nma model Search Results


core diabetes model  (IQVIA Inc)
90
IQVIA Inc core diabetes model
Core Diabetes Model, supplied by IQVIA 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/nma+model/pmc06349296-112-15-14?v=IQVIA+Inc
Average 90 stars, based on 1 article reviews
core diabetes model - by Bioz Stars, 2026-08
90/100 stars
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nma model  (STATA Corporation)
99
STATA Corporation nma model
Nma Model, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pmc06935494-121-4-18?v=STATA+Corporation
Average 99 stars, based on 1 article reviews
nma model - by Bioz Stars, 2026-08
99/100 stars
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non-normal mode analysis  (Schmid GmbH)
90
Schmid GmbH non-normal mode analysis
Non Normal Mode Analysis, supplied by Schmid GmbH, 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/nma+model/10__1017_slash_s0022112009993417-48-5-40?v=Schmid+GmbH
Average 90 stars, based on 1 article reviews
non-normal mode analysis - by Bioz Stars, 2026-08
90/100 stars
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random effects model nma  (STATA Corporation)
99
STATA Corporation random effects model nma
Random Effects Model Nma, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pmc06258639-178-7-26?v=STATA+Corporation
Average 99 stars, based on 1 article reviews
random effects model nma - by Bioz Stars, 2026-08
99/100 stars
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imods  (Molecular Dynamics Inc)
86
Molecular Dynamics Inc imods
Imods, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pm41699076-154-12-0?v=Molecular+Dynamics+Inc
Average 86 stars, based on 1 article reviews
imods - by Bioz Stars, 2026-08
86/100 stars
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version 16  (STATA Corporation)
99
STATA Corporation version 16
Version 16, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pmc08801998-93-14-16?v=STATA+Corporation
Average 99 stars, based on 1 article reviews
version 16 - by Bioz Stars, 2026-08
99/100 stars
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summary effect 197 estimates  (STATA Corporation)
99
STATA Corporation summary effect 197 estimates
Summary Effect 197 Estimates, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pmc06731894__bmjopen___2019___031138__draft_revisions-69-13-27?v=STATA+Corporation
Average 99 stars, based on 1 article reviews
summary effect 197 estimates - by Bioz Stars, 2026-08
99/100 stars
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mode analysis nma module  (Molecular Dynamics Inc)
86
Molecular Dynamics Inc mode analysis nma module
(A) B factors derived from normal mode analysis <t>(NMA)</t> showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize <t>the</t> <t>receptor</t> in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.
Mode Analysis Nma Module, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nma+model/pmc12860517-76-9-0?v=Molecular+Dynamics+Inc
Average 86 stars, based on 1 article reviews
mode analysis nma module - by Bioz Stars, 2026-08
86/100 stars
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random-effects nma model  (Schwarzer GmbH)
90
Schwarzer GmbH random-effects nma model
(A) B factors derived from normal mode analysis <t>(NMA)</t> showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize <t>the</t> <t>receptor</t> in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.
Random Effects Nma Model, supplied by Schwarzer GmbH, 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/nma+model/pmc07049189-114-24-36?v=Schwarzer+GmbH
Average 90 stars, based on 1 article reviews
random-effects nma model - by Bioz Stars, 2026-08
90/100 stars
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r studio version 1.2.5033  (RStudio)
90
RStudio r studio version 1.2.5033
(A) B factors derived from normal mode analysis <t>(NMA)</t> showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize <t>the</t> <t>receptor</t> in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.
R Studio Version 1.2.5033, supplied by RStudio, 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/nma+model/pm37130094-41-17-15?v=RStudio
Average 90 stars, based on 1 article reviews
r studio version 1.2.5033 - by Bioz Stars, 2026-08
90/100 stars
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ar231453 n-(2-fluoro-4-methanesulfonylphenyl)-(6-[4-(3-isopropyl-[1,2,4]oxadiazol-5-yl)-piperidin-1-yl]-5-nitropyrimidin-4-yl)amine (ar231453)  (Enzo Biochem)
90
Enzo Biochem ar231453 n-(2-fluoro-4-methanesulfonylphenyl)-(6-[4-(3-isopropyl-[1,2,4]oxadiazol-5-yl)-piperidin-1-yl]-5-nitropyrimidin-4-yl)amine (ar231453)
(A) B factors derived from normal mode analysis <t>(NMA)</t> showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize <t>the</t> <t>receptor</t> in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.
Ar231453 N (2 Fluoro 4 Methanesulfonylphenyl) (6 [4 (3 Isopropyl [1,2,4]Oxadiazol 5 Yl) Piperidin 1 Yl] 5 Nitropyrimidin 4 Yl)amine (Ar231453), supplied by Enzo Biochem, 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/nma+model/10__1002_slash_jcc__25079-71-7-13?v=Enzo+Biochem
Average 90 stars, based on 1 article reviews
ar231453 n-(2-fluoro-4-methanesulfonylphenyl)-(6-[4-(3-isopropyl-[1,2,4]oxadiazol-5-yl)-piperidin-1-yl]-5-nitropyrimidin-4-yl)amine (ar231453) - by Bioz Stars, 2026-08
90/100 stars
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kcnma1  (Taconic Biosciences)
N/A
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Image Search Results


(A) B factors derived from normal mode analysis (NMA) showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize the receptor in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.

Journal: Chemistry & Biodiversity

Article Title: Serotonergic Neuromodulation of Natural Products Isoreserpine and Isoreserpiline in Adult Zebrafish: An in Silico and In Vivo Investigation

doi: 10.1002/cbdv.202501738

Figure Lengend Snippet: (A) B factors derived from normal mode analysis (NMA) showing intrinsically flexible regions of the 5‐HT3A subunit (black line), highlighting the segment between residues 332–333. (B) RMS mobility profiles per residue (RMS mean) of the 5‐HT3A/IRPN (green) and 5‐HT3A/IRPL (red) complexes, indicating that both ligands stabilize the receptor in a similar manner, with greater local fluctuations concentrated in the distal domain (residues 302–349). (C, D) Convergence of the morphing trajectory for the two complexes, monitored by the RMSD of Cα atoms throughout the iterations. (C) The 5‐HT3A/IRPN complex converged to a final RMSD of 1.49 Å in ∼1.35 × 10 4 iterations, while the (D) 5‐HT3A/IRPL complex converged to 1.48 Å in ∼1.45 × 10 4 iterations.

Article Snippet: Molecular dynamics (MD) simulations were conducted using the normal mode analysis (NMA) module to observe the deformability of the ligand–receptor complex that the compounds form when binding to the 5‐HT3A receptor.

Techniques: Derivative Assay, Residue