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:
Allostery, engineering and inhibition of tryptophan synthase
Rebecca N. D’Amico, David D. Boehr
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102657-102657
Closed Access | Times Cited: 4
Rebecca N. D’Amico, David D. Boehr
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102657-102657
Closed Access | Times Cited: 4
Showing 4 citing articles:
Fungi Tryptophan Synthases: What Is the Role of the Linker Connecting the α and β Structural Domains in Hemileia vastatrix TRPS? A Molecular Dynamics Investigation
N. F. Martins, Marcos Viana, Bernard Maigret
Molecules (2024) Vol. 29, Iss. 4, pp. 756-756
Open Access | Times Cited: 1
N. F. Martins, Marcos Viana, Bernard Maigret
Molecules (2024) Vol. 29, Iss. 4, pp. 756-756
Open Access | Times Cited: 1
Tryptophan production by catalysis of a putative tryptophan synthase protein
Lulu Cao, Jiaqi Zhang, Jia Chen, et al.
Archives of Microbiology (2024) Vol. 206, Iss. 9
Closed Access | Times Cited: 1
Lulu Cao, Jiaqi Zhang, Jia Chen, et al.
Archives of Microbiology (2024) Vol. 206, Iss. 9
Closed Access | Times Cited: 1
Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit
Cristina Duran, Thomas Kinateder, Caroline Hiefinger, et al.
ACS Catalysis (2024) Vol. 14, Iss. 22, pp. 16986-16995
Closed Access | Times Cited: 1
Cristina Duran, Thomas Kinateder, Caroline Hiefinger, et al.
ACS Catalysis (2024) Vol. 14, Iss. 22, pp. 16986-16995
Closed Access | Times Cited: 1
Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them
Subhadra Dalwani, A. Metz, Franziska U. Huschmann, et al.
Acta Crystallographica Section D Structural Biology (2024) Vol. 80, Iss. 8, pp. 605-619
Open Access
Subhadra Dalwani, A. Metz, Franziska U. Huschmann, et al.
Acta Crystallographica Section D Structural Biology (2024) Vol. 80, Iss. 8, pp. 605-619
Open Access
