Rodrigo Gallardo

3.7k total citations · 1 hit paper
41 papers, 2.8k citations indexed

About

Rodrigo Gallardo is a scholar working on Molecular Biology, Physiology and Cell Biology. According to data from OpenAlex, Rodrigo Gallardo has authored 41 papers receiving a total of 2.8k indexed citations (citations by other indexed papers that have themselves been cited), including 31 papers in Molecular Biology, 15 papers in Physiology and 6 papers in Cell Biology. Recurrent topics in Rodrigo Gallardo's work include Protein Structure and Dynamics (12 papers), Alzheimer's disease research and treatments (12 papers) and Prion Diseases and Protein Misfolding (5 papers). Rodrigo Gallardo is often cited by papers focused on Protein Structure and Dynamics (12 papers), Alzheimer's disease research and treatments (12 papers) and Prion Diseases and Protein Misfolding (5 papers). Rodrigo Gallardo collaborates with scholars based in Belgium, United Kingdom and Germany. Rodrigo Gallardo's co-authors include Frédéric Rousseau, Joost Schymkowitz, Sheena E. Radford, Neil A. Ranson, Joost Van Durme, Frederik De Smet, José R. Couceiro, Stanislav G. Rudyak, Hannah Wilkinson and Yong Xu and has published in prestigious journals such as Cell, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Rodrigo Gallardo

40 papers receiving 2.7k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover

2017 402 citations Egon Deyaert, Lina Wauters et al. Nature Communications profile →

Peers

Rodrigo Gallardo

PHYSI

ONCOL

András Micsonai Hungary

Jack Nguyen United States

Josep Vendrell Spain

Rui Zhou China

Débora Foguel Brazil

Luitgard Nagel‐Steger Germany

Pietro Sormanni United Kingdom

Dimitri Y. Chirgadze United Kingdom

Michał Dadlez Poland

Jenny J. Yang United States

András Micsonai Hungary

Rodrigo Gallardo

1.8k ×1.0

467 ×0.6

PHYSI

201 ×0.7

155 ×0.5

ONCOL

358 ×1.3

Citations per year, relative to Rodrigo Gallardo Rodrigo Gallardo (= 1×) peers András Micsonai

Countries citing papers authored by Rodrigo Gallardo

Since Specialization

Citations

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

Fields of papers citing papers by Rodrigo Gallardo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rodrigo Gallardo

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Louros, Nikolaos, Martin Wilkinson, Meine Ramakers, et al.. (2024). Local structural preferences in shaping tau amyloid polymorphism. Nature Communications. 15(1). 1028–1028. 16 indexed citations

Wilkinson, Martin, Rodrigo Gallardo, Roberto Maya‐Martinez, et al.. (2023). Disease-relevant β2-microglobulin variants share a common amyloid fold. Nature Communications. 14(1). 1190–1190. 12 indexed citations

Wilkinson, Martin, et al.. (2023). Structural evolution of fibril polymorphs during amyloid assembly. Cell. 186(26). 5798–5811.e26. 48 indexed citations

Khodaparast, Ladan, Laleh Khodaparast, Guiqin Wu, et al.. (2023). Exploiting the aggregation propensity of beta-lactamases to design inhibitors that induce enzyme misfolding. Nature Communications. 14(1). 5571–5571. 4 indexed citations

Wu, Guiqin, Laleh Khodaparast, Ladan Khodaparast, et al.. (2023). Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship. PLoS ONE. 18(3). e0283674–e0283674. 2 indexed citations

Houben, Bert, Francesco A. Aprile, Renée I. Seinstra, et al.. (2021). The cellular modifier MOAG‐4/SERF drives amyloid formation through charge complementation. The EMBO Journal. 40(21). e107568–e107568. 15 indexed citations

Benner, Peter, et al.. (2021). Factorized solution of generalized stable Sylvester equations using many-core GPU accelerators. The Journal of Supercomputing. 77(9). 10152–10164. 3 indexed citations

Khodaparast, Ladan, Laleh Khodaparast, Filip Claes, et al.. (2021). Synthetic Pept-Ins as a Generic Amyloid-Like Aggregation-Based Platform for In Vivo PET Imaging of Intracellular Targets. Bioconjugate Chemistry. 32(9). 2052–2064. 3 indexed citations

Houben, Bert, Emiel Michiels, Meine Ramakers, et al.. (2020). Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues. The EMBO Journal. 39(11). e102864–e102864. 32 indexed citations

10.

Behrendt, Marc, Siyuan Zhao, Florian Mohr, et al.. (2020). The structural basis for an on–off switch controlling Gβγ-mediated inhibition of TRPM3 channels. Proceedings of the National Academy of Sciences. 117(46). 29090–29100. 23 indexed citations

11.

Michiels, Emiel, Shu Liu, Rodrigo Gallardo, et al.. (2020). Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments. Cell Reports. 30(8). 2834–2845.e3. 10 indexed citations

12.

Deyaert, Egon, Lina Wauters, Giambattista Guaitoli, et al.. (2017). A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nature Communications. 8(1). 1008–1008. 402 indexed citations breakdown →

13.

Szaruga, María, Bogdan Munteanu, Sam Lismont, et al.. (2017). Alzheimer’s-Causing Mutations Shift Aβ Length by Destabilizing γ-Secretase-Aβn Interactions. Cell. 170(3). 443–456.e14. 187 indexed citations

14.

Kant, Rob van der, Anne R. Karow‐Zwick, Joost Van Durme, et al.. (2017). Prediction and Reduction of the Aggregation of Monoclonal Antibodies. Journal of Molecular Biology. 429(8). 1244–1261. 115 indexed citations

15.

Betti, Camilla, Isabelle Vanhoutte, Kiril Mishev, et al.. (2016). Sequence-specific protein aggregation generates defined protein knockdowns in plants. PLANT PHYSIOLOGY. 171(2). pp.00335.2016–pp.00335.2016. 24 indexed citations

16.

Ganesan, Ashok, Aleksandra Siekierska, Marijke Brams, et al.. (2016). Structural hot spots for the solubility of globular proteins. Nature Communications. 7(1). 10816–10816. 57 indexed citations

17.

Durme, Joost Van, Greet De Baets, Rob van der Kant, et al.. (2016). Solubis: a webserver to reduce protein aggregation through mutation. Protein Engineering Design and Selection. 29(8). 285–289. 57 indexed citations

18.

Couceiro, José R., Rodrigo Gallardo, Frederik De Smet, et al.. (2014). Sequence-dependent Internalization of Aggregating Peptides. Journal of Biological Chemistry. 290(1). 242–258. 19 indexed citations

19.

Xu, Jie, Joke Reumers, José R. Couceiro, et al.. (2011). Gain of function of mutant p53 by coaggregation with multiple tumor suppressors. Nature Chemical Biology. 7(5). 285–295. 427 indexed citations

20.

Durme, Joost Van, Sebastian Maurer‐Stroh, Rodrigo Gallardo, et al.. (2009). Accurate Prediction of DnaK-Peptide Binding via Homology Modelling and Experimental Data. PLoS Computational Biology. 5(8). e1000475–e1000475. 105 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.

Explore authors with similar magnitude of impact