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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:

Protocols for Molecular Modeling with Rosetta3 and RosettaScripts
Brian J. Bender, Alberto Cisneros, Amanda M. Duran, et al.
Biochemistry (2016) Vol. 55, Iss. 34, pp. 4748-4763
Open Access | Times Cited: 204

Showing 1-25 of 204 citing articles:

Ultrafast neuronal imaging of dopamine dynamics with designed genetically encoded sensors
Tommaso Patriarchi, Jounhong Ryan Cho, Katharina Merten, et al.
Science (2018) Vol. 360, Iss. 6396
Open Access | Times Cited: 973
Macromolecular modeling and design in Rosetta: recent methods and frameworks
Julia Koehler Leman, Brian D. Weitzner, Steven M. Lewis, et al.
Nature Methods (2020) Vol. 17, Iss. 7, pp. 665-680
Open Access | Times Cited: 710
A practical guide to large-scale docking
Brian J. Bender, Stefan Gahbauer, Andreas Luttens, et al.
Nature Protocols (2021) Vol. 16, Iss. 10, pp. 4799-4832
Open Access | Times Cited: 383
Cryo-electron microscopy for structural analysis of dynamic biological macromolecules
Kazuyoshi Murata, Matthias Wolf
Biochimica et Biophysica Acta (BBA) - General Subjects (2017) Vol. 1862, Iss. 2, pp. 324-334
Open Access | Times Cited: 294
An expanded palette of dopamine sensors for multiplex imaging in vivo
Tommaso Patriarchi, Ali Mohebi, Junqing Sun, et al.
Nature Methods (2020) Vol. 17, Iss. 11, pp. 1147-1155
Open Access | Times Cited: 191
Deep learning extends de novo protein modelling coverage of genomes using iteratively predicted structural constraints
Joe G. Greener, Shaun M. Kandathil, David T. Jones
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 184
Directed Evolution of a Selective and Sensitive Serotonin Sensor via Machine Learning
Elizabeth K. Unger, Jacob P. Keller, Michael Altermatt, et al.
Cell (2020) Vol. 183, Iss. 7, pp. 1986-2002.e26
Open Access | Times Cited: 150
Structural basis of ligand binding modes at the neuropeptide Y Y1 receptor
Zhenlin Yang, Shuo Han, Max Keller, et al.
Nature (2018) Vol. 556, Iss. 7702, pp. 520-524
Open Access | Times Cited: 127
Predicting changes in protein thermodynamic stability upon point mutation with deep 3D convolutional neural networks
Bian Li, Yucheng Yang, John A. Capra, et al.
PLoS Computational Biology (2020) Vol. 16, Iss. 11, pp. e1008291-e1008291
Open Access | Times Cited: 109
Pharmacological evaluation of new constituents of “Spice”: synthetic cannabinoids based on indole, indazole, benzimidazole and carbazole scaffolds
Clara T. Schoeder, Cornelius Heß, Burkhard Madea, et al.
Forensic Toxicology (2018) Vol. 36, Iss. 2, pp. 385-403
Open Access | Times Cited: 108
On-target Resistance to the Mutant-Selective EGFR Inhibitor Osimertinib Can Develop in an Allele-Specific Manner Dependent on the Original EGFR-Activating Mutation
Benjamin P. Brown, Yunkai Zhang, David Westover, et al.
Clinical Cancer Research (2019) Vol. 25, Iss. 11, pp. 3341-3351
Open Access | Times Cited: 98
Structural basis for antiarrhythmic drug interactions with the human cardiac sodium channel
Phuong T. Nguyen, Kevin R. DeMarco, Igor Vorobyov, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 8, pp. 2945-2954
Open Access | Times Cited: 97
Protein engineering: the potential of remote mutations
Matthew Wilding, Nansook Hong, Matthew A. Spence, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 701-711
Open Access | Times Cited: 86
De novo metalloprotein design
Matthew J. Chalkley, Samuel I. Mann, William F. DeGrado
Nature Reviews Chemistry (2021) Vol. 6, Iss. 1, pp. 31-50
Open Access | Times Cited: 84
Co-occurring gain-of-function mutations in HER2 and HER3 modulate HER2/HER3 activation, oncogenesis, and HER2 inhibitor sensitivity
Ariella B. Hanker, Benjamin P. Brown, Jens Meiler, et al.
Cancer Cell (2021) Vol. 39, Iss. 8, pp. 1099-1114.e8
Open Access | Times Cited: 68
Hierarchical Materials from High Information Content Macromolecular Building Blocks: Construction, Dynamic Interventions, and Prediction
Li Shao, Jinrong Ma, Jesse L. Prelesnik, et al.
Chemical Reviews (2022) Vol. 122, Iss. 24, pp. 17397-17478
Open Access | Times Cited: 46
Recent Advances in NMR Protein Structure Prediction with ROSETTA
Julia Koehler Leman, Georg Künze
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 9, pp. 7835-7835
Open Access | Times Cited: 23
Unlocking the potential of enzyme engineering via rational computational design strategies
Lei Zhou, Chunmeng Tao, Xiaolin Shen, et al.
Biotechnology Advances (2024) Vol. 73, pp. 108376-108376
Closed Access | Times Cited: 15
Web-accessible molecular modeling with Rosetta: The Rosetta Online Server that Includes Everyone (ROSIE)
Rocco Moretti, Sergey Lyskov, Rhiju Das, et al.
Protein Science (2017) Vol. 27, Iss. 1, pp. 259-268
Open Access | Times Cited: 69
Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of ‘quasi-ordered’ states
Amanda F. Clouser, Hannah E.R. Baughman, Benjamin Basanta, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 61
Nicotinic cholinergic system and COVID-19: In silico evaluation of nicotinic acetylcholine receptor agonists as potential therapeutic interventions
Nikolaos Alexandris, George Lagoumintzis, Christos T. Chasapis, et al.
Toxicology Reports (2020) Vol. 8, pp. 73-83
Open Access | Times Cited: 60
Web-based tools for computational enzyme design
Sérgio M. Marques, Joan Planas-Iglesias, Jir̆ı́ Damborský
Current Opinion in Structural Biology (2021) Vol. 69, pp. 19-34
Open Access | Times Cited: 55
Nicotinic cholinergic system and COVID-19: In silico identification of interactions between α7 nicotinic acetylcholine receptor and the cryptic epitopes of SARS-Co-V and SARS-CoV-2 Spike glycoproteins
George Lagoumintzis, Christos T. Chasapis, Nikolaos Alexandris, et al.
Food and Chemical Toxicology (2021) Vol. 149, pp. 112009-112009
Open Access | Times Cited: 52
Modeling Immunity with Rosetta: Methods for Antibody and Antigen Design
Clara T. Schoeder, Samuel Schmitz, Jared Adolf‐Bryfogle, et al.
Biochemistry (2021) Vol. 60, Iss. 11, pp. 825-846
Open Access | Times Cited: 50
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures
Paula Blázquez‐Sánchez, Felipe Engelberger, Jerónimo Cifuentes-Anticevic, et al.
Applied and Environmental Microbiology (2021) Vol. 88, Iss. 1
Open Access | Times Cited: 44
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