Pablo Sobrado

2.4k total citations
84 papers, 1.8k citations indexed

About

Pablo Sobrado is a scholar working on Molecular Biology, Biochemistry and Organic Chemistry. According to data from OpenAlex, Pablo Sobrado has authored 84 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 25 papers in Biochemistry and 18 papers in Organic Chemistry. Recurrent topics in Pablo Sobrado's work include Amino Acid Enzymes and Metabolism (24 papers), Enzyme Structure and Function (16 papers) and Carbohydrate Chemistry and Synthesis (15 papers). Pablo Sobrado is often cited by papers focused on Amino Acid Enzymes and Metabolism (24 papers), Enzyme Structure and Function (16 papers) and Carbohydrate Chemistry and Synthesis (15 papers). Pablo Sobrado collaborates with scholars based in United States, Costa Rica and Argentina. Pablo Sobrado's co-authors include John J. Tanner, Paul F. Fitzpatrick, Reeder M. Robinson, Somayesadat Badieyan, Brian G. Fox, Julia S. Martín del Campo, Yonghong Bai, E.J. Levin, Ming Zhou and Jason G. McCoy and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Pablo Sobrado

79 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Pablo Sobrado United States	25	1.1k	379	295	293	272	84	1.8k
M.W. Vetting United States	32	2.5k 2.3×	202 0.5×	295 1.0×	256 0.9×	693 2.5×	59	3.4k
Koen H. G. Verschueren Belgium	14	2.3k 2.0×	296 0.8×	198 0.7×	397 1.4×	603 2.2×	23	3.3k
Chris J. Hamilton United Kingdom	27	1.3k 1.2×	252 0.7×	348 1.2×	35 0.1×	262 1.0×	69	2.2k
Robert H. H. van den Heuvel Netherlands	32	1.8k 1.6×	209 0.6×	98 0.3×	142 0.5×	471 1.7×	54	2.8k
John R. Coggins United Kingdom	33	2.3k 2.0×	170 0.4×	404 1.4×	221 0.8×	569 2.1×	111	3.1k
Daniël J. Steenkamp South Africa	26	1.1k 1.0×	418 1.1×	163 0.6×	70 0.2×	241 0.9×	50	1.8k
Xiaofeng Zhu China	24	1.1k 1.0×	72 0.2×	321 1.1×	81 0.3×	101 0.4×	75	2.0k
Maria Krook Sweden	15	1.6k 1.4×	232 0.6×	115 0.4×	80 0.3×	495 1.8×	18	2.4k
Rémi Zallot United States	19	1.2k 1.1×	134 0.4×	116 0.4×	63 0.2×	162 0.6×	26	1.6k
Lars I. Leichert Germany	25	1.7k 1.6×	313 0.8×	111 0.4×	41 0.1×	217 0.8×	59	2.7k

Countries citing papers authored by Pablo Sobrado

Since Specialization

Citations

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

Fields of papers citing papers by Pablo Sobrado

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Pablo Sobrado

This figure shows the co-authorship network connecting the top 25 collaborators of Pablo Sobrado. A scholar is included among the top collaborators of Pablo Sobrado 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 Pablo Sobrado. Pablo Sobrado 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

Sobrado, Pablo, et al.. (2024). Methods for biochemical characterization of flavin-dependent N-monooxygenases involved in siderophore biosynthesis. Methods in enzymology on CD-ROM/Methods in enzymology. 702. 247–280.

Sobrado, Pablo, et al.. (2024). Kinetic Characterization and Identification of Key Active Site Residues of the L‐Aspartate N‐Hydroxylase, CreE. ChemBioChem. 25(14). e202400350–e202400350.

Sobrado, Pablo, et al.. (2024). Kinetic characterization of a flavin-dependent monooxygenase from the insect food crop pest, Zonocerus variegatus. Archives of Biochemistry and Biophysics. 754. 109949–109949. 3 indexed citations

Tanner, John J., et al.. (2022). Kinetic and Structural Characterization of a Flavin-Dependent Putrescine N-Hydroxylase from Acinetobacter baumannii. Biochemistry. 61(22). 2607–2620. 6 indexed citations

Korasick, David A., et al.. (2021). Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from Acinetobacter baumannii. ACS Omega. 6(28). 18537–18547. 9 indexed citations

Stiers, Kyle M., et al.. (2020). Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. Journal of Biological Chemistry. 295(38). 13239–13249. 13 indexed citations

Campo, Julia S. Martín del, et al.. (2020). Biochemical Characterization of the Two-Component Flavin-Dependent Monooxygenase Involved in Valanimycin Biosynthesis. Biochemistry. 60(1). 31–40. 9 indexed citations

Schuermann, Jonathan P., et al.. (2020). Structure and function of a flavin-dependent S-monooxygenase from garlic (Allium sativum). Journal of Biological Chemistry. 295(32). 11042–11055. 17 indexed citations

Robinson, Reeder M., et al.. (2020). Structural Determinants of Flavin Dynamics in a Class B Monooxygenase. Biochemistry. 59(48). 4609–4616. 8 indexed citations

10.

Campo, Julia S. Martín del, et al.. (2020). Biosynthesis of desferrioxamine siderophores initiated by decarboxylases: A functional investigation of two lysine/ornithine-decarboxylases from Gordonia rubripertincta CWB2 and Pimelobacter simplex 3E. Archives of Biochemistry and Biophysics. 689. 108429–108429. 9 indexed citations

11.

Dai, Yumin, et al.. (2018). Structural Evidence for Rifampicin Monooxygenase Inactivating Rifampicin by Cleaving Its Ansa-Bridge. Biochemistry. 57(14). 2065–2068. 16 indexed citations

12.

Tanner, John J., et al.. (2018). Steric Control of the Rate-Limiting Step of UDP-Galactopyranose Mutase. Biochemistry. 57(26). 3713–3721. 3 indexed citations

13.

Dai, Yumin, et al.. (2017). Flavin‐N5 Covalent Intermediate in a Nonredox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme. ChemBioChem. 19(1). 53–57. 5 indexed citations

14.

Robinson, Reeder M., et al.. (2015). Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Archives of Biochemistry and Biophysics. 585. 25–31. 13 indexed citations

15.

Robinson, Reeder M., S. Franceschini, Pedro Rodríguez, et al.. (2014). Arg279 is the key regulator of coenzyme selectivity in the flavin-dependent ornithine monooxygenase SidA. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(4). 778–784. 17 indexed citations

16.

Tanner, John J., et al.. (2013). Targeting UDP-Galactopyranose Mutases from Eukaryotic Human Pathogens. Current Pharmaceutical Design. 19(14). 2561–2573. 20 indexed citations

17.

Singh, Harkewal, et al.. (2012). Crystal Structures and Small-angle X-ray Scattering Analysis of UDP-galactopyranose Mutase from the Pathogenic Fungus Aspergillus fumigatus. Journal of Biological Chemistry. 287(12). 9041–9051. 33 indexed citations

18.

LeBlanc-Straceski, Janine, et al.. (2009). Developmental expression of Xenopus myosin 1d and identification of a myo1d tail homology that overlaps TH1. Development Growth & Differentiation. 51(4). 443–451. 2 indexed citations

19.

LeBlanc-Straceski, Janine, et al.. (2006). The lift pool method for isolation of cDNA clones from lambda phage libraries. Electronic Journal of Biotechnology. 9(4). 0–0. 1 indexed citations

20.

Sobrado, Pablo. (2004). Postdoctoral Training in South America: Opportunities in Chile. Electronic Journal of Biotechnology. 7(3). 16–17.

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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