OpenAlex Citation Counts

OpenAlex Citations Logo

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:

A comparative study on the leishmanicidal activity of the L-amino acid oxidases BjussuLAAO-II and BmooLAAO-II isolated from Brazilian Bothrops snake venoms
Luana Gonçalves Barbosa, Tássia R. Costa, Isabela Pacheco Borges, et al.
International Journal of Biological Macromolecules (2020) Vol. 167, pp. 267-278
Closed Access | Times Cited: 12

Showing 12 citing articles:

Antimicrobial properties of L-amino acid oxidase: biochemical features and biomedical applications
Kosuke Kasai, Manabu Nakano, Masami Ohishi, et al.
Applied Microbiology and Biotechnology (2021) Vol. 105, Iss. 12, pp. 4819-4832
Open Access | Times Cited: 33

Revealing the Key Organelle in the Pathophysiology and Clinical Applications of Animal Toxins: Mitochondria
Linfeng Wang, Jiahao Liu, Sheng Zhou, et al.
Toxicon (2025), pp. 108323-108323
Closed Access

Roles of Bothrops jararacussu toxins I and II: Antiviral findings against Zika virus
Natasha Marques Cassani, Igor Andrade Santos, Victória Riquena Grosche, et al.
International Journal of Biological Macromolecules (2022) Vol. 227, pp. 630-640
Open Access | Times Cited: 15

BjussuLAAO-II, an l-amino acid oxidase from Bothrops jararacussu snake venom, impairs Toxoplasma gondii infection in human trophoblast cells and villous explants from the third trimester of pregnancy
Thales Alves de Melo Fernandes, Samuel Cota Teixeira, Tássia Rafaela Costa, et al.
Microbes and Infection (2023) Vol. 25, Iss. 6, pp. 105123-105123
Open Access | Times Cited: 8

Unlocking the potential of snake venom-based molecules against the malaria, Chagas disease, and leishmaniasis triad
José R. Almeida, Ana Gomes, Bruno Mendes, et al.
International Journal of Biological Macromolecules (2023) Vol. 242, pp. 124745-124745
Open Access | Times Cited: 7

Viperidae snakes infected by mammalian-associated trypanosomatids and a free-living kinetoplastid
Wesley Arruda Gimenes Nantes, Sany Caroline Liberal, Filipe Martins Santos, et al.
Infection Genetics and Evolution (2024) Vol. 123, pp. 105630-105630
Open Access | Times Cited: 2

Oxidative stress induced by Pollonein-LAAO, a new L-amino acid oxidase from Bothrops moojeni venom, prompts prostate tumor spheroid cell death and impairs the cellular invasion process in vitro
Lorena Polloni, Tássia R. Costa, Lorena Pinheiro Morais, et al.
Cellular Signalling (2023) Vol. 109, pp. 110785-110785
Closed Access | Times Cited: 6

Antiprotozoal Effect of Snake Venoms and Their Fractions: A Systematic Review
Zainab Abdullahi, Salihu S. Musa, Daihai He, et al.
Pathogens (2021) Vol. 10, Iss. 12, pp. 1632-1632
Open Access | Times Cited: 13

Bothrops snake venom L-amino acid oxidases impair biofilm formation of clinically relevant bacteria
Thales Alves de Melo Fernandes, Tássia R. Costa, Ralciane de Paula Menezes, et al.
Toxicon (2023) Vol. 238, pp. 107569-107569
Closed Access | Times Cited: 4

The Potassium Channel Blocker β-Bungarotoxin from the Krait Bungarus multicinctus Venom Manifests Antiprotozoal Activity
Alexey V. Osipov, Е. Г. Черемных, Rustam Ziganshin, et al.
Biomedicines (2023) Vol. 11, Iss. 4, pp. 1115-1115
Open Access | Times Cited: 2

ئAntiparasitic activity of Cerastes cerastes venom on Schistosoma mansoni infected mice‏
Asmaa Mahdy, Osama Mostafa, Marwa Aboueldahab, et al.
Experimental Parasitology (2024), pp. 108866-108866
Closed Access

Biochemical characterization and assessment of leishmanicidal effects of a new L-amino acid oxidase from Crotalus durissus collilineatus snake venom (CollinLA AO-I)
Vitor de Freitas, Tássia R. Costa, Amanda Rodrigues Nogueira, et al.
Toxicon (2023) Vol. 230, pp. 107156-107156
Closed Access | Times Cited: 1

Page 1

Scroll to top