Neutral ceramidase-active site inhibitor chemotypes and binding modes

Coant, Nicolas; Bickel, John; Rahaim, Ronald J.; Otsuka, Yuka; Choi, Yong‐Mi; Xu, Ruijuan; Simoes, Michael; Cariello, Chris; Mao, Cungui; Saied, Essa M.; Spicer, Timothy; Bannister, Thomas D.; Tonge, Peter J.; Airola, Michael V.; Scampavia, Louis; Hannun, Yusuf A.; Rizzo, Robert C.; Haley, John D.

doi:10.1016/j.bioorg.2023.106747

Search citation statements

Order By: Relevance

Paper Sections

Select...

Molecular Docking Simulations1

Citation Types

Supporting

Mentioning

Contrasting

Unclassified

Year Published

2023

2024

Publication Types

Select...

Article2

Relationship

Self Cite1

Independent1

Authors

Journals

Cited by 2 publications

(2 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The most favorable docking positions were visualized using Discovery Studio 4.5 (Studio, 2008). [96][97][98][99][100][101] Molecular dynamics simulation (MDS) study For the Molecular Dynamics Simulation (MDS) analysis, we conducted simulations on the complex labelled as '1M17_3b' using the 'Desmond' module developed by Schrödinger, Inc., New York, USA (2023). In this simulation setup, we employed an explicit solvent model, which included TIP3P water molecules and the OPLS-2005 force eld.…”

Section: Molecular Docking Simulationsmentioning

confidence: 99%

See 1 more Smart Citation

Novel 2-substituted-quinoxaline analogs with potential antiproliferative activity against breast cancer: insights into cell cycle arrest, topoisomerase II, and EGFR activity

Salem,

Abu El-ata,

Elsayed

et al. 2023

RSC Adv.

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Molecular Docking Simulationsmentioning

confidence: 99%

“…50. MS analysis (m/z, %): 302(100), 299(43.17), 274 (6.68), 221 (31.52), 193 (29.27), 166 (5.73), 118 (2.87), 111 (2.80), 102 (4.56), 96 (4.02), 77 (6.35), 63 (2.98). Anal.…”

unclassified

Novel 2-substituted-quinoxaline analogs with potential antiproliferative activity against breast cancer: insights into cell cycle arrest, topoisomerase II, and EGFR activity

Salem,

Abu El-ata,

Elsayed

et al. 2023

RSC Adv.

Self Cite

View full text Add to dashboard Cite

show abstract

Mutations in Mig6 reduce inhibition of the epidermal growth factor receptor

Hayashi,

Pak,

Torlentino

et al. 2024

The FASEB Journal

View full text Add to dashboard Cite

Mitogen‐inducible gene 6 (Mig6) is a cellular inhibitor of epidermal growth factor receptor (EGFR) that binds directly to the EGFR kinase domain and interferes with signaling. Reduced Mig6 expression is correlated with increased EGFR activity in multiple cancer models. Here, we investigated whether disease‐associated point mutations could reduce the inhibitory potency of Mig6. We show that several cancer‐associated mutations, and a mutation derived from Alzheimer's Disease patients, diminish the ability of Mig6 to bind and inhibit EGFR in vitro. In mammalian cells, the mutations decreased the Mig6‐induced suppression of basal and EGF‐stimulated autophosphorylation, MAP kinase phosphorylation, and cell migration. To probe the mechanisms by which the mutations could lead to reduced Mig6 inhibition, we constructed atomic‐level computational models of Mig6 complexed with the EGFR catalytic domain, and performed molecular dynamics simulations for wild‐type and mutant complexes.

show abstract

Neutral ceramidase-active site inhibitor chemotypes and binding modes

Cited by 2 publications

References 54 publications

Novel 2-substituted-quinoxaline analogs with potential antiproliferative activity against breast cancer: insights into cell cycle arrest, topoisomerase II, and EGFR activity

Novel 2-substituted-quinoxaline analogs with potential antiproliferative activity against breast cancer: insights into cell cycle arrest, topoisomerase II, and EGFR activity

Mutations in Mig6 reduce inhibition of the epidermal growth factor receptor

Contact Info

Product

Resources

About