Ghader Bashiri

1.7k total citations
51 papers, 1.3k citations indexed

About

Ghader Bashiri is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Ghader Bashiri has authored 51 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 21 papers in Materials Chemistry and 19 papers in Infectious Diseases. Recurrent topics in Ghader Bashiri's work include Biochemical and Molecular Research (27 papers), Enzyme Structure and Function (21 papers) and Tuberculosis Research and Epidemiology (19 papers). Ghader Bashiri is often cited by papers focused on Biochemical and Molecular Research (27 papers), Enzyme Structure and Function (21 papers) and Tuberculosis Research and Epidemiology (19 papers). Ghader Bashiri collaborates with scholars based in New Zealand, United States and China. Ghader Bashiri's co-authors include Edward N. Baker, Nicole J. Moreland, C.J. Squire, Aisyah Mohamed Rehan, David Greenwood, James M. Dickson, Jonathan Sperry, Ivanhoe K. H. Leung, J. Shaun Lott and Yi Tang and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Ghader Bashiri

50 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
Ghader Bashiri New Zealand 22 852 364 269 261 219 51 1.3k
Leslie W. Tari Canada 21 1.2k 1.4× 102 0.3× 73 0.3× 153 0.6× 308 1.4× 40 1.8k
Francis Blanche France 34 2.2k 2.6× 201 0.6× 88 0.3× 311 1.2× 257 1.2× 60 2.7k
Adolfo M. Iribarren Argentina 21 1.4k 1.6× 247 0.7× 183 0.7× 46 0.2× 58 0.3× 96 1.6k
Ken-Ichi Oinuma Japan 18 494 0.6× 73 0.2× 103 0.4× 112 0.4× 80 0.4× 47 778
Robert van der Geize Netherlands 24 1.8k 2.1× 340 0.9× 152 0.6× 82 0.3× 161 0.7× 30 2.1k
Steffen Schaffer Germany 20 1.4k 1.6× 89 0.2× 65 0.2× 138 0.5× 259 1.2× 27 1.6k
Irina A. Rodionova United States 22 883 1.0× 111 0.3× 80 0.3× 32 0.1× 178 0.8× 36 1.3k
Tsung‐Lin Li Taiwan 23 733 0.9× 50 0.1× 54 0.2× 348 1.3× 86 0.4× 75 1.5k
Naoko Morisaki Japan 23 496 0.6× 204 0.6× 206 0.8× 279 1.1× 18 0.1× 69 1.5k
Juan Aguilar Spain 24 1.1k 1.3× 76 0.2× 82 0.3× 51 0.2× 316 1.4× 57 1.7k

