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:
Functional characterization of PLP fold type IV transaminase with a mixed type of activity from Haliangium ochraceum
Yulia S. Zeifman, Konstantin M. Boyko, A.Y. Nikolaeva, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2019) Vol. 1867, Iss. 6, pp. 575-585
Closed Access | Times Cited: 18
Yulia S. Zeifman, Konstantin M. Boyko, A.Y. Nikolaeva, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2019) Vol. 1867, Iss. 6, pp. 575-585
Closed Access | Times Cited: 18
Showing 18 citing articles:
Structural insight into the substrate specificity of PLP fold type IV transaminases
Ekaterina Yu. Bezsudnova, Vladimir O. Popov, Konstantin M. Boyko
Applied Microbiology and Biotechnology (2020) Vol. 104, Iss. 6, pp. 2343-2357
Closed Access | Times Cited: 42
Ekaterina Yu. Bezsudnova, Vladimir O. Popov, Konstantin M. Boyko
Applied Microbiology and Biotechnology (2020) Vol. 104, Iss. 6, pp. 2343-2357
Closed Access | Times Cited: 42
Non-Canonical Amino Acid-Based Engineering of (R)-Amine Transaminase
Amol D. Pagar, Hyunwoo Jeon, Taresh P. Khobragade, et al.
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 18
Amol D. Pagar, Hyunwoo Jeon, Taresh P. Khobragade, et al.
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 18
Creation of (R)-Amine Transaminase Activity within an α-Amino Acid Transaminase Scaffold
Moritz Voß, Chao Xiang, Jérémy Esque, et al.
ACS Chemical Biology (2020) Vol. 15, Iss. 2, pp. 416-424
Open Access | Times Cited: 27
Moritz Voß, Chao Xiang, Jérémy Esque, et al.
ACS Chemical Biology (2020) Vol. 15, Iss. 2, pp. 416-424
Open Access | Times Cited: 27
The Uncommon Active Site of D-Amino Acid Transaminase from Haliscomenobacter hydrossis: Biochemical and Structural Insights into the New Enzyme
Alina K. Bakunova, A.Y. Nikolaeva, Tatiana V. Rakitina, et al.
Molecules (2021) Vol. 26, Iss. 16, pp. 5053-5053
Open Access | Times Cited: 22
Alina K. Bakunova, A.Y. Nikolaeva, Tatiana V. Rakitina, et al.
Molecules (2021) Vol. 26, Iss. 16, pp. 5053-5053
Open Access | Times Cited: 22
Root-soil-microbiome interaction in the rhizosphere of Masson pine (Pinus massoniana) under different levels of heavy metal pollution
Yingjie Wu, Haidong Wang, Peng Lü, et al.
Ecotoxicology and Environmental Safety (2024) Vol. 283, pp. 116779-116779
Open Access | Times Cited: 2
Yingjie Wu, Haidong Wang, Peng Lü, et al.
Ecotoxicology and Environmental Safety (2024) Vol. 283, pp. 116779-116779
Open Access | Times Cited: 2
Expanding the Toolbox of R‐Selective Amine Transaminases by Identification and Characterization of New Members
Aline Telzerow, Juraj Paris, M. Håkansson, et al.
ChemBioChem (2020) Vol. 22, Iss. 7, pp. 1232-1242
Open Access | Times Cited: 17
Aline Telzerow, Juraj Paris, M. Håkansson, et al.
ChemBioChem (2020) Vol. 22, Iss. 7, pp. 1232-1242
Open Access | Times Cited: 17
Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase from Chloroflexi bacterium
Chen Wang, Kexin Tang, Ya Dai, et al.
ACS Omega (2021) Vol. 6, Iss. 26, pp. 17058-17070
Open Access | Times Cited: 13
Chen Wang, Kexin Tang, Ya Dai, et al.
ACS Omega (2021) Vol. 6, Iss. 26, pp. 17058-17070
Open Access | Times Cited: 13
Exemplifying Natural (R)-β-Transamination Potential of Fold Type-IV Transaminase for Kinetic Resolution of rac-β-Amino Acids Synthesized from Aldehydes
Amol D. Pagar, Taresh P. Khobragade, Pritam Giri, et al.
ACS Sustainable Chemistry & Engineering (2024) Vol. 12, Iss. 19, pp. 7226-7234
Closed Access | Times Cited: 1
Amol D. Pagar, Taresh P. Khobragade, Pritam Giri, et al.
ACS Sustainable Chemistry & Engineering (2024) Vol. 12, Iss. 19, pp. 7226-7234
Closed Access | Times Cited: 1
Metagenomic Type IV Aminotransferases Active toward (R)-Methylbenzylamine
Rokas Statkevičius, Justas Vaitekūnas, Rūta Stanislauskienė, et al.
