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:

Protein ensembles link genotype to phenotype
Ruth Nussinov, Chung‐Jung Tsai, Hyunbum Jang
PLoS Computational Biology (2019) Vol. 15, Iss. 6, pp. e1006648-e1006648
Open Access | Times Cited: 85

Showing 1-25 of 85 citing articles:

Structural and functional complexity of HSP90 in cellular homeostasis and disease
Gabriela Chiosis, Chander Singh Digwal, Jane B. Trepel, et al.
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 11, pp. 797-815
Open Access | Times Cited: 76

Molecular principles underlying aggressive cancers
Ruth Nussinov, Bengi Ruken Yavuz, Hyunbum Jang
Signal Transduction and Targeted Therapy (2025) Vol. 10, Iss. 1
Open Access | Times Cited: 3

Morphological profiling of small molecules
Slava Ziegler, Sonja Sievers, Herbert Waldmann
Cell chemical biology (2021) Vol. 28, Iss. 3, pp. 300-319
Open Access | Times Cited: 62

Ensemble-function relationships to dissect mechanisms of enzyme catalysis
Filip Yabukarski, Tzanko Doukov, Margaux M. Pinney, et al.
Science Advances (2022) Vol. 8, Iss. 41
Open Access | Times Cited: 39

Protein conformational ensembles in function: roles and mechanisms
Ruth Nussinov, Yonglan Liu, Wengang Zhang, et al.
RSC Chemical Biology (2023) Vol. 4, Iss. 11, pp. 850-864
Open Access | Times Cited: 34

Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation
Anna Rodina, Chao Xu, Chander Singh Digwal, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 25

Molecular determinants of protein evolvability
Karol Buda, C.M. Miton, Xingyu Cara Fan, et al.
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 9, pp. 751-760
Closed Access | Times Cited: 22

Machine Learning Prediction of Allosteric Drug Activity from Molecular Dynamics
Filippo Marchetti, Elisabetta Moroni, Alessandro Pandini, et al.
The Journal of Physical Chemistry Letters (2021) Vol. 12, Iss. 15, pp. 3724-3732
Open Access | Times Cited: 46

A revised central dogma for the 21st century: All biology is cognitive information processing
William B. Miller, František Baluška, Arthur S. Reber
Progress in Biophysics and Molecular Biology (2023) Vol. 182, pp. 34-48
Closed Access | Times Cited: 19

How aberrant N-glycosylation can alter protein functionality and ligand binding: An atomistic view
Matteo Castelli, Pengrong Yan, Anna Rodina, et al.
Structure (2023) Vol. 31, Iss. 8, pp. 987-1004.e8
Open Access | Times Cited: 16

Global analysis of aging-related protein structural changes uncovers enzyme-polymerization-based control of longevity
Jurgita Paukštytė, Rosa María López Cabezas, Yuehan Feng, et al.
Molecular Cell (2023) Vol. 83, Iss. 18, pp. 3360-3376.e11
Open Access | Times Cited: 16

Review: Cancer and neurodevelopmental disorders: multi-scale reasoning and computational guide
Ruth Nussinov, Bengi Ruken Yavuz, Habibe Cansu Demirel, et al.
Frontiers in Cell and Developmental Biology (2024) Vol. 12
Open Access | Times Cited: 6

Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases
Joan Gizzio, Abhishek Thakur, Allan Haldane, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6

Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone
Pengrong Yan, Hardik J. Patel, Sahil Sharma, et al.
Cell Reports (2020) Vol. 31, Iss. 13, pp. 107840-107840
Open Access | Times Cited: 46

Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators
Helene J. Bustad, Juha P. Kallio, Marta Vorland, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 2, pp. 675-675
Open Access | Times Cited: 39

The allosteric mechanism of mTOR activation can inform bitopic inhibitor optimization
Yonglan Liu, Mingzhen Zhang, Hyunbum Jang, et al.
Chemical Science (2023) Vol. 15, Iss. 3, pp. 1003-1017
Open Access | Times Cited: 13

Proteostatic tuning underpins the evolution of novel multicellular traits
Kristopher Montrose, T. Dung, Anthony Burnetti, et al.
Science Advances (2024) Vol. 10, Iss. 10
Open Access | Times Cited: 5

Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases
Joan Gizzio, Abhishek Thakur, Allan Haldane, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5

Analysis of limited proteolysis-coupled mass spectrometry data
Luise Nagel, Jan Großbach, Valentina Cappelletti, et al.
Molecular & Cellular Proteomics (2025), pp. 100934-100934
Closed Access

The generative capacity of probabilistic protein sequence models
Francisco McGee, Sandro Hauri, Quentin Novinger, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 30

Mechanism of activation and the rewired network: New drug design concepts
Ruth Nussinov, Mingzhen Zhang, Ryan Maloney, et al.
Medicinal Research Reviews (2021) Vol. 42, Iss. 2, pp. 770-799
Open Access | Times Cited: 27

CXCL14 in prostate cancer: complex interactions in the tumor microenvironment and future prospects
Lei Tang, Xin Chen, Jianquan Hou, et al.
Journal of Translational Medicine (2025) Vol. 23, Iss. 1
Open Access

Advancing Molecular Simulations: Merging Physical Models, Experiments, and AI to Tackle Multiscale Complexity
Giorgio Bonollo, Gauthier Trèves, Д. В. Комаров, et al.
The Journal of Physical Chemistry Letters (2025), pp. 3606-3615
Open Access

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