Barış Bi̇nay

1.3k total citations
54 papers, 1.0k citations indexed

About

Barış Bi̇nay is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Barış Bi̇nay has authored 54 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 14 papers in Materials Chemistry and 11 papers in Biochemistry. Recurrent topics in Barış Bi̇nay's work include Enzyme Catalysis and Immobilization (30 papers), Enzyme Structure and Function (13 papers) and Amino Acid Enzymes and Metabolism (9 papers). Barış Bi̇nay is often cited by papers focused on Enzyme Catalysis and Immobilization (30 papers), Enzyme Structure and Function (13 papers) and Amino Acid Enzymes and Metabolism (9 papers). Barış Bi̇nay collaborates with scholars based in Türkiye, Finland and United Kingdom. Barış Bi̇nay's co-authors include Deniz Yıldırım, Ossi Turunen, Saadet Alpdağtaş, Nicholas J. Turner, Jarkko Valjakka, Burcu Gündüz Ergün, Nevin Gül Karagüler, Ayhan Çelik, Ersin Karataş and Patrick Fickers and has published in prestigious journals such as SHILAP Revista de lepidopterología, Journal of Cleaner Production and Tetrahedron.

In The Last Decade

Barış Bi̇nay

53 papers receiving 1.0k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Barış Bi̇nay Türkiye 21 770 222 155 123 122 54 1.0k
Ranjitha Singh South Korea 12 554 0.7× 205 0.9× 270 1.7× 106 0.9× 186 1.5× 15 1.0k
Jan Muschiol Denmark 19 809 1.1× 320 1.4× 81 0.5× 229 1.9× 82 0.7× 25 1.4k
Tuck Seng Wong United Kingdom 24 1.2k 1.6× 328 1.5× 63 0.4× 136 1.1× 114 0.9× 50 1.8k
Chunling Ma China 19 597 0.8× 188 0.8× 158 1.0× 228 1.9× 121 1.0× 74 1.2k
William R. Birmingham United Kingdom 17 639 0.8× 269 1.2× 49 0.3× 59 0.5× 71 0.6× 25 867
Raushan Kumar Singh South Korea 23 917 1.2× 471 2.1× 397 2.6× 269 2.2× 275 2.3× 52 1.8k
Aditya M. Kunjapur United States 20 950 1.2× 322 1.5× 183 1.2× 234 1.9× 60 0.5× 34 1.3k
Young Joo Yeon South Korea 16 422 0.5× 189 0.9× 101 0.7× 54 0.4× 67 0.5× 40 699
Marie Zarevúcká Czechia 17 560 0.7× 348 1.6× 41 0.3× 60 0.5× 94 0.8× 52 1.0k

Countries citing papers authored by Barış Bi̇nay

Since Specialization
Citations

This map shows the geographic impact of Barış Bi̇nay's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Barış Bi̇nay with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Barış Bi̇nay more than expected).

Fields of papers citing papers by Barış Bi̇nay

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Barış Bi̇nay. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Barış Bi̇nay. The network helps show where Barış Bi̇nay may publish in the future.

