Muhammad Akhtar

3.4k total citations
164 papers, 2.7k citations indexed

About

Muhammad Akhtar is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, Muhammad Akhtar has authored 164 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 101 papers in Molecular Biology, 38 papers in Biotechnology and 31 papers in Biomedical Engineering. Recurrent topics in Muhammad Akhtar's work include Enzyme Production and Characterization (32 papers), Biofuel production and bioconversion (29 papers) and Enzyme Structure and Function (24 papers). Muhammad Akhtar is often cited by papers focused on Enzyme Production and Characterization (32 papers), Biofuel production and bioconversion (29 papers) and Enzyme Structure and Function (24 papers). Muhammad Akhtar collaborates with scholars based in Pakistan, United Kingdom and United States. Muhammad Akhtar's co-authors include Muhammed Iqbal, Asma Saeed, Naeem Rashid, Peter M. Jordan, Kalsoom Akhtar, Ahmad Mukhtar Khalid, Saima Sadaf, A.M. Khalid, J. Neville Wright and Muhammad Sajjad and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Journal of Neuroscience.

In The Last Decade

Muhammad Akhtar

154 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Muhammad Akhtar Pakistan 25 1.3k 495 467 452 258 164 2.7k
Na Wei United States 36 2.4k 1.8× 181 0.4× 1.3k 2.8× 228 0.5× 131 0.5× 137 4.4k
Kohsuke Honda Japan 28 1.7k 1.3× 116 0.2× 509 1.1× 221 0.5× 293 1.1× 126 2.4k
Min Wang China 34 754 0.6× 105 0.2× 482 1.0× 140 0.3× 235 0.9× 180 3.3k
Dandan Zhang China 31 1.6k 1.2× 246 0.5× 386 0.8× 83 0.2× 314 1.2× 110 3.5k
Haiyan Yu China 27 1.3k 1.0× 208 0.4× 321 0.7× 100 0.2× 239 0.9× 96 2.9k
Abha Sharma India 31 1.7k 1.3× 163 0.3× 209 0.4× 186 0.4× 208 0.8× 129 4.4k
Gary J. Lye United Kingdom 37 2.8k 2.1× 223 0.5× 1.9k 4.1× 253 0.6× 309 1.2× 152 4.4k
Jianhua Huang China 33 1.0k 0.8× 194 0.4× 461 1.0× 108 0.2× 191 0.7× 126 3.8k
Yingping Zhuang China 38 3.2k 2.4× 164 0.3× 1.5k 3.2× 538 1.2× 210 0.8× 284 4.8k
Sathyanarayana N. Gummadi India 28 1.3k 1.0× 145 0.3× 806 1.7× 480 1.1× 210 0.8× 159 3.1k

Countries citing papers authored by Muhammad Akhtar

Since Specialization
Citations

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

Fields of papers citing papers by Muhammad Akhtar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Muhammad Akhtar