Catalysts (2023) Vol. 13, Iss. 3, pp. 587-587
Open Access | Times Cited: 2
Rokas Statkevičius, Justas Vaitekūnas, Rūta Stanislauskienė, et al.
Catalysts (2023) Vol. 13, Iss. 3, pp. 587-587
Open Access | Times Cited: 2
Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from Blastococcus saxobsidens
Sofia A. Shilova, Ilya O. Matyuta, Elizaveta S. Petrova, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 22, pp. 16194-16194
Open Access | Times Cited: 2
Sofia A. Shilova, Ilya O. Matyuta, Elizaveta S. Petrova, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 22, pp. 16194-16194
Open Access | Times Cited: 2
Efficient Synthesis of Key Chiral Intermediate in Painkillers (R)-1-[3,5-Bis(trifluoromethyl)phenyl]ethanamine by Bienzyme Cascade System with R-ω-Transaminase and Alcohol Dehydrogenase Functions
Lu Yuan, Jinmei Wang, Haobo Xu, et al.
Molecules (2022) Vol. 27, Iss. 21, pp. 7331-7331
Open Access | Times Cited: 4
Lu Yuan, Jinmei Wang, Haobo Xu, et al.
Molecules (2022) Vol. 27, Iss. 21, pp. 7331-7331
Open Access | Times Cited: 4
Discovery of Novel R-Selective Aminotransferase Motifs through Computational Screening
Ashish Runthala, Pulla Sai Satya Sri, Aayush Sasikumar Nair, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Ashish Runthala, Pulla Sai Satya Sri, Aayush Sasikumar Nair, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Decoding transaminase motifs: Tracing the unknown patterns for enhancing the accuracy of computational screening methodologies
Ashish Runthala, Pulla Sai Satya Sri, Aayush Sasikumar Nair, et al.
Gene (2024), pp. 149091-149091
Closed Access
Ashish Runthala, Pulla Sai Satya Sri, Aayush Sasikumar Nair, et al.
Gene (2024), pp. 149091-149091
Closed Access
The Promising Role of Amine Transaminase Cascades in the Synthesis of Non-Canonical Amino Acids
Najme Gord Noshahri, Jens Rudat
Processes (2024) Vol. 12, Iss. 11, pp. 2566-2566
Open Access
Najme Gord Noshahri, Jens Rudat
Processes (2024) Vol. 12, Iss. 11, pp. 2566-2566
Open Access
From Structure to Function: Analysis of the First Monomeric Pyridoxal-5′-Phosphate-Dependent Transaminase from the Bacterium Desulfobacula toluolica
Alina K. Bakunova, Ilya O. Matyuta, A.Y. Nikolaeva, et al.
Biomolecules (2024) Vol. 14, Iss. 12, pp. 1591-1591
Open Access
Alina K. Bakunova, Ilya O. Matyuta, A.Y. Nikolaeva, et al.
Biomolecules (2024) Vol. 14, Iss. 12, pp. 1591-1591
Open Access
Three-Dimensional Structure of Branched-Chain Amino Acid Transaminase from Thermoproteus uzoniensis in Complex with L-Norvaline
Konstantin M. Boyko, A.Y. Nikolaeva, В. И. Тимофеев, et al.
Crystallography Reports (2020) Vol. 65, Iss. 5, pp. 740-743
Closed Access | Times Cited: 2
Konstantin M. Boyko, A.Y. Nikolaeva, В. И. Тимофеев, et al.
Crystallography Reports (2020) Vol. 65, Iss. 5, pp. 740-743
Closed Access | Times Cited: 2
Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum
Ekaterina Yu. Bezsudnova, A.Y. Nikolaeva, Alina K. Bakunova, et al.
PLoS ONE (2021) Vol. 16, Iss. 7, pp. e0255098-e0255098
Open Access | Times Cited: 2
Ekaterina Yu. Bezsudnova, A.Y. Nikolaeva, Alina K. Bakunova, et al.
PLoS ONE (2021) Vol. 16, Iss. 7, pp. e0255098-e0255098
Open Access | Times Cited: 2
Identification, Characterization and Site-Saturation Mutagenesis of a Thermostable ω-Transaminase From Chloroflexi Bacterium
Chen Wang, Kexin Tang, Ya Dai, et al.
Research Square (Research Square) (2021)
Open Access
Chen Wang, Kexin Tang, Ya Dai, et al.
Research Square (Research Square) (2021)
Open Access
