Alejandro Beldarraı́n

401 total citations
19 papers, 335 citations indexed

About

Alejandro Beldarraı́n is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Physical and Theoretical Chemistry. According to data from OpenAlex, Alejandro Beldarraı́n has authored 19 papers receiving a total of 335 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 4 papers in Radiology, Nuclear Medicine and Imaging and 3 papers in Physical and Theoretical Chemistry. Recurrent topics in Alejandro Beldarraı́n's work include Protein purification and stability (6 papers), Protein Structure and Dynamics (4 papers) and Monoclonal and Polyclonal Antibodies Research (4 papers). Alejandro Beldarraı́n is often cited by papers focused on Protein purification and stability (6 papers), Protein Structure and Dynamics (4 papers) and Monoclonal and Polyclonal Antibodies Research (4 papers). Alejandro Beldarraı́n collaborates with scholars based in Cuba, Spain and Mexico. Alejandro Beldarraı́n's co-authors include José Luis López‐Lacomba, Manuel Cortijo, Niuris Acosta, Carlos G. Genzor, Carlos Gómez‐Moreno, Javier Sancho, Luis L. Rodrı́guez, Tirso Pons, Glay Chinea and Osvaldo Olmea and has published in prestigious journals such as SHILAP Revista de lepidopterología, Biochemistry and International Journal of Pharmaceutics.

In The Last Decade

Alejandro Beldarraı́n

19 papers receiving 324 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alejandro Beldarraı́n Cuba 11 229 73 67 64 54 19 335
L. M. Likhosherstov Russia 12 503 2.2× 79 1.1× 60 0.9× 75 1.2× 32 0.6× 56 666
Daotian Fu United States 11 293 1.3× 58 0.8× 109 1.6× 139 2.2× 18 0.3× 13 461
Barbara J. Allan United States 12 172 0.8× 55 0.8× 110 1.6× 44 0.7× 25 0.5× 23 522
Bingyuan Wu United States 10 439 1.9× 62 0.8× 80 1.2× 46 0.7× 34 0.6× 13 539
Corné J.M. Stroop Netherlands 13 400 1.7× 77 1.1× 117 1.7× 30 0.5× 16 0.3× 14 533
Gregory M. Watt United Kingdom 10 383 1.7× 27 0.4× 75 1.1× 33 0.5× 96 1.8× 15 594
Kirsten Arnvig McGuire Denmark 11 249 1.1× 23 0.3× 52 0.8× 12 0.2× 45 0.8× 13 404
M V Krishna Sastry India 7 327 1.4× 57 0.8× 31 0.5× 26 0.4× 21 0.4× 8 370
Astrid Hilde Myrset Norway 11 245 1.1× 39 0.5× 11 0.2× 29 0.5× 20 0.4× 24 418
Musleh M. Muthana United States 12 527 2.3× 42 0.6× 84 1.3× 94 1.5× 14 0.3× 18 612

