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:
Iterative Alanine Scanning Mutagenesis Confers Aromatic Ketone Specificity and Activity of L‐Amine Dehydrogenases
Xiaoqing Mu, Tao Wu, Yong Mao, et al.
ChemCatChem (2021) Vol. 13, Iss. 24, pp. 5243-5253
Closed Access | Times Cited: 13
Xiaoqing Mu, Tao Wu, Yong Mao, et al.
ChemCatChem (2021) Vol. 13, Iss. 24, pp. 5243-5253
Closed Access | Times Cited: 13
Showing 13 citing articles:
Reshaping Substrate-Binding Pocket of Leucine Dehydrogenase for Bidirectionally Accessing Structurally Diverse Substrates
Tao Wu, Yinmiao Wang, Ningxin Zhang, et al.
ACS Catalysis (2022) Vol. 13, Iss. 1, pp. 158-168
Closed Access | Times Cited: 40
Tao Wu, Yinmiao Wang, Ningxin Zhang, et al.
ACS Catalysis (2022) Vol. 13, Iss. 1, pp. 158-168
Closed Access | Times Cited: 40
Biocatalytic reductive aminations with NAD(P)H-dependent enzymes: enzyme discovery, engineering and synthetic applications
Bo Yuan, Dameng Yang, Ge Qu, et al.
Chemical Society Reviews (2023) Vol. 53, Iss. 1, pp. 227-262
Closed Access | Times Cited: 28
Bo Yuan, Dameng Yang, Ge Qu, et al.
Chemical Society Reviews (2023) Vol. 53, Iss. 1, pp. 227-262
Closed Access | Times Cited: 28
Amine dehydrogenases: Current status and potential value for chiral amine synthesis
Jianqiao Liu, Weixi Kong, Jing Bai, et al.
Chem Catalysis (2022) Vol. 2, Iss. 6, pp. 1288-1314
Open Access | Times Cited: 29
Jianqiao Liu, Weixi Kong, Jing Bai, et al.
Chem Catalysis (2022) Vol. 2, Iss. 6, pp. 1288-1314
Open Access | Times Cited: 29
Shield Machine-like Substrate Walking Strategy-Based Pocket Engineering of F-Amine Dehydrogenase for Accessing Structurally Diverse Fused-Ring and Linked-Ring Aryl Ketones
Tao Wu, Yan Xu, Yao Nie, et al.
ACS Catalysis (2024) Vol. 14, Iss. 4, pp. 2685-2695
Closed Access | Times Cited: 4
Tao Wu, Yan Xu, Yao Nie, et al.
ACS Catalysis (2024) Vol. 14, Iss. 4, pp. 2685-2695
Closed Access | Times Cited: 4
Substrate-Specific Engineering of Amino Acid Dehydrogenase Superfamily for Synthesis of a Variety of Chiral Amines and Amino Acids
Feng Zhou, Yan Xu, Yao Nie, et al.
Catalysts (2022) Vol. 12, Iss. 4, pp. 380-380
Open Access | Times Cited: 16
Feng Zhou, Yan Xu, Yao Nie, et al.
Catalysts (2022) Vol. 12, Iss. 4, pp. 380-380
Open Access | Times Cited: 16
Substrate-Specific Evolution of Amine Dehydrogenases for Accessing Structurally Diverse Enantiopure (R)-β-Amino Alcohols
Xinjian Yin, Wenzhong Gong, Yujing Zeng, et al.
ACS Catalysis (2024) Vol. 14, Iss. 2, pp. 837-845
Open Access | Times Cited: 2
Xinjian Yin, Wenzhong Gong, Yujing Zeng, et al.
ACS Catalysis (2024) Vol. 14, Iss. 2, pp. 837-845
Open Access | Times Cited: 2
Engineering the substrate acceptance of l-amine dehydrogenase enables the collective biocatalytic synthesis of N-heterocyclic primary amines
Tao Wu, Yan Xu, Yao Nie, et al.
Chemical Engineering Journal (2024) Vol. 490, pp. 151735-151735
Closed Access | Times Cited: 2
Tao Wu, Yan Xu, Yao Nie, et al.
Chemical Engineering Journal (2024) Vol. 490, pp. 151735-151735
Closed Access | Times Cited: 2
Expanding the Substrate Scope of Native Amine Dehydrogenases through In Silico Structural Exploration and Targeted Protein Engineering
Laurine Ducrot, Megan Bennett, Gwenaëlle André, et al.
ChemCatChem (2022) Vol. 14, Iss. 22
Open Access | Times Cited: 8
Laurine Ducrot, Megan Bennett, Gwenaëlle André, et al.
ChemCatChem (2022) Vol. 14, Iss. 22
Open Access | Times Cited: 8
Reshaping the active pocket of an aldo-keto reductase to enhance its detoxification activity towards 3-keto-deoxynivalenol
Jiafeng Niu, Bin Ma, Hao Zhu, et al.
Deleted Journal (2024)
Open Access | Times Cited: 1
Jiafeng Niu, Bin Ma, Hao Zhu, et al.
Deleted Journal (2024)
Open Access | Times Cited: 1
High coenzyme affinity chimeric amine dehydrogenase based on domain engineering
Jialin Li, Xiaoqing Mu, Tao Wu, et al.
Bioresources and Bioprocessing (2022) Vol. 9, Iss. 1
Open Access | Times Cited: 6
Jialin Li, Xiaoqing Mu, Tao Wu, et al.
Bioresources and Bioprocessing (2022) Vol. 9, Iss. 1
Open Access | Times Cited: 6
Efficient synthesis of (R)-4-methoxyamphetamine and its analogues under low ammonium concentration using engineered amine dehydrogenase
Yuyang Luo, Yixuan Li, Weiting Kong, et al.
Molecular Catalysis (2023) Vol. 553, pp. 113802-113802
Closed Access | Times Cited: 2
Yuyang Luo, Yixuan Li, Weiting Kong, et al.
Molecular Catalysis (2023) Vol. 553, pp. 113802-113802
Closed Access | Times Cited: 2
Construction of an enzymatic-chemical cascade involving engineered amine dehydrogenases for the synthesis of chiral non-α-amino acids by substrate engineering and enzyme evolution
Z. LAI, Tao Wu, Feng Zhou, et al.
Molecular Catalysis (2024) Vol. 559, pp. 114099-114099
Closed Access
Z. LAI, Tao Wu, Feng Zhou, et al.
Molecular Catalysis (2024) Vol. 559, pp. 114099-114099
Closed Access
Unlocking the Substrate Acceptance of Phenylalanine Amine Dehydrogenase Enables the Asymmetric Synthesis of Pharmaceutical N-Heterocyclic Primary Amines
Tao Wu, Yao Nie, Jiaxing Xu, et al.
ACS Catalysis (2024), pp. 877-888
Closed Access
Tao Wu, Yao Nie, Jiaxing Xu, et al.
ACS Catalysis (2024), pp. 877-888
Closed Access
