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psim  (Powersim Inc)

 
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    Structured Review

    Powersim Inc psim
    Psim, supplied by Powersim Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/psim/psim/us12362660-112-22-23
    Average 90 stars, based on 1 article reviews
    psim - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    other:

    Article Title: Chattering Free Adaptive Sliding Mode Controller for Photovoltaic Panels with Maximum Power Point Tracking
    Article Snippet: The simulations of PV module and power electronic converter with MPPT controller are performed in PSIM (PowerSim).

    Article Title: Power converter controlled capacitor circuits and methods
    Article Snippet: FIG. 5 shows the voltage and current waveforms for operation of the PCCC circuit of FIG. 4, obtained by a simulation using PSIM (PowerSim, Rockville, Md., USA).

    Article Title: Resonant power converters and control methods for wide input and output voltage ranges
    Article Snippet: A simulation was conducted using PSIM (PowerSim, Rockville, Md., USA) based on the design parameters of Table 1, with output voltage Vo=10V for non-doubler mode, and 2Vo=20V for voltage doubler mode of operation.

    Article Title: Power converter controlled capacitor circuits and methods
    Article Snippet: FIG. 5 shows the voltage and current waveforms for operation of the PCCC circuit of FIG. 4, obtained by a simulation using PSIM (PowerSim, Rockville, MD, USA).

    Software:

    Article Title: Design and Implementation of an Integrated Control Scheme for GaN-Based Multiple Power Converters.
    Article Snippet: .. Operating Mode Simulation and Analysis In this paper, the software, PowerSIM (PSIM), is used for obtaining results of vari- ous scenario simulations, which can be used to compare the results from the hardware implementation and to verify the correctness of the designed controllers and the feasi- Figure 15. ..

    Article Title: Pv Based Battery Less Cooling And Lighting Solution
    Article Snippet: .. PSIM is a simulation software developed by Powersim Inc. PSIM is designed for power electronics, motor control, and simulation of dynamic systems. ..

    Comparison:

    Article Title: Line power extension for capacitor size reduction in AC-DC converters
    Article Snippet: .. Performance Comparison A simulation was conducted using PSIM (Powersim Inc., Rockville, Md., USA) to determine the required capacitance value of Cin for a line power extension embodiment and a conventional full bridge, for designs based on different Vbus_min and a 60 W load. ..

    Control:

    Article Title: Pv Based Battery Less Cooling And Lighting Solution
    Article Snippet: .. PSIM is a simulation software developed by Powersim Inc. PSIM is designed for power electronics, motor control, and simulation of dynamic systems. ..



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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    psim  (Seqirus Inc)
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    phosphatase inhibitor mixture psim  (Beyotime)
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
    Phosphatase Inhibitor Mixture Psim, supplied by Beyotime, 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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    psim module  (ASPEC Technologies Limited)
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    ASPEC Technologies Limited psim module
    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , <t>PsiM</t> , and PsiK , or ( B ) OsCYP71P1 <t>,</t> <t>RmNMT</t> , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).
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    Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

    Journal: Science Advances

    Article Title: Complete biosynthesis of psychedelic tryptamines from three kingdoms in plants

    doi: 10.1126/sciadv.aeb3034

    Figure Lengend Snippet: Comparison of absolute concentrations of indolethylamine products (median ± SD; n = 4 biological replicates; values are given in micrograms per gram per fresh weight) following transient expression of different combinations of AroG , PvTDC2 , and ( A ) PvNMT1 , PsiH , PsiM , and PsiK , or ( B ) OsCYP71P1 , RmNMT , AtCOMT , the mutant AtCOMTA160G , and PvNMT1 in N. benthamiana leaves. Absolute concentrations were according to external calibration curves. Concentrations of bufotenin 7 and 5-methoxy- N -methyltryptamine (5-MeO-NMT 9 ) were semiquantified using the calibration curves of psilocin 16 and 5-methoxy- N , N -dimethyltryptamine (5-MeO-DMT 10 ), respectively. Samples were collected 1 week following agroinfiltration. Unless otherwise stated, statistical significance was assessed using one-way ANOVA followed by Tukey’s post hoc test; different letters denote statistically significant differences ( P < 0.05). For psilocin 16 , 5-MeO-NMT 9 , and 5-MeO-DMT 10 , where ANOVA could not be applied due to zero variance in several gene combinations, statistical significance was assessed using two-tailed unpaired Student’s t test assuming unequal variance (** P < 0.01 and **** P < 0.0001; ns, not significant). Chemical structures of products are shown for reference and are colored according to . Additional pathway intermediates are shown in figs. S10 and S11. Plus signs indicate the biosynthetic genes included in each experiment; boxes mark the last enzyme added in a set of coexpressed genes. ( C ) AlphaFold3 model of AtCOMT bound to the cofactor SAM and substrate bufotenin 7 . Active sites of AtCOMT and the AtCOMTA160G variant are shown in insets I and II, respectively. Inset I: Steric overlap is observed between the residue of A160 (magenta) and the methyl groups of bufotenin 7 (purple spheres). Inset II: Substitution A160G (magenta, indicated by arrow) resolves the steric overlap, by removing the clashing methyl of A160, accommodating the bufotenin 7 methyl groups (purple spheres).

    Article Snippet: RmNMT , PsiH , PsiK , PsiM , OsCYP71P1 , AtCOMT , AtCOMTA160G , RebF , RebH , PyrH , and SttH coding sequences were codon optimized for expression in N. tabacum and synthesized by Twist Biosciences.

    Techniques: Comparison, Expressing, Mutagenesis, Two Tailed Test, Variant Assay, Residue