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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:

RIP kinases as modulators of inflammation and immunity
Sudan He, Xiaodong Wang
Nature Immunology (2018) Vol. 19, Iss. 9, pp. 912-922
Closed Access | Times Cited: 207

Showing 26-50 of 207 citing articles:

An overview of DNA-encoded libraries: A versatile tool for drug discovery
Daniel H. Madsen, Carlos Azevedo, Iolanda Micco, et al.
Progress in medicinal chemistry (2020), pp. 181-249
Closed Access | Times Cited: 67
Host Cell Death Responses to Non-typhoidal Salmonella Infection
Madeleine A. Wemyss, Jaclyn S. Pearson
Frontiers in Immunology (2019) Vol. 10
Open Access | Times Cited: 63
Genetic Regulation of RIPK1 and Necroptosis
Daichao Xu, Chengyu Zou, Junying Yuan
Annual Review of Genetics (2021) Vol. 55, Iss. 1, pp. 235-263
Open Access | Times Cited: 49
Caspase-8 auto-cleavage regulates programmed cell death and collaborates with RIPK3/MLKL to prevent lymphopenia
Xiao‐Ming Li, Fang Li, Xixi Zhang, et al.
Cell Death and Differentiation (2022) Vol. 29, Iss. 8, pp. 1500-1512
Open Access | Times Cited: 38
Osmotic stress activates RIPK3/MLKL-mediated necroptosis by increasing cytosolic pH through a plasma membrane Na + /H + exchanger
Wenbin Zhang, Weiliang Fan, Jia Guo, et al.
Science Signaling (2022) Vol. 15, Iss. 734
Closed Access | Times Cited: 35
Receptor-interacting protein kinase 2 (RIPK2) stabilizes c-Myc and is a therapeutic target in prostate cancer metastasis
Yiwu Yan, Bo Zhou, Qian Chen, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 34
The role of RHIM in necroptosis
Theresa Riebeling, Ulrich Kunzendorf, Stefan Krautwald
Biochemical Society Transactions (2022) Vol. 50, Iss. 4, pp. 1197-1205
Open Access | Times Cited: 31
The resurrection of RIP kinase 1 as an early cell death checkpoint regulator—a potential target for therapy in the necroptosis era
Eunjin Ju, Kyeong Ah Park, Han‐Ming Shen, et al.
Experimental & Molecular Medicine (2022) Vol. 54, Iss. 9, pp. 1401-1411
Open Access | Times Cited: 31
Receptor-interacting Protein Kinase 2 Is an Immunotherapy Target in Pancreatic Cancer
Wenhua Sang, Yiduo Zhou, Haiyan Chen, et al.
Cancer Discovery (2023) Vol. 14, Iss. 2, pp. 326-347
Closed Access | Times Cited: 22
HSPA8 acts as an amyloidase to suppress necroptosis by inhibiting and reversing functional amyloid formation
Erpeng Wu, Wenyan He, Chenlu Wu, et al.
Cell Research (2023) Vol. 33, Iss. 11, pp. 851-866
Open Access | Times Cited: 21
RIPK1 in the inflammatory response and sepsis: Recent advances, drug discovery and beyond
Xiaoyu Liu, A-Ling Tang, Jie Chen, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 20
Protein phosphorylation and kinases: Potential therapeutic targets in necroptosis
Yihui Shi, Chengkun Wu, Jiayi Shi, et al.
European Journal of Pharmacology (2024) Vol. 970, pp. 176508-176508
Closed Access | Times Cited: 8
FePd Nanozyme- and SKN-Encapsulated Functional Lipid Nanoparticles for Cancer Nanotherapy via ROS-Boosting Necroptosis
Wensheng Xie, Ying Li, Zhenhu Guo, et al.
ACS Applied Materials & Interfaces (2024) Vol. 16, Iss. 15, pp. 18411-18421
Closed Access | Times Cited: 7
Recognition of necroptosis: From molecular mechanisms to detection methods
Ting Zhu, Bowen Wu
Biomedicine & Pharmacotherapy (2024) Vol. 178, pp. 117196-117196
Open Access | Times Cited: 7
RIPK3-mediated inflammation is a conserved β cell response to ER stress
Bingyuan Yang, Lisette A. Maddison, Karolina E. Zaborska, et al.
Science Advances (2020) Vol. 6, Iss. 51
Open Access | Times Cited: 47
Pattern recognition receptors as potential drug targets in inflammatory disorders
Declan P. McKernan
Advances in protein chemistry and structural biology (2019), pp. 65-109
Closed Access | Times Cited: 46
SMAC mimetics and RIPK inhibitors as therapeutics for chronic inflammatory diseases
Simone Jensen, Jakob Benedict Seidelin, Eric C. LaCasse, et al.
Science Signaling (2020) Vol. 13, Iss. 619
Open Access | Times Cited: 46
A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase‐8
Hiroshi Ashida, Chihiro Sasakawa, Toshihiko Suzuki
The EMBO Journal (2020) Vol. 39, Iss. 17
Open Access | Times Cited: 45
The interplay of autophagy and non-apoptotic cell death pathways
Dannah Miller, Scott D. Cramer, Andrew Thorburn
International review of cell and molecular biology (2020), pp. 159-187
Open Access | Times Cited: 43
Influenza-Induced Oxidative Stress Sensitizes Lung Cells to Bacterial-Toxin-Mediated Necroptosis
Norberto González-Juarbe, Ashleigh N. Riegler, Alexander S. Jureka, et al.
Cell Reports (2020) Vol. 32, Iss. 8, pp. 108062-108062
Open Access | Times Cited: 43
RIPK2 NODs to XIAP and IBD
Joseph Topal, Mads Gyrd‐Hansen
Seminars in Cell and Developmental Biology (2020) Vol. 109, pp. 144-150
Closed Access | Times Cited: 41
Molecular mechanisms of necroptosis and relevance for neurodegenerative diseases
Pedro A. Dionísio, Joana D. Amaral, Cecília M. P. Rodrigues
International review of cell and molecular biology (2020), pp. 31-82
Closed Access | Times Cited: 40
IAP-Mediated Protein Ubiquitination in Regulating Cell Signaling
Baptiste Dumétier, Aymeric Zadoroznyj, Laurence Dubrez
Cells (2020) Vol. 9, Iss. 5, pp. 1118-1118
Open Access | Times Cited: 40
The latest information on the RIPK1 post-translational modifications and functions
Qiong Wang, Danping Fan, Ya Xia, et al.
Biomedicine & Pharmacotherapy (2021) Vol. 142, pp. 112082-112082
Open Access | Times Cited: 37
Pan-cancer analysis reveals RIPK2 predicts prognosis and promotes immune therapy resistance via triggering cytotoxic T lymphocytes dysfunction
Junquan Song, Runyu Yang, Rongyuan Wei, et al.
Molecular Medicine (2022) Vol. 28, Iss. 1
Open Access | Times Cited: 28

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