Nunilo Cremades

6.7k total citations · 4 hit papers
49 papers, 4.8k citations indexed

About

Nunilo Cremades is a scholar working on Neurology, Physiology and Molecular Biology. According to data from OpenAlex, Nunilo Cremades has authored 49 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Neurology, 28 papers in Physiology and 22 papers in Molecular Biology. Recurrent topics in Nunilo Cremades's work include Parkinson's Disease Mechanisms and Treatments (30 papers), Alzheimer's disease research and treatments (28 papers) and Protein Structure and Dynamics (10 papers). Nunilo Cremades is often cited by papers focused on Parkinson's Disease Mechanisms and Treatments (30 papers), Alzheimer's disease research and treatments (28 papers) and Protein Structure and Dynamics (10 papers). Nunilo Cremades collaborates with scholars based in Spain, United Kingdom and United States. Nunilo Cremades's co-authors include Christopher M. Dobson, Serene W. Chen, David Klenerman, Nicholas Wood, Andrey Y. Abramov, Tuomas P. J. Knowles, Francesco A. Aprile, Emma Deas, Roberta Cascella and Cristina Cecchi and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Nunilo Cremades

49 papers receiving 4.7k 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.

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

2012 709 citations Nunilo Cremades, Samuel I. A. Cohen et al. Cell profile →
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

2017 520 citations Giuliana Fusco, Serene W. Chen et al. Science profile →
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

2015 368 citations Serene W. Chen, Srdja Drakulić et al. Proceedings of the National Academy of Sciences profile →
The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

2021 166 citations Roberta Cascella, Serene W. Chen et al. Nature Communications profile →

Peers

Nunilo Cremades

PHYSI

NEURO

CMN

Alfonso De Simone United Kingdom

Leonid Breydo United States

Alexander K. Buell United Kingdom

Francesco A. Aprile United Kingdom

Janet R. Kumita United Kingdom

Michael R. Sierks United States

Georg Meisl United Kingdom

Céline Galvagnion United Kingdom

Patrizia Polverino de Laureto Italy

James D. Harper United States

Alfonso De Simone United Kingdom

Nunilo Cremades

3.5k ×1.6

1.8k ×0.8

PHYSI

1.4k ×0.7

NEURO

628 ×0.9

CMN

572 ×1.2

Citations per year, relative to Nunilo Cremades Nunilo Cremades (= 1×) peers Alfonso De Simone

Countries citing papers authored by Nunilo Cremades

Since Specialization

Citations

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

Fields of papers citing papers by Nunilo Cremades

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Nunilo Cremades

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

Limbocker, Ryan, Nunilo Cremades, Roberta Cascella, et al.. (2023). Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. Accounts of Chemical Research. 56(12). 1395–1405. 31 indexed citations

Gracia, Pablo, et al.. (2022). Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau. Nature Communications. 13(1). 4586–4586. 58 indexed citations

Gracia, Pablo, et al.. (2022). Characterisation of Amyloid Aggregation and Inhibition by Diffusion-Based Single-Molecule Fluorescence Techniques. SHILAP Revista de lepidopterología. 2(4). 506–524. 1 indexed citations

Gracia, Pablo & Nunilo Cremades. (2022). Single-Particle Analysis of the Interaction Between Molecules and Protein Aggregated Species by Dual-Color Time-Resolved Fluorescence Spectroscopy. Methods in molecular biology. 2551. 379–394. 1 indexed citations

Cascella, Roberta, Alessandra Bigi, Nunilo Cremades, & Cristina Cecchi. (2022). Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies. Cellular and Molecular Life Sciences. 79(3). 174–174. 72 indexed citations

Gracia, Pablo, Adai Colom, José D. Camino, et al.. (2021). All-or-none amyloid disassembly via chaperone-triggered fibril unzipping favors clearance of α-synuclein toxic species. Proceedings of the National Academy of Sciences. 118(36). 28 indexed citations

Cascella, Roberta, Serene W. Chen, Alessandra Bigi, et al.. (2021). The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells. Nature Communications. 12(1). 1814–1814. 166 indexed citations breakdown →

Camino, José D., Pablo Gracia, & Nunilo Cremades. (2020). The role of water in the primary nucleation of protein amyloid aggregation. Biophysical Chemistry. 269. 106520–106520. 56 indexed citations

Froula, Jessica M., José D. Camino, Serene W. Chen, et al.. (2019). Defining α-synuclein species responsible for Parkinson’s disease phenotypes in mice. Journal of Biological Chemistry. 294(27). 10392–10406. 97 indexed citations

10.

Fusco, Giuliana, Serene W. Chen, Philip T. F. Williamson, et al.. (2017). Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. Science. 358(6369). 1440–1443. 520 indexed citations breakdown →

11.

Chen, Serene W., Srdja Drakulić, Emma Deas, et al.. (2015). Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation. Proceedings of the National Academy of Sciences. 112(16). E1994–2003. 368 indexed citations breakdown →

12.

Tosatto, Laura, Mathew H. Horrocks, Alexander J. Dear, et al.. (2015). Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants. Scientific Reports. 5(1). 16696–16696. 86 indexed citations

13.

Tosatto, Laura, Mathew H. Horrocks, Nunilo Cremades, et al.. (2014). Single Molecule FRET Characterization of Oligomers from Alpha-Synuclein Early Onset Parkinson's Disease Mutants. Biophysical Journal. 106(2). 269a–269a. 1 indexed citations

14.

Guilliams, Tim, Farah El-Turk, Alexander K. Buell, et al.. (2013). Nanobodies Raised against Monomeric α-Synuclein Distinguish between Fibrils at Different Maturation Stages. Journal of Molecular Biology. 425(14). 2397–2411. 89 indexed citations

15.

Cremades, Nunilo, Samuel I. A. Cohen, Emma Deas, et al.. (2012). Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein. Cell. 149(5). 1048–1059. 709 indexed citations breakdown →

16.

Zambelli, Barbara, Nunilo Cremades, Paolo Neyroz, et al.. (2011). Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPaseenzyme. Molecular BioSystems. 8(1). 220–228. 37 indexed citations

17.

Pey, Ángel L., Ming Ying, Nunilo Cremades, et al.. (2008). Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria. Journal of Clinical Investigation. 118(8). 2858–2867. 136 indexed citations

18.

Cremades, Nunilo, Marta Bueno, José L. Neira, Adrián Velázquez‐Campoy, & Javier Sancho. (2007). Conformational Stability of Helicobacter pylori Flavodoxin. Journal of Biological Chemistry. 283(5). 2883–2895. 14 indexed citations

19.

Martínez‐Júlvez, Marta, Nunilo Cremades, Marta Bueno, et al.. (2007). Common conformational changes in flavodoxins induced by FMN and anion binding: The structure of Helicobacter pylori apoflavodoxin. Proteins Structure Function and Bioinformatics. 69(3). 581–594. 24 indexed citations

20.

Hoffman, Paul S., Gary Sisson, Matthew A. Croxen, et al.. (2006). Antiparasitic Drug Nitazoxanide Inhibits the Pyruvate Oxidoreductases of Helicobacter pylori , Selected Anaerobic Bacteria and Parasites, and Campylobacter jejuni. Antimicrobial Agents and Chemotherapy. 51(3). 868–876. 197 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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