Melisa Lázaro

542 total citations
9 papers, 379 citations indexed

About

Melisa Lázaro is a scholar working on Molecular Biology, Cell Biology and Structural Biology. According to data from OpenAlex, Melisa Lázaro has authored 9 papers receiving a total of 379 indexed citations (citations by other indexed papers that have themselves been cited), including 5 papers in Molecular Biology, 4 papers in Cell Biology and 2 papers in Structural Biology. Recurrent topics in Melisa Lázaro's work include RNA modifications and cancer (3 papers), RNA and protein synthesis mechanisms (3 papers) and Autophagy in Disease and Therapy (2 papers). Melisa Lázaro is often cited by papers focused on RNA modifications and cancer (3 papers), RNA and protein synthesis mechanisms (3 papers) and Autophagy in Disease and Therapy (2 papers). Melisa Lázaro collaborates with scholars based in Spain, United States and Switzerland. Melisa Lázaro's co-authors include David Gil‐Carton, Mikel Valle, Sjors H. W. Scheres, Wolfgang Wintermeyer, Andrey L. Konevega, Marina V. Rodnina, Roberto Melero, Gorka Lasso, Óscar Llorca and Henning Urlaub and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Nature Communications.

In The Last Decade

Melisa Lázaro

9 papers receiving 378 citations

Peers

Melisa Lázaro

MB

ONCOL

GENET

MC

CB

Rodrigo F. Ortiz‐Meoz United States

Brian J. Belmont United States

Mohsin M. Naqvi United Kingdom

K. Lakomek Germany

Lukas Kater Germany

Kaige Yan China

Kristina Döring Germany

Jochen Ismer Germany

Rafael Ayala United Kingdom

Aman Makaju United States

Rodrigo F. Ortiz‐Meoz United States

Melisa Lázaro

637 ×1.9

MB

29 ×0.7

ONCOL

72 ×2.0

GENET

37 ×1.1

MC

16 ×0.5

CB

Citations per year, relative to Melisa Lázaro Melisa Lázaro (= 1×) peers Rodrigo F. Ortiz‐Meoz

Countries citing papers authored by Melisa Lázaro

Since Specialization

Citations

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

Fields of papers citing papers by Melisa Lázaro

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Melisa Lázaro

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

All Works

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9 of 9 papers shown

1.

Lázaro, Melisa, Mikel Valle, Dorotea Fracchiolla, et al.. (2023). Effect of ATG12–ATG5-ATG16L1 autophagy E3-like complex on the ability of LC3/GABARAP proteins to induce vesicle tethering and fusion. Cellular and Molecular Life Sciences. 80(2). 56–56. 27 indexed citations

2.

Lázaro, Melisa, Ana Rosa Viguera, L. Ruth Montes, et al.. (2022). Autophagy protein LC3C binding to phospholipid and interaction with lipid membranes. International Journal of Biological Macromolecules. 212. 432–441. 5 indexed citations

3.

López‐Alonso, Jorge P., Melisa Lázaro, David Gil‐Carton, et al.. (2022). CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase. Nature Communications. 13(1). 6185–6185. 15 indexed citations

4.

Lázaro, Melisa, Roberto Melero, Jorge P. López‐Alonso, et al.. (2021). 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. Communications Biology. 4(1). 684–684. 8 indexed citations

5.

Fernández-Millán, Pablo, Melisa Lázaro, Joachim M. Gerhold, et al.. (2015). The hexameric structure of the human mitochondrial replicative helicase Twinkle. Nucleic Acids Research. 43(8). 4284–4295. 39 indexed citations

6.

Lasso, Gorka, Linda Yu, David Gil‐Carton, et al.. (2014). Functional Conformations for Pyruvate Carboxylase during Catalysis Explored by Cryoelectron Microscopy. Structure. 22(6). 911–922. 19 indexed citations

7.

Melero, Roberto, Gretel Buchwald, Monika Raabe, et al.. (2012). The cryo-EM structure of the UPF–EJC complex shows UPF1 poised toward the RNA 3′ end. Nature Structural & Molecular Biology. 19(5). 498–505. 63 indexed citations

8.

Melero, Roberto, S. Rajagopalan, Melisa Lázaro, et al.. (2010). Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA. Proceedings of the National Academy of Sciences. 108(2). 557–562. 63 indexed citations

9.

Konevega, Andrey L., Sjors H. W. Scheres, Melisa Lázaro, et al.. (2008). Structure of ratcheted ribosomes with tRNAs in hybrid states. Proceedings of the National Academy of Sciences. 105(44). 16924–16927. 140 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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