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:

Utility of B-Factors in Protein Science: Interpreting Rigidity, Flexibility, and Internal Motion and Engineering Thermostability
Zhoutong Sun, Qian Liu, Ge Qu, et al.
Chemical Reviews (2019) Vol. 119, Iss. 3, pp. 1626-1665
Closed Access | Times Cited: 421

Showing 26-50 of 421 citing articles:

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: 38

Tuning an Imine Reductase for the Asymmetric Synthesis of Azacycloalkylamines by Concise Structure‐Guided Engineering
Jun Zhang, Daohong Liao, Rongchang Chen, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 24
Closed Access | Times Cited: 37

Accurate Prediction of Enzyme Thermostabilization with Rosetta Using AlphaFold Ensembles
Francesca Peccati, Sara Alunno-Rufini, Gonzalo Jiménez‐Osés
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 3, pp. 898-909
Open Access | Times Cited: 26

Marine enzymes: Classification and application in various industries
Saba Ghattavi, Ahmad Homaei
International Journal of Biological Macromolecules (2023) Vol. 230, pp. 123136-123136
Closed Access | Times Cited: 25

Revisiting the Ramachandran plot based on statistical analysis of static and dynamic characteristics of protein structures
Soon Woo Park, Byung Ho Lee, Seung‐Hun Song, et al.
Journal of Structural Biology (2023) Vol. 215, Iss. 1, pp. 107939-107939
Closed Access | Times Cited: 24

Enhanced Thermostability of Candida Ketoreductase by Computation-Based Cross-Regional Combinatorial Mutagenesis
Cheng Chen, Bi-Han Guan, Qiang Geng, et al.
ACS Catalysis (2023) Vol. 13, Iss. 11, pp. 7407-7416
Closed Access | Times Cited: 24

Engineering lipase at the molecular scale for cleaner biodiesel production - A review
Zhongbiao Tan, Gang Chen, Silu Chen, et al.
Molecular Catalysis (2023) Vol. 546, pp. 113271-113271
Closed Access | Times Cited: 22

FireProt 2.0: web-based platform for the fully automated design of thermostable proteins
Miloš Musil, Andrej Jezik, Jana Horackova, et al.
Briefings in Bioinformatics (2023) Vol. 25, Iss. 1
Open Access | Times Cited: 22

Alteration of Chain-Length Selectivity and Thermostability of Rhizopus oryzae Lipase via Virtual Saturation Mutagenesis Coupled with Disulfide Bond Design
Jinsha Huang, Shuhan Dai, Xiying Chen, et al.
Applied and Environmental Microbiology (2023) Vol. 89, Iss. 1
Open Access | Times Cited: 21

Effective Molecular Dynamics from Neural Network-Based Structure Prediction Models
Alexander Jussupow, Ville R. I. Kaila
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 7, pp. 1965-1975
Open Access | Times Cited: 21

Computer-Aided Rational Design Strategy to Improve the Thermal Stability of Alginate Lyase AlyMc
Yongyan Cui, Yang Min, Nan Liu, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 6, pp. 3055-3065
Closed Access | Times Cited: 9

Enzymatic Stereodivergent Access to Fluorinated β-Lactam Pharmacophores via Triple-Parameter Engineered Ketoreductases
Ze-Long Mei, Congcong Li, Xu Han, et al.
ACS Catalysis (2024) Vol. 14, Iss. 8, pp. 6358-6368
Closed Access | Times Cited: 9

Machine-learned molecular mechanics force fields from large-scale quantum chemical data
Kenichiro Takaba, Anika J. Friedman, Chapin E. Cavender, et al.
Chemical Science (2024) Vol. 15, Iss. 32, pp. 12861-12878
Open Access | Times Cited: 8

Enzyme engineering for functional lipids synthesis: recent advance and perspective
Ailin Guan, Yue Hou, Run Yang, et al.
Bioresources and Bioprocessing (2024) Vol. 11, Iss. 1
Open Access | Times Cited: 7

Linking ATP and allosteric sites to achieve superadditive binding with bivalent EGFR kinase inhibitors
Florian Wittlinger, Blessing C. Ogboo, Ekaterina Shevchenko, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 7

Thermostability Enhancement of Tagatose 4-Epimerase through Protein Engineering and Whole-Cell Immobilization
Zhanzhi Liu, Xuehong Guo, Ying Xu, et al.
Journal of Agricultural and Food Chemistry (2025)
Closed Access

A review on computational models for predicting protein solubility
Teerapat Pimtawong, Jun Ren, Jingyu Lee, et al.
The Journal of Microbiology (2025) Vol. 63, Iss. 1, pp. e:2408001-e:2408001
Closed Access

Biochemical Characterization and Mechanism of Thermostability of the Thermophilic Hyaluronate Lyase TcHly8D
Yuzhu Zhang, Hao Wu, Zheng Fu, et al.
Journal of Agricultural and Food Chemistry (2025)
Closed Access

Protein Engineering for Industrial Biocatalysis: Principles, Approaches, and Lessons from Engineered PETases
Konstantinos Grigorakis, Christina Ferousi, Evangelos Topakas
Catalysts (2025) Vol. 15, Iss. 2, pp. 147-147
Open Access

Assessment of enzyme active site positioning and tests of catalytic mechanisms through X-ray–derived conformational ensembles
Filip Yabukarski, J.T. Biel, Margaux M. Pinney, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 52, pp. 33204-33215
Open Access | Times Cited: 61

A Novel d -Allulose 3-Epimerase Gene from the Metagenome of a Thermal Aquatic Habitat and d -Allulose Production by Bacillus subtilis Whole-Cell Catalysis
Satya Narayan Patel, Girija Kaushal, Sudhir P. Singh
Applied and Environmental Microbiology (2019) Vol. 86, Iss. 5
Open Access | Times Cited: 60

Focused rational iterative site-specific mutagenesis (FRISM)
Danyang Li, Qi Wu, Manfred T. Reetz
Methods in enzymology on CD-ROM/Methods in enzymology (2020), pp. 225-242
Closed Access | Times Cited: 57

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