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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:

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

Showing 14 citing articles:

Biogenic Synthesis of Copper Nanoparticles Using Bacterial Strains Isolated from an Antarctic Consortium Associated to a Psychrophilic Marine Ciliate: Characterization and Potential Application as Antimicrobial Agents
Maria Sindhura John, Joseph Amruthraj Nagoth, Marco Zannotti, et al.
Marine Drugs (2021) Vol. 19, Iss. 5, pp. 263-263
Open Access | Times Cited: 70
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
Phage‐derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens
Dahee Choi, Sangryeol Ryu, Minsuk Kong
Comprehensive Reviews in Food Science and Food Safety (2025) Vol. 24, Iss. 2
Closed Access
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
Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin into N,N′-diacetylchitobiose
Xue‐Bing Ren, Yan‐Ru Dang, Shasha Liu, et al.
Marine Drugs (2022) Vol. 20, Iss. 3, pp. 165-165
Open Access | Times Cited: 22
The GH19 Engineering Database: Sequence diversity, substrate scope, and evolution in glycoside hydrolase family 19
Marco Orlando, Patrick C. F. Buchholz, Marina Lotti, et al.
PLoS ONE (2021) Vol. 16, Iss. 10, pp. e0256817-e0256817
Open Access | Times Cited: 26
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
Characterization of a Novel Alginate Lyase with Two Alginate Lyase Domains from the Marine Bacterium Vibrio sp. C42
Xiaomeng Sun, Xue Zhao, Mei‐Ling Sun, et al.
Marine Drugs (2022) Vol. 20, Iss. 12, pp. 746-746
Open Access | Times Cited: 10
Characterization of a Peptidoglycan-Degrading Protein: Biochemical and Antimicrobial Characteristics, Antibiotic Synergism, and Delivery System Innovation
Viviane de Cássia Oliveira, Nathália Gonsales da Rosa-Garzon, Amanda Carolina Souza Delfino da Rocha, et al.
Probiotics and Antimicrobial Proteins (2024)
Closed Access | Times Cited: 1
A myxobacterial GH19 lysozyme with bacteriolytic activity on both Gram-positive and negative phytopathogens
Yueqiu Li, Xiaoli Zhou, Xianjiao Zhang, et al.
AMB Express (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 8
REGULATION OF ENZYME-DEPENDENT LYSIS OF MICROBIAL CELLS: IS THE EFFECTOR TARGET ENZYME OR SUBSTRATE?
Nikolay V. Rastriga, Н. Л. Еремеев, Д. А. Климов, et al.
Lomonosov chemistry journal (2024) Vol. 65, Iss. №3, 2024, pp. 235-244
Open Access
Regulation of Enzyme-Dependent Lysis of Microbial Cells: Is the Effector Target an Enzyme or Substrate?
Nikolay V. Rastriga, Н. Л. Еремеев, Д. А. Климов, et al.
Moscow University Chemistry Bulletin (2024) Vol. 79, Iss. 3, pp. 195-202
Closed Access
A GH19 lysozyme and peptidase from Myoviridae cyanophages lacking the typical holin-endolysin system exhibit lytic activity
Lihui Meng, Fei Ke, Qi-Ya Zhang, et al.
Enzyme and Microbial Technology (2023) Vol. 173, pp. 110368-110368
Closed Access
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