mps1 kinase domain Search Results


mps1 kinase domain  (Addgene inc)
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Addgene inc mps1 kinase domain
Fluorescence polarization assay for specific <t>Mps1</t> activity. A, the overall scheme of the FP assay; the peptide (green bar) is fluorescently labeled (yellow star). B, FP measurements of WT Mps1 kinase activity (blue) by titrating the Bub1–Bub3 complex. Gray and black circles represent the measurement in the presence of NMS-P715 and Cpd-5, respectively.
Mps1 Kinase Domain, supplied by Addgene inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Fluorescence polarization assay for specific Mps1 activity. A, the overall scheme of the FP assay; the peptide (green bar) is fluorescently labeled (yellow star). B, FP measurements of WT Mps1 kinase activity (blue) by titrating the Bub1–Bub3 complex. Gray and black circles represent the measurement in the presence of NMS-P715 and Cpd-5, respectively.

Journal: The Journal of Biological Chemistry

Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures

doi: 10.1074/jbc.M117.783555

Figure Lengend Snippet: Fluorescence polarization assay for specific Mps1 activity. A, the overall scheme of the FP assay; the peptide (green bar) is fluorescently labeled (yellow star). B, FP measurements of WT Mps1 kinase activity (blue) by titrating the Bub1–Bub3 complex. Gray and black circles represent the measurement in the presence of NMS-P715 and Cpd-5, respectively.

Article Snippet: Protein production The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).

Techniques: Fluorescence, Activity Assay, FP Assay, Labeling

Characterization of Mps1 C604Y mutant and inhibitors. A, C, and E, FP assay for the Mps1 kinase variants in the presence of inhibitors; WT and C604Y/C604W kinase activities are shown in circles and triangles, respectively. IC50 values were calculated by titrating Cpd-5 (black) and NMS-P715 (gray). B, D, and F, binding affinity measurements of the Mps1 variants with inhibitors, measured by MST.

Journal: The Journal of Biological Chemistry

Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures

doi: 10.1074/jbc.M117.783555

Figure Lengend Snippet: Characterization of Mps1 C604Y mutant and inhibitors. A, C, and E, FP assay for the Mps1 kinase variants in the presence of inhibitors; WT and C604Y/C604W kinase activities are shown in circles and triangles, respectively. IC50 values were calculated by titrating Cpd-5 (black) and NMS-P715 (gray). B, D, and F, binding affinity measurements of the Mps1 variants with inhibitors, measured by MST.

Article Snippet: Protein production The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).

Techniques: Mutagenesis, FP Assay, Binding Assay

Comparison of the Cpd-5 and NMS-P715 bound to C604Y/C604W structures. A, 2mFo − DFc electron density map of Cpd-5 in Mps1 kinase contoured at 1.0σ (carved at 2.5 Å from the Cpd-5 atoms). B, Cpd-5 in the ATP-binding pocket of Mps1 C604Y; Cpd-5, the side chains of Gln541, Tyr604, and Lys553 as well as residue Gly605 are depicted as sticks; hydrogen bonds are depicted as black dotted lines. Figures were made in CCP4mg (38). C, Cpd-5 interactions with Mps1 kinase drawn by the Lidia routine in COOT. D–F, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. G–I, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. J–L, the same as A–C for the interaction of NMS-P715 with Mps1 C604W.

Journal: The Journal of Biological Chemistry

Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures

doi: 10.1074/jbc.M117.783555

Figure Lengend Snippet: Comparison of the Cpd-5 and NMS-P715 bound to C604Y/C604W structures. A, 2mFo − DFc electron density map of Cpd-5 in Mps1 kinase contoured at 1.0σ (carved at 2.5 Å from the Cpd-5 atoms). B, Cpd-5 in the ATP-binding pocket of Mps1 C604Y; Cpd-5, the side chains of Gln541, Tyr604, and Lys553 as well as residue Gly605 are depicted as sticks; hydrogen bonds are depicted as black dotted lines. Figures were made in CCP4mg (38). C, Cpd-5 interactions with Mps1 kinase drawn by the Lidia routine in COOT. D–F, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. G–I, the same as A–C for the interaction of Cpd-5 with Mps1 C604W. J–L, the same as A–C for the interaction of NMS-P715 with Mps1 C604W.

Article Snippet: Protein production The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).

Techniques: Comparison, Binding Assay, Residue

Comparison of the binding modes of Cpd-5, NMS-P715, and reversine. A, NMS-P715 and Cpd-5 in the ATP-binding pocket of Mps1 C604Y; B, NMS-P715 and Cpd-5 in the ATP-binding pocket of Mps1 C604W; C, reversine and Cpd-5 in the ATP-binding pocket of Mps1 C604Y.

Journal: The Journal of Biological Chemistry

Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures

doi: 10.1074/jbc.M117.783555

Figure Lengend Snippet: Comparison of the binding modes of Cpd-5, NMS-P715, and reversine. A, NMS-P715 and Cpd-5 in the ATP-binding pocket of Mps1 C604Y; B, NMS-P715 and Cpd-5 in the ATP-binding pocket of Mps1 C604W; C, reversine and Cpd-5 in the ATP-binding pocket of Mps1 C604Y.

Article Snippet: Protein production The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).

Techniques: Comparison, Binding Assay

Comparison of the Cpd-5 and NMS-P715 C604Y/C604W binding modes. A, Cpd-5 in the ATP-binding pocket of Mps1 C604Y/C604W; the C604W structure is shown with thin lines for comparison. B, NMS-P715 in the ATP-binding pocket of Mps1 C604Y/C604W.

Journal: The Journal of Biological Chemistry

Article Title: Understanding inhibitor resistance in Mps1 kinase through novel biophysical assays and structures

doi: 10.1074/jbc.M117.783555

Figure Lengend Snippet: Comparison of the Cpd-5 and NMS-P715 C604Y/C604W binding modes. A, Cpd-5 in the ATP-binding pocket of Mps1 C604Y/C604W; the C604W structure is shown with thin lines for comparison. B, NMS-P715 in the ATP-binding pocket of Mps1 C604Y/C604W.

Article Snippet: Protein production The plasmid containing a construct of the Mps1 kinase domain (residues 519–808) was a gift from Dr. Nicola Burgess-Brown (Addgene plasmid number 38907) ( 22 ).

Techniques: Comparison, Binding Assay