María Á. Chávez

433 total citations
24 papers, 356 citations indexed

About

María Á. Chávez is a scholar working on Molecular Biology, Biotechnology and Oncology. According to data from OpenAlex, María Á. Chávez has authored 24 papers receiving a total of 356 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 7 papers in Biotechnology and 6 papers in Oncology. Recurrent topics in María Á. Chávez's work include Protein Hydrolysis and Bioactive Peptides (6 papers), Peptidase Inhibition and Analysis (6 papers) and Marine Sponges and Natural Products (4 papers). María Á. Chávez is often cited by papers focused on Protein Hydrolysis and Bioactive Peptides (6 papers), Peptidase Inhibition and Analysis (6 papers) and Marine Sponges and Natural Products (4 papers). María Á. Chávez collaborates with scholars based in Cuba, Spain and Chile. María Á. Chávez's co-authors include José Andrés Morgado‐Díaz, Francesc Avilés, Kurt D. Berndt, Salvatore G. De-Simone, Walfrido Antuch, Kurt Wüthrich, Mariana S. Araújo, David Reverter, Aparecida S. Tanaka and Stephen J. Trejo and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Analytical Biochemistry.

In The Last Decade

María Á. Chávez

23 papers receiving 348 citations

Peers

María Á. Chávez

BIOTE

ONCOL

PHEOH

MICRO

Sonia Verma India

Walfrido Antuch Germany

Patrick Hauske Germany

Joy L. Silen United States

Brian J. Fennell Ireland

Michael Meltzer Germany

Lorraine Hewitt United Kingdom

Viola Beier Germany

Fana B. Mersha United States

Denise Ochs United States

Sonia Verma India

María Á. Chávez

191 ×0.9

31 ×0.3

BIOTE

36 ×0.6

ONCOL

90 ×1.7

PHEOH

10 ×0.3

MICRO

Citations per year, relative to María Á. Chávez María Á. Chávez (= 1×) peers Sonia Verma

Countries citing papers authored by María Á. Chávez

Since Specialization

Citations

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

Fields of papers citing papers by María Á. Chávez

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by María Á. Chávez. 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 María Á. Chávez. The network helps show where María Á. Chávez may publish in the future.

Co-authorship network of co-authors of María Á. Chávez

This figure shows the co-authorship network connecting the top 25 collaborators of María Á. Chávez. A scholar is included among the top collaborators of María Á. Chávez 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 María Á. Chávez. María Á. Chávez 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

Chávez, María Á., et al.. (2025). Effect of Mannoprotein-Producing Yeast on Viscosity and Mouthfeel of Red Wine. Foods. 14(3). 462–462. 1 indexed citations

Chávez, María Á., et al.. (2021). La administración pública del futuro. 1 indexed citations

Hernández, Martha, Stephen J. Trejo, Javier García‐Pardo, et al.. (2019). Characterization, Recombinant Production and Structure-Function Analysis of NvCI, A Picomolar Metallocarboxypeptidase Inhibitor from the Marine Snail Nerita versicolor. Marine Drugs. 17(9). 511–511. 4 indexed citations

Trejo, Stephen J., et al.. (2017). Intensity fading MALDI-TOF mass spectrometry and functional proteomics assignments to identify protease inhibitors in marine invertebrates. Journal of Proteomics. 165. 75–92. 7 indexed citations

Espinoza, Luis, et al.. (2016). Synthesis of New Hydrated Geranylphenols and in Vitro Antifungal Activity against Botrytis cinerea. International Journal of Molecular Sciences. 17(6). 840–840. 4 indexed citations

Méndez, Yanira, et al.. (2014). Combinatorial Multicomponent Access to Natural‐Products‐Inspired Peptidomimetics: Discovery of Selective Inhibitors of Microbial Metallo‐aminopeptidases. ChemMedChem. 9(10). 2351–2359. 18 indexed citations

Trejo, Stephen J., et al.. (2013). A Noncanonical Mechanism of Carboxypeptidase Inhibition Revealed by the Crystal Structure of the Tri-Kunitz SmCI in Complex with Human CPA4. Structure. 21(7). 1118–1126. 11 indexed citations

Chávez, María Á., et al.. (2012). Crystal Structure of Novel Metallocarboxypeptidase Inhibitor from Marine Mollusk Nerita versicolor in Complex with Human Carboxypeptidase A4. Journal of Biological Chemistry. 287(12). 9250–9258. 24 indexed citations

Trejo, Stephen J., et al.. (2012). Tri-domain Bifunctional Inhibitor of Metallocarboxypeptidases A and Serine Proteases Isolated from Marine Annelid Sabellastarte magnifica. Journal of Biological Chemistry. 287(19). 15427–15438. 24 indexed citations

10.

Pons, Tirso, Markus Perbandt, Pedro A. Valiente, et al.. (2012). Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor. Journal of Structural Biology. 180(2). 271–279. 18 indexed citations

11.

Chávez, María Á., et al.. (2011). Screening of protease inhibitory activity in extracts of five Ascidian species from Cuban coasts. SHILAP Revista de lepidopterología. 4 indexed citations

12.

Trejo, Stephen J., et al.. (2009). A novel metallocarboxypeptidase‐like enzyme from the marine annelid Sabellastarte magnifica– a step into the invertebrate world of proteases. FEBS Journal. 276(17). 4875–4890. 13 indexed citations

13.

Morgado‐Díaz, José Andrés, et al.. (2007). Effects of serine protease inhibitors on viability and morphology of Leishmania (Leishmania) amazonensis promastigotes. Parasitology Research. 101(6). 1627–1635. 46 indexed citations

14.

Pons, Tirso, Jeovanis Gil, Vladimir Besada, et al.. (2007). Characterization and comparative 3D modeling of CmPI-II, a novel ‘non-classical’ Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca). Biological Chemistry. 388(11). 1183–1194. 26 indexed citations

15.

Tanaka, Aparecida S., et al.. (2006). Purification and partial characterization of human neutrophil elastase inhibitors from the marine snail Cenchritis muricatus (Mollusca). Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology. 146(4). 506–513. 28 indexed citations

16.

Reyes, Osvaldo, et al.. (2004). A heterogeneous enzymatic assay for quantification of Plasmepsin II activity and the evaluation of its inhibitors. Journal of Pharmaceutical and Biomedical Analysis. 34(4). 833–840. 5 indexed citations

17.

Araújo, Mariana S., et al.. (2004). Purification and preliminary characterization of a plasma kallikrein inhibitor isolated from sea hares Aplysia dactylomela Rang, 1828. Toxicon. 43(2). 219–223. 7 indexed citations

18.

Oliva, Maria Luiza Vilela, et al.. (2003). Partial purification and characterization of a serine proteinase isolated from sea hares Aplysia dactylomela. 17(2). 93–98. 1 indexed citations

19.

Lissi, E. A., Gabriel Castrillo, Osvaldo Reyes, et al.. (2002). An immunoenzymatic solid-phase assay for quantitative determination of HIV-1 protease activity. Analytical Biochemistry. 307(1). 18–24. 23 indexed citations

20.

Antuch, Walfrido, et al.. (1993). The NMR solution structure of a Kunitz‐type proteinase inhibitor from the sea anemone Stichodactyla helianthus. European Journal of Biochemistry. 212(3). 675–684. 58 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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