M.V.B. Dias

1.2k total citations
53 papers, 844 citations indexed

About

M.V.B. Dias is a scholar working on Molecular Biology, Infectious Diseases and Materials Chemistry. According to data from OpenAlex, M.V.B. Dias has authored 53 papers receiving a total of 844 indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 16 papers in Infectious Diseases and 14 papers in Materials Chemistry. Recurrent topics in M.V.B. Dias's work include Biochemical and Molecular Research (26 papers), Enzyme Structure and Function (14 papers) and Tuberculosis Research and Epidemiology (13 papers). M.V.B. Dias is often cited by papers focused on Biochemical and Molecular Research (26 papers), Enzyme Structure and Function (14 papers) and Tuberculosis Research and Epidemiology (13 papers). M.V.B. Dias collaborates with scholars based in Brazil, United Kingdom and South Sudan. M.V.B. Dias's co-authors include Walter Filgueira de Azevedo, Luiz Augusto Basso, Diógenes Santiago Santos, Mário Sérgio Palma, Fernanda Canduri, Tom L. Blundell, Peter F. Leadlay, Fanglu Huang, Gerardo Andrés Libreros-Zúñiga and Fernanda Ely and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

M.V.B. Dias

52 papers receiving 828 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.V.B. Dias Brazil 19 599 203 159 154 150 53 844
Ramachandran Vijayan India 17 635 1.1× 132 0.7× 118 0.7× 138 0.9× 131 0.9× 50 1.1k
Luís Fernando Saraiva Macedo Timmers Brazil 16 558 0.9× 214 1.1× 69 0.4× 156 1.0× 95 0.6× 68 908
Amit Nargotra India 22 641 1.1× 238 1.2× 215 1.4× 326 2.1× 45 0.3× 54 1.2k
R. Krishna India 22 699 1.2× 103 0.5× 136 0.9× 261 1.7× 105 0.7× 83 1.1k
Shahzaib Ahamad India 21 614 1.0× 128 0.6× 94 0.6× 163 1.1× 60 0.4× 47 1.1k
Woong‐Hee Shin South Korea 18 756 1.3× 108 0.5× 83 0.5× 89 0.6× 174 1.2× 43 1.1k
Fenglin Yin United States 10 577 1.0× 198 1.0× 132 0.8× 131 0.9× 81 0.5× 13 877
Esther M. M. Bulloch New Zealand 18 562 0.9× 175 0.9× 84 0.5× 83 0.5× 125 0.8× 36 764
M.T. Hilgers United States 15 686 1.1× 428 2.1× 103 0.6× 136 0.9× 75 0.5× 17 1.1k
Clare V. Smith United States 10 931 1.6× 267 1.3× 185 1.2× 193 1.3× 157 1.0× 10 1.2k

Countries citing papers authored by M.V.B. Dias

Since Specialization
Citations

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

Fields of papers citing papers by M.V.B. Dias

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.V.B. Dias. 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 M.V.B. Dias. The network helps show where M.V.B. Dias may publish in the future.

