Laishram Rajendrakumar Singh

1.2k total citations
42 papers, 876 citations indexed

About

Laishram Rajendrakumar Singh is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Laishram Rajendrakumar Singh has authored 42 papers receiving a total of 876 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Cell Biology. Recurrent topics in Laishram Rajendrakumar Singh's work include Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (10 papers) and Redox biology and oxidative stress (6 papers). Laishram Rajendrakumar Singh is often cited by papers focused on Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (10 papers) and Redox biology and oxidative stress (6 papers). Laishram Rajendrakumar Singh collaborates with scholars based in India, United States and Saudi Arabia. Laishram Rajendrakumar Singh's co-authors include Tanveer Ali Dar, Faizan Ahmad, Nitesh Kumar Poddar, Sangeeta Goomer, Safikur Rahman, Hamidur Rahaman, Raj Kumar, Pervaiz Dar, Gurumayum Suraj Sharma and Liqun Wang and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Scientific Reports.

In The Last Decade

Laishram Rajendrakumar Singh

42 papers receiving 870 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Laishram Rajendrakumar Singh India 17 532 120 105 97 90 42 876
Hiroshi Ueno Japan 18 423 0.8× 55 0.5× 88 0.8× 104 1.1× 148 1.6× 82 905
Sohei Ito Japan 24 993 1.9× 203 1.7× 111 1.1× 106 1.1× 146 1.6× 78 1.6k
Jarl Underhaug Norway 19 570 1.1× 107 0.9× 50 0.5× 58 0.6× 36 0.4× 41 869
Sutton Mooney United States 11 342 0.6× 68 0.6× 44 0.4× 39 0.4× 79 0.9× 16 723
Jamshid Davoodi Iran 19 1.1k 2.1× 94 0.8× 28 0.3× 93 1.0× 88 1.0× 46 1.7k
Hai‐Meng Zhou China 19 740 1.4× 228 1.9× 46 0.4× 139 1.4× 59 0.7× 56 1.0k
Joong Myung Cho South Korea 19 930 1.7× 100 0.8× 79 0.8× 59 0.6× 175 1.9× 36 1.3k
Beatrice Cobucci‐Ponzano Italy 24 950 1.8× 126 1.1× 35 0.3× 55 0.6× 198 2.2× 60 1.5k
V. Gadjeva Bulgaria 20 332 0.6× 157 1.3× 61 0.6× 31 0.3× 96 1.1× 62 1.1k
C. Salerno Italy 18 509 1.0× 52 0.4× 28 0.3× 69 0.7× 117 1.3× 69 914

Countries citing papers authored by Laishram Rajendrakumar Singh

Since Specialization
Citations

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

Fields of papers citing papers by Laishram Rajendrakumar Singh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Laishram Rajendrakumar Singh. 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 Laishram Rajendrakumar Singh. The network helps show where Laishram Rajendrakumar Singh may publish in the future.

Co-authorship network of co-authors of Laishram Rajendrakumar Singh

This figure shows the co-authorship network connecting the top 25 collaborators of Laishram Rajendrakumar Singh. A scholar is included among the top collaborators of Laishram Rajendrakumar Singh 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 Laishram Rajendrakumar Singh. Laishram Rajendrakumar Singh 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.
Rahaman, Hamidur, et al.. (2023). Structural and Functional Diversity of the Peroxiredoxin 6 Enzyme Family. Antioxidants and Redox Signaling. 40(13-15). 759–775. 9 indexed citations
2.
Rahaman, Hamidur, et al.. (2021). pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature. Scientific Reports. 11(1). 9657–9657. 17 indexed citations
3.
Sharma, Gurumayum Suraj, et al.. (2021). Structural and Functional Characterization of Covalently Modified Proteins Formed By a Glycating Agent, Glyoxal. ACS Omega. 6(32). 20887–20894. 8 indexed citations
4.
Ahmad, Khurshid, et al.. (2020). N-Acetylaspartate Is an Important Brain Osmolyte. Biomolecules. 10(2). 286–286. 16 indexed citations
5.
6.
Rahaman, Hamidur, et al.. (2020). Structural basis of peroxidase catalytic cycle of human Prdx6. Scientific Reports. 10(1). 17416–17416. 19 indexed citations
7.
Potshangbam, Angamba Meetei, et al.. (2019). Hyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State. Antioxidants. 8(2). 33–33. 18 indexed citations
8.
Rahman, Safikur, et al.. (2019). The Extracellular Protein, Transthyretin Is an Oxidative Stress Biomarker. Frontiers in Physiology. 10. 5–5. 54 indexed citations
9.
Rehman, Md Tabish, et al.. (2018). Osmolytes in vaccine production, flocculation and storage: a critical review. Human Vaccines & Immunotherapeutics. 15(2). 514–525. 8 indexed citations
10.
Rahaman, Hamidur, et al.. (2017). UNDERSTANDING STRUCTURAL BASIS FOR REDOX REGULATION OF PEROXIREDOXIN 6 USING IN SILICO APPROACH. Journal of Proteins and Proteomics. 8(4). 2 indexed citations
11.
Singh, Laishram Rajendrakumar & Tanveer Ali Dar. (2017). Cellular Osmolytes. DIAL (Catholic University of Leuven). 7 indexed citations
12.
Sharma, Gurumayum Suraj, et al.. (2015). Effect of Dextran 70 on the thermodynamic and structural properties of proteins. International Journal of Biological Macromolecules. 79. 86–94. 14 indexed citations
13.
Dar, Tanveer Ali, et al.. (2014). Ignored Avenues in Alpha-Synuclein Associated Proteopathy. CNS & Neurological Disorders - Drug Targets. 13(7). 1246–1257. 6 indexed citations
14.
Dar, Tanveer Ali, et al.. (2013). RECENT TRENDS IN TREATING NEURONAL PROTEINOPATHIES. Journal of Proteins and Proteomics. 4(2). 1 indexed citations
15.
Singh, Laishram Rajendrakumar, et al.. (2013). POLYAMINES IN MODULATING PROTEIN AGGREGATION. Journal of Proteins and Proteomics. 3(2). 13 indexed citations
16.
Singh, Laishram Rajendrakumar, et al.. (2013). Denatured State Structural Property Determines Protein Stabilization by Macromolecular Crowding: A Thermodynamic and Structural Approach. PLoS ONE. 8(11). e78936–e78936. 47 indexed citations
17.
Singh, Laishram Rajendrakumar, Nitesh Kumar Poddar, Tanveer Ali Dar, Raj Kumar, & Faizan Ahmad. (2010). Protein and DNA destabilization by osmolytes: The other side of the coin. Life Sciences. 88(3-4). 117–125. 87 indexed citations
18.
Jamal, Shazia, Nitesh Kumar Poddar, Laishram Rajendrakumar Singh, et al.. (2009). Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes. FEBS Journal. 276(20). 6024–6032. 48 indexed citations
19.
Singh, Laishram Rajendrakumar, Tanveer Ali Dar, & Faizan Ahmad. (2009). Living with urea stress. Journal of Biosciences. 34(2). 321–331. 12 indexed citations
20.
Majtán, Tomáš, Laishram Rajendrakumar Singh, Liqun Wang, Warren D. Kruger, & Jan P. Kraus. (2008). Active Cystathionine β-Synthase Can Be Expressed in Heme-free Systems in the Presence of Metal-substituted Porphyrins or a Chemical Chaperone. Journal of Biological Chemistry. 283(50). 34588–34595. 53 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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