Rosario Recacha

556 total citations
22 papers, 423 citations indexed

About

Rosario Recacha is a scholar working on Molecular Biology, Cell Biology and Public Health, Environmental and Occupational Health. According to data from OpenAlex, Rosario Recacha has authored 22 papers receiving a total of 423 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 6 papers in Cell Biology and 5 papers in Public Health, Environmental and Occupational Health. Recurrent topics in Rosario Recacha's work include Malaria Research and Control (5 papers), Erythrocyte Function and Pathophysiology (3 papers) and Cellular transport and secretion (3 papers). Rosario Recacha is often cited by papers focused on Malaria Research and Control (5 papers), Erythrocyte Function and Pathophysiology (3 papers) and Cellular transport and secretion (3 papers). Rosario Recacha collaborates with scholars based in United States, Finland and Latvia. Rosario Recacha's co-authors include Bruce E. Maryanoff, Debasish Chattopadhyay, Michael J. Costanzo, Bruno Goud, Amir R. Khan, Anne Houdusse, Solange Monier, Florence Jollivet, Annick Boulet and Patricia Andrade‐Gordon and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Scientific Reports.

In The Last Decade

Rosario Recacha

21 papers receiving 417 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Rosario Recacha United States	11	227	96	93	51	45	22	423
Paul Workman United Kingdom	5	279 1.2×	159 1.7×	62 0.7×	34 0.7×	32 0.7×	5	483
Jacob A. McPhail Canada	11	249 1.1×	126 1.3×	60 0.6×	46 0.9×	27 0.6×	16	400
Stephan Krapp Germany	9	345 1.5×	64 0.7×	86 0.9×	47 0.9×	40 0.9×	14	456
Nancy S. Wang United States	5	290 1.3×	66 0.7×	36 0.4×	38 0.7×	22 0.5×	7	460
Elizabeth A. Blackburn United Kingdom	15	433 1.9×	97 1.0×	28 0.3×	52 1.0×	31 0.7×	33	566
Monika Suchanek Germany	5	469 2.1×	153 1.6×	101 1.1×	49 1.0×	35 0.8×	5	682
Timothy S. Strutzenberg United States	13	463 2.0×	33 0.3×	21 0.2×	50 1.0×	32 0.7×	21	617
Stefan O. Ochiana United States	11	471 2.1×	78 0.8×	80 0.9×	72 1.4×	18 0.4×	14	590
Mitchell Vamos United States	8	494 2.2×	131 1.4×	63 0.7×	125 2.5×	30 0.7×	11	891
Patrick R. Cushing United States	10	346 1.5×	148 1.5×	30 0.3×	46 0.9×	14 0.3×	14	503

Countries citing papers authored by Rosario Recacha

Since Specialization

Citations

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

Fields of papers citing papers by Rosario Recacha

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rosario Recacha

This figure shows the co-authorship network connecting the top 25 collaborators of Rosario Recacha. A scholar is included among the top collaborators of Rosario Recacha 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 Rosario Recacha. Rosario Recacha 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

1.

Recacha, Rosario, et al.. (2024). Bulky hydrophobic side chains in the β1-sandwich of microsomal triglyceride transfer protein are critical for the transfer of both triglycerides and phospholipids. Journal of Biological Chemistry. 300(3). 105726–105726. 2 indexed citations

2.

Recacha, Rosario, et al.. (2023). Production of neutralizing antibody fragment variants in the cytoplasm of E. coli for rapid screening: SARS-CoV-2 a case study. Scientific Reports. 13(1). 4408–4408. 6 indexed citations

3.

Wilson, Meredith H., Sujith Rajan, Richard White, et al.. (2020). A point mutation decouples the lipid transfer activities of microsomal triglyceride transfer protein. PLoS Genetics. 16(8). e1008941–e1008941. 25 indexed citations

4.

Zhang, Chi, et al.. (2020). Efficient soluble production of folded cat allergen Fel d 1 in Escherichia coli. Protein Expression and Purification. 180. 105809–105809. 1 indexed citations

5.

Santiago, César, Gaurav Mudgal, Juan Reguera, et al.. (2017). Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection. Scientific Reports. 7(1). 46045–46045. 26 indexed citations

6.

