Vanina E. Álvarez

1.1k total citations
27 papers, 783 citations indexed

About

Vanina E. Álvarez is a scholar working on Epidemiology, Molecular Biology and Public Health, Environmental and Occupational Health. According to data from OpenAlex, Vanina E. Álvarez has authored 27 papers receiving a total of 783 indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Epidemiology, 13 papers in Molecular Biology and 12 papers in Public Health, Environmental and Occupational Health. Recurrent topics in Vanina E. Álvarez's work include Trypanosoma species research and implications (24 papers), Research on Leishmaniasis Studies (11 papers) and Peptidase Inhibition and Analysis (5 papers). Vanina E. Álvarez is often cited by papers focused on Trypanosoma species research and implications (24 papers), Research on Leishmaniasis Studies (11 papers) and Peptidase Inhibition and Analysis (5 papers). Vanina E. Álvarez collaborates with scholars based in Argentina, United States and Brazil. Vanina E. Álvarez's co-authors include Juan José Cazzulo, Gregor Kosec, Vito Türk, Boris Turk, Pedro Romero, Carlos F. Arias, Susana López, Celso Sant’Anna, Juan José Cazzulo and Fernán Agüero and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Vanina E. Álvarez

26 papers receiving 772 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Vanina E. Álvarez Argentina 15 522 320 309 126 125 27 783
Jens Milbradt Germany 23 971 1.9× 547 1.7× 84 0.3× 155 1.2× 140 1.1× 35 1.3k
Adriana Parodi‐Talice Uruguay 15 574 1.1× 291 0.9× 527 1.7× 145 1.2× 63 0.5× 24 822
Matthew A. Child United States 12 159 0.3× 363 1.1× 197 0.6× 186 1.5× 90 0.7× 21 777
Jessica E. Kim United States 11 219 0.4× 281 0.9× 120 0.4× 266 2.1× 66 0.5× 12 585
Pius N. Nde United States 15 338 0.6× 218 0.7× 247 0.8× 63 0.5× 68 0.5× 36 618
Hosam Shams-Eldin Germany 17 299 0.6× 336 1.1× 209 0.7× 143 1.1× 181 1.4× 33 748
Jean-Christophe Barale France 17 171 0.3× 325 1.0× 676 2.2× 254 2.0× 72 0.6× 29 1.1k
Gaspar E. Cánepa Argentina 21 438 0.8× 398 1.2× 670 2.2× 98 0.8× 58 0.5× 44 1.0k
Michael Milhausen United States 14 523 1.0× 541 1.7× 250 0.8× 98 0.8× 16 0.1× 21 918
F. Fase-Fowler Netherlands 14 749 1.4× 411 1.3× 661 2.1× 193 1.5× 71 0.6× 14 1.1k

Countries citing papers authored by Vanina E. Álvarez

Since Specialization
Citations

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

Fields of papers citing papers by Vanina E. Álvarez

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Vanina E. Álvarez. 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 Vanina E. Álvarez. The network helps show where Vanina E. Álvarez may publish in the future.

