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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:

AlphaFold2 reveals commonalities and novelties in protein structure space for 21 model organisms
Nicola Bordin, Ian Sillitoe, Vamsi Nallapareddy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 24

Showing 24 citing articles:

DALI shines a light on remote homologs: One hundred discoveries
Liisa Holm, Aleksi Laiho, Petri Törönen, et al.
Protein Science (2022) Vol. 32, Iss. 1
Open Access | Times Cited: 360
The impact of AlphaFold Protein Structure Database on the fields of life sciences
Mihály Váradi, Sameer Velankar
PROTEOMICS (2022) Vol. 23, Iss. 17
Open Access | Times Cited: 80
TMbed: transmembrane proteins predicted through language model embeddings
Michael Bernhofer, Burkhard Rost
BMC Bioinformatics (2022) Vol. 23, Iss. 1
Open Access | Times Cited: 56
RCSB Protein Data Bank: Efficient Searching and Simultaneous Access to One Million Computed Structure Models Alongside the PDB Structures Enabled by Architectural Advances
Sebastian Bittrich, Charmi Bhikadiya, Chunxiao Bi, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 14, pp. 167994-167994
Open Access | Times Cited: 41
AlphaFold2 Predicts Whether Proteins Interact Amidst Confounding Structural Compatibility
Juliette Martin
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 5, pp. 1473-1480
Open Access | Times Cited: 8
SETH predicts nuances of residue disorder from protein embeddings
Dagmar Ilzhöfer, Michael Heinzinger, Burkhard Rost
Frontiers in Bioinformatics (2022) Vol. 2
Open Access | Times Cited: 34
The opportunities and challenges posed by the new generation of deep learning-based protein structure predictors
Mihály Váradi, Nicola Bordin, Christine Orengo, et al.
Current Opinion in Structural Biology (2023) Vol. 79, pp. 102543-102543
Open Access | Times Cited: 17
Clustering predicted structures at the scale of the known protein universe
Inigo Barrio‐Hernandez, Jingi Yeo, Jürgen Jänes, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
KinFams: De-Novo Classification of Protein Kinases Using CATH Functional Units
Tolulope Adeyelu, Nicola Bordin, Vaishali Waman, et al.
Biomolecules (2023) Vol. 13, Iss. 2, pp. 277-277
Open Access | Times Cited: 12
3D-Beacons: decreasing the gap between protein sequences and structures through a federated network of protein structure data resources
Mihály Váradi, Sreenath Nair, Ian Sillitoe, et al.
GigaScience (2022) Vol. 11
Open Access | Times Cited: 17
Beyond sequence: Structure-based machine learning
Janani Durairaj, Dick de Ridder, Aalt D. J. van Dijk
Computational and Structural Biotechnology Journal (2022) Vol. 21, pp. 630-643
Open Access | Times Cited: 16
Alternative Reading Frames are an Underappreciated Source of Protein Sequence Novelty
Zachary Ardern
Journal of Molecular Evolution (2023) Vol. 91, Iss. 5, pp. 570-580
Closed Access | Times Cited: 9
LambdaPP: Fast and accessible protein‐specific phenotype predictions
Tobias Olenyi, Céline Marquet, Michael Heinzinger, et al.
Protein Science (2022) Vol. 32, Iss. 1
Open Access | Times Cited: 14
SETH predicts nuances of residue disorder from protein embeddings
Dagmar Ilzhoefer, Michael Heinzinger, Burkhard Rost
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 13
Explainable protein function annotation using local structure embeddings
Alexander Derry, Russ B. Altman
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 7
COLLAPSE: A representation learning framework for identification and characterization of protein structural sites
Alexander Derry, Russ B. Altman
Protein Science (2022) Vol. 32, Iss. 2
Open Access | Times Cited: 9
Clustering predicted structures at the scale of the known protein universe
Martin Steinegger, Pedro Beltrão, Sameer Velankar, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 4
Does AlphaFold2 model proteins’ intracellular conformations? An experimental test using cross-linking mass spectrometry of endogenous ciliary proteins
Caitlyn L McCafferty, Erin L. Pennington, Ophelia Papoulas, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 7
LambdaPP: Fast and accessible protein-specific phenotype predictions
Tobias Olenyi, Céline Marquet, Michael Heinzinger, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6
AlphaFold2 predicts interactions amidst confounding structural compatibility
Juliette Martin
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
A pathogen effector FOLD diversified in symbiotic fungi
Albin Teulet, Clément Quan, Édouard Evangelisti, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 4
TMbed – Transmembrane proteins predicted through Language Model embeddings
Michael Bernhofer, Burkhard Rost
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3
COLLAPSE: A representation learning framework for identification and characterization of protein structural sites
Alexander Derry, Russ B. Altman
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3
What is hidden in the darkness? Characterization of AlphaFold structural space
Janani Durairaj, Joana Pereira, Mehmet Akdel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
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