Recacha, Rosario, Kristaps Jaudzems, Ināra Akopjana, Aigars Jirgensons, & Kaspars Tārs. (2016). Crystal structure ofPlasmodium falciparumproplasmepsin IV: the plasticity of proplasmepsins. Acta Crystallographica Section F Structural Biology Communications. 72(9). 659–666. 6 indexed citations

7.

Recacha, Rosario, Kristaps Jaudzems, Ināra Akopjana, Aigars Jirgensons, & Kaspars Tārs. (2016). Crystal Structure of Plasmodium Falciparum Proplasmepsin IV: the Plasticity of Proplasmepsins. 72. 659–666. 1 indexed citations

8.

Recacha, Rosario, et al.. (2015). Structures of Plasmepsin II from Plasmodium Falciparum in Complex with Two Hydroxyethylamine-based Inhibitors. publication.editionName. 71. 1531–1539.

9.

Rasiņa, Dace, Mārtiņš Otikovs, Ja̅nis Leita̅ns, et al.. (2015). Fragment-Based Discovery of 2-Aminoquinazolin-4(3H)-ones As Novel Class Nonpeptidomimetic Inhibitors of the Plasmepsins I, II, and IV. Journal of Medicinal Chemistry. 59(1). 374–387. 46 indexed citations

10.

Recacha, Rosario, Ja̅nis Leita̅ns, Ināra Akopjana, et al.. (2015). Structures of plasmepsin II fromPlasmodium falciparumin complex with two hydroxyethylamine-based inhibitors. Acta Crystallographica Section F Structural Biology Communications. 71(12). 1531–1539. 16 indexed citations

11.

Recacha, Rosario, et al.. (2014). Crystal structures of an ICAM-5 ectodomain fragment show electrostatic-based homophilic adhesions. Acta Crystallographica Section D Biological Crystallography. 70(7). 1934–1943. 7 indexed citations

12.

Recacha, Rosario, Annick Boulet, Florence Jollivet, et al.. (2009). Structural Basis for Recruitment of Rab6-Interacting Protein 1 to Golgi via a RUN Domain. Structure. 17(1). 21–30. 68 indexed citations

13.

Fernandes, Humberto, Edward Franklin, Rosario Recacha, et al.. (2009). Structural aspects of Rab6–effector complexes. Biochemical Society Transactions. 37(5). 1037–1041. 22 indexed citations

14.

Recacha, Rosario, Michael J. Costanzo, Bruce E. Maryanoff, & Debasish Chattopadhyay. (2002). Crystal structure of human carbonic anhydrase II complexed with ananti-convulsant sugar sulphamate. Biochemical Journal. 361(3). 437–437. 30 indexed citations

15.

Recacha, Rosario, Michael J. Costanzo, Bruce E. Maryanoff, & Debasish Chattopadhyay. (2002). Crystal structure of human carbonic anhydrase II complexed with ananti-convulsant sugar sulphamate. Biochemical Journal. 361(3). 437–441. 25 indexed citations

16.

Recacha, Rosario, Michael J. Costanzo, Bruce E. Maryanoff, et al.. (2000). Structure of human α-thrombin complexed with RWJ-51438 at 1.7 Å: unusual perturbation of the 60A–60I insertion loop. Acta Crystallographica Section D Biological Crystallography. 56(11). 1395–1400. 4 indexed citations

17.

Recacha, Rosario, et al.. (2000). Toxoplasma gondii adenosine kinase: expression, purification, characterization, crystallization and preliminary crystallographic analysis. Acta Crystallographica Section D Biological Crystallography. 56(1). 76–78. 6 indexed citations

18.

Chattopadhyay, Debasish, et al.. (2000). Structure of the nucleotide-binding domain ofPlasmodium falciparumRab6 in the GDP-bound form. Acta Crystallographica Section D Biological Crystallography. 56(8). 937–944. 25 indexed citations

19.

Recacha, Rosario, et al.. (1999). Structure of the RWJ-51084–bovine pancreatic β-trypsin complex at 1.8 Å. Acta Crystallographica Section D Biological Crystallography. 55(11). 1785–1791. 4 indexed citations

20.

Recacha, Rosario, Núria Verdaguer, & Juan A. Subirana. (1997). Structure and supramolecular packing features of the dipeptide Arg‐Val acetate. Journal of Peptide Research. 50(5). 388–392. 1 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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