Co-authorship network of co-authors of Vanina E. Álvarez

This figure shows the co-authorship network connecting the top 25 collaborators of Vanina E. Álvarez. A scholar is included among the top collaborators of Vanina E. Álvarez 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 Vanina E. Álvarez. Vanina E. Álvarez 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.
Coria, Lorena M., et al.. (2024). Depolymerization of SUMO chains induces slender to stumpy differentiation in T. brucei bloodstream parasites. PLoS Pathogens. 20(4). e1012166–e1012166. 2 indexed citations
2.
Midlej, Victor, Alicia Saura, Elmer A. Fernández, et al.. (2023). Antibodies to variable surface antigens induce antigenic variation in the intestinal parasite Giardia lamblia. Nature Communications. 14(1). 2537–2537. 9 indexed citations
3.
Álvarez, Vanina E., et al.. (2020). Update on relevant trypanosome peptidases: Validated targets and future challenges. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1869(2). 140577–140577. 17 indexed citations
4.
Carmona, Adriana K., et al.. (2019). Potent and selective inhibitors for M32 metallocarboxypeptidases identified from high-throughput screening of anti-kinetoplastid chemical boxes. PLoS neglected tropical diseases. 13(7). e0007560–e0007560. 3 indexed citations
5.
Cazzulo, Juan José, et al.. (2018). Simplified inducible system for Trypanosoma brucei. PLoS ONE. 13(10). e0205527–e0205527. 7 indexed citations
7.
Gaudenzi, Javier G. De, et al.. (2018). SUMO polymeric chains are involved in nuclear foci formation and chromatin organization in Trypanosoma brucei procyclic forms. PLoS ONE. 13(2). e0193528–e0193528. 9 indexed citations
8.
Madauss, Kevin P., et al.. (2017). Novel scaffolds for inhibition of Cruzipain identified from high-throughput screening of anti-kinetoplastid chemical boxes. Scientific Reports. 7(1). 12073–12073. 28 indexed citations
10.
Cazzulo, Juan José, et al.. (2015). Biosynthesis of SUMOylated Proteins in Bacteria Using the Trypanosoma brucei Enzymatic System. PLoS ONE. 10(8). e0134950–e0134950. 8 indexed citations
11.
Álvarez, Vanina E., et al.. (2013). Metacaspases, Autophagins and Metallocarboxypeptidases: Potential New Targets for Chemotherapy of the Trypanosomiases. Current Medicinal Chemistry. 20(25). 3069–3077. 11 indexed citations
12.
Li, Zhu‐Hong, Javier G. De Gaudenzi, Vanina E. Álvarez, et al.. (2012). A 43-Nucleotide U-rich Element in 3′-Untranslated Region of Large Number of Trypanosoma cruzi Transcripts Is Important for mRNA Abundance in Intracellular Amastigotes. Journal of Biological Chemistry. 287(23). 19058–19069. 24 indexed citations
13.
Cazzulo, Juan José, et al.. (2012). Antagonic activities of Trypanosoma cruzi metacaspases affect the balance between cell proliferation, death and differentiation. Cell Death and Differentiation. 19(8). 1358–1369. 45 indexed citations
14.
Li, Zhu‐Hong, Vanina E. Álvarez, Javier G. De Gaudenzi, et al.. (2011). Hyperosmotic Stress Induces Aquaporin-dependent Cell Shrinkage, Polyphosphate Synthesis, Amino Acid Accumulation, and Global Gene Expression Changes in Trypanosoma cruzi. Journal of Biological Chemistry. 286(51). 43959–43971. 36 indexed citations
15.
Obado, Samson O., et al.. (2010). Centromere-associated topoisomerase activity in bloodstream form Trypanosoma brucei. Nucleic Acids Research. 39(3). 1023–1033. 21 indexed citations
16.
Álvarez, Vanina E., et al.. (2008). Blocking autophagy to prevent parasite differentiation: A possible new strategy for fighting parasitic infections?. Autophagy. 4(3). 361–363. 33 indexed citations
17.
Álvarez, Vanina E., Gregor Kosec, Celso Sant’Anna, et al.. (2007). Autophagy Is Involved in Nutritional Stress Response and Differentiation in Trypanosoma cruzi. Journal of Biological Chemistry. 283(6). 3454–3464. 113 indexed citations
18.
Kosec, Gregor, Vanina E. Álvarez, & Juan José Cazzulo. (2006). Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators. Biocell. 30(3). 479–490. 25 indexed citations
19.
Kosec, Gregor, Vanina E. Álvarez, Fernán Agüero, et al.. (2005). Metacaspases of Trypanosoma cruzi: Possible candidates for programmed cell death mediators. Molecular and Biochemical Parasitology. 145(1). 18–28. 93 indexed citations
20.
Álvarez, Vanina E., Fabiola Parussini, Lena Åslund, & Juan José Cazzulo. (2002). Expression in insect cells of active mature cruzipain from Trypanosoma cruzi, containing its C-terminal domain. Protein Expression and Purification. 26(3). 467–475. 10 indexed citations

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