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OpenAlex Citation Counts

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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:

eIF4E‐homologous protein (4EHP): a multifarious cap‐binding protein
Mary Christie, Cátia Igreja
FEBS Journal (2021) Vol. 290, Iss. 2, pp. 266-285
Open Access | Times Cited: 21

Showing 21 citing articles:

The molecular basis of translation initiation and its regulation in eukaryotes
Jailson Brito Querido, Irene Díaz‐López, V. Ramakrishnan
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 168-186
Closed Access | Times Cited: 87
RNA modifications in cancer
Qiling Tang, Lvyuan Li, Yumin Wang, et al.
British Journal of Cancer (2023) Vol. 129, Iss. 2, pp. 204-221
Open Access | Times Cited: 68
SARS-CoV-2 impairs interferon production via NSP2-induced repression of mRNA translation
Xu Zhang, Jung‐Hyun Choi, David L. Dai, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 32
Open Access | Times Cited: 60
The nexus between RNA-binding proteins and their effectors
Shiyang He, Eugene Valkov, Sihem Cheloufi, et al.
Nature Reviews Genetics (2022) Vol. 24, Iss. 5, pp. 276-294
Open Access | Times Cited: 54
Cytoplasmic mRNA decay and quality control machineries in eukaryotes
Megan E. Dowdle, Jens Lykke‐Andersen
Nature Reviews Genetics (2025)
Closed Access | Times Cited: 1
The SARS-CoV-2 protein NSP2 impairs the silencing capacity of the human 4EHP-GIGYF2 complex
Limei Zou, Clara Moch, Marc Graille, et al.
iScience (2022) Vol. 25, Iss. 7, pp. 104646-104646
Open Access | Times Cited: 24
Non-canonical mRNA translation initiation in cell stress and cancer
Mélanie Mahé, Tiffany J. Rios-Fuller, Olga Katsara, et al.
NAR Cancer (2024) Vol. 6, Iss. 2
Open Access | Times Cited: 5
Plant eIF4E isoforms as factors of susceptibility and resistance to potyviruses
Nikolay Zlobin, Vasiliy Taranov
Frontiers in Plant Science (2023) Vol. 14
Open Access | Times Cited: 11
The Proteins Diversity of the eIF4E Family in the eIF4F Complex
Viktoriya V Kolesnikova, Oleg Nikonov, Tien Do Phat, et al.
Biochemistry (Moscow) (2025) Vol. 90, Iss. S1, pp. S60-S85
Closed Access
The Unified Theory of Neurodegeneration Pathogenesis Based on Axon Deamidation
Daniel P. Joseph
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 9, pp. 4143-4143
Open Access
eIF4EHP promotes Ldh mRNA translation in and fruit fly adaptation to hypoxia
Manfei Liang, Clara Hody, Vanessa Yammine, et al.
EMBO Reports (2023) Vol. 24, Iss. 7
Open Access | Times Cited: 6
eIF4E as a molecular wildcard in metazoans RNA metabolism
Greco Hernández, Paula Vázquez‐Pianzola
Biological reviews/Biological reviews of the Cambridge Philosophical Society (2023) Vol. 98, Iss. 6, pp. 2284-2306
Closed Access | Times Cited: 6
Relationship Between Sphingomyelin and Risk of Alzheimer’s Disease: A Bidirectional Mendelian Randomization Study
Haohao Zhu, Rongrong Lu, Qin Zhou, et al.
Journal of Alzheimer s Disease Reports (2023) Vol. 7, Iss. 1, pp. 1289-1297
Open Access | Times Cited: 5
Drosophila Me31B is a Dual eIF4E-Interacting Protein
Carla Layana, Emiliano Salvador Vilardo, Gonzalo Corujo, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 5, pp. 167949-167949
Open Access | Times Cited: 4
eIF4E plays the role of a pathogenic gene in psoriasis, and the inhibition of eIF4E phosphorylation ameliorates psoriasis‐like skin damage
Ruijie Wang, Luan Yang, Yunyue Zhen, et al.
Experimental Dermatology (2024) Vol. 33, Iss. 1
Closed Access | Times Cited: 1
Two germ granule eIF4E isoforms reside in different mRNPs to hand offC elegansmRNAs from translational repression to activation
Gita Gajjar, Hayden P. Huggins, Eun Suk Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
C8ORF88: A Novel eIF4E-Binding Protein
Lauren Pugsley, Sai Kiran Naineni, Mehdi Amiri, et al.
Genes (2023) Vol. 14, Iss. 11, pp. 2076-2076
Open Access | Times Cited: 1
Analysis of eIF4E-family members in Fungi contributes to their classification in eukaryotes
Greco Hernández, Daniela Ross‐Kaschitza, Gabriel Moreno‐Hagelsieb, et al.
Journal of Biological Chemistry (2024), pp. 108129-108129
Open Access
SARS-CoV-2 impairs interferon production via NSP2-induced repression of mRNA translation
Jung‐Hyun Choi, Xu Zhang, Christine Zhang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
The SARS-CoV-2 protein NSP2 impairs the microRNA-induced silencing capacity of human cells
Limei Zou, Clara Moch, Marc Graille, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
Drosophila cap-binding protein eiF4EHP promotes translation via a 3’UTR-dependent mechanism under hypoxia and contributes to fruit fly adaptation to oxygen variations
Manfei Liang, Clara Hody, Vanessa Yammine, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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