Deviprasad R. Gollapalli

1.2k total citations
28 papers, 948 citations indexed

About

Deviprasad R. Gollapalli is a scholar working on Molecular Biology, Epidemiology and Parasitology. According to data from OpenAlex, Deviprasad R. Gollapalli has authored 28 papers receiving a total of 948 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 14 papers in Epidemiology and 9 papers in Parasitology. Recurrent topics in Deviprasad R. Gollapalli's work include Biochemical and Molecular Research (14 papers), Retinal Development and Disorders (9 papers) and Parasitic Infections and Diagnostics (9 papers). Deviprasad R. Gollapalli is often cited by papers focused on Biochemical and Molecular Research (14 papers), Retinal Development and Disorders (9 papers) and Parasitic Infections and Diagnostics (9 papers). Deviprasad R. Gollapalli collaborates with scholars based in United States, South Africa and Italy. Deviprasad R. Gollapalli's co-authors include Lizbeth Hedstrom, Robert R. Rando, Pranab Maiti, Marcus J. C. Long, Linlong Xue, Wan Jin Jahng, Minjia Zhang, Gregory D. Cuny, Joanna B. Goldberg and George W. Liechti and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Deviprasad R. Gollapalli

27 papers receiving 939 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Deviprasad R. Gollapalli United States	17	752	261	176	164	132	28	948
Ernst Hempelmann South Africa	12	183 0.2×	41 0.2×	60 0.3×	51 0.3×	13 0.1×	15	647
Marisa E. McGrath United States	12	284 0.4×	187 0.7×	148 0.8×	32 0.2×	3 0.0×	19	655
Kristofor J. Webb United States	22	1.1k 1.5×	85 0.3×	104 0.6×	31 0.2×	3 0.0×	33	1.4k
Fred Widmer Australia	19	434 0.6×	262 1.0×	249 1.4×	27 0.2×	2 0.0×	28	912
Matthew S. Kelker United States	13	502 0.7×	110 0.4×	27 0.2×	11 0.1×	5 0.0×	14	1.0k
Kathrin Buchholz United States	12	167 0.2×	81 0.3×	67 0.4×	78 0.5×	3 0.0×	12	674
Xiaokai Li China	11	332 0.4×	49 0.2×	136 0.8×	13 0.1×	6 0.0×	32	639
Aaron S. Abramovitz United States	17	430 0.6×	192 0.7×	52 0.3×	9 0.1×	4 0.0×	23	853
Carlos Madrid-Aliste United States	13	368 0.5×	97 0.4×	28 0.2×	131 0.8×	2 0.0×	19	607
Nicolas C. Stephanou United States	7	607 0.8×	205 0.8×	182 1.0×	11 0.1×	3 0.0×	7	821

Countries citing papers authored by Deviprasad R. Gollapalli

Since Specialization

Citations

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

Fields of papers citing papers by Deviprasad R. Gollapalli

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Deviprasad R. Gollapalli. 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 Deviprasad R. Gollapalli. The network helps show where Deviprasad R. Gollapalli may publish in the future.

Co-authorship network of co-authors of Deviprasad R. Gollapalli

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

All Works

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20 of 20 papers shown

Singh, Vinayak, Deviprasad R. Gollapalli, Thomas R. Ioerger, et al.. (2022). A d-Phenylalanine-Benzoxazole Derivative Reveals the Role of the Essential Enzyme Rv3603c in the Pantothenate Biosynthetic Pathway of Mycobacterium tuberculosis. ACS Infectious Diseases. 8(2). 330–342. 4 indexed citations

Boshoff, Helena I., Vinayak Singh, Davide M. Ferraris, et al.. (2018). Expanding Benzoxazole-Based Inosine 5′-Monophosphate Dehydrogenase (IMPDH) Inhibitor Structure–Activity As Potential Antituberculosis Agents. Journal of Medicinal Chemistry. 61(11). 4739–4756. 28 indexed citations

Kim, Youngchang, M. Makowska-Grzyska, Suresh Kumar Gorla, et al.. (2015). Structure ofCryptosporidiumIMP dehydrogenase bound to an inhibitor within vivoantiparasitic activity. Acta Crystallographica Section F Structural Biology Communications. 71(5). 531–538. 11 indexed citations

Makowska-Grzyska, M., Youngchang Kim, N. Maltseva, et al.. (2015). A Novel Cofactor-binding Mode in Bacterial IMP Dehydrogenases Explains Inhibitor Selectivity. Journal of Biological Chemistry. 290(9). 5893–5911. 33 indexed citations