This figure shows the co-authorship network connecting the top 25 collaborators of Muhammad Akhtar. A scholar is included among the top collaborators of Muhammad Akhtar 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 Muhammad Akhtar. Muhammad Akhtar 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.
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Rajan, Ronnie, et al.. (2025). Population-scale cross-sectional observational study for AI-powered TB screening on one million CXRs. npj Digital Medicine. 8(1). 418–418. 1 indexed citations
3.
Mikolajek, Halina, Peter J. Harrison, Neil G. Paterson, et al.. (2024). Structural and functional snapshots of a broad-specificity endoglucanase from Thermogutta terrifontis for biomass saccharification. Archives of Biochemistry and Biophysics. 764. 110274–110274. 3 indexed citations
4.
Abo‐Dahab, S. M., Aftab Ahmad Khan, A. M. Abd-Alla, Muhammad Akhtar, & A. A. Kilany. (2023). Magneto-thermoelastic surface waves in a rotating nonhomogeneous electrically conducting fiber-reinforced anisotropic general viscoelastic media of higher order with voids and gravity under four theories. Waves in Random and Complex Media. 1–28. 1 indexed citations
5.
Akhtar, Muhammad, et al.. (2023). SPEECH AND LANGUAGE IMPAIRMENT AFTER CHILDHOOD ARTERIAL ISCHEMIC STROKE. SHILAP Revista de lepidopterología. 73(1). 143–46. 1 indexed citations
6.
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Batool, Sana, et al.. (2023). Improved catalytic efficiency of chimeric xylanase 10B from Thermotoga petrophila RKU1 and its synergy with cellulases. Enzyme and Microbial Technology. 166. 110213–110213. 6 indexed citations
8.
Sajjad, Muhammad, Hisham N. Altayb, Syed Sarim Imam, et al.. (2022). Engineering processive cellulase of Clostridium thermocellum to divulge the role of the carbohydrate‐binding module. Biotechnology and Applied Biochemistry. 70(1). 290–305. 4 indexed citations
9.
Bijnsdorp, Irene V., Franziska Böttger, Sander R. Piersma, et al.. (2022). Secreted protein markers in oral squamous cell carcinoma (OSCC). Clinical Proteomics. 19(1). 4–4. 19 indexed citations
10.
Ali, Imran, Hafiz Muzzammel Rehman, Muhammad Usman Mirza, et al.. (2020). Enhanced Thermostability and Enzymatic Activity of cel6A Variants from Thermobifida fusca by Empirical Domain Engineering. Biology. 9(8). 214–214. 8 indexed citations
11.
Akram, Afia Muhammad, Humera Kausar, Asma Chaudhary, et al.. (2018). Detection of Exon 12 and 14 Mutations in Janus Kinase 2 Gene Including a Novel Mutant in V617F Negative Polycythemia Vera Patients from Pakistan. Journal of Cancer. 9(23). 4341–4345. 2 indexed citations
12.
Rashid, Naeem, et al.. (2017). Escherichia coli signal peptidase recognizes and cleaves archaeal signal sequence. Biochemistry (Moscow). 82(7). 821–825. 3 indexed citations
13.
Rashid, Naeem, et al.. (2017). Preventing the N-terminal processing of human interferon α-2b and its chimeric derivatives expressed in Escherichia coli. Bioorganic Chemistry. 76. 294–302. 6 indexed citations
14.
Butler, Danica, Darren A. Thompson, Mohammed G. Sarwar, et al.. (2016). Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans,Escherichia coliand the hyperthermophilePyrobaculum calidifontis. Acta Crystallographica Section D Structural Biology. 73(1). 9–21. 24 indexed citations
15.
Malik, Bela, Naeem Rashid, Nasir Ahmad, & Muhammad Akhtar. (2013). Escherichia coli signal peptidase recognizes and cleaves the signal sequence of α-amylase originating from Bacillus licheniformis. Biochemistry (Moscow). 78(8). 958–962. 3 indexed citations
16.
Riaz, Samreen, et al.. (2010). Proteomic Identification of Human Urinary Biomarkers in Diabetes Mellitus Type 2. Diabetes Technology & Therapeutics. 12(12). 979–988. 32 indexed citations
17.
Tayyab, Muhammad, Naeem Rashid, & Muhammad Akhtar. (2010). Isolation and identification of lipase producing thermophilic Geobacillus sp. SBS-4S: Cloning and characterization of the lipase. Journal of Bioscience and Bioengineering. 111(3). 272–278. 44 indexed citations
18.
Awan, Muhammad Siddique, et al.. (2009). Production and Characterization of α-Galactosidase by a Multiple Mutant of Aspergillus niger in Solid-State Fermentation. SHILAP Revista de lepidopterología. 7 indexed citations
19.
Sajjad, Muhammad, et al.. (2009). Enhanced expression and activity yields of Clostridium thermocellum xylanases without non-catalytic domains. Journal of Biotechnology. 145(1). 38–42. 31 indexed citations
20.
Akhtar, Muhammad, et al.. (1993). Phosphorylatio of solubilised dark‐adapted rhodopsin. European Journal of Biochemistry. 213(2). 881–890. 17 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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