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embl accessions  (Taxon Biosciences)
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Taxon Biosciences embl accessions
Embl Accessions, supplied by Taxon Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession no. nm_152490  (Biotechnology Information)
90
Biotechnology Information genbank accession no. nm_152490
Genbank Accession No. Nm 152490, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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national center for biotechnology information genbank accession no. nm_174990  (Biotechnology Information)
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Biotechnology Information national center for biotechnology information genbank accession no. nm_174990
National Center For Biotechnology Information Genbank Accession No. Nm 174990, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession number kt581023  (Biotechnology Information)
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Biotechnology Information genbank accession number kt581023
Genbank Accession Number Kt581023, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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full-length human recombinant histone h2a (nm_021052, cat#hmt-11–146)  (Reaction Biology Corporation)
90
Reaction Biology Corporation full-length human recombinant histone h2a (nm_021052, cat#hmt-11–146)
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Full Length Human Recombinant Histone H2a (Nm 021052, Cat#Hmt 11–146), supplied by Reaction Biology Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession numbers ab019236, ab026633, ab013395 and ac002291  (Blackwell Science Ltd)
90
Blackwell Science Ltd genbank accession numbers ab019236, ab026633, ab013395 and ac002291
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Genbank Accession Numbers Ab019236, Ab026633, Ab013395 And Ac002291, supplied by Blackwell Science Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession 1517012  (Biotechnology Information)
90
Biotechnology Information genbank accession 1517012
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Genbank Accession 1517012, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession number  (Compugen Inc)
90
Compugen Inc genbank accession number
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Genbank Accession Number, supplied by Compugen Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession no  (Blackwell Science Ltd)
90
Blackwell Science Ltd genbank accession no
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Genbank Accession No, supplied by Blackwell Science Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession no. kp090294  (Biotechnology Information)
90
Biotechnology Information genbank accession no. kp090294
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
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gene expression omnibus number  (Biotechnology Information)
90
Biotechnology Information gene expression omnibus number
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Gene Expression Omnibus Number, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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genbank accession its mh221478  (Kemper GmbH)
90
Kemper GmbH genbank accession its mh221478
JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone <t>H2A,</t> and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.
Genbank Accession Its Mh221478, supplied by Kemper GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone H2A, and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.

Journal: Molecular Cancer Therapeutics

Article Title: Discovery and Pharmacological Characterization of JNJ-64619178, a Novel Small-Molecule Inhibitor of PRMT5 with Potent Antitumor Activity

doi: 10.1158/1535-7163.MCT-21-0367

Figure Lengend Snippet: JNJ-64619178 potently inhibits the PRMT5/MEP50 complex with a long-residence–binding time mechanism through interaction with PRMT5's SAM and substrate binding pockets. A, JNJ-64619178 chemical structure. B, Inhibition of PRMT5 by JNJ-64619178 was studied in a reaction mixture of 10 μmol/L SAM, 1 μmol/L histone H2A, and 0.156 nmol/L enzyme in the absence or presence of JNJ-64619178 at different concentrations as depicted in . Production of SAdenosyl–L-homocysteine (SAH) was followed as a function of reaction time. Reaction progress curves were fit to Eq. 1 to derive the inhibition rate constant k obs at each compound concentration. C, Plot of derived k obs versus JNJ-64619178 concentration was fit to a hyperbolic function of Eq. 2. Binding and dissociation curves to and from immobilized PRMT5/MEP50 complex were measured by surface plasmon resonance (SPR for ( D ) JNJ-64619178 and ( E ) Cpd-2. PRMT5/MEP50 complex was immobilized on a CM5 sensor chip and increasing concentrations of JNJ-64619178 or Cpd-2 (1.56–100 nmol/L) were added to determine the binding kinetics. Compound association to and dissociation from the immobilized PRMT5/MEP50 complex, described previously as SPR response units (RU), were plotted against time (s). F, X-ray co-crystal structure of JNJ-64619178 bound to the active site of the PRMT5:MEP50 complex (PDB ID: 6RLQ). JNJ-64619178 is shown in yellow and key PRMT5 interaction residues are shown as gray sticks. Oxygen atoms are colored red, nitrogen atoms blue, and the bromine atom in maroon. Hydrogen bonds are depicted as black-dashed lines and the halogen bond as an orange-dashed line. The binding site surface of PRMT5 is depicted and the putative SAM-binding site is colored in ivory whereas the substrate-binding site is colored in cyan.

Article Snippet: Full-length human recombinant histone H2A (NM_021052, Cat#HMT-11–146) was purchased from Reaction Biology Corporation, SAM (Cat#13956) and S-Adenosyl–L-homocysteine (SAH; Cat#13603) from Cayman Chemical Company, and Cycloheximide (CHX) from Merck–Millipore (Cat#239764).

Techniques: Binding Assay, Inhibition, Concentration Assay, Derivative Assay, SPR Assay