Makowska-Grzyska, M., Minjia Zhang, Chalada Suebsuwong, et al.. (2014). Synthesis, in Vitro Evaluation and Cocrystal Structure of 4-Oxo-[1]benzopyrano[4,3-c]pyrazoleCryptosporidium parvumInosine 5′-Monophosphate Dehydrogenase (CpIMPDH) Inhibitors. Journal of Medicinal Chemistry. 57(24). 10544–10550. 27 indexed citations

Long, Marcus J. C., Deviprasad R. Gollapalli, & Lizbeth Hedstrom. (2012). Inhibitor Mediated Protein Degradation. Chemistry & Biology. 19(5). 629–637. 108 indexed citations

Gorla, Suresh Kumar, Minjia Zhang, Xiaoping Liu, et al.. (2012). Selective and Potent Urea Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase. Journal of Medicinal Chemistry. 55(17). 7759–7771. 39 indexed citations

Patton, Gregory C., Pål Stenmark, Deviprasad R. Gollapalli, et al.. (2011). Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes. Nature Chemical Biology. 7(12). 950–958. 30 indexed citations

Gollapalli, Deviprasad R., et al.. (2011). Specific biotinylation of IMP dehydrogenase. Bioorganic & Medicinal Chemistry Letters. 21(5). 1363–1365. 1 indexed citations

10.

Hedstrom, Lizbeth, George W. Liechti, Joanna B. Goldberg, & Deviprasad R. Gollapalli. (2011). The Antibiotic Potential of Prokaryotic IMP Dehydrogenase Inhibitors. Current Medicinal Chemistry. 18(13). 1909–1918. 55 indexed citations

11.

D’Souza, Francis, Sushanta K. Das, Atula S. D. Sandanayaka, et al.. (2011). Photoinduced charge separation in three-layer supramolecular nanohybrids: fullerene–porphyrin–SWCNT. Physical Chemistry Chemical Physics. 14(8). 2940–2940. 14 indexed citations

12.

Gollapalli, Deviprasad R., Iain Macpherson, George W. Liechti, et al.. (2010). Structural Determinants of Inhibitor Selectivity in Prokaryotic IMP Dehydrogenases. Chemistry & Biology. 17(10). 1084–1091. 38 indexed citations

13.

Sharling, Lisa, Xiaoping Liu, Deviprasad R. Gollapalli, et al.. (2010). A Screening Pipeline for Antiparasitic Agents Targeting Cryptosporidium Inosine Monophosphate Dehydrogenase. PLoS neglected tropical diseases. 4(8). e794–e794. 49 indexed citations

14.

Maurya, Sushil K., et al.. (2009). Triazole Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase. Journal of Medicinal Chemistry. 52(15). 4623–4630. 75 indexed citations

15.

Gollapalli, Deviprasad R., Lisa Sharling, Jennifer Lu, et al.. (2008). Targeting a Prokaryotic Protein in a Eukaryotic Pathogen: Identification of Lead Compounds against Cryptosporidiosis. Chemistry & Biology. 15(1). 70–77. 70 indexed citations

16.

Gollapalli, Deviprasad R., et al.. (2008). Targeting a Prokaryotic Protein in a Eukaryotic Pathogen: Identification of Lead Compounds against Cryptosporidiosis. Chemistry & Biology. 15(2). 200–200. 2 indexed citations

17.

Xue, Linlong, Deviprasad R. Gollapalli, Pranab Maiti, Wan Jin Jahng, & Robert R. Rando. (2004). A Palmitoylation Switch Mechanism in the Regulation of the Visual Cycle. Cell. 117(6). 761–771. 112 indexed citations

18.

Gollapalli, Deviprasad R. & Robert R. Rando. (2004). The specific binding of retinoic acid to RPE65 and approaches to the treatment of macular degeneration. Proceedings of the National Academy of Sciences. 101(27). 10030–10035. 33 indexed citations

19.

Gollapalli, Deviprasad R., Pranab Maiti, & Robert R. Rando. (2003). RPE65 Operates in the Vertebrate Visual Cycle by Stereospecifically Binding All-trans-Retinyl Esters. Biochemistry. 42(40). 11824–11830. 59 indexed citations

20.

Gollapalli, Deviprasad R. & Robert R. Rando. (2003). Specific inactivation of isomerohydrolase activity by 11-cis-retinoids. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1651(1-2). 93–101. 9 indexed citations

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