In recent years, much scientific effort and funding has focused on developing drugs that target an enzyme with the unwieldy name of Src homology 2-containing protein tyrosine phosphatase 2 or more briefly, Shp2.
Nov 9, 2021
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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 ...
Aug 12, 2020
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A team with members affiliated with several institutions in the U.S. has found that disabling the gene responsible for the production of the protein tyrosine phosphatase D (PTPRD) caused test mice to self-administer less ...
A new drug discovery system allows scientists to specifically target members of an important family of enzymes, called phosphatases, which were previously considered mostly "undruggable".
Jul 26, 2018
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Affecting as many as 650 million people worldwide, obesity has become one of the most serious global health issues. Among its detrimental effects, it increases the risk of developing metabolic conditions, and primarily type ...
Nov 28, 2017
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Investigators at Rush University Medical Center and the Brigham and Women's Hospital in Boston reported the discovery of a new gene that is associated with susceptibility to a common form of brain pathology called Tau that ...
Mar 24, 2017
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In 2011, Igor Stagljar, a professor in the University of Toronto's Donnelly Centre, came across a study that genetically linked two genes in the cell to a hard-to-treat (triple negative) breast cancer. It was not clear how ...
Jan 5, 2017
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A specific protein implicated in the cognitive decline of Alzheimer's disease also appears to play a role in genetic predisposition to schizophrenia, meaning that a drug that targets that protein could treat a variety of ...
Oct 19, 2016
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An enzyme therapy may prevent skeletal abnormalities associated with the genetic disorder neurofibromatosis type-1, Vanderbilt investigators have discovered.
Aug 14, 2014
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Triple-negative breast cancer (TNBC) is one of the most aggressive forms of the disease and affects almost one in seven of the 1.5 million women diagnosed with breast cancer worldwide each year. TNBC tumors are missing three ...
Feb 26, 2014
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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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