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14 results about "Phosphoprotein phosphatase" patented technology

A protein phosphatase is a phosphatase enzyme that removes a phosphate group from the phosphorylated amino acid residue of its substrate protein. Protein phosphorylation is one of the most common forms 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 79.3, 16.9 and 3.8% 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. The protein pseudophosphatases form part of the larger phosphatase family, and in most cases are thought to be catalytically inert, instead functioning as phosphate-binding proteins, integrators of signalling or subcellular traps. Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. A complete comparative analysis of human phosphatases and pseudophosphatases has been completed by Manning and colleagues, forming a companion piece to the ground-breaking analysis of the human kinome, which encodes the complete set of ~536 human protein kinases.

Decreasing gene expression for increased protein content in plants

Provided herein are plants, plant parts, a population of plants or plant parts, and plant products (e.g., seed composition, protein composition) comprising reduced activity of a protein-related polypeptide [e.g., stomatal cytokinesis defective 2 (SCD2), SCD2A, SCD2B, response to dehydration 22 (RD22), glucuronidase 3 (GUS3), GUS3A, glycosyl hydrolase family 10 protein B (GH10B), protein phosphatase 2A beta subunit (PP2AB), PPA2BA, PP2ABAB, alpha / beta-hydrolases superfamily protein (ABH), ABHA, ABHB, calmodulin-binding transcription activator protein 2 (CAMTA2), CAMTA2A, CAMTA2B, cinnamyl-alcohol dehydrogenase (CAD1), beta-ketoacyl reductase 1 (KCR1), KCR1A, or KCR1B], and compositions and methods of producing such plants and plant parts. The plants, plant parts, population of plants or plant parts, or plant products can have a genetic mutation that reduces the protein-related polypeptide activity, which can be one located at least partially in a protein-related gene (e.g., CAD1) or its homolog or in its regulatory region, and can have increased protein content and / or white flake protein content.
Owner:CONFLUENCE GENETICS LLC

PP2A / ZnO-PDA / GCE electrochemical biosensor and preparation method and application thereof

The invention provides a PP2A / PDA-ZnO / GCE electrochemical biosensor as well as a preparation method and application of the PP2A / PDA-ZnO / GCE electrochemical biosensor. The sensor comprises a glassy carbon electrode, an immobilized enzyme layer is arranged on the surface of the glassy carbon electrode, and the immobilized enzyme layer comprises protein phosphatase 2A and nano-zinc oxide coated with polydopamine; the mass ratio of the protein phosphatase 2A in the immobilized enzyme layer to the polydopamine-coated nano-zinc oxide is 5: 8-5: 2, and the molar ratio of dopamine hydrochloride used as raw materials of the polydopamine-coated nano-zinc oxide to the nano-zinc oxide is 1: 3-1: 2. The invention also provides a preparation method of the electrochemical biosensor. The electrochemical biosensor can be used for detecting diarrhetic shellfish poison in seawater and marine organisms, especially okadaic acid and dinosporin; the polydopamine-coated nano zinc oxide and the protein phosphatase 2A have a synergistic effect, so that the binding force is strong, the enzyme activity is good, the performance is stable, the reutilization is realized, and the cost is low.
Owner:OCEANOGRAPHIC INSTR RES INST SHANDONG ACAD OF SCI +1

Corn protein phosphatase gene ZmPRH20 and application thereof

The invention is applicable to the technical field of molecular biology and biology, and provides a corn protein phosphatase gene ZmPRH20 and application thereof, the sequence of genome DNA of the corn protein phosphatase gene ZmPRH20 is shown as SEQ ID NO: 1, the sequence of cDNA of the corn protein phosphatase gene ZmPRH20 is shown as SEQ ID NO: 2, and the sequence of CDS of the corn protein phosphatase gene ZmPRH20 is shown as SEQ ID NO: 3. The invention provides a protein phosphatase ZmPRH20 gene related to corn drought stress, the protein phosphatase ZmPRH20 gene can positively regulate the drought resistance of a plant, the drought resistance survival rate is remarkably improved compared with that of a wild type after overexpression in arabidopsis thaliana, and the ZmPRH20 protein coded by the gene participates in ABA signal transduction and regulates stress response gene expression through interaction with ABA receptor protein.
Owner:JILIN UNIVERSITY

