Alejandro Buschiazzo

4.7k total citations
82 papers, 3.3k citations indexed

About

Alejandro Buschiazzo is a scholar working on Molecular Biology, Epidemiology and Genetics. According to data from OpenAlex, Alejandro Buschiazzo has authored 82 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 30 papers in Epidemiology and 19 papers in Genetics. Recurrent topics in Alejandro Buschiazzo's work include Trypanosoma species research and implications (25 papers), Biochemical and Molecular Research (21 papers) and Bacterial Genetics and Biotechnology (17 papers). Alejandro Buschiazzo is often cited by papers focused on Trypanosoma species research and implications (25 papers), Biochemical and Molecular Research (21 papers) and Bacterial Genetics and Biotechnology (17 papers). Alejandro Buschiazzo collaborates with scholars based in France, Uruguay and Argentina. Alejandro Buschiazzo's co-authors include Pedro M. Alzari, Alberto C.C. Frasch, Felipe Trajtenberg, M.F. Amaya, Stephen G. Withers, Andrew G. Watts, María Laura Cremona, Marcelo E. Guerin, Iben Damager and Diego de Mendoza and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Alejandro Buschiazzo

82 papers receiving 3.3k citations

Peers

Alejandro Buschiazzo
J.A. Brannigan United Kingdom
Rupert J. Russell United Kingdom
Paul G. Hitchen United Kingdom
Raymond C. Sowder United States
Alejandro Buschiazzo
Citations per year, relative to Alejandro Buschiazzo Alejandro Buschiazzo (= 1×) peers André Zapun

Countries citing papers authored by Alejandro Buschiazzo

Since Specialization
Citations

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

Fields of papers citing papers by Alejandro Buschiazzo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Alejandro Buschiazzo

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

All Works

20 of 20 papers shown
1.
Álvarez, Beatriz, et al.. (2023). An allosteric switch ensures efficient unidirectional information transmission by the histidine kinase DesK from Bacillus subtilis. Science Signaling. 16(769). eabo7588–eabo7588. 6 indexed citations
2.
Nieves, Cecilia, Antony T. Vincent, Leticia Zarantonelli, et al.. (2022). Horizontal transfer of therfbcluster inLeptospirais a genetic determinant of serovar identity. Life Science Alliance. 6(2). e202201480–e202201480. 12 indexed citations
3.
Mondino, Sonia, et al.. (2022). 3D cryo-EM imaging of bacterial flagella: Novel structural and mechanistic insights into cell motility. Journal of Biological Chemistry. 298(7). 102105–102105. 18 indexed citations
4.
Morande, Pablo Elías, Xiao‐Jie Yan, Cecilia Abreu, et al.. (2021). AID overexpression leads to aggressive murine CLL and nonimmunoglobulin mutations that mirror human neoplasms. Blood. 138(3). 246–258. 8 indexed citations
5.
Diacovich, Lautaro, Felipe Trajtenberg, N. Larrieux, et al.. (2020). Mycobacterium tuberculosis FasR senses long fatty acyl-CoA through a tunnel and a hydrophobic transmission spine. Nature Communications. 11(1). 3703–3703. 18 indexed citations
6.
Trajtenberg, Felipe & Alejandro Buschiazzo. (2019). Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems. Methods in molecular biology. 2077. 1–18. 1 indexed citations
7.
Simpkin, Adam J., Felix Šimkovic, Jens M. H. Thomas, et al.. (2018). SIMBAD: a sequence-independent molecular-replacement pipeline. Acta Crystallographica Section D Structural Biology. 74(7). 595–605. 21 indexed citations
8.
Méchaly, Ariel, Ahmed Haouz, Nathalie Sassoon, et al.. (2018). Conformational plasticity of the response regulator CpxR, a key player in Gammaproteobacteria virulence and drug-resistance. Journal of Structural Biology. 204(2). 165–171. 11 indexed citations
9.
Méchaly, Ariel, et al.. (2017). Structural Coupling between Autokinase and Phosphotransferase Reactions in a Bacterial Histidine Kinase. Structure. 25(6). 939–944.e3. 33 indexed citations
10.
East, Alexandra, Ariel Méchaly, Gerard H. M. Huysmans, et al.. (2015). Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis. Structure. 24(1). 92–104. 26 indexed citations
11.
Correa, Agustín, Felipe Trajtenberg, Gonzalo Obal, et al.. (2013). Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation. Acta Crystallographica Section D Biological Crystallography. 69(3). 388–397. 26 indexed citations
12.
Albanesi, Daniela, Marcelo E. Guerin, Francis Schaeffer, et al.. (2013). Structural Basis for Feed-Forward Transcriptional Regulation of Membrane Lipid Homeostasis in Staphylococcus aureus. PLoS Pathogens. 9(1). e1003108–e1003108. 32 indexed citations
13.
Albanesi, Daniela, Mariana Martín, Felipe Trajtenberg, et al.. (2009). Structural plasticity and catalysis regulation of a thermosensor histidine kinase. Proceedings of the National Academy of Sciences. 106(38). 16185–16190. 151 indexed citations
14.
Graña, Martín, Marco Bellinzoni, Isabelle Miras, et al.. (2009). Structure ofMycobacterium tuberculosisRv2714, a representative of a duplicated gene family in Actinobacteria. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(10). 972–977. 6 indexed citations
15.
Buchini, Sabrina, Alejandro Buschiazzo, & Stephen G. Withers. (2008). A New Generation of Specific Trypanosoma cruzi trans‐Sialidase Inhibitors. Angewandte Chemie International Edition. 47(14). 2700–2703. 77 indexed citations
16.
Guerin, Marcelo E., Jana Korduláková, Francis Schaeffer, et al.. (2007). Molecular Recognition and Interfacial Catalysis by the Essential Phosphatidylinositol Mannosyltransferase PimA from Mycobacteria. Journal of Biological Chemistry. 282(28). 20705–20714. 114 indexed citations
17.
Amaya, M.F., Andrew G. Watts, Iben Damager, et al.. (2004). Structural Insights into the Catalytic Mechanism of Trypanosoma cruzi trans-Sialidase. Structure. 12(5). 775–784. 184 indexed citations
18.
Buschiazzo, Alejandro, Juan E. Ugalde, Marcelo E. Guerin, et al.. (2004). Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. The EMBO Journal. 23(16). 3196–3205. 136 indexed citations
19.
Bontempi, Esteban J., et al.. (2000). The tyrosine aminotransferase fromTrypanosoma rangeli: sequence and genomic characterization. FEMS Microbiology Letters. 189(2). 253–257. 3 indexed citations
20.
Buschiazzo, Alejandro, María Laura Cremona, Oscar Campetella, Alberto C.C. Frasch, & Daniel O. Sánchez. (1993). Sequence of a Trypanosoma rangeli gene closely related to Trypanosoma cruzi trans-sialidase. Molecular and Biochemical Parasitology. 62(1). 115–116. 18 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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