Khosro Khajeh

1.5k total citations
67 papers, 1.2k citations indexed

About

Khosro Khajeh is a scholar working on Molecular Biology, Biotechnology and Plant Science. According to data from OpenAlex, Khosro Khajeh has authored 67 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 22 papers in Biotechnology and 16 papers in Plant Science. Recurrent topics in Khosro Khajeh's work include Enzyme Production and Characterization (17 papers), Enzyme Catalysis and Immobilization (14 papers) and bioluminescence and chemiluminescence research (8 papers). Khosro Khajeh is often cited by papers focused on Enzyme Production and Characterization (17 papers), Enzyme Catalysis and Immobilization (14 papers) and bioluminescence and chemiluminescence research (8 papers). Khosro Khajeh collaborates with scholars based in Iran, Australia and Hungary. Khosro Khajeh's co-authors include Bijan Ranjbar, Hossein Naderi‐Manesh, Saman Hosseinkhani, Mohammad Ali Amoozegar, Mahmoud Shavandi, Seyed Mohammad Mehdi Dastgheib, Mohsen Nemat‐Gorgani, António Ventosa, Nasrin Mollania and Ali Akbar Moosavi‐Movahedi and has published in prestigious journals such as SHILAP Revista de lepidopterología, Bioresource Technology and Scientific Reports.

In The Last Decade

Khosro Khajeh

65 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Khosro Khajeh Iran 21 696 338 224 180 173 67 1.2k
J. M. Khire India 25 1.2k 1.7× 508 1.5× 518 2.3× 549 3.0× 147 0.8× 57 1.9k
Jozef Nahálka Slovakia 21 921 1.3× 196 0.6× 94 0.4× 162 0.9× 34 0.2× 51 1.3k
Xing Qin China 20 530 0.8× 239 0.7× 348 1.6× 198 1.1× 56 0.3× 69 1.3k
Tsutomu Fujii Japan 21 1.0k 1.5× 292 0.9× 310 1.4× 343 1.9× 52 0.3× 97 1.6k
Tamotsu Kanai Japan 27 1.8k 2.6× 330 1.0× 183 0.8× 291 1.6× 71 0.4× 82 2.5k
César A. Ramírez‐Sarmiento Chile 18 721 1.0× 111 0.3× 54 0.2× 191 1.1× 408 2.4× 56 1.4k
A. Tanaka Japan 22 1.0k 1.4× 292 0.9× 127 0.6× 278 1.5× 38 0.2× 58 1.5k
Maarten D. Sollewijn Gelpke United States 17 613 0.9× 406 1.2× 712 3.2× 334 1.9× 121 0.7× 26 1.8k
Han‐Seung Lee South Korea 20 531 0.8× 131 0.4× 130 0.6× 105 0.6× 21 0.1× 53 1.1k

Countries citing papers authored by Khosro Khajeh

Since Specialization
Citations

This map shows the geographic impact of Khosro Khajeh'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 Khosro Khajeh with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Khosro Khajeh more than expected).

Fields of papers citing papers by Khosro Khajeh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Khosro Khajeh. 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 Khosro Khajeh. The network helps show where Khosro Khajeh may publish in the future.

