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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:

Solubility, Stability, and Avidity of Recombinant Antibody Fragments Expressed in Microorganisms
Tae Hyun Kang, Baik Lin Seong
Frontiers in Microbiology (2020) Vol. 11
Open Access | Times Cited: 63

Showing 1-25 of 63 citing articles:

Protein Design: From the Aspect of Water Solubility and Stability
Rui Qing, Shilei Hao, Eva Smorodina, et al.
Chemical Reviews (2022) Vol. 122, Iss. 18, pp. 14085-14179
Open Access | Times Cited: 146
Unveiling the new chapter in nanobody engineering: advances in traditional construction and AI-driven optimization
Ji‐Wei Liu, Lei Wu, Anqi Xie, et al.
Journal of Nanobiotechnology (2025) Vol. 23, Iss. 1
Open Access | Times Cited: 2
EGFR-Targeted Photodynamic Therapy
Luca Ulfo, Paolo Emidio Costantini, Matteo Di Giosia, et al.
Pharmaceutics (2022) Vol. 14, Iss. 2, pp. 241-241
Open Access | Times Cited: 64
Antibody‐Incorporated Nanomedicines for Cancer Therapy
Shun‐Yu Wu, Fu‐Gen Wu, Xiaoyuan Chen
Advanced Materials (2022) Vol. 34, Iss. 24
Closed Access | Times Cited: 64
Camelid Single-Domain Antibodies: Promises and Challenges as Lifesaving Treatments
Mehdi Arbabi‐Ghahroudi
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 9, pp. 5009-5009
Open Access | Times Cited: 60
Mechanisms of Action and Limitations of Monoclonal Antibodies and Single Chain Fragment Variable (scFv) in the Treatment of Cancer
Cynthia Rodríguez-Nava, Carlos Ortuño‐Pineda, Berenice Illades‐Aguiar, et al.
Biomedicines (2023) Vol. 11, Iss. 6, pp. 1610-1610
Open Access | Times Cited: 28
Molecular and functional insight into anti-EGFR nanobody: Theranostic implications for malignancies
Rajan K. Tripathy, Abhay H. Pande
Life Sciences (2024) Vol. 345, pp. 122593-122593
Closed Access | Times Cited: 9
Monoclonal Antibodies as a Therapeutic Strategy against Multidrug-Resistant Bacterial Infections in a Post-COVID-19 Era
Hsiao-Chun Chen, Yu-Ling Pan, Ying Chen, et al.
Life (2024) Vol. 14, Iss. 2, pp. 246-246
Open Access | Times Cited: 8
Recombinant monoclonal antibody production in yeasts: Challenges and considerations
Prabir Kumar Das, Ansuman Sahoo, Venkata Dasu Veeranki
International Journal of Biological Macromolecules (2024) Vol. 266, pp. 131379-131379
Closed Access | Times Cited: 7
Lateral flow immunoassay for small-molecules detection in phytoproducts: a review
Poomraphie Nuntawong, Waraporn Putalun, Hiroyuki Tanaka, et al.
Journal of Natural Medicines (2022) Vol. 76, Iss. 3, pp. 521-545
Open Access | Times Cited: 27
Development of CAR T Cell Therapy in Children—A Comprehensive Overview
Michael Boettcher, Alexander Joechner, Ziduo Li, et al.
Journal of Clinical Medicine (2022) Vol. 11, Iss. 8, pp. 2158-2158
Open Access | Times Cited: 24
Antibody-receptor bioengineering and its implications in designing bioelectronic devices
Daphika S. Dkhar, Rohini Kumari, Supratim Mahapatra, et al.
International Journal of Biological Macromolecules (2022) Vol. 218, pp. 225-242
Closed Access | Times Cited: 23
Review of phage display: A jack-of-all-trades and master of most biomolecule display
Brenda Pei Chui Song, Angela Chiew Wen Ch’ng, Theam Soon Lim
International Journal of Biological Macromolecules (2023) Vol. 256, pp. 128455-128455
Closed Access | Times Cited: 15
Understanding and controlling the molecular mechanisms of protein aggregation in mAb therapeutics
Kuin Tian Pang, Yuansheng Yang, Wei Zhang, et al.
Biotechnology Advances (2023) Vol. 67, pp. 108192-108192
Open Access | Times Cited: 14
Improving Pharmacokinetics of Peptides Using Phage Display
Mallika Asar, Jessica Newton‐Northup, Mette Soendergaard
Viruses (2024) Vol. 16, Iss. 4, pp. 570-570
Open Access | Times Cited: 5
Single‐chain fragment variable produced by phage display technology: Construction, selection, mutation, expression, and recent applications in food safety
Long Li, Shuangmin Wu, Yu Si, et al.
Comprehensive Reviews in Food Science and Food Safety (2022) Vol. 21, Iss. 5, pp. 4354-4377
Closed Access | Times Cited: 22
Integrating Biochemical and Computational Approaches Reveal Structural Insights in Trastuzumab scFv-Fc Antibody Engineering
Olga Bednova, Jessica Pougoue Ketchemen, Hazem Mslati, et al.
Biomolecules (2025) Vol. 15, Iss. 5, pp. 606-606
Open Access
Deep mining of antibody phage-display selections using Oxford Nanopore Technologies and Dual Unique Molecular Identifiers
Oscar Mejias-Gomez, Marta Braghetto, Morten Kielsgaard Dziegiel Sørensen, et al.
New Biotechnology (2024) Vol. 80, pp. 56-68
Open Access | Times Cited: 3
A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments
Yang Wang, Wenjie Yuan, Siqi Guo, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 15
The use of peptides, aptamers, and variable domains of heavy chain only antibodies in tissue engineering and regenerative medicine
Michelle Koerselman, Lisanne Morshuis, Marcel Karperien
Acta Biomaterialia (2023) Vol. 170, pp. 1-14
Open Access | Times Cited: 7
Development, High-Throughput Profiling, and Biopanning of a Large Phage Display Single-Domain Antibody Library
H Lee, Ah Hyun Cho, Jae Hyeon Hwang, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 9, pp. 4791-4791
Open Access | Times Cited: 2
A comparative study of the developability of full-length antibodies, fragments, and bispecific formats reveals higher stability risks for engineered constructs
Itzel Condado Morales, Fabian Dingfelder, Isabel Waibel, et al.
mAbs (2024) Vol. 16, Iss. 1
Open Access | Times Cited: 2
Insights into the Binding Profile of Anti-chlorpyrifos Recombinant Antibodies: From Computational Simulation to Immunoassay Validation
Rubing Zou, Yuanhao Guo, Yan Wang, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 30, pp. 11287-11295
Closed Access | Times Cited: 6
Engineered fast-dissociating antibody fragments for multiplexed super-resolution microscopy
Qianli Zhang, Akitoshi Miyamoto, Shin Watanabe, et al.
Cell Reports Methods (2022) Vol. 2, Iss. 10, pp. 100301-100301
Open Access | Times Cited: 9
Principles of Affinity Selection
George P. Smith
Cold Spring Harbor Protocols (2023) Vol. 2024, Iss. 6, pp. pdb.over107894-pdb.over107894
Open Access | Times Cited: 4
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