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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:

Scalable molecular dynamics on CPU and GPU architectures with NAMD
J. C. Phillips, David J. Hardy, Julio D. C. Maia, et al.
The Journal of Chemical Physics (2020) Vol. 153, Iss. 4
Open Access | Times Cited: 2398

Showing 1-25 of 2398 citing articles:

LAMMPS - a flexible simulation tool for particle-based materials modeling at the atomic, meso, and continuum scales
Aidan P. Thompson, Hasan Metin Aktulga, Richard A. Berger, et al.
Computer Physics Communications (2021) Vol. 271, pp. 108171-108171
Open Access | Times Cited: 6683
Software for the frontiers of quantum chemistry: An overview of developments in the Q-Chem 5 package
Evgeny Epifanovsky, Andrew T. B. Gilbert, Xintian Feng, et al.
The Journal of Chemical Physics (2021) Vol. 155, Iss. 8
Open Access | Times Cited: 917
Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development
Outi M. H. Salo‐Ahen, Ida Alanko, Rajendra Bhadane, et al.
Processes (2020) Vol. 9, Iss. 1, pp. 71-71
Open Access | Times Cited: 373
Multiple rereads of single proteins at single–amino acid resolution using nanopores
Henry Brinkerhoff, Albert S. W. Kang, Jingqian Liu, et al.
Science (2021) Vol. 374, Iss. 6574, pp. 1509-1513
Open Access | Times Cited: 330
SARS-CoV-2 escapein vitrofrom a highly neutralizing COVID-19 convalescent plasma
Emanuele Andreano, Giulia Piccini, Danilo Licastro, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 277
Identification of 3-chymotrypsin like protease (3CLPro) inhibitors as potential anti-SARS-CoV-2 agents
Vicky Mody, Joanna Ho, Savannah Wills, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 219
The transformational role of GPU computing and deep learning in drug discovery
Mohit Pandey, Michael Fernández, Francesco Gentile, et al.
Nature Machine Intelligence (2022) Vol. 4, Iss. 3, pp. 211-221
Open Access | Times Cited: 178
Two decades of Martini: Better beads, broader scope
‪Siewert J. Marrink, Luca Monticelli, Manuel N. Melo, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 164
AI-driven multiscale simulations illuminate mechanisms of SARS-CoV-2 spike dynamics
Lorenzo Casalino, Abigail C. Dommer, Zied Gaieb, et al.
The International Journal of High Performance Computing Applications (2021) Vol. 35, Iss. 5, pp. 432-451
Open Access | Times Cited: 145
ChAdOx1 interacts with CAR and PF4 with implications for thrombosis with thrombocytopenia syndrome
Alexander T. Baker, Ryan J. Boyd, Daipayan Sarkar, et al.
Science Advances (2021) Vol. 7, Iss. 49
Open Access | Times Cited: 144
Molecular dynamics simulation of the interaction of food proteins with small molecules
Xia Hu, Zhen Zeng, Jing Zhang, et al.
Food Chemistry (2022) Vol. 405, pp. 134824-134824
Closed Access | Times Cited: 139
Transmissible SARS-CoV-2 variants with resistance to clinical protease inhibitors
Seyed Arad Moghadasi, Emmanuel Heilmann, Ahmed Magdy Khalil, et al.
Science Advances (2023) Vol. 9, Iss. 13
Open Access | Times Cited: 132
Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoN
Nicholas H. Moeller, Ke Shi, Özlem Demir, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 9
Open Access | Times Cited: 125
Cadmium in food: Source, distribution and removal
Ruoyu Wang, Panting Sang, Yahui Guo, et al.
Food Chemistry (2022) Vol. 405, pp. 134666-134666
Closed Access | Times Cited: 125
Visualizing translation dynamics at atomic detail inside a bacterial cell
Liang Xue, Swantje Lenz, Maria Zimmermann‐Kogadeeva, et al.
Nature (2022) Vol. 610, Iss. 7930, pp. 205-211
Open Access | Times Cited: 121
A Guide to In Silico Drug Design
Yiqun Chang, Bryson A. Hawkins, Jonathan J. Du, et al.
Pharmaceutics (2022) Vol. 15, Iss. 1, pp. 49-49
Open Access | Times Cited: 121
Application advances of deep learning methods for de novo drug design and molecular dynamics simulation
Qifeng Bai, Shuo Liu, Yanan Tian, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2021) Vol. 12, Iss. 3
Closed Access | Times Cited: 109
Accurate determination of protein:ligand standard binding free energies from molecular dynamics simulations
Haohao Fu, Haochuan Chen, Marharyta Blazhynska, et al.
Nature Protocols (2022) Vol. 17, Iss. 4, pp. 1114-1141
Open Access | Times Cited: 108
Structures of the TMC-1 complex illuminate mechanosensory transduction
Hanbin Jeong, Sarah Clark, April Goehring, et al.
Nature (2022) Vol. 610, Iss. 7933, pp. 796-803
Open Access | Times Cited: 105
Using molecular docking and molecular dynamics to investigate protein-ligand interactions
Connor J. Morris, Dennis Della Corte
Modern Physics Letters B (2021) Vol. 35, Iss. 08, pp. 2130002-2130002
Closed Access | Times Cited: 104
Structure of the Shaker Kv channel and mechanism of slow C-type inactivation
Xiao-Feng Tan, Chanhyung Bae, Robyn Stix, et al.
Science Advances (2022) Vol. 8, Iss. 11
Open Access | Times Cited: 87
Unidirectional single-file transport of full-length proteins through a nanopore
Luning Yu, Xinqi Kang, Fanjun Li, et al.
Nature Biotechnology (2023) Vol. 41, Iss. 8, pp. 1130-1139
Open Access | Times Cited: 82
Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7
Luke S. Ferro, Qianglin Fang, Lisa Eshun-Wilson, et al.
Science (2022) Vol. 375, Iss. 6578, pp. 326-331
Open Access | Times Cited: 81
In situ architecture of the ER–mitochondria encounter structure
Michael R. Wozny, Andrea Di Luca, Dustin R. Morado, et al.
Nature (2023) Vol. 618, Iss. 7963, pp. 188-192
Open Access | Times Cited: 72
Bioinformatics approaches to discovering food-derived bioactive peptides: Reviews and perspectives
Zhenjiao Du, Jeffrey Comer, Yonghui Li
TrAC Trends in Analytical Chemistry (2023) Vol. 162, pp. 117051-117051
Open Access | Times Cited: 69
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