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:

Potent and selective chemical probe of hypoxic signalling downstream of HIF-α hydroxylation via VHL inhibition
Julianty Frost, Carles Galdeano, Pedro Soares, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 200

Showing 1-25 of 200 citing articles:

Structural basis of PROTAC cooperative recognition for selective protein degradation
Morgan S. Gadd, Andrea Testa, Xavier Lucas, et al.
Nature Chemical Biology (2017) Vol. 13, Iss. 5, pp. 514-521
Open Access | Times Cited: 979

Proteolysis-Targeting Chimeras as Therapeutics and Tools for Biological Discovery
George M. Burslem, Craig M. Crews
Cell (2020) Vol. 181, Iss. 1, pp. 102-114
Open Access | Times Cited: 780

PROteolysis TArgeting Chimeras (PROTACs) — Past, present and future
Mariell Pettersson, Craig M. Crews
Drug Discovery Today Technologies (2019) Vol. 31, pp. 15-27
Open Access | Times Cited: 601

PROTACs: past, present and future
Ke Li, Craig M. Crews
Chemical Society Reviews (2022) Vol. 51, Iss. 12, pp. 5214-5236
Open Access | Times Cited: 426

CRISPR-Mediated Tagging of Endogenous Proteins with a Luminescent Peptide
Marie K. Schwinn, Thomas Machleidt, Kris Zimmerman, et al.
ACS Chemical Biology (2017) Vol. 13, Iss. 2, pp. 467-474
Open Access | Times Cited: 351

Discovery of ARD-69 as a Highly Potent Proteolysis Targeting Chimera (PROTAC) Degrader of Androgen Receptor (AR) for the Treatment of Prostate Cancer
Xin Han, Chao Wang, Chong Qin, et al.
Journal of Medicinal Chemistry (2019) Vol. 62, Iss. 2, pp. 941-964
Closed Access | Times Cited: 334

Hypoxia induces rapid changes to histone methylation and reprograms chromatin
Michael Batie, Julianty Frost, Mark Frost, et al.
Science (2019) Vol. 363, Iss. 6432, pp. 1222-1226
Open Access | Times Cited: 326

Quantitative Live-Cell Kinetic Degradation and Mechanistic Profiling of PROTAC Mode of Action
Kristin M. Riching, Sarah D. Mahan, Cesear Corona, et al.
ACS Chemical Biology (2018) Vol. 13, Iss. 9, pp. 2758-2770
Open Access | Times Cited: 266

Extracellular vesicle-loaded hydrogels for tissue repair and regeneration
Yikun Ju, Yue Hu, Yang Pu, et al.
Materials Today Bio (2022) Vol. 18, pp. 100522-100522
Open Access | Times Cited: 259

Small-Molecule Modulation of Protein Homeostasis
George M. Burslem, Craig M. Crews
Chemical Reviews (2017) Vol. 117, Iss. 17, pp. 11269-11301
Closed Access | Times Cited: 255

Degradation of proteins by PROTACs and other strategies
Yang Wang, Xueyang Jiang, Feng Feng, et al.
Acta Pharmaceutica Sinica B (2019) Vol. 10, Iss. 2, pp. 207-238
Open Access | Times Cited: 255

E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones
Tasuku Ishida, Alessio Ciulli
SLAS DISCOVERY (2020) Vol. 26, Iss. 4, pp. 484-502
Open Access | Times Cited: 255

Inhibitors of protein–protein interactions (PPIs): an analysis of scaffold choices and buried surface area
Ran Xu, Jason E. Gestwicki
Current Opinion in Chemical Biology (2018) Vol. 44, pp. 75-86
Open Access | Times Cited: 233

Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation
Chiara Maniaci, Scott J. Hughes, Andrea Testa, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 215

Molecular recognition of ternary complexes: a new dimension in the structure-guided design of chemical degraders
Scott J. Hughes, Alessio Ciulli
Essays in Biochemistry (2017) Vol. 61, Iss. 5, pp. 505-516
Open Access | Times Cited: 214

Trivalent PROTACs enhance protein degradation via combined avidity and cooperativity
Satomi Imaide, Kristin M. Riching, Nikolai Makukhin, et al.
Nature Chemical Biology (2021) Vol. 17, Iss. 11, pp. 1157-1167
Open Access | Times Cited: 176

Proteolysis‐targeting chimeras in drug development: A safety perspective
Kévin Moreau, Muireann Coen, Andrew X. Zhang, et al.
British Journal of Pharmacology (2020) Vol. 177, Iss. 8, pp. 1709-1718
Open Access | Times Cited: 164

Proteolysis targeting chimeras (PROTACs) come of age: entering the third decade of targeted protein degradation
Michael J. Bond, Craig M. Crews
RSC Chemical Biology (2021) Vol. 2, Iss. 3, pp. 725-742
Open Access | Times Cited: 162

A small molecule HIF-1α stabilizer that accelerates diabetic wound healing
Guodong Li, Chung-Nga Ko, Dan Li, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 159

Recent Developments in PROTAC‐Mediated Protein Degradation: From Bench to Clinic
Zhenyi Hu, Craig M. Crews
ChemBioChem (2021) Vol. 23, Iss. 2
Open Access | Times Cited: 159

Degradation of Polycomb Repressive Complex 2 with an EED-Targeted Bivalent Chemical Degrader
Frances Potjewyd, Anne‐Marie W. Turner, Joshua Beri, et al.
Cell chemical biology (2019) Vol. 27, Iss. 1, pp. 47-56.e15
Open Access | Times Cited: 152

Discovery of Potent and Selective Epidermal Growth Factor Receptor (EGFR) Bifunctional Small-Molecule Degraders
Meng Cheng, Xufen Yu, Kaylene Lu, et al.
Journal of Medicinal Chemistry (2020) Vol. 63, Iss. 3, pp. 1216-1232
Open Access | Times Cited: 151

VH298-loaded extracellular vesicles released from gelatin methacryloyl hydrogel facilitate diabetic wound healing by HIF-1α-mediated enhancement of angiogenesis
Yaxi Wang, Zhen Cao, Wei Qian, et al.
Acta Biomaterialia (2022) Vol. 147, pp. 342-355
Closed Access | Times Cited: 144

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