OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!
If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.
Requested Article:
In silico approaches to evaluate the molecular properties of organophosphate compounds to inhibit acetylcholinesterase activity in housefly
Parthiban Marimuthu, Yongjin Lee, Byung‐Hoon Kim, et al.
Journal of Biomolecular Structure and Dynamics (2018) Vol. 37, Iss. 2, pp. 307-320
Closed Access | Times Cited: 12
Parthiban Marimuthu, Yongjin Lee, Byung‐Hoon Kim, et al.
Journal of Biomolecular Structure and Dynamics (2018) Vol. 37, Iss. 2, pp. 307-320
Closed Access | Times Cited: 12
Showing 12 citing articles:
A critical review of effect modeling for ecological risk assessment of plant protection products
Floriane Larras, Sandrine Charles, Arnaud Chaumot, et al.
Environmental Science and Pollution Research (2022) Vol. 29, Iss. 29, pp. 43448-43500
Open Access | Times Cited: 29
Floriane Larras, Sandrine Charles, Arnaud Chaumot, et al.
Environmental Science and Pollution Research (2022) Vol. 29, Iss. 29, pp. 43448-43500
Open Access | Times Cited: 29
Assessment of scoring functions and in silico parameters for AChE-ligand interactions as a tool for predicting inhibition potency
Goran Šinko
Chemico-Biological Interactions (2019) Vol. 308, pp. 216-223
Closed Access | Times Cited: 30
Goran Šinko
Chemico-Biological Interactions (2019) Vol. 308, pp. 216-223
Closed Access | Times Cited: 30
Trends in the Recent Patent Literature on Cholinesterase Reactivators (2016–2019)
Alexandre A. de Castro, Letícia C. Assis, Flávia V. Soares, et al.
Biomolecules (2020) Vol. 10, Iss. 3, pp. 436-436
Open Access | Times Cited: 19
Alexandre A. de Castro, Letícia C. Assis, Flávia V. Soares, et al.
Biomolecules (2020) Vol. 10, Iss. 3, pp. 436-436
Open Access | Times Cited: 19
Homology modeling, docking, molecular dynamics and in vitro studies to identify Rhipicephalus microplus acetylcholinesterase inhibitors
Amanda Ponce Morais Cerqueira, Isis Bugia Santana, Janay Stefany Carneiro Araújo, et al.
Journal of Biomolecular Structure and Dynamics (2021) Vol. 40, Iss. 15, pp. 6787-6797
Closed Access | Times Cited: 12
Amanda Ponce Morais Cerqueira, Isis Bugia Santana, Janay Stefany Carneiro Araújo, et al.
Journal of Biomolecular Structure and Dynamics (2021) Vol. 40, Iss. 15, pp. 6787-6797
Closed Access | Times Cited: 12
Reducing health & environmental impacts of chemical warfare agents: Computational chemistry contributions
Georgia Melagraki
Chemosphere (2021) Vol. 288, pp. 132564-132564
Closed Access | Times Cited: 8
Georgia Melagraki
Chemosphere (2021) Vol. 288, pp. 132564-132564
Closed Access | Times Cited: 8
Cytotoxic effects of parathion, paraoxon, and their methylated derivatives on a mouse neuroblastoma cell line NB41A3
Yunbiao Wang, Byung‐Hoon Kim, Ashley R. Walker, et al.
Fundamental Toxicological Sciences (2019) Vol. 6, Iss. 2, pp. 45-56
Open Access | Times Cited: 7
Yunbiao Wang, Byung‐Hoon Kim, Ashley R. Walker, et al.
Fundamental Toxicological Sciences (2019) Vol. 6, Iss. 2, pp. 45-56
Open Access | Times Cited: 7
Unraveling the molecular mechanism of benzothiophene and benzofuran scaffold-merged compounds binding to anti-apoptotic Myeloid cell leukemia 1
Parthiban Marimuthu, Kalaimathy Singaravelu
Journal of Biomolecular Structure and Dynamics (2018) Vol. 37, Iss. 8, pp. 1992-2003
Closed Access | Times Cited: 6
Parthiban Marimuthu, Kalaimathy Singaravelu
Journal of Biomolecular Structure and Dynamics (2018) Vol. 37, Iss. 8, pp. 1992-2003
Closed Access | Times Cited: 6
Poisoning and mutagenesis in rural workers: a sentinel surveillance study
Joana D’arc Santana, Josefa Castro Balsa, Luan Felipe Santana Costa, et al.
Caderno Pedagógico (2024) Vol. 21, Iss. 13, pp. e12680-e12680
Closed Access
Joana D’arc Santana, Josefa Castro Balsa, Luan Felipe Santana Costa, et al.
Caderno Pedagógico (2024) Vol. 21, Iss. 13, pp. e12680-e12680
Closed Access
Investigating the Molecular Basis of N-Substituted 1-Hydroxy-4-Sulfamoyl-2-Naphthoate Compounds Binding to Mcl1
Kalaimathy Singaravelu, Pavithra K. Balasubramanian, Parthiban Marimuthu
Processes (2019) Vol. 7, Iss. 4, pp. 224-224
Open Access | Times Cited: 3
Kalaimathy Singaravelu, Pavithra K. Balasubramanian, Parthiban Marimuthu
Processes (2019) Vol. 7, Iss. 4, pp. 224-224
Open Access | Times Cited: 3
Binding organophosphate pesticides to acetylcholinesterase: risk assessment using the Monte Carlo method
Alla P. Toropova, Andrey A. Toropov, Alessandra Roncaglioni, et al.
Toxicological & Environmental Chemistry Reviews (2023) Vol. 105, Iss. 1-7, pp. 19-27
Open Access | Times Cited: 1
Alla P. Toropova, Andrey A. Toropov, Alessandra Roncaglioni, et al.
Toxicological & Environmental Chemistry Reviews (2023) Vol. 105, Iss. 1-7, pp. 19-27
Open Access | Times Cited: 1
Binding organophosphate pesticides to acetylcholinesterase: Risk assessment using the Monte Carlo method
Alla P. Toropova, Andrey A. Toropov, Alessandra Roncaglioni, et al.
Research Square (Research Square) (2022)
Open Access | Times Cited: 1
Alla P. Toropova, Andrey A. Toropov, Alessandra Roncaglioni, et al.
Research Square (Research Square) (2022)
Open Access | Times Cited: 1
Advances Toward the Development of New Therapeutic Strategies Targeting Acetylcholinesterase and Its Remediation Processes
Alexandre A. de Castro, Letícia C. Assis, Giovanna Cardoso Gajo, et al.
Engineering materials (2021), pp. 619-647
Closed Access
Alexandre A. de Castro, Letícia C. Assis, Giovanna Cardoso Gajo, et al.
Engineering materials (2021), pp. 619-647
Closed Access