Countries citing papers authored by Ghader Bashiri

Since Specialization
Citations

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

Fields of papers citing papers by Ghader Bashiri

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Ghader Bashiri

This figure shows the co-authorship network connecting the top 25 collaborators of Ghader Bashiri. A scholar is included among the top collaborators of Ghader Bashiri 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 Ghader Bashiri. Ghader Bashiri 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.
Bashiri, Ghader, Esther M. M. Bulloch, Paul G. Young, et al.. (2024). Poly-γ-glutamylation of biomolecules. Nature Communications. 15(1). 1310–1310. 4 indexed citations
2.
Zhang, Bo, Wanqing Wei, Jiapeng Zhu, et al.. (2022). AvmM catalyses macrocyclization through dehydration/Michael-type addition in alchivemycin A biosynthesis. Nature Communications. 13(1). 4499–4499. 13 indexed citations
3.
De, Bidhan Chandra, Wenjun Zhang, Chunfang Yang, et al.. (2022). Flavin-enabled reductive and oxidative epoxide ring opening reactions. Nature Communications. 13(1). 4896–4896. 21 indexed citations
4.
Barra, Lena, et al.. (2021). β-NAD as a building block in natural product biosynthesis. Nature. 600(7890). 754–758. 46 indexed citations
5.
Shi, Jing, Xiang Xu, Bo Zhang, et al.. (2021). Discovery and biosynthesis of guanipiperazine from a NRPS-like pathway. Chemical Science. 12(8). 2925–2930. 25 indexed citations
6.
Zhang, Bo, Lan Wang, Wen Wang, et al.. (2021). Redox Modifications in the Biosynthesis of Alchivemycin A Enable the Formation of Its Key Pharmacophore. Journal of the American Chemical Society. 143(12). 4751–4757. 14 indexed citations
7.
Bashiri, Ghader. (2021). Lipid transport across the mycobacterial cell envelope. IUCrJ. 8(5). 711–712. 1 indexed citations
8.
Rifat, Dalin, Si-Yang Li, Thomas R. Ioerger, et al.. (2020). Mutations in fbiD ( Rv2983 ) as a Novel Determinant of Resistance to Pretomanid and Delamanid in Mycobacterium tuberculosis. Antimicrobial Agents and Chemotherapy. 65(1). 56 indexed citations
9.
Bashiri, Ghader, Tyler L. Grove, Subray S. Hegde, et al.. (2019). The active site of the Mycobacterium tuberculosis branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase contains a 2Fe–2S cluster. Journal of Biological Chemistry. 294(35). 13158–13170. 16 indexed citations
10.
Bashiri, Ghader, Janine N. Copp, Brian D. Palmer, et al.. (2019). A revised biosynthetic pathway for the cofactor F420 in prokaryotes. Nature Communications. 10(1). 1558–1558. 51 indexed citations
11.
Bhusal, Ram Prasad, Wanting Jiao, Jóhannes Reynisson, et al.. (2019). Acetyl-CoA-mediated activation of Mycobacterium tuberculosis isocitrate lyase 2. Nature Communications. 10(1). 4639–4639. 23 indexed citations
12.
Bhusal, Ram Prasad, Krunal Patel, Ghader Bashiri, et al.. (2017). Development of NMR and thermal shift assays for the evaluation ofMycobacterium tuberculosisisocitrate lyase inhibitors. MedChemComm. 8(11). 2155–2163. 12 indexed citations
13.
Bhusal, Ram Prasad, et al.. (2017). Targeting isocitrate lyase for the treatment of latent tuberculosis. Drug Discovery Today. 22(7). 1008–1016. 43 indexed citations
14.
Gand, Martin, et al.. (2016). A NADH-accepting imine reductase variant: Immobilization and cofactor regeneration by oxidative deamination. Journal of Biotechnology. 230. 11–18. 35 indexed citations
15.
Bashiri, Ghader, Jodie M. Johnston, Genevieve L. Evans, et al.. (2015). Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex. Acta Crystallographica Section D Biological Crystallography. 71(11). 2297–2308. 20 indexed citations
16.
Bashiri, Ghader, et al.. (2014). Characterization of the proline-utilization pathway inMycobacterium tuberculosisthrough structural and functional studies. Acta Crystallographica Section D Biological Crystallography. 70(4). 968–980. 15 indexed citations
17.
18.
Wang, Peng, Ghader Bashiri, Xue Gao, M.R. Sawaya, & Yi Tang. (2013). Uncovering the Enzymes that Catalyze the Final Steps in Oxytetracycline Biosynthesis. Journal of the American Chemical Society. 135(19). 7138–7141. 77 indexed citations
19.
Dogra, Mridula, Ghader Bashiri, Malcolm D. Tingle, et al.. (2010). Comparative bioactivation of the novel anti‐tuberculosis agent PA‐824 inMycobacteriaand a subcellular fraction of human liver. British Journal of Pharmacology. 162(1). 226–236. 21 indexed citations
20.
Bashiri, Ghader, C.J. Squire, Edward N. Baker, & Nicole J. Moreland. (2007). Expression, purification and crystallization of native and selenomethionine labeled Mycobacterium tuberculosis FGD1 (Rv0407) using a Mycobacterium smegmatis expression system. Protein Expression and Purification. 54(1). 38–44. 38 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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