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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:

Functional divergence caused by mutations in an energetic hotspot in ERK2
C.A. Taylor th, Kevin W. Cormier, Shannon E. Keenan, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 31, pp. 15514-15523
Closed Access | Times Cited: 18

Showing 18 citing articles:

Navigating the ERK1/2 MAPK Cascade
Ana Martín-Vega, Melanie H. Cobb
Biomolecules (2023) Vol. 13, Iss. 10, pp. 1555-1555
Open Access | Times Cited: 43
ERK pathway agonism for cancer therapy: evidence, insights, and a target discovery framework
Oleg Timofeev, Philippe Giron, Steffen Lawo, et al.
npj Precision Oncology (2024) Vol. 8, Iss. 1
Open Access | Times Cited: 22
Development of small molecule extracellular signal-regulated kinases (ERKs) inhibitors for cancer therapy
Xiaoli Pan, Junping Pei, Aoxue Wang, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 12, Iss. 5, pp. 2171-2192
Open Access | Times Cited: 51
Interference with ERK-dimerization at the nucleocytosolic interface targets pathological ERK1/2 signaling without cardiotoxic side-effects
Angela Tomasovic, Theresa Brand, Constanze Schanbacher, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 52
Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required forToxoplasmaapical complex biogenesis
P. Back, William O’Shaughnessy, Andy S. Moon, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 22, pp. 12164-12173
Open Access | Times Cited: 49
Non-Canonical Caspase Activity Antagonizes p38 MAPK Stress-Priming Function to Support Development
Benjamin P. Weaver, Yi M. Weaver, Shizue Omi, et al.
Developmental Cell (2020) Vol. 53, Iss. 3, pp. 358-369.e6
Open Access | Times Cited: 34
Mutations That Confer Drug-Resistance, Oncogenicity and Intrinsic Activity on the ERK MAP Kinases—Current State of the Art
Karina Smorodinsky-Atias, Nadine Soudah, David Engelberg
Cells (2020) Vol. 9, Iss. 1, pp. 129-129
Open Access | Times Cited: 33
A Phosphorylated Intermediate in the Activation of WNK Kinases
Radha Akella, Mateusz Dróżdż, John M. Humphreys, et al.
Biochemistry (2020) Vol. 59, Iss. 18, pp. 1747-1755
Open Access | Times Cited: 21
Inference of Multisite Phosphorylation Rate Constants and Their Modulation by Pathogenic Mutations
Eyan Yeung, Sarah McFann, Lewis Marsh, et al.
Current Biology (2020) Vol. 30, Iss. 5, pp. 877-882.e6
Open Access | Times Cited: 19
Mutation in the Common Docking Domain Affects MAP Kinase ERK2 Catalysis and Stability
Leonore Novak, Maria Petrosino, Alessandra Pasquo, et al.
Cancers (2023) Vol. 15, Iss. 11, pp. 2938-2938
Open Access | Times Cited: 4
Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases
Jaylissa Torres Robles, Hua Jane Lou, Guangda Shi, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 48
Open Access | Times Cited: 4
Molecular mechanisms underlying cellular effects of human MEK1 mutations
Robert A. Marmion, Liu Yang, Yogesh Goyal, et al.
Molecular Biology of the Cell (2021) Vol. 32, Iss. 9, pp. 974-983
Open Access | Times Cited: 9
Algebra, Geometry and Topology of ERK Kinetics
Lewis Marsh, Emilie Dufresne, Helen M. Byrne, et al.
Bulletin of Mathematical Biology (2022) Vol. 84, Iss. 12
Open Access | Times Cited: 6
Disruptor: Computational identification of oncogenic mutants disrupting protein-protein and protein-DNA interactions
Valentina Kugler, Andreas Lieb, Nathan Guerin, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 3
Protein dynamics analysis identifies candidate cancer driver genes and mutations inTCGAdata
Jan Fehmi Sayılgan, Türkan Haliloğlu, Mehmet Gönen
Proteins Structure Function and Bioinformatics (2021) Vol. 89, Iss. 6, pp. 721-730
Closed Access | Times Cited: 7
Cancer Mutations: Molecular MEKanisms
Lee Bardwell
Current Biology (2020) Vol. 30, Iss. 5, pp. R222-R224
Open Access | Times Cited: 4
Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required for Toxoplasma apical complex biogenesis
P. Back, William O’Shaughnessy, Andy S. Moon, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 1
A Toolbox of Structural Biology and Enzyme Kinetics Reveals the Case for ERK Docking Site Inhibition
Rachel M. Sammons, Kevin N. Dalby
Springer eBooks (2020), pp. 109-139
Closed Access
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