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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:

The co‐existence of cold activity and thermal stability in an Antarctic GH42 β‐galactosidase relies on its hexameric quaternary arrangement
Marco Mangiagalli, Michela Lapi, S. Maione, et al.
FEBS Journal (2020) Vol. 288, Iss. 2, pp. 546-565
Open Access | Times Cited: 37

Showing 1-25 of 37 citing articles:

Comprehensive insights on environmental adaptation strategies in Antarctic bacteria and biotechnological applications of cold adapted molecules
Kesava Priyan Ramasamy, Lovely Mahawar, Raju Rajasabapathy, et al.
Frontiers in Microbiology (2023) Vol. 14
Open Access | Times Cited: 23
Polysaccharide degradation in an Antarctic bacterium: Discovery of glycoside hydrolases from remote regions of the sequence space
Marco Orlando, Alessandro Marchetti, Luca Bombardi, et al.
International Journal of Biological Macromolecules (2025), pp. 140113-140113
Open Access
Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties
Ryutaro Furukawa, Wakako Toma, Koji Yamazaki, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 53
Cold-Active β-Galactosidases: Insight into Cold Adaptation Mechanisms and Biotechnological Exploitation
Marco Mangiagalli, Marina Lotti
Marine Drugs (2021) Vol. 19, Iss. 1, pp. 43-43
Open Access | Times Cited: 41
Cold-adapted enzymes: mechanisms, engineering and biotechnological application
Yan Liu, Kai‐Zhi Jia, Hongyang Chen, et al.
Bioprocess and Biosystems Engineering (2023) Vol. 46, Iss. 10, pp. 1399-1410
Closed Access | Times Cited: 15
Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme
Ram Karan, Sam Mathew, Reyhan Muhammad, et al.
Microorganisms (2020) Vol. 8, Iss. 10, pp. 1594-1594
Open Access | Times Cited: 43
Psychrophilic enzymes: strategies for cold-adaptation
Tony Collins, Georges Feller
Essays in Biochemistry (2023) Vol. 67, Iss. 4, pp. 701-713
Open Access | Times Cited: 12
Horizontal gene transfer and silver nanoparticles production in a new Marinomonas strain isolated from the Antarctic psychrophilic ciliate Euplotes focardii
Maria Sindhura John, Joseph Amruthraj Nagoth, Kesava Priyan Ramasamy, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 32
Synthesis of Bioactive Silver Nanoparticles Using New Bacterial Strains from an Antarctic Consortium
Maria Sindhura John, Joseph Amruthraj Nagoth, Kesava Priyan Ramasamy, et al.
Marine Drugs (2022) Vol. 20, Iss. 9, pp. 558-558
Open Access | Times Cited: 18
Synthesis of Bioactive Nickel Nanoparticles Using Bacterial Strains from an Antarctic Consortium
Joseph Amruthraj Nagoth, Maria Sindhura John, Kesava Priyan Ramasamy, et al.
Marine Drugs (2024) Vol. 22, Iss. 2, pp. 89-89
Open Access | Times Cited: 2
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1
Louise J. Gourlay, Marco Mangiagalli, Elisabetta Moroni, et al.
FEBS Journal (2024) Vol. 291, Iss. 13, pp. 2897-2917
Open Access | Times Cited: 2
Evolutionary history and activity towards oligosaccharides and polysaccharides of GH3 glycosidases from an Antarctic marine bacterium
Alessandro Marchetti, Marco Orlando, Luca Bombardi, et al.
International Journal of Biological Macromolecules (2024) Vol. 275, pp. 133449-133449
Open Access | Times Cited: 2
A novel cold-adapted phospho-beta-galactosidase from Bacillus velezensis and its potential application for lactose hydrolysis in milk
Yang Liu, Zufang Wu, Xiaoxiong Zeng, et al.
International Journal of Biological Macromolecules (2020) Vol. 166, pp. 760-770
Closed Access | Times Cited: 22
A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
Maria Dalgaard Mikkelsen, Cao Thi Thuy Hang, Thomas Roret, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 15
An acid-tolerant and cold-active β-galactosidase potentially suitable to process milk and whey samples
Monika Thakur, Amit Kumar, Sudhir P. Singh
Applied Microbiology and Biotechnology (2022) Vol. 106, Iss. 9-10, pp. 3599-3610
Closed Access | Times Cited: 11
Cold-active enzymes in the dairy industry: Insight into cold adaption mechanisms and their applications
Qiuming Chen, Yanchang Wu, Zhaolin Huang, et al.
Trends in Food Science & Technology (2022) Vol. 125, pp. 126-135
Closed Access | Times Cited: 9
β‐Galactosidase: Insights into source variability, genetic engineering, immobilisation and diverse applications in food, industry and medicine
Yang Zhou, Yuelin Liu, Fu-kang Gao, et al.
International Journal of Dairy Technology (2024) Vol. 77, Iss. 3, pp. 651-679
Closed Access | Times Cited: 1
Endolysins from Antarctic Pseudomonas Display Lysozyme Activity at Low Temperature
Marco Orlando, Sandra Pucciarelli, Marina Lotti
Marine Drugs (2020) Vol. 18, Iss. 11, pp. 579-579
Open Access | Times Cited: 14
Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism
Nehad Noby, Husam Sabah Auhim, Samuel D. Winter, et al.
Open Biology (2021) Vol. 11, Iss. 12
Open Access | Times Cited: 13
Antarctic Rahnella inusitata: A Producer of Cold-Stable β-Galactosidase Enzymes
Kattia Núñez-Montero, Rodrigo Salazar, Andrés Santos, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 8, pp. 4144-4144
Open Access | Times Cited: 11
Some Clues about Enzymes from Psychrophilic Microorganisms
Roberta Rapuano, Giuseppe Graziano
Microorganisms (2022) Vol. 10, Iss. 6, pp. 1161-1161
Open Access | Times Cited: 7
Substrate recognition mode of a glycoside hydrolase family 42 β-galactosidase from Bifidobacterium longum subspecies infantis(BiBga42A) revealed by crystallographic and mutational analyses
Aina Gotoh, Masafumi Hidaka, Haruko Sakurama, et al.
Microbiome Research Reports (2023) Vol. 2, pp. 20-20
Open Access | Times Cited: 3
β-Galactosidase: a traditional enzyme given multiple roles through protein engineering
Peng Liu, Yuehua Chen, Cuiqing Ma, et al.
Critical Reviews in Food Science and Nutrition (2023), pp. 1-20
Closed Access | Times Cited: 3
Tuning of Conformational Dynamics Through Evolution-Based Design Modulates the Catalytic Adaptability of an Extremophilic Kinase
Ricardo A. Zamora, César A. Ramírez‐Sarmiento, Víctor Castro‐Fernández, et al.
ACS Catalysis (2020) Vol. 10, Iss. 19, pp. 10847-10857
Closed Access | Times Cited: 9
Molecular mechanisms behind the cold and hot adaptation in extremozymes
J. Angelin, M. Kavitha
Elsevier eBooks (2022), pp. 141-176
Closed Access | Times Cited: 6
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