Deepankar Gahloth

513 total citations
18 papers, 409 citations indexed

About

Deepankar Gahloth is a scholar working on Molecular Biology, Biotechnology and Cell Biology. According to data from OpenAlex, Deepankar Gahloth has authored 18 papers receiving a total of 409 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Biotechnology and 3 papers in Cell Biology. Recurrent topics in Deepankar Gahloth's work include Biochemical and biochemical processes (4 papers), Enzyme Catalysis and Immobilization (4 papers) and Cellular transport and secretion (3 papers). Deepankar Gahloth is often cited by papers focused on Biochemical and biochemical processes (4 papers), Enzyme Catalysis and Immobilization (4 papers) and Cellular transport and secretion (3 papers). Deepankar Gahloth collaborates with scholars based in United Kingdom, India and United States. Deepankar Gahloth's co-authors include David Leys, Nicholas J. Turner, Mark S. Dunstan, Godwin A. Aleku, Sasha R. Derrington, Ashwani Kumar Sharma, Nigel S. Scrutton, Daniela Quaglia, Michael P. Lockhart‐Cairns and James L. Galman and has published in prestigious journals such as Journal of Biological Chemistry, Scientific Reports and Methods in enzymology on CD-ROM/Methods in enzymology.

In The Last Decade

Deepankar Gahloth

17 papers receiving 408 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Deepankar Gahloth United Kingdom 12 320 85 62 47 45 18 409
Anita Emmerstorfer‐Augustin Austria 13 418 1.3× 69 0.8× 87 1.4× 24 0.5× 47 1.0× 28 503
Wenchi Zhang China 13 384 1.2× 53 0.6× 29 0.5× 31 0.7× 48 1.1× 37 559
Tamara Wriessnegger Austria 10 535 1.7× 67 0.8× 100 1.6× 48 1.0× 44 1.0× 16 582
Tian Jiang China 17 536 1.7× 64 0.8× 98 1.6× 18 0.4× 32 0.7× 48 692
Jidong Wang China 12 199 0.6× 50 0.6× 21 0.3× 24 0.5× 69 1.5× 30 342
Simone Savino Netherlands 11 238 0.7× 41 0.5× 54 0.9× 18 0.4× 58 1.3× 18 328
Yongzhi He China 10 251 0.8× 56 0.7× 58 0.9× 23 0.5× 19 0.4× 14 334
Federica Rigoldi Italy 9 264 0.8× 83 1.0× 70 1.1× 18 0.4× 20 0.4× 12 367
Radu-Cristian Moldovan Romania 11 133 0.4× 43 0.5× 85 1.4× 41 0.9× 47 1.0× 28 446
S.R. Bharath India 12 319 1.0× 33 0.4× 18 0.3× 35 0.7× 36 0.8× 21 408

Countries citing papers authored by Deepankar Gahloth

Since Specialization
Citations

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

Fields of papers citing papers by Deepankar Gahloth

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Deepankar Gahloth

This figure shows the co-authorship network connecting the top 25 collaborators of Deepankar Gahloth. A scholar is included among the top collaborators of Deepankar Gahloth 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 Deepankar Gahloth. Deepankar Gahloth is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

