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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:

Modulators of Protein–Protein Interactions
L.‐G. Milroy, Tom N. Grossmann, Sven Hennig, et al.
Chemical Reviews (2014) Vol. 114, Iss. 9, pp. 4695-4748
Open Access | Times Cited: 453

Showing 1-25 of 453 citing articles:

Natural Products as Sources of New Drugs from 1981 to 2014
David Newman, Gordon M. Cragg
Journal of Natural Products (2016) Vol. 79, Iss. 3, pp. 629-661
Open Access | Times Cited: 5360
Trends in peptide drug discovery
Markus Muttenthaler, Glenn F. King, David J. Adams, et al.
Nature Reviews Drug Discovery (2021) Vol. 20, Iss. 4, pp. 309-325
Closed Access | Times Cited: 1294
Therapeutic peptides: current applications and future directions
Lei Wang, Nanxi Wang, Wenping Zhang, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 1123
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Michelle R. Arkin, Yinyan Tang, James A. Wells
Chemistry & Biology (2014) Vol. 21, Iss. 9, pp. 1102-1114
Open Access | Times Cited: 955
Lessons in PROTAC Design from Selective Degradation with a Promiscuous Warhead
Daniel P. Bondeson, Blake E. Smith, George M. Burslem, et al.
Cell chemical biology (2017) Vol. 25, Iss. 1, pp. 78-87.e5
Open Access | Times Cited: 737
Structure‐Based Design of Inhibitors of Protein–Protein Interactions: Mimicking Peptide Binding Epitopes
Marta Pelay‐Gimeno, Adrian Glas, Oliver Koch, et al.
Angewandte Chemie International Edition (2015) Vol. 54, Iss. 31, pp. 8896-8927
Open Access | Times Cited: 635
Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials
Haiying Lu, Qiaodan Zhou, Jun He, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 624
Protein Assembly: Versatile Approaches to Construct Highly Ordered Nanostructures
Quan Luo, Chunxi Hou, Yushi Bai, et al.
Chemical Reviews (2016) Vol. 116, Iss. 22, pp. 13571-13632
Closed Access | Times Cited: 506
Structural basis of lenalidomide-induced CK1α degradation by the CRL4CRBN ubiquitin ligase
Georg Petzold, Eric S. Fischer, Nicolas H. Thomä
Nature (2016) Vol. 532, Iss. 7597, pp. 127-130
Closed Access | Times Cited: 487
A Map of Protein-Metabolite Interactions Reveals Principles of Chemical Communication
Ilaria Piazza, Karl Kochanowski, Valentina Cappelletti, et al.
Cell (2018) Vol. 172, Iss. 1-2, pp. 358-372.e23
Open Access | Times Cited: 460
Hydrocarbon Stapled Peptides as Modulators of Biological Function
Philipp M. Cromm, Jochen Spiegel, Tom N. Grossmann
ACS Chemical Biology (2015) Vol. 10, Iss. 6, pp. 1362-1375
Closed Access | Times Cited: 282
Late-Stage Diversification of Natural Products
Benke Hong, Tuoping Luo, Xiaoguang Lei
ACS Central Science (2020) Vol. 6, Iss. 5, pp. 622-635
Open Access | Times Cited: 274
Modulating protein–protein interactions: the potential of peptides
Laura Nevola, Ernest Giralt
Chemical Communications (2014) Vol. 51, Iss. 16, pp. 3302-3315
Closed Access | Times Cited: 273
Modulators of 14-3-3 Protein–Protein Interactions
Loes M. Stevers, Eline Sijbesma, Maurizio Botta, et al.
Journal of Medicinal Chemistry (2017) Vol. 61, Iss. 9, pp. 3755-3778
Open Access | Times Cited: 256
Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP
Sindhuja Sridharan, Nils Kurzawa, Thilo Werner, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 237
Molecularly Imprinted Polymers for Cell Recognition
Stanislav S. Piletsky, Francesco Canfarotta, Alessandro Poma, et al.
Trends in biotechnology (2019) Vol. 38, Iss. 4, pp. 368-387
Open Access | Times Cited: 223
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: 211
Protein Assembly by Design
Jie Zhu, Nicole Avakyan, A. Kakkis, et al.
Chemical Reviews (2021) Vol. 121, Iss. 22, pp. 13701-13796
Open Access | Times Cited: 195
Supramolecular Chemistry Targeting Proteins
Sam van Dun, Christian Ottmann, L.‐G. Milroy, et al.
Journal of the American Chemical Society (2017) Vol. 139, Iss. 40, pp. 13960-13968
Open Access | Times Cited: 188
Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view
Shaoyong Lu, Hyunbum Jang, Shuo Gu, et al.
Chemical Society Reviews (2016) Vol. 45, Iss. 18, pp. 4929-4952
Open Access | Times Cited: 172
Systematic Targeting of Protein–Protein Interactions
Ashley E. Modell, Sarah L. Blosser, Paramjit S. Arora
Trends in Pharmacological Sciences (2016) Vol. 37, Iss. 8, pp. 702-713
Open Access | Times Cited: 168
Small-Molecule Inhibitors of the Coronavirus Spike: ACE2 Protein–Protein Interaction as Blockers of Viral Attachment and Entry for SARS-CoV-2
Damir Bojadzic, Óscar Garnica, Jinshui Chen, et al.
ACS Infectious Diseases (2021) Vol. 7, Iss. 6, pp. 1519-1534
Open Access | Times Cited: 122
Rational Design of Peptide-Based Inhibitors Disrupting Protein-Protein Interactions
Xuefei Wang, Duan Ni, Yaqin Liu, et al.
Frontiers in Chemistry (2021) Vol. 9
Open Access | Times Cited: 107
Chasing molecular glue degraders: screening approaches
Ana Domostegui, Luis Nieto‐Barrado, Carles Perez‐Lopez, et al.
Chemical Society Reviews (2022) Vol. 51, Iss. 13, pp. 5498-5517
Open Access | Times Cited: 100
Metabolite interactions between host and microbiota during health and disease: Which feeds the other?
Yan Zhang, Rui Chen, DuoDuo Zhang, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 160, pp. 114295-114295
Open Access | Times Cited: 66
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