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289 results for “Phosphatase”

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zenodo32/100

Proteomics and phosphoproteomics analysis of the tyrosine phosphatase SHP2 acquired resistance to SHP099 in the context of AML

<p>Proteomics analysis of AML cell lines (MV-4-11, MOLM-13, EOL-1 and OCI-M1) presenting acquired resistance to SHP099 and their parent sensitive cells in presence of the SHP2 allosteric inhibitor SHP099 or DMSO (control). These samples were labelled with TMT and analysed by mass spectrometry.&nbsp;</p> <p>The same approach was conducted to analyse the phosphoproteome of MV-4-11 cells (parent and resistant) upon SHP099 treatment.</p> <p>These data are associated with the manuscript &quot;<strong>Tyr-62 phosphorylation of the tyrosine phosphatase SHP2 enables acquired resistance to SHP2 allosteric inhibitors</strong>&quot;</p>

openbsd-2-clause-netbsdJan 2021View details →
zenodo32/100

Dataset for manuscript Meier et al. 2024 -- Leveraging the Histidine Kinase-Phosphatase Duality to Sculpt Two-Component Signaling

<p>Dataset for manuscript Meier et al. 2024 -- Leveraging the Histidine Kinase-Phosphatase Duality to Sculpt Two-Component Signaling</p>

opencc-by-4.0Feb 2024View details →
zenodo32/100

Raw data of manuscript "Downregulated dual-specificity protein phosphatase 1 in ovarian carcinoma: a comprehensive study with multiple methods" submitted to PeerJ

<p>Some raw data and original calculating results of this manuscript.</p>

opencc-by-4.0Dec 2021View details →
zenodo32/100

Structural insights into the inhibition site in the phosphorylcholine phosphatase enzyme of Pseudomonas aeruginosa

<p>Inputs for the simulations (MDs and FEP), plus scripts used to obtain results of the manuscript entitled &quot;Structural insights into the inhibition site in the phosphorylcholine phosphatase enzyme of Pseudomonas aeruginosa&quot;</p>

opencc-by-4.0May 2022View details →
zenodo32/100

MOVIE#1 -Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis.

<p>Movie&nbsp;of paced activation acquired during perfusion of an isolated rabbit heart&nbsp;with CaMKII inhibitor KN93</p>

opencc-by-4.0Feb 2019View details →
zenodo32/100

MOVIE#4 -Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis.

<p>Movie&nbsp;of arrhythmia acquired during perfusion of an isolated rabbit heart&nbsp;with PKA inhibitor H89.</p>

opencc-by-4.0Feb 2019View details →
zenodo32/100

MOVIES#1-4 -Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis.

<p>Movies of paced activation and of arrhythmia acquired during perfusion of isolated rabbit hearts with CaMKII inhibitor KN93 or PKA inhibitor H89.</p>

opencc-by-4.0Feb 2019View details →
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MOVIE#3 -Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis.

<p>Movie&nbsp;of paced activation acquired during perfusion of an isolated rabbit heart&nbsp;with PKA inhibitor H89</p>

opencc-by-4.0Feb 2019View details →
zenodo32/100

MOVIE#2 -Conduction in the Right and Left Ventricle is Differentially Regulated by Protein Kinases and Phosphatases: Implications for Arrhythmogenesis.

<p>Movie&nbsp;of arrhythmia acquired during perfusion of an isolated rabbit heart&nbsp;with CaMKII inhibitor KN93.</p>

opencc-by-4.0Feb 2019View details →
zenodo32/100

Figure EV2 of 'Structural basis for the specificity of PPM1H phosphatase for Rab GTPases'

<p><strong>Raw data for Figure EV2 from manuscript &#39;Structural basis for the specificity of PPM1H phosphatase for Rab GTPases&#39;, Dieter Waschb&uuml;sch, Kerryn Berndsen, Pawel Lis, Axel Knebel, Yuko P. Y. Lam, Dario R. Alessi, Amir R. Khan</strong><br> &nbsp;</p> <p><strong>Figure EV2C Malachite.xlsx:</strong></p> <p>Numerical data for the chart shown in Fig.EV2C</p>

opencc-by-4.0May 2021View details →
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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.

opennotspecifiedFeb 2020View details →
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Fig. 4 in Oleanane hemiacetal glycosides from Gymnema latifolium and their inhibitory effects on protein tyrosine phosphatase 1B

Fig. 4. Key NOESY correlations of compounds 1 (a: the aglycone, b: sugar moiety), 5 and 6. Fig. 4 c showed the chemical shifts and coupling constants of the protons on the glycosides. HMBC correlations bridging two sugar moieties were measured. All the discussions about COSY, NOESY and the coupling constant rules to identify the relative configuration of the sugar moiety were suggested at Results and discussion of compound 1.

opennotspecifiedFeb 2020View details →
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Fig. 1 in Oleanane hemiacetal glycosides from Gymnema latifolium and their inhibitory effects on protein tyrosine phosphatase 1B

Fig. 1. Morphological characteristics of Gymnema latifolium Wall ex. Wight. (a) Old stem showing wing-like cork (b) Living form; (c) Young branch with pairs of inflorescensces; (d) Adaxial leaf; (e) Abaxial leaf; (f) Inflorescence; (g) Dense bronze hairs on the young leaf; (h) A flower; (i) Calyx; (j) Corolla; (k) Gynostegium cylindric; (l) Pollinarium; (m) Stigma head; (n) Follicles.

opennotspecifiedFeb 2020View details →
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Fig. 3 in Azaphilones with protein tyrosine phosphatase inhibitory activity isolated from the fungus Aspergillus deflectus

Fig. 3. Graph of 13C-Dp4+ probabilities obtained by correlating the calculated and experimental 13C NMR data of 4 (1: 2′S-isomer; 2: 2′R-isomer).

opennotspecifiedFeb 2020View details →
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Fig. 5 in Protein tyrosine phosphatase 1B inhibitors from the fungus Malbranchea albolutea

Fig. 5. Structural models of the binding sites of the PTP1B ligand complexes. In the center, the protein PTP1B is shown in orange cartoons, red sticks (1), green sticks (2), blue sticks (3), and magenta sticks (6). The images were created with the PyMOL and Maestro programs. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedApr 2021View details →
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Fig. 2 in Protein tyrosine phosphatase 1B inhibitors from the fungus Malbranchea albolutea

Fig. 2. Comparison of the experimental ECD spectrum of 1 (black dotted) with calculated for the enantiomers 5aS,8R,15bR,16aR (orange) and 5aR,8S,15bS,16aS (red) [a]. Comparison of the experimental ECD spectrum of 3 (black dotted) with calculated for the enantiomers 5aR,8R,15bS,16aR (red) and 5aS,8S,15bR,16aS (orange) [b]. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedApr 2021View details →
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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.

opennotspecifiedApr 2021View details →
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Fig. 3 in Protein tyrosine phosphatase 1B inhibitors from the fungus Malbranchea albolutea

Fig. 3. Comparison of the experimental ECD spectrum of 2 (dotted black) with the enantiomers 5aS,8S,15bR,16aR (red) and 5aR,8R,15bS,16aS (blue). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

opennotspecifiedApr 2021View details →
zenodo32/100

Fig. 7 in Protein tyrosine phosphatase 1B inhibitors from the fungus Malbranchea albolutea

Fig. 7. Structural models of PTP1B-3 complex from 0 to 100 ns of MD. The structures used in the simulation were 149T.pdb. The analyzes and figures were made with CPPTRAJ and PyMOL.

opennotspecifiedApr 2021View details →
zenodo32/100

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>

opencc-by-4.0Jun 2023View details →

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