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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:

Genomics and evolution of protein phosphatases
Jinan Chen, Jack E. Dixon, Gerard Manning
Science Signaling (2017) Vol. 10, Iss. 474
Closed Access | Times Cited: 270

Showing 1-25 of 270 citing articles:

SubCellBarCode: Proteome-wide Mapping of Protein Localization and Relocalization
Lukas M. Orre, Mattias Vesterlund, Yanbo Pan, et al.
Molecular Cell (2019) Vol. 73, Iss. 1, pp. 166-182.e7
Open Access | Times Cited: 191
Coordination between Two Branches of the Unfolded Protein Response Determines Apoptotic Cell Fate
Tsun-Kai Chang, David A. Lawrence, Min Lu, et al.
Molecular Cell (2018) Vol. 71, Iss. 4, pp. 629-636.e5
Open Access | Times Cited: 169
Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates
David L. Brautigan, Shirish Shenolikar
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 921-964
Closed Access | Times Cited: 163
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Qian Zhong, Xina Xiao, Yijie Qiu, et al.
MedComm (2023) Vol. 4, Iss. 3
Open Access | Times Cited: 124
Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders
Stephanie M. Stanford, Nunzio Bottini
Nature Reviews Drug Discovery (2023) Vol. 22, Iss. 4, pp. 273-294
Open Access | Times Cited: 72
The intrinsic substrate specificity of the human tyrosine kinome
Tomer M. Yaron, Brian A. Joughin, Emily M. Huntsman, et al.
Nature (2024) Vol. 629, Iss. 8014, pp. 1174-1181
Open Access | Times Cited: 40
Defining the KRAS- and ERK-dependent transcriptome in KRAS-mutant cancers
Jeffrey A. Klomp, Jennifer E. Klomp, Clint A. Stalnecker, et al.
Science (2024) Vol. 384, Iss. 6700
Open Access | Times Cited: 35
Determining the ERK-regulated phosphoproteome driving KRAS-mutant cancer
Jennifer E. Klomp, J. Nathaniel Diehl, Jeffrey A. Klomp, et al.
Science (2024) Vol. 384, Iss. 6700
Open Access | Times Cited: 21
New Perspectives, Opportunities, and Challenges in Exploring the Human Protein Kinome
Leah Wilson, Adam J. Linley, Dean E. Hammond, et al.
Cancer Research (2017) Vol. 78, Iss. 1, pp. 15-29
Open Access | Times Cited: 145
PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins
Kerryn Berndsen, Paweł Lis, Wondwossen M Yeshaw, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 115
Turn and Face the Strange: A New View on Phosphatases
Maja Köhn
ACS Central Science (2020) Vol. 6, Iss. 4, pp. 467-477
Open Access | Times Cited: 109
Tracing the origin and evolution of pseudokinases across the tree of life
Annie Kwon, Steven Thomas Scott, Rahil Taujale, et al.
Science Signaling (2019) Vol. 12, Iss. 578
Open Access | Times Cited: 106
Protein phosphatases in the regulation of mitosis
Jakob Nilsson
The Journal of Cell Biology (2018) Vol. 218, Iss. 2, pp. 395-409
Open Access | Times Cited: 101
Live and let die: insights into pseudoenzyme mechanisms from structure
James M. Murphy, Peter D. Mace, Patrick A. Eyers
Current Opinion in Structural Biology (2017) Vol. 47, pp. 95-104
Closed Access | Times Cited: 94
Metal-dependent Ser/Thr protein phosphatase PPM family: Evolution, structures, diseases and inhibitors
Rui Kamada, Fuki Kudoh, Shogo Ito, et al.
Pharmacology & Therapeutics (2020) Vol. 215, pp. 107622-107622
Closed Access | Times Cited: 91
Emerging concepts in pseudoenzyme classification, evolution, and signaling
António J. M. Ribeiro, Sayoni Das, Natalie L. Dawson, et al.
Science Signaling (2019) Vol. 12, Iss. 594
Closed Access | Times Cited: 88
Effects of the NO/soluble guanylate cyclase/cGMP system on the functions of human platelets
Stephanie Makhoul, Elena Walter, Oliver Pagel, et al.
Nitric Oxide (2018) Vol. 76, pp. 71-80
Closed Access | Times Cited: 87
Phosphatases in Mitosis: Roles and Regulation
Margarida Moura, Carlos Conde
Biomolecules (2019) Vol. 9, Iss. 2, pp. 55-55
Open Access | Times Cited: 86
WIDENING THE BOTTLENECK OF PHOSPHOPROTEOMICS: EVOLVING STRATEGIES FOR PHOSPHOPEPTIDE ENRICHMENT
Teck Yew Low, M. Aiman Mohtar, Pey Yee Lee, et al.
Mass Spectrometry Reviews (2020) Vol. 40, Iss. 4, pp. 309-333
Closed Access | Times Cited: 82
Time-resolved proteomics profiling of the ciliary Hedgehog response
Elena A. May, Marian Kalocsay, Inès Galtier D’Auriac, et al.
The Journal of Cell Biology (2021) Vol. 220, Iss. 5
Open Access | Times Cited: 74
Dual Proteome-scale Networks Reveal Cell-specific Remodeling of the Human Interactome
Edward L. Huttlin, Raphael J. Bruckner, Jose Navarrete‐Perea, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 72
Protein phosphatases in the RNAPII transcription cycle: erasers, sculptors, gatekeepers, and potential drug targets
Giacomo Cossa, Pabitra K. Parua, Martin Eilers, et al.
Genes & Development (2021) Vol. 35, Iss. 9-10, pp. 658-676
Open Access | Times Cited: 59
Demystifying the O-GlcNAc Code: A Systems View
Junfeng Ma, Chunyan Hou, Ci Wu
Chemical Reviews (2022) Vol. 122, Iss. 20, pp. 15822-15864
Closed Access | Times Cited: 58
Targeted protein posttranslational modifications by chemically induced proximity for cancer therapy
Yunhua Peng, Jing Liu, Hiroyuki Inuzuka, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 4, pp. 104572-104572
Open Access | Times Cited: 32
Substrate and phosphorylation site selection by phosphoprotein phosphatases
Hieu Nguyen, Arminja N. Kettenbach
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 8, pp. 713-725
Open Access | Times Cited: 25
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