18 of 18 papers shown
1.
Gahloth, Deepankar, Karl Fisher, Stephen Marshall, & David Leys. (2024). The prFMNH2-binding chaperone LpdD assists UbiD decarboxylase activation. Journal of Biological Chemistry. 300(2). 105653–105653. 2 indexed citations
2.
Gahloth, Deepankar, Karl Fisher, K.A.P. Payne, et al.. (2022). Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase. Journal of Biological Chemistry. 298(4). 101771–101771. 11 indexed citations
3.
Aleku, Godwin A., Sasha R. Derrington, Irina Gostimskaya, et al.. (2020). Enzymatic C–H activation of aromatic compounds through CO2 fixation. Nature Chemical Biology. 16(11). 1255–1260. 32 indexed citations
4.
Marshall, Stephen, K.A.P. Payne, Karl Fisher, et al.. (2019). Heterologous production, reconstitution and EPR spectroscopic analysis of prFMN dependent enzymes. Methods in enzymology on CD-ROM/Methods in enzymology. 620. 489–508. 9 indexed citations
5.
Gahloth, Deepankar, Godwin A. Aleku, & David Leys. (2019). Carboxylic acid reductase: Structure and mechanism. Journal of Biotechnology. 307. 107–113. 36 indexed citations
6.
Galman, James L., Deepankar Gahloth, Fabio Parmeggiani, et al.. (2018). Characterization of a Putrescine Transaminase From Pseudomonas putida and its Application to the Synthesis of Benzylamine Derivatives. Frontiers in Bioengineering and Biotechnology. 6. 205–205. 14 indexed citations
7.
Gahloth, Deepankar, Colin Levy, Louise A. Walker, et al.. (2017). Structural Basis for Specific Interaction of TGFβ Signaling Regulators SARA/Endofin with HD-PTP. Structure. 25(7). 1011–1024.e4. 13 indexed citations
8.
Gahloth, Deepankar, Mark S. Dunstan, Daniela Quaglia, et al.. (2017). Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis. Nature Chemical Biology. 13(9). 975–981. 120 indexed citations
9.
Gahloth, Deepankar, Thomas A. Jowitt, A. Paul Mould, et al.. (2017). The open architecture of HD-PTP phosphatase provides new insights into the mechanism of regulation of ESCRT function. Scientific Reports. 7(1). 9151–9151. 22 indexed citations
10.
Gahloth, Deepankar, Colin Levy, A. Paul Mould, et al.. (2016). Structural Basis for Selective Interaction between the ESCRT Regulator HD-PTP and UBAP1. Structure. 24(12). 2115–2126. 23 indexed citations
11.
Parmeggiani, Fabio, Syed T. Ahmed, Matthew P. Thompson, et al.. (2016). Single‐Biocatalyst Synthesis of Enantiopure d‐Arylalanines Exploiting an Engineered d‐Amino Acid Dehydrogenase. Advanced Synthesis & Catalysis. 358(20). 3298–3306. 54 indexed citations
12.
Mishra, Pushkar, et al.. (2014). Purification, Characterisation and Cloning of a 2S Albumin with DNase, RNase and Antifungal Activities from Putranjiva Roxburghii. Applied Biochemistry and Biotechnology. 174(2). 471–482. 19 indexed citations
13.
Gahloth, Deepankar, et al.. (2011). Molecular Evolution of Miraculin-Like Proteins in Soybean Kunitz Super-Family. Journal of Molecular Evolution. 73(5-6). 369–379. 20 indexed citations
14.
Gahloth, Deepankar, et al.. (2011). Bioinsecticidal activity of Murraya koenigii miraculin‐like protein against Helicoverpa armigera and Spodoptera litura. Archives of Insect Biochemistry and Physiology. 78(3). 132–144. 9 indexed citations
15.
Gahloth, Deepankar & Ashwani Kumar Sharma. (2010). Identification and Partial Characterization of Trypsin Inhibitory Activity in Seed of Some Fruit Plants. Journal of Plant Biochemistry and Biotechnology. 19(2). 235–237. 3 indexed citations
16.
Patel, Girijesh Kumar, et al.. (2010). Stability of Murraya koenigii miraculin-like protein in different physicochemical conditions. Medicinal Chemistry Research. 20(9). 1542–1549.
17.
Gahloth, Deepankar, et al.. (2009). Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii. Archives of Biochemistry and Biophysics. 494(1). 15–22. 20 indexed citations
18.
Shee, Chandan, et al.. (2008). Identification of a Peptide-like Compound with Antimicrobial and Trypsin Inhibitory Activity from Seeds of Bottle Gourd (Lagenaria siceraria). Journal of Plant Biochemistry and Biotechnology. 18(1). 101–104. 2 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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