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Dataset results
32 results for “PTP1B”
Apo PTP1B by Native S-SAD at Room Temperature
<p>Intermediate processing results used to solve a structure of apo PTP1B by native S-SAD at room temperature.</p>
PanDDA analysis of PTP1B screened against fragment libraries
<p>Tyrosine phosphatase, PTP1B, screened against multiple fragment libraries via X-ray crystallography.</p>
PanDDA analysis of PTP1B re-screened against fragment libraries at RT
<p>PTP1B re-screened against multiple fragment libraries with RT crystallography</p>
Fig. 5. A. PTP1B in Oleanane hemiacetal glycosides from Gymnema latifolium and their inhibitory effects on protein tyrosine phosphatase 1B
Fig. 5. A. PTP1B inhibitory activities of compounds 1–9. B. Lineweaver-Burk plots for determination of the type of PTP1B inhibition of compounds 2 and 3 using pNPP assay. The conditions were as follows: 4 mM substrate, 0.05–0.1 μg/mL of PTP1B enzyme, 50 mM Tris (pH 7.5), at room temperature. In the presence of different concentrations of compounds for lines from bottom to top: A. Compound 2 (20, 30 and 40 μM); B. Compound 3 (10, 20 and 30 μM). The data were evaluated in three replicates at each substrate concentration.
Fig. 2. Selected 1H–1H in Coumaronochromones, flavanones, and isoflavones from the twigs and leaves of Erythrina subumbrans inhibit PTP1B and nitric oxide production
Fig. 2. Selected 1H–1H COSY (green bold lines) and HMBC (blue arrows) correlations of compounds 1, 2, 4–7, 15, 25, and 26. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
Fig. 5 in Coumaronochromones, flavanones, and isoflavones from the twigs and leaves of Erythrina subumbrans inhibit PTP1B and nitric oxide production
Fig. 5. Experimental ECD spectra of 15a and 15b and calculated ECD spectra for (1′′R,2′′R)-15 and (1′′S,2′′S)-15.
Fig. 8 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 8. Molecular docking related α-glucosidase inhibition by acarbose (green stick), BIP (red stick), 20 (cyan and yellow stick), and 26 (magenta stick) (a). 2D diagram of α-glucosidase inhibition by 20 [b (at the catalytic site) and c (at the allosteric site)] and 26 (d). The figure was generated using PyMOL and Discovery Studio Visualizer. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 7. Molecular docking related PTP1B in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 7. Molecular docking related PTP1B inhibition by compound C (magenta stick) and compound A (red stick), 20 (green stick), and 26 (yellow and blue stick) (a). 2D diagram of PTP1B inhibition by 20 (b) and 26 [c (at the catalytic site) and d (at the allosteric site)]. The figure was generated using PyMOL and Discovery Studio Visualizer. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
Fig. 6 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 6. Dixon plots (a and c), Lineweaver Burk plots (d and f), and secondary plots (b and e) for the α-glucosidase inhibition by 20 (a, b, d, and e) and 26 (c and f).
Fig. 5 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 5. Lineweaver plots [a and b], Dixon plots [d and e], and secondary plots [c and f] for the inhibition of PTP1B enzyme by 20 (a and d) and 26 (b, c, e, and f), respectively.
Fig. 4. Kinetic analysis for 3 versus PTP1B in Protein tyrosine phosphatase 1B inhibitors from the fungus Malbranchea albolutea
Fig. 4. Kinetic analysis for 3 versus PTP1B. The double-reciprocal curves in which inverse velocity versus inverse substrate concentration are plotted. The curves represent different concentrations of compound 3.
Dataset for Multiscale in silico study of mechanism of activation of RtcB ligase by PTP1B phosphatase.
<p>The pdb structures of the RtcB_PTP1B complex after protein-protein docking and after 1000ns MD simulation, 1000ns MD trajectory, and a video captured from the QM/MM WT-MetaD simulation trajectory showing the reaction mechanism</p>
Correlation Between PTP1B Expression and Organ Failure During Sepsis
ClinicalTrials.gov study NCT02295514. IPD Sharing: Not stated. Countries: 1. Publications: 6.
Fig. 4 in Coumaronochromones, flavanones, and isoflavones from the twigs and leaves of Erythrina subumbrans inhibit PTP1B and nitric oxide production
Fig. 4. Key ROESY correlations of compound 15.
Fig. 3. ECD spectra for compounds 1–3 in Coumaronochromones, flavanones, and isoflavones from the twigs and leaves of Erythrina subumbrans inhibit PTP1B and nitric oxide production
Fig. 3. ECD spectra for compounds 1–3.
Fig. 1 in Coumaronochromones, flavanones, and isoflavones from the twigs and leaves of Erythrina subumbrans inhibit PTP1B and nitric oxide production
Fig. 1. Chemical structures of compounds 1–27.
Fig. 4 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 4. Chemical structures of known compounds 7 32.
Fig. 2 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 2. Key HMBC, COSY, and NOESY correlations of 1–6 and 9.
Fig. 3 in PTP1B and α-glucosidase inhibitory activities of the chemical constituents from Hedera rhombea fruits: Kinetic analysis and molecular docking simulation
Fig. 3. Experimental and calculated ECD spectra of compounds 1–4.
Fig. 9. PTP1B in Lignanamides from the roots of Limonium gmelinii (Willd.) Kuntze and their anti-diabetic, cytotoxic and anti-inflammatory activities
Fig. 9. PTP1B and α-glucosidase inhibitory activity of compounds 1–6, 8–19.
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International Brain Laboratory public data
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OpenNeuro
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