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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:

Directed Evolution Methods for Enzyme Engineering
Saurabh Nirantar
Molecules (2021) Vol. 26, Iss. 18, pp. 5599-5599
Open Access | Times Cited: 23

Showing 23 citing articles:

Enabling technology and core theory of synthetic biology
Xian‐En Zhang, Chenli Liu, Junbiao Dai, et al.
Science China Life Sciences (2023) Vol. 66, Iss. 8, pp. 1742-1785
Open Access | Times Cited: 30
Innovative approaches for enzyme immobilization in milk processing: advancements and industrial applications
Mati Ullah Khan, A. Farid, Shuang Liu, et al.
Critical Reviews in Food Science and Nutrition (2025), pp. 1-20
Closed Access
A novel, genetically encoded whole-cell biosensor for directed evolution of myrcene synthase in Escherichia coli
Chang Chen, Jiajia Liu, Ge Yao, et al.
Biosensors and Bioelectronics (2023) Vol. 228, pp. 115176-115176
Closed Access | Times Cited: 14
Design of Artificial Enzymes Bearing Several Active Centers: New Trends, Opportunities and Problems
Diego Carballares, Roberto Morellon‐Sterling, Roberto Fernandéz‐Lafuente
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 10, pp. 5304-5304
Open Access | Times Cited: 21
Enzyme immobilization studied through molecular dynamic simulations
Nicholus Bhattacharjee, Lur Alonso‐Cotchico, Maria Fátima Lucas
Frontiers in Bioengineering and Biotechnology (2023) Vol. 11
Open Access | Times Cited: 11
Biocatalytic approach for the synthesis of chiral alcohols for the development of pharmaceutical intermediates and other industrial applications: A review
Mohd. Javed Naim, Mohd Fazli Mohammat, Putri Nur Arina Mohd Ariff, et al.
Enzyme and Microbial Technology (2024) Vol. 180, pp. 110483-110483
Closed Access | Times Cited: 3
Data-driven strategies for the computational design of enzyme thermal stability: trends, perspectives, and prospects
Zhixin Dou, Yuqing Sun, Xukai Jiang, et al.
Acta Biochimica et Biophysica Sinica (2023) Vol. 55, Iss. 3, pp. 343-355
Open Access | Times Cited: 9
The multifaceted role of proteases and modern analytical methods for investigation of their catalytic activity
Tatiana A. Filippova, Rami A. Masamrekh, Yulia Yu. Khudoklinova, et al.
Biochimie (2024) Vol. 222, pp. 169-194
Closed Access | Times Cited: 2
Progress and Prospects of Natural Glycoside Sweetener Biosynthesis: A Review
Guanyi Qu, Yanfeng Liu, Qinyuan Ma, et al.
Journal of Agricultural and Food Chemistry (2023) Vol. 71, Iss. 43, pp. 15926-15941
Closed Access | Times Cited: 6
Advances in metabolic engineering of yeasts for the production of fatty acid-derived hydrocarbon fuels
Ran Lu, Tian‐Qiong Shi, Lu Lin, et al.
Green Chemical Engineering (2022) Vol. 3, Iss. 4, pp. 289-303
Open Access | Times Cited: 10
The artificial amino acid change in the sialic acid-binding domain of the hemagglutinin neuraminidase of newcastle disease virus increases its specificity to HCT 116 colorectal cancer cells and tumor suppression effect
Bo‐Kyoung Jung, Yong An, Sung Hoon Jang, et al.
Virology Journal (2024) Vol. 21, Iss. 1
Open Access | Times Cited: 1
In Vitro Biotransformation of High-Titer d-Glucarate by Stepwise-Added Enzyme Cocktails
Yuan Li, Chun You, Y.‐H. Percival Zhang
Organic Process Research & Development (2024) Vol. 28, Iss. 2, pp. 478-486
Closed Access | Times Cited: 1
Impact of single-residue mutations on protein thermal stability: The case of threonine 83 of BC2L-CN lectin
Megumi Hoya, Ryo Matsunaga, Satoru Nagatoishi, et al.
International Journal of Biological Macromolecules (2024) Vol. 272, pp. 132682-132682
Open Access | Times Cited: 1
Rapid, Label‐Free Screening of Diverse Biotransformations by Flow‐Injection Mass Spectrometry
Sarah A. Berger, Christopher Grimm, Jonathan Nyenhuis, et al.
ChemBioChem (2023) Vol. 24, Iss. 11
Open Access | Times Cited: 4
A Promiscuous rSAM Enzyme Enables Diverse Peptide Cross-linking
Karsten A. S. Eastman, Marcus C. Mifflin, P.F. Oblad, et al.
ACS Bio & Med Chem Au (2023) Vol. 3, Iss. 6, pp. 480-493
Open Access | Times Cited: 3
The Pursuit for Sustainable Green Chemistry in Polymer Research
H. N. Cheng, Richard A. Gross
ACS symposium series (2023), pp. 1-14
Closed Access | Times Cited: 2
A circuitous route for in vitro multi-enzyme cascade production of cytidine triphosphate to overcome the thermodynamic bottleneck
Zonglin Li, Yahui Zhong, Zhou-lei Qing, et al.
Bioresources and Bioprocessing (2024) Vol. 11, Iss. 1
Open Access
Recent advances in screening and identification of PET-degrading enzymes
Shengwei Sun
Environmental Reviews (2024) Vol. 32, Iss. 3, pp. 294-314
Closed Access
Microbial biosynthesis of enzymes for food applications
Janeth M. Ventura-Sobrevilla, Daniel Boone-Villa, Lilia Arely Prado‐Barragán, et al.
Elsevier eBooks (2024), pp. 91-108
Closed Access
Investigating functional and folding stability of an engineered E. coli L-asparaginase harboring Y176F/S241C mutations
Mahrokh Dastmalchi, Maryam Hamzeh‐Mivehroud, Hassan Rezazadeh, et al.
Advanced Pharmaceutical Bulletin (2024) Vol. 14, Iss. 3, pp. 675-685
Open Access
Hydroxamate Assays for High‐Throughput Screening of Transketolase Libraries Against Arylated Substrates
Inés Fúster Fernández, Michael Kickstein, Wolf‐Dieter Fessner
Advanced Synthesis & Catalysis (2023) Vol. 365, Iss. 22, pp. 3861-3871
Open Access | Times Cited: 1
Enhanced Thermal Stability of Polyphosphate-Dependent Glucomannokinase by Directed Evolution
Heming Sun, Wenlong Zhu, Qinfei Zhang, et al.
Catalysts (2022) Vol. 12, Iss. 10, pp. 1112-1112
Open Access | Times Cited: 2
Exploring the mechanism of compromised thermostability of aromatic l-amino acid decarboxylase from Bacillus atrophaeus through comparative molecular dynamics simulations
Heng Zhang, Yuanxin Cheng, Qiongqiong Ge, et al.
Computational and Theoretical Chemistry (2022) Vol. 1219, pp. 113972-113972
Open Access
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