Co-authorship network of co-authors of M.V.B. Dias

This figure shows the co-authorship network connecting the top 25 collaborators of M.V.B. Dias. A scholar is included among the top collaborators of M.V.B. Dias 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 M.V.B. Dias. M.V.B. Dias 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.
Salata, Giovanna Cassone, et al.. (2025). PEP-1 fused to glutathione peroxidase from Trichoderma reesei: a safe and effective antioxidant active ingredient for cutaneous applications. Journal of Drug Delivery Science and Technology. 110. 107054–107054.
2.
Huang, Fanglu, Yuan Li, Jiahai Zhou, et al.. (2024). Structural and Functional Basis of GenB2 Isomerase Activity from Gentamicin Biosynthesis. ACS Chemical Biology. 19(9). 2002–2011. 2 indexed citations
3.
Ishida, Kelly, et al.. (2023). Crystal structure of dihydrofolate reductase from the emerging pathogenic fungus Candida auris. Acta Crystallographica Section D Structural Biology. 79(8). 735–745. 1 indexed citations
4.
Bakali, Jamal El, M. Błaszczyk, Joanna C. Evans, et al.. (2023). Chemical Validation of Mycobacterium tuberculosis Phosphopantetheine Adenylyltransferase Using Fragment Linking and CRISPR Interference**. Angewandte Chemie International Edition. 62(17). e202300221–e202300221. 8 indexed citations
5.
Bakali, Jamal El, M. Błaszczyk, Joanna C. Evans, et al.. (2023). Chemical Validation of Mycobacterium tuberculosis Phosphopantetheine Adenylyltransferase Using Fragment Linking and CRISPR Interference**. Angewandte Chemie. 135(17). e202300221–e202300221. 1 indexed citations
6.
Abell, Chris, et al.. (2023). Fragment‐Merging Strategies with Known Pyrimidine Scaffolds Targeting Dihydrofolate Reductase from Mycobacterium tuberculosis. ChemMedChem. 18(15). e202300240–e202300240. 1 indexed citations
7.
Dias, M.V.B., et al.. (2023). Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line. Genetics and Molecular Biology. 46(1 suppl 2). e20220261–e20220261. 7 indexed citations
8.
Dias, M.V.B., et al.. (2023). The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate. Journal of Structural Biology. 215(2). 107957–107957. 1 indexed citations
9.
Li, Yanyan, et al.. (2022). Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis. Journal of Molecular Structure. 1267. 133576–133576. 1 indexed citations
10.
Li, Sicong, Fanglu Huang, Junhong Guo, et al.. (2021). Mechanistic Insights into Dideoxygenation in Gentamicin Biosynthesis. ACS Catalysis. 11(19). 12274–12283. 11 indexed citations
11.
Oliveira, Luciana G. de, et al.. (2020). An epoxide hydrolase from endophyticStreptomycesshows unique structural features and wide biocatalytic activity. Acta Crystallographica Section D Structural Biology. 76(9). 868–875. 2 indexed citations
12.
Kronenberger, Thales, Gláucio Monteiro Ferreira, Soraya da Silva Santos, et al.. (2020). Design, synthesis and biological activity of novel substituted 3-benzoic acid derivatives as MtDHFR inhibitors. Bioorganic & Medicinal Chemistry. 28(15). 115600–115600. 11 indexed citations
13.
Little, Rory F., Robert L. Jenkins, Hui Hong, et al.. (2019). Unexpected enzyme-catalysed [4+2] cycloaddition and rearrangement in polyether antibiotic biosynthesis. Nature Catalysis. 2(11). 1045–1054. 26 indexed citations
14.
Tavares, Maurício T., et al.. (2019). Crystal Structure of GenD2, an NAD-Dependent Oxidoreductase Involved in the Biosynthesis of Gentamicin. ACS Chemical Biology. 14(5). 925–933. 12 indexed citations
15.
Huang, Fanglu, et al.. (2017). Structural Basis of the Selectivity of GenN, an Aminoglycoside N-Methyltransferase Involved in Gentamicin Biosynthesis. ACS Chemical Biology. 12(11). 2779–2787. 18 indexed citations
16.
Chambergo, Felipe S., et al.. (2017). Structure of a soluble epoxide hydrolase identified in Trichoderma reesei. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865(8). 1039–1045. 11 indexed citations
17.
Dias, M.V.B., Petros A. Tyrakis, Romênia R. Domingues, Adriana Franco Paes Leme, & Tom L. Blundell. (2013). Mycobacterium tuberculosis Dihydrofolate Reductase Reveals Two Conformational States and a Possible Low Affinity Mechanism to Antifolate Drugs. Structure. 22(1). 94–103. 29 indexed citations
18.
Truman, Andrew W., M.V.B. Dias, Shu‐Hsing Wu, et al.. (2009). Chimeric Glycosyltransferases for the Generation of Hybrid Glycopeptides. Chemistry & Biology. 16(6). 676–685. 45 indexed citations
19.
Dias, M.V.B., Fernanda Canduri, Nelson José Freitas da Silveira, et al.. (2006). Molecular Models of Tryptophan Synthase From Mycobacterium tuberculosis Complexed With Inhibitors. Cell Biochemistry and Biophysics. 44(3). 375–384. 13 indexed citations
20.
Mayrink, Wilson, et al.. (1991). Tratamento da leishmaniose tegumentar americana utilizando vacina. Anais Brasileiros de Dermatologia. 66(2). 55–59. 6 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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