Margarida Archer

2.7k total citations
66 papers, 2.1k citations indexed

About

Margarida Archer is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Margarida Archer has authored 66 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 16 papers in Materials Chemistry and 9 papers in Organic Chemistry. Recurrent topics in Margarida Archer's work include Enzyme Structure and Function (14 papers), Photosynthetic Processes and Mechanisms (10 papers) and Biochemical and Molecular Research (8 papers). Margarida Archer is often cited by papers focused on Enzyme Structure and Function (14 papers), Photosynthetic Processes and Mechanisms (10 papers) and Biochemical and Molecular Research (8 papers). Margarida Archer collaborates with scholars based in Portugal, Germany and United Kingdom. Margarida Archer's co-authors include Inês A. C. Pereira, Isabel Moura, José J. G. