A.F. Pinto

750 total citations
19 papers, 559 citations indexed

About

A.F. Pinto is a scholar working on Molecular Biology, Inorganic Chemistry and Oncology. According to data from OpenAlex, A.F. Pinto has authored 19 papers receiving a total of 559 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Inorganic Chemistry and 6 papers in Oncology. Recurrent topics in A.F. Pinto's work include Metal-Catalyzed Oxygenation Mechanisms (8 papers), Toxin Mechanisms and Immunotoxins (5 papers) and PARP inhibition in cancer therapy (4 papers). A.F. Pinto is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (8 papers), Toxin Mechanisms and Immunotoxins (5 papers) and PARP inhibition in cancer therapy (4 papers). A.F. Pinto collaborates with scholars based in Portugal, Germany and Sweden. A.F. Pinto's co-authors include H. Schüler, T. Karlberg, T. Ekblad, A.G. Thorsell, Michael S. Cohen, M. Moche, L. Tresaugues, Miguel Teixeira, João V. Rodrigues and Mikael Elofsson and has published in prestigious journals such as Nature Communications, Biochemistry and Journal of Medicinal Chemistry.

In The Last Decade

A.F. Pinto

19 papers receiving 551 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
A.F. Pinto Portugal 11 308 289 88 81 63 19 559
Jessica De Ingeniis United States 10 420 1.4× 62 0.2× 32 0.4× 28 0.3× 9 0.1× 10 585
J. Krausze Germany 16 430 1.4× 216 0.7× 7 0.1× 151 1.9× 58 0.9× 29 853
Chang Sun China 12 261 0.8× 75 0.3× 28 0.3× 20 0.2× 82 1.3× 26 552
D. K. Nilov Russia 13 240 0.8× 135 0.5× 40 0.5× 35 0.4× 5 0.1× 38 346
Petr Kolenko Czechia 14 230 0.7× 51 0.2× 40 0.5× 114 1.4× 45 0.7× 43 504
Tanya M Budiarto United States 6 203 0.7× 137 0.5× 27 0.3× 34 0.4× 18 0.3× 6 378
Jyoti Singh United States 14 349 1.1× 50 0.2× 14 0.2× 10 0.1× 18 0.3× 30 691
V. Romanov United States 12 292 0.9× 64 0.2× 14 0.2× 62 0.8× 15 0.2× 20 502
Shigeko Yamazaki United States 12 434 1.4× 70 0.2× 12 0.1× 41 0.5× 22 0.3× 19 615
Alexandra Vergnes France 9 411 1.3× 63 0.2× 10 0.1× 32 0.4× 23 0.4× 17 636

Countries citing papers authored by A.F. Pinto

Since Specialization
Citations

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

Fields of papers citing papers by A.F. Pinto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by A.F. Pinto. 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 A.F. Pinto. The network helps show where A.F. Pinto may publish in the future.

Co-authorship network of co-authors of A.F. Pinto

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

All Works

19 of 19 papers shown
1.
Pinto, Teresa, A.F. Pinto, & Alice Vilela. (2023). Edible Coatings and Films for Preparation of Grapevine By-Product Infusions and in Freshly Processed Products. Coatings. 13(8). 1350–1350. 11 indexed citations
2.
Vilela, Alice, et al.. (2022). Sensory and Nutraceutical Properties of Infusions Prepared with Grape Pomace and Edible-Coated Dried–Minced Grapes. Coatings. 12(4). 443–443. 10 indexed citations
3.
Karlberg, T., P. Hornyak, A.F. Pinto, et al.. (2018). 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface. Nature Communications. 9(1). 3785–3785. 40 indexed citations
4.
Romão, Célia V., Pedro M. Matias, Filipa G. Pinho, et al.. (2018). Insights into the Structures of Superoxide Reductases from the Symbionts Ignicoccus hospitalis and Nanoarchaeum equitans. Biochemistry. 57(36). 5271–5281. 5 indexed citations
5.
Sundin, Charlotta, et al.. (2017). Structure–activity relationships for inhibitors of Pseudomonas aeruginosa exoenzyme S ADP-ribosyltransferase activity. European Journal of Medicinal Chemistry. 143. 568–576. 15 indexed citations
6.
Pinto, A.F., et al.. (2016). Identification of Inhibitors of Pseudomonas aeruginosa Exotoxin-S ADP-Ribosyltransferase Activity. SLAS DISCOVERY. 21(6). 590–595. 12 indexed citations
7.
Cortes, Rui, Samantha Jane Hughes, Ana M. Coimbra, et al.. (2016). A multiple index integrating different levels of organization. Ecotoxicology and Environmental Safety. 132. 270–278. 10 indexed citations
8.
Thorsell, A.G., T. Ekblad, T. Karlberg, et al.. (2016). Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors. Journal of Medicinal Chemistry. 60(4). 1262–1271. 273 indexed citations
9.
Pinto, A.F., Célia V. Romão, Harald Huber, et al.. (2014). Superoxide reduction by a superoxide reductase lacking the highly conserved lysine residue. JBIC Journal of Biological Inorganic Chemistry. 20(1). 155–164. 7 indexed citations
10.
Horch, Marius, A.F. Pinto, Tillmann Utesch, et al.. (2014). Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study. Physical Chemistry Chemical Physics. 16(27). 14220–14230. 10 indexed citations
11.
Pinto, A.F. & H. Schüler. (2014). Comparative Structural Analysis of the Putative Mono-ADP-Ribosyltransferases of the ARTD/PARP Family. Current topics in microbiology and immunology. 384. 153–166. 14 indexed citations
12.
Horch, Marius, A.F. Pinto, María Andrea Mroginski, et al.. (2014). Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase. RSC Advances. 4(96). 54091–54095. 9 indexed citations
13.
Lindgren, Anders E. G., T. Karlberg, A.G. Thorsell, et al.. (2013). PARP Inhibitor with Selectivity Toward ADP-Ribosyltransferase ARTD3/PARP3. ACS Chemical Biology. 8(8). 1698–1703. 49 indexed citations
14.
Bandeiras, Tiago M., et al.. (2011). Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin. Protein Expression and Purification. 81(2). 193–200. 11 indexed citations
15.
Pinho, Filipa G., A.F. Pinto, Harald Huber, et al.. (2011). Superoxide reductase fromNanoarchaeum equitans: expression, purification, crystallization and preliminary X-ray crystallographic analysis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(5). 591–595. 2 indexed citations
16.
Pinho, Filipa G., Célia V. Romão, A.F. Pinto, et al.. (2010). Cloning, purification, crystallization and X-ray crystallographic analysis ofIgnicoccus hospitalisneelaredoxin. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(5). 605–607. 5 indexed citations
17.
Pinto, A.F., Smilja Todorović, Peter Hildebrandt, et al.. (2010). Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein. JBIC Journal of Biological Inorganic Chemistry. 16(3). 501–510. 14 indexed citations
18.
Pinto, A.F., João V. Rodrigues, & Miguel Teixeira. (2009). Reductive elimination of superoxide: Structure and mechanism of superoxide reductases. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804(2). 285–297. 51 indexed citations
19.
Todorović, Smilja, João V. Rodrigues, A.F. Pinto, et al.. (2009). Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a ‘natural variant’. Physical Chemistry Chemical Physics. 11(11). 1809–1809. 11 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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