Co-authorship network of co-authors of Barış Bi̇nay

This figure shows the co-authorship network connecting the top 25 collaborators of Barış Bi̇nay. A scholar is included among the top collaborators of Barış Bi̇nay based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Barış Bi̇nay. Barış Bi̇nay is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Yıldırım, Deniz, et al.. (2025). A novel thermostable PETase from Kibdelosporangium aridum: Heterologous expression, immobilization and poly(ethelene terephthalate) decomposition applications. Journal of Cleaner Production. 510. 145624–145624. 4 indexed citations
2.
Valjakka, Jarkko, et al.. (2025). Novel Thermus thermophilus L-Alanine dehydrogenase mutants: Synthesis of L-alanine derivatives with reductive amination. International Journal of Biological Macromolecules. 319(Pt 4). 145507–145507.
3.
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Bi̇nay, Barış, et al.. (2023). Utilization potential of agro-industrial by-products and waste sources: Laccase production in bioreactor with Pichia pastoris. Biochemical Engineering Journal. 193. 108854–108854. 11 indexed citations
5.
Bi̇nay, Barış, et al.. (2023). Sustainable production of formic acid from CO2 by a novel immobilized mutant formate dehydrogenase. Separation and Purification Technology. 309. 123090–123090. 33 indexed citations
6.
Valjakka, Jarkko, et al.. (2023). Application of reductive amination by heterologously expressed Thermomicrobium roseum L-alanine dehydrogenase to synthesize L-alanine derivatives. Enzyme and Microbial Technology. 169. 110265–110265. 6 indexed citations
7.
Ergün, Burcu Gündüz, et al.. (2022). Second generation Pichia pastoris strain and bioprocess designs. SHILAP Revista de lepidopterología. 15(1). 150–150. 32 indexed citations
8.
Karataş, Ersin, et al.. (2021). From Secretion in Pichia pastoris to Application in Apple Juice Processing: Exo-Polygalacturonase from Sporothrix schenckii 1099-18. Protein and Peptide Letters. 28(7). 817–830. 3 indexed citations
9.
Bi̇nay, Barış, et al.. (2021). Antibacterial hybrid coatings from halloysite-immobilized lysostaphin and waterborne polyurethanes. Progress in Organic Coatings. 156. 106248–106248. 16 indexed citations
10.
Bi̇nay, Barış, et al.. (2021). Enhancing recombinant Chaetomium thermophilium Formate Dehydrogenase Expression with CRISPR Technology. The Protein Journal. 40(4). 504–511. 1 indexed citations
11.
Bulut, Huri, et al.. (2020). Effect of Metal Ions on the Activity of Ten NAD-Dependent Formate Dehydrogenases. The Protein Journal. 39(5). 519–530. 12 indexed citations
12.
Woodley, John M., et al.. (2020). High-level heterologous expression of active Chaetomium thermophilum FDH in Pichia pastoris. Enzyme and Microbial Technology. 137. 109552–109552. 12 indexed citations
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15.
Alpdağtaş, Saadet, et al.. (2018). Discovery of an acidic, thermostable and highly NADP+ dependent formate dehydrogenase from Lactobacillus buchneri NRRL B-30929. Biotechnology Letters. 40(7). 1135–1147. 35 indexed citations
16.
Yıldırım, Deniz, et al.. (2016). OUP accepted manuscript. Protein Engineering Design and Selection. 30(1). 47–55. 26 indexed citations
17.
Birmingham, William R., et al.. (2016). Semi-Rational Design of Geobacillus stearothermophilus L-Lactate Dehydrogenase to Access Various Chiral α-Hydroxy Acids. Applied Biochemistry and Biotechnology. 179(3). 474–484. 16 indexed citations
18.
Bi̇nay, Barış, Dilek Alagöz, Deniz Yıldırım, Ayhan Çelik, & S. Seyhan Tükel. (2016). Highly stable and reusable immobilized formate dehydrogenases: Promising biocatalysts for in situ regeneration of NADH. Beilstein Journal of Organic Chemistry. 12. 271–277. 27 indexed citations
19.
Bi̇nay, Barış, Richard B. Sessions, & Nevin Gül Karagüler. (2013). A double mutant of highly purified Geobacillus stearothermophilus lactate dehydrogenase recognises l-mandelic acid as a substrate. Enzyme and Microbial Technology. 52(6-7). 393–399. 9 indexed citations
20.
Bi̇nay, Barış & Nevin Gül Karagüler. (2007). Attempting to remove the substrate inhibition ofL-lactate dehydrogenase fromBacillus stearothermophilus by site-directed mutagenesis. Applied Biochemistry and Biotechnology. 141(2-3). 265–272. 12 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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