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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:

Engineering of β-Glucosidase Bgl15 with Simultaneously Enhanced Glucose Tolerance and Thermostability To Improve Its Performance in High-Solid Cellulose Hydrolysis
Lichuang Cao, Ran Chen, Xin Huang, et al.
Journal of Agricultural and Food Chemistry (2020) Vol. 68, Iss. 19, pp. 5391-5401
Closed Access | Times Cited: 24

Showing 24 citing articles:

Simultaneously optimizing multiple properties of β-glucosidase Bgl6 using combined (semi-)rational design strategies and investigation of the underlying mechanisms
Shuifeng Li, Lichuang Cao, Xiangpeng Yang, et al.
Bioresource Technology (2023) Vol. 374, pp. 128792-128792
Closed Access | Times Cited: 30
High-Throughput Screening Techniques for the Selection of Thermostable Enzymes
Lanxue Li, Xiaoqing Liu, Yingguo Bai, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 8, pp. 3833-3845
Closed Access | Times Cited: 9
Thermostable cellulose saccharifying microbial enzymes: Characteristics, recent advances and biotechnological applications
Anica Dadwal, Shilpa Sharma, T. Satyanarayana
International Journal of Biological Macromolecules (2021) Vol. 188, pp. 226-244
Closed Access | Times Cited: 46
Current understanding and optimization strategies for efficient lignin-enzyme interaction: A review
Mohan Li, Bo Jiang, Wenjuan Wu, et al.
International Journal of Biological Macromolecules (2021) Vol. 195, pp. 274-286
Closed Access | Times Cited: 42
Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review
Bei Ouyang, Guoping Wang, Nian Zhang, et al.
Molecules (2023) Vol. 28, Iss. 13, pp. 4990-4990
Open Access | Times Cited: 19
Significance of glycans in cellulolytic enzymes for lignocellulosic biorefinery – A review
Cheng‐Di Dong, Anil Kumar Patel, Aravind Madhavan, et al.
Bioresource Technology (2023) Vol. 379, pp. 128992-128992
Closed Access | Times Cited: 13
Exploring the diversity of β-glucosidase: Classification, catalytic mechanism, molecular characteristics, kinetic models, and applications
Mehmet Emre Erkanli, Khalid El‐Halabi, Jin Ryoun Kim
Enzyme and Microbial Technology (2023) Vol. 173, pp. 110363-110363
Closed Access | Times Cited: 13
Enzyme synergy for plant cell wall polysaccharide degradation
Ahmed Khamassi, Claire Dumon
Essays in Biochemistry (2023) Vol. 67, Iss. 3, pp. 521-531
Closed Access | Times Cited: 11
A novel β-glucosidase from a hot-spring metagenome shows elevated thermal stability and tolerance to glucose and ethanol
Girija Kaushal, Amit Kumar, Sudhir P. Singh
Enzyme and Microbial Technology (2021) Vol. 145, pp. 109764-109764
Closed Access | Times Cited: 25
Fungal cellulases: protein engineering and post-translational modifications
Ruiqin Zhang, Cheng-Hao Cao, Jiahua Bi, et al.
Applied Microbiology and Biotechnology (2021) Vol. 106, Iss. 1, pp. 1-24
Closed Access | Times Cited: 21
Native to designed: microbial α-amylases for industrial applications
Si Jie Lim, Siti Nurbaya Oslan
PeerJ (2021) Vol. 9, pp. e11315-e11315
Open Access | Times Cited: 14
Structural Insights and Functional Characterization of a Novel β-Glucosidase Derived from Thermotoga profunda
Yanchao Guo, Anke Chen, Kelin Liu, et al.
Biochemical and Biophysical Research Communications (2024) Vol. 732, pp. 150405-150405
Closed Access
Rational Engineering of a β-Glucosidase (H0HC94) from Glycosyl Hydrolase Family I (GH1) to Improve Catalytic Performance on Cellobiose
Sauratej Sengupta, Pinaki Chanda, Bharat Manna, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 36, pp. 8628-8640
Closed Access
Advancing sustainable biotechnology through protein engineering
Amelia R. Bergeson, Hal S. Alper
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 11, pp. 955-968
Closed Access
Enhancing the rigidity of the catalytic pocket entrance to improve catalytic efficiency and thermal stability of alginate Lyase from Pseudoalteromonas
Qiuya Gu, Ke Wang, Shuoqi Jiang, et al.
Molecular Catalysis (2024) Vol. 565, pp. 114406-114406
Closed Access
Expression of a thermostable glucose-stimulated β-glucosidase from a hot-spring metagenome and its promising application to produce gardenia blue
Haiying Mo, Xin Chen, Manwen Tang, et al.
Bioorganic Chemistry (2023) Vol. 143, pp. 107036-107036
Closed Access | Times Cited: 1
Optimization of fermentation conditions for the production of acidophilic β-glucosidase by Trichoderma reesei S12 from mangrove soil
Nan Sun, Xiaoxuan Liu, Xuemei Wang, et al.
Biotechnology & Biotechnological Equipment (2021) Vol. 35, Iss. 1, pp. 1838-1849
Open Access | Times Cited: 2
Rational engineering of a β-glucosidase (H0HC94) from glycosyl family I (GH1) to improve catalytic performance on cellobiose
Sauratej Sengupta, Pinaki Chanda, Bharat Manna, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Closed Access
Peer Review #1 of "Native to designed: microbial α-amylases for industrial applications (v0.2)"
Yaaser Q. Almulaiky
(2021)
Open Access
Peer Review #1 of "Native to designed: microbial α-amylases for industrial applications (v0.1)"
Yaaser Q. Almulaiky
(2021)
Open Access
Peer Review #3 of "Native to designed: microbial α-amylases for industrial applications (v0.2)"

(2021)
Open Access
Peer Review #2 of "Native to designed: microbial α-amylases for industrial applications (v0.1)"

(2021)
Open Access
Peer Review #3 of "Native to designed: microbial α-amylases for industrial applications (v0.1)"

(2021)
Open Access
Peer Review #2 of "Native to designed: microbial α-amylases for industrial applications (v0.2)"

(2021)
Open Access
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