Broad spectrum anti-cancer compounds

ActiveUS12630527B2Sugar derivativesAntineoplastic agentsAntisense nucleic acidMethyltransferase
Described herein, inter alia, are compounds for treating cancer and methods of use. This disclosure features chemical entities (e.g., small hairpin RNAs (shRNAs), micro RNA (miRNAs), small interfering RNA (siRNAs), small molecule inhibitors, antisense nucleic acids, peptides, viruses, CRISPR-sgRNAs, or combinations thereof) that inhibit one or more of m6A writers (e.g., methyltransferase like 3 (Mettl3 or MT-A70) or methyltransferase like-14 (Mettl14)), m6Am writers (e.g., phosphorylated CTD interacting factor I (PCIF 1), or Mettl3 / 14), m6A erasers (e.g., fat-mass and obesity-associated protein (FTO) or ALKB homolog 5 (ALKBH5)), m6Am erasers (e.g., FTO), m6A readers (e.g., YTH domain-containing family proteins (YTHs)), YTF domain family member 1 (YTHDF 1), YTF domain family member 2 (YTHDF 2), YTF domain family member 3 (YTHDF 3), or tyrosine-protein phosphatase non-receptor type 2 (PTPN2).
Owner:RGT UNIV OF CALIFORNIA

Catalytic inhibitor of protein phosphatase 5 activates the extrinsic apoptotic pathway by disrupting complex ii

Protein phosphatase 5 (PP5) is a serine / threonine protein phosphatase involved in the maturation and activation of numerous signaling pathways essential for cancer growth. PP5 activity is essential for the survival of clear cell renal cell carcinoma (ccRCC), however the mechanism remains unclear. Data demonstrates that PP5 interacts with caspase-8, FADD, and RIPK1, components of extrinsic apoptotic pathway Complex II. Specifically, PP5 dephosphorylates and inactivates the death effector proteins RIPK1 and FADD, preserving Complex II integrity and regulating extrinsic apoptosis. Protein phosphatases are considered to be ‘undruggable,’ however we have developed a specific inhibitor of PP5 (P-053) that prevents substrate binding to the active site. Encouragingly, PP5 inhibition using P-53 in VHL-null ccRCC robustly induces extrinsic apoptosis. Taken together, the data suggests that PP5 promotes ccRCC survival by suppressing extrinsic apoptosis, and small molecule inhibition of PP5 presents a viable therapeutic strategy for ccRCC.
Owner:SYRACUSE UNIVERSITY

Protein phosphatase 2a activators

Disclosed herein are compounds with protein phosphatase 2A agonizing activity. In some embodiments, the compounds may be used in the treatment of cellular disorders, including cancer. In some embodiments, the compounds are used to treat colorectal cancer, including FOLFOX resistant colorectal cancer.
Owner:THE PENN STATE RES FOUND INC +1

7-oxabicyclo [2.2. 1] heptane-2, 3-dicarboxylic acid derivatives and application thereof

The invention belongs to the technical field of medicinal chemistry, and discloses a 7-oxabicyclo [2.2. 1] heptane-2, 3-dicarboxylic acid derivative and an application of the 7-oxabicyclo [2.2. 1] heptane-2, 3-dicarboxylic acid derivative in preparation of a protein phosphatase 5 degradation agent. The compound can directly target PP5 and induce the PP5 to degrade, has the advantages of novel structure and excellent physical and chemical properties, and shows high selectivity to PP5. In various biological evaluations, the molecules all show remarkable anti-proliferative activity and degradation effect.
Owner:CHINA PHARM UNIV

7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid derivative, preparation method therefor, and use thereof

A 7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid derivative, a preparation method therefor, and the use thereof in the preparation of a protein phosphatase 5 (PP5) inhibitor. The 7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid derivative has good physicochemical properties, and is an active small molecule with good stability, safety, and druggability.
Owner:CHINA PHARM UNIV

Use of a drug, miltefosine, in promoting bone formation and preventing and treating osteoporosis

The application discloses application of a medicine, miltefosine, in promoting bone formation and preventing and treating osteoporosis. In the bone formation process, the expression of protein phosphatase PPM1A in osteoblasts is significantly increased, the dephosphorylation of a core protein Smad2 of a TGF-beta signal path is regulated, the TGF-beta signal path is inhibited, the expression of an osteogenic marker is promoted, and the osteogenic ability of the organism is enhanced. The application discloses that the medicine, miltefosine, is used as a PPM1A enzyme activity catalyst, the in-vivo intervention of the medicine can significantly accelerate bone repair and delay bone loss of postmenopausal osteoporosis, a mechanism is that the enzyme activity of PPM1A of osteoblasts is catalyzed, the dephosphorylation of Smad2 protein is promoted, the TGF-beta / Smad2 signal path activity is inhibited, bone formation is promoted, bone repair is accelerated, and bone loss is prevented. Therefore, the miltefosine has a good application prospect in clinical treatment of promoting osteogenesis and preventing and treating osteoporosis.
Owner:THE FIRST AFFILIATED HOSPITAL OF ZHEJIANG CHINESE MEDICAL UNIVERSITY

A 4-chromane ketone-cyclohexane spiro ring trimer compound, a preparation method and application thereof

PendingCN122277511AOrganic synthesisKetone
This invention pertains to organic synthesis and medicinal chemistry, specifically relating to a 4-chromone-cyclohexane spirocyclic trimer compound, its preparation method, and its applications. The 4-chromone-cyclohexane spirocyclic trimer compound has the structure shown in Formula I, II, III, or IV, or stereoisomers of the structures shown in Formulas I to IV. This invention also provides a method for preparing this compound, using 2-hydroxyacetophenone or its derivatives as a starting material, reacting it with dihalomethane in the presence of a base and additives to construct a spirocyclic trimer skeleton in one step. The compound of this invention can inhibit PPM1E and PPM1F protein phosphatases with high activity and high selectivity, achieving nanomolar inhibitory activity against PPM1E and sub-enzyme selectivity exceeding 100-fold. The compound of this invention can be used to prepare drugs for cancers associated with PPM1E / PPM1F overexpression.
Owner:SIX-D PHARMA CO LTD

Cotton serine / threonine protein phosphatase ghTOPP4, encoding gene and application thereof

ActiveCN116103262BTransferasesFermentationThreoninePhosphoprotein phosphatase
The application discloses a cotton serine / threonine protein phosphatase GhTOPP4, a coding gene thereof and application of the cotton serine / threonine protein phosphatase GhTOPP4. The GhTOPP4 is a protein as shown in a), b), c) or d) below: a) a protein consisting of an amino acid sequence shown in SEQ ID No. 1; b) a fusion protein obtained by connecting a tag to an N terminal and / or a C terminal of the protein shown in SEQ ID No. 1; c) a protein obtained by substituting, deleting and / or adding one or more amino acid residues to the amino acid sequence shown in SEQ ID No. 1 and having the same function; and d) a protein having more than 80 % homology with the amino acid sequence defined in any one of a) to c) and having the same function. It is found by the application that the cotton GhTOPP4 protein can regulate plant stress resistance, and lays a good molecular foundation for effectively improving plant salt tolerance, drought tolerance and ABA stress resistance.
Owner:CHINA AGRI UNIV

A protein phosphatase agonist and uses thereof

The application discloses a benzopyrazoloxazine derivative or a pharmaceutically acceptable salt thereof, which is shown as formula I, R is selected from hydrogen, halogen, alkyl and alkoxy; m is an integer from 1 to 3; X is selected from oxygen or sulfur; R1 is selected from hydrogen, alkyl and acyl. The application also discloses application of the benzopyrazoloxazine derivative in preparation of a medicine for preventing and treating diseases caused by absence of PP2A activity or reduction of PP2A function. The application discloses application of the benzopyrazoloxazine derivative in preparation of a protein phosphatase agonist.
Owner:NANJING ZHONGRUI PHARMA

Gene editing system suitable for cotton, application of gene editing system and gene editing method

The invention relates to the field of nucleic acid editing, in particular to a gene editing system suitable for cotton, application of the gene editing system and a gene editing method, and the gene editing system CRISPR / Cas12i. 3 contains targeted site sgRNAs and Cas12i. 3 protein; wherein the Cas12i. 3 protein has an amino acid sequence as shown in SEQ ID NO: 1, and the targeting site sgRNAs has a base sequence as shown in SEQ ID NO: 2. According to a gene editing method for cotton multi-gene knockout by utilizing a gene editing system, a corresponding target site sgRNAs is designed aiming at a salt-sensitive protein phosphatase GhTOPP4 target gene, then the sgRNAs, a cotton endogenous Pol III type promoter and Cas12i. 3 protein are mixed to form a compound, and the compound realizes effective editing of cotton genes in a cotton protoplast transformation mode.
Owner:CHINA AGRI UNIV