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:
Resolving the Hydride Transfer Pathway in Oxidative Conversion of Proline to Pyrrole
Atanu Acharya, Dongqi Yi, Ànna Pavlova, et al.
Biochemistry (2022) Vol. 61, Iss. 3, pp. 206-215
Closed Access | Times Cited: 6
Atanu Acharya, Dongqi Yi, Ànna Pavlova, et al.
Biochemistry (2022) Vol. 61, Iss. 3, pp. 206-215
Closed Access | Times Cited: 6
Showing 6 citing articles:
Elucidation of Chalkophomycin Biosynthesis Reveals N-Hydroxypyrrole-Forming Enzymes
Anne Marie Crooke, Anika K. Chand, Zheng Cui, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 23, pp. 16268-16280
Open Access | Times Cited: 7
Anne Marie Crooke, Anika K. Chand, Zheng Cui, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 23, pp. 16268-16280
Open Access | Times Cited: 7
Elucidation of chalkophomycin biosynthesis revealsN-hydroxypyrrole-forming enzymes
Anne Marie Crooke, Anika K. Chand, Zheng Cui, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Anne Marie Crooke, Anika K. Chand, Zheng Cui, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Antibacterial Synnepyrroles from Human-Associated Nocardiopsis sp. Show Protonophore Activity and Disrupt the Bacterial Cytoplasmic Membrane
Lei Zhang, Lidia Alejo Esquembre, Shu-Ning Xia, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 10, pp. 2836-2848
Closed Access | Times Cited: 5
Lei Zhang, Lidia Alejo Esquembre, Shu-Ning Xia, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 10, pp. 2836-2848
Closed Access | Times Cited: 5
Essential Role of Loop Dynamics in Type II NRPS Biomolecular Recognition
Joshua C. Corpuz, Ashay Patel, Tony D. Davis, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 10, pp. 2890-2898
Open Access | Times Cited: 4
Joshua C. Corpuz, Ashay Patel, Tony D. Davis, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 10, pp. 2890-2898
Open Access | Times Cited: 4
Towards pharmaceutical protein stabilization: DFT and statistical learning studies on non-enzymatic peptide hydrolysis degradation mechanisms
Katherine E. Lawson, Joseph K. Dekle, Andrew J. Adamczyk
Computational and Theoretical Chemistry (2022) Vol. 1218, pp. 113938-113938
Closed Access | Times Cited: 3
Katherine E. Lawson, Joseph K. Dekle, Andrew J. Adamczyk
Computational and Theoretical Chemistry (2022) Vol. 1218, pp. 113938-113938
Closed Access | Times Cited: 3
peri-Interactions in 1,8-bis(dimethylamino)naphthalene ortho-ketimine cations facilitate [1,5]-hydride shift: selective synthesis of 1,2,3,4-tetrahydrobenzo[h]quinazolines
Vladimir Y. Mikshiev, Peter M. Tolstoy, Aleksandra M. Puzyk, et al.
Organic & Biomolecular Chemistry (2022) Vol. 20, Iss. 22, pp. 4559-4568
Closed Access | Times Cited: 2
Vladimir Y. Mikshiev, Peter M. Tolstoy, Aleksandra M. Puzyk, et al.
Organic & Biomolecular Chemistry (2022) Vol. 20, Iss. 22, pp. 4559-4568
Closed Access | Times Cited: 2
