Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

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

Showing 14 citing articles:

Impact of Various Forced Oxidative Stress Factors in Rapid Degradation of mAb: Trastuzumab as a Case Study
Shravan Sreenivasan, Anurag S. Rathore
Pharmaceutical Research (2025) Vol. 42, Iss. 2, pp. 335-351
Closed Access | Times Cited: 1
Potential risk factors of protein aggregation in syringe handling during antibody drug dilution for intravenous administration
Masakazu Fukuda, S. Nagae, Toru Takarada, et al.
Journal of Pharmaceutical Sciences (2025)
Closed Access
Influence of physicochemical conditions on liquid-liquid phase separation and stability of immunoglobulin Y for storage and application
Yuzhang Hu, Mei Dang, Xiaoying Zhang
International Journal of Biological Macromolecules (2025) Vol. 306, pp. 141393-141393
Open Access
Prediction of long-term stability of high-concentration formulations to support rapid development of antibodies against SARS-CoV-2
Lin Luo, Michael Meleties, Julie M. Beaudet, et al.
mAbs (2025) Vol. 17, Iss. 1
Open Access
Rapid In Vivo Screening of Monoclonal Antibody Cocktails Using Hydrodynamic Delivery of DNA-Encoded Modified Antibodies
Hugues Fausther‐Bovendo, George Babuadze, Teodora Ivanciuc, et al.
Biomedicines (2025) Vol. 13, Iss. 3, pp. 637-637
Open Access
Optimized Protein–Excipient Interactions in the Martini 3 Force Field
Tobias M. Prass, Kresten Lindorff‐Larsen, Patrick Garidel, et al.
Journal of Chemical Information and Modeling (2025)
Open Access
Aggregation of therapeutic monoclonal antibodies due to thermal and air/liquid interfacial agitation stress: Occurrence, stability assessment strategies, aggregation mechanism, influencing factors, and ways to enhance stability
Shravan Sreenivasan, Christian Schöneich, Anurag S. Rathore
International Journal of Pharmaceutics (2024), pp. 124735-124735
Closed Access | Times Cited: 3
Stability of Protein Pharmaceuticals: Recent Advances
Mark C. Manning, Ryan E. Holcomb, R. W. Payne, et al.
Pharmaceutical Research (2024) Vol. 41, Iss. 7, pp. 1301-1367
Closed Access | Times Cited: 2
Aggrescan4D: A comprehensive tool for pH‐dependent analysis and engineering of protein aggregation propensity
M. Zalewski, Valentín Iglesias, Oriol Bárcenas, et al.
Protein Science (2024) Vol. 33, Iss. 10
Open Access | Times Cited: 2
Investigation on environmental factors contributing to bispecific antibody stability and the reversal of self-associated aggregates
Nattha Ingavat, Nuruljannah Dzulkiflie, Jia Min Liew, et al.
Bioresources and Bioprocessing (2024) Vol. 11, Iss. 1
Open Access | Times Cited: 1
Impact of fed-batch process intensification on the productivity and product quality of two CHO cell lines expressing unique novel molecular format proteins
Nicolas Wolnick, Marissa Dickson, Thaddaeus A. Webster, et al.
Bioprocess and Biosystems Engineering (2024) Vol. 47, Iss. 8, pp. 1227-1240
Open Access | Times Cited: 1
Strategy for Developing a Stable CHO Cell Line that Produces Large Titers of Trastuzumab Antibody
Boulenouar Hafsa Hadj, Nadia Bouchoutrouch, Youssef Amar, et al.
Frontiers in Bioscience-Elite (2023) Vol. 15, Iss. 4
Open Access | Times Cited: 3
“IgG’s: contending with aggregating circumstances”
Paul Toran, Lisa Arvidson, Alexandra Vachon, et al.
International Journal of Molecular Biology Open Access (2024) Vol. 7, Iss. 1, pp. 32-33
Open Access
Thermal and pH stress dictate distinct mechanisms of monoclonal antibody aggregation
Huan Meng, Kuin Tian Pang, Corrine Wan, et al.
International Journal of Biological Macromolecules (2024), pp. 136601-136601
Closed Access
Page 1

Scroll to top