important form of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 86, 12 and 2% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg2+- or Mn2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third.

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