Co-authorship network of co-authors of Khosro Khajeh

This figure shows the co-authorship network connecting the top 25 collaborators of Khosro Khajeh. A scholar is included among the top collaborators of Khosro Khajeh 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 Khosro Khajeh. Khosro Khajeh 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.
Nabi‐Afjadi, Mohsen, Bahareh Dabirmanesh, S. Mohsen Asghari, et al.. (2025). Design, synthesis, and evaluation of the effect of potential peptides against CD38: An in silico and in vitro study. Biomedicine & Pharmacotherapy. 189. 118347–118347.
2.
Mohseni‐Dargah, Masoud, Christopher J. Pastras, Payal Mukherjee, et al.. (2024). Performance of personalised prosthesis under static pressure: Numerical analysis and experimental validation. Journal of the mechanical behavior of biomedical materials. 151. 106396–106396. 3 indexed citations
3.
Homaei, Ahmad, et al.. (2022). Production of a Novel Marine Pseudomonas aeruginosa Recombinant L-Asparaginase: Insight on the Structure and Biochemical Characterization. Marine Biotechnology. 24(3). 599–613. 45 indexed citations
4.
Amoozegar, Mohammad Ali, et al.. (2019). Isolation and screening of extracellular anticancer enzymes from halophilic and halotolerant bacteria from different saline environments in Iran. Molecular Biology Reports. 46(3). 3275–3286. 35 indexed citations
5.
Badoei-Dalfard, Arastoo, Khosro Khajeh, & Zahra Karami. (2019). Protein Engineering of a Metalloprotease in Order to Improve Organic Solvents Stability and Activity. Catalysis Letters. 150(5). 1219–1229. 6 indexed citations
6.
Mollania, Nasrin, et al.. (2017). Chromium bioremediation by Alcaligenes sp. strain newly isolated from chromite mine of Sabzevar. SHILAP Revista de lepidopterología. 5(4). 220–232. 3 indexed citations
7.
Farnoosh, Gholamreza, Ali Mohammad Latifi, Khosro Khajeh, Hossein Aghamollaei, & Ali Najafi. (2016). Enzymatic Degradation of Organophosphate Compounds: Evaluation of High-level Production, Solubility and Stability. 2(4). 339–344. 3 indexed citations
8.
Latifi, Ali Mohammad, et al.. (2015). The Cytoplasmic and Periplasmic Expression Levels and Folding of Organophosphorus Hydrolase Enzyme in Escherichia coli. Jundishapur Journal of Microbiology. 8(12). e17790–e17790. 15 indexed citations
9.
Zarinkamar, Fatemeh, et al.. (2014). A study of the changes in laccase activity of Festuca's vegetative organs under petroleum pollution conditions. 5(2). 1–5. 1 indexed citations
10.
Ghollasi, Marzieh, et al.. (2013). Improvement of thermal stability of a mutagenised α-amylase by manipulation of the calcium-binding site. Enzyme and Microbial Technology. 53(6-7). 406–413. 22 indexed citations
11.
12.
Asghari, S. Mohsen, Khosro Khajeh, Arastoo Badoei-Dalfard, Mohammad Pazhang, & Hamid Reza Karbalaei‐Heidari. (2011). Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium. BMB Reports. 44(10). 665–668. 3 indexed citations
13.
Ghollasi, Marzieh, Khosro Khajeh, Hossein Naderi‐Manesh, & Atiyeh Ghasemi. (2010). Engineering of a Bacillus α-Amylase with Improved Thermostability and Calcium Independency. Applied Biochemistry and Biotechnology. 162(2). 444–459. 23 indexed citations
14.
Khajeh, Khosro, Bijan Ranjbar, Hossein Naderi‐Manesh, et al.. (2010). Structure ofBacillus amyloliquefaciensα-amylase at high resolution: implications for thermal stability. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(2). 121–129. 50 indexed citations
15.
Ataei, Farangis, Saman Hosseinkhani, & Khosro Khajeh. (2009). Limited Proteolysis of Luciferase as a Reporter in Nanosystem Biology: A Comparative Study. Photochemistry and Photobiology. 85(5). 1162–1167. 16 indexed citations
16.
Aminzadeh, Saeed, et al.. (2007). Isolation and Characterization of Polygalacturonase Produced by Tetracoccosporium sp.. Iranian Journal of Chemistry & Chemical Engineering-international English Edition. 26(1). 47–54. 11 indexed citations
17.
Gholivand, Khodayar, et al.. (2006). Anticholinesterase activity of some major intermediates in carbacylamidophosphate synthesis: Preparation, spectral characterization and inhibitory potency determination. Journal of Enzyme Inhibition and Medicinal Chemistry. 21(1). 105–111. 11 indexed citations
18.
Mirshahi, Manouchehr, et al.. (2006). A novel monoclonal antibody with catalytic activity against beta human chorionic gonadotropin. Immunology Letters. 106(1). 57–62. 2 indexed citations
19.
Gholivand, Khodayar, Zahra Shariatinia‬, Khosro Khajeh, & Hossein Naderi‐Manesh. (2006). Syntheses and spectroscopic characterization of some phosphoramidates as reversible inhibitors of human acetylcholinesterase and determination of their potency. Journal of Enzyme Inhibition and Medicinal Chemistry. 21(1). 31–35. 20 indexed citations
20.
Karbalaei‐Heidari, Hamid Reza, Azadeh Ebrahim‐Habibi, Khosro Khajeh, Bijan Ranjbar, & Mohsen Nemat‐Gorgani. (2004). Interaction of an Intermediate Structure of <I>Bacillus subtilis</I> α-Amylase With Alkyl-Substituted Sepharose 4B: A Model of Membrane Translocation. Applied Biochemistry and Biotechnology. 117(2). 123–132. 3 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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