Countries citing papers authored by Alejandro Beldarraı́n

Since Specialization
Citations

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

Fields of papers citing papers by Alejandro Beldarraı́n

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Alejandro Beldarraı́n

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

All Works

19 of 19 papers shown
1.
Beldarraı́n, Alejandro, et al.. (2015). Stability Studies of a Freeze-Dried Recombinant Human Epidermal Growth Factor Formulation for Wound Healing. PDA Journal of Pharmaceutical Science and Technology. 69(3). 399–416. 2 indexed citations
2.
Chinea, Glay, et al.. (2014). Stabilization of a recombinant human epidermal growth factor parenteral formulation through freeze-drying. Biologicals. 42(6). 322–333. 12 indexed citations
3.
Campana, Patrícia T., et al.. (2013). Screening for stability and compatibility conditions of recombinant human epidermal growth factor for parenteral formulation: Effect of pH, buffers, and excipients. International Journal of Pharmaceutics. 452(1-2). 52–62. 41 indexed citations
4.
Garcı́a, José L., et al.. (2012). Aplicación del análisis de riesgo a la producción de proteínas recombinantes expresadas en Escherichia coli. SHILAP Revista de lepidopterología. 1 indexed citations
5.
Gómez, Leonardo D., et al.. (2005). Optimisation of the coupled monoclonal antibody density for recombinant hepatitis B virus surface antigen immunopurification. Journal of Chromatography B. 816(1-2). 1–6. 11 indexed citations
6.
Beldarraı́n, Alejandro, Niuris Acosta, Lázaro Betancourt, Luis Javier González, & Tirso Pons. (2003). Enzymic, spectroscopic and calorimetric studies of a recombinant dextranase expressed in Pichia pastoris. Biotechnology and Applied Biochemistry. 38(3). 211–221. 7 indexed citations
7.
Beldarraı́n, Alejandro, et al.. (2002). Chromatographic removal combined with heat, acid and chaotropic inactivation of four model viruses. Journal of Biotechnology. 96(3). 251–258. 18 indexed citations
8.
Beldarraı́n, Alejandro. (2001). Aplicaciones de la calorimetría diferencial de barrido al estudio de la estabilidad de las proteínas. Biotecnología aplicada. 18(1). 10–16. 1 indexed citations
9.
Beldarraı́n, Alejandro, et al.. (2001). Multidomain Structure of a Recombinant Streptokinase. A Differential Scanning Calorimetry Study. Journal of Protein Chemistry. 20(1). 9–17. 8 indexed citations
10.
Beldarraı́n, Alejandro, et al.. (2001). Purification and conformational properties of a human interferon α2b produced inEscherichia coli. Biotechnology and Applied Biochemistry. 33(3). 173–182. 34 indexed citations
11.
Beldarraı́n, Alejandro, et al.. (2000). Characterization of Mucor pusillus rennin expressed in Pichia pastoris: enzymic, spectroscopic and calorimetric studies. Biotechnology and Applied Biochemistry. 31(2). 77–84. 12 indexed citations
12.
Acosta, Niuris, et al.. (2000). Characterization of recombinant invertase expressed in methylotrophic yeasts. Biotechnology and Applied Biochemistry. 32(3). 179–187. 13 indexed citations
13.
Martínez, Eduardo, Julio C. Sánchez, Eugenio Hardy, et al.. (1999). Molecular characterization of recombinant human interferon alpha-2b produced in Cuba. Biotecnología aplicada. 16(3). 154–159. 11 indexed citations
14.
Beldarraı́n, Alejandro, et al.. (1999). Thermal Denaturation of Human γ-Interferon. A Calorimetric and Spectroscopic Study. Biochemistry. 38(24). 7865–7873. 14 indexed citations
15.
Pons, Tirso, Glay Chinea, Osvaldo Olmea, et al.. (1998). Structural model of Dex protein fromPenicillium minioluteumand its implications in the mechanism of catalysis. Proteins Structure Function and Bioinformatics. 31(4). 345–354. 6 indexed citations
16.
Pons, Tirso, Osvaldo Olmea, Glay Chinea, et al.. (1998). Structural model for family 32 of glycosyl-hydrolase enzymes. Proteins Structure Function and Bioinformatics. 33(3). 383–395. 58 indexed citations
17.
Genzor, Carlos G., Carlos Gómez‐Moreno, Javier Sancho, et al.. (1996). Conformational stability of apoflavodoxin. Protein Science. 5(7). 1376–1388. 70 indexed citations
18.
Cortijo, Miguel, et al.. (1995). Digital control of a differential scanning microcalorimeter. Measurement Science and Technology. 6(8). 1086–1092. 7 indexed citations
19.
Pérez‐Gil, Jesús, José Luis López‐Lacomba, Antonio Cruz, Alejandro Beldarraı́n, & Cristina Casals. (1994). Deacylated pulmonary surfactant protein SP-C has different effects on the thermotroplc behaviour of bilayers of dipalmitoylphosphatidyl-glycerol (DPPG) than the native acylated protein. Biochemical Society Transactions. 22(3). 372S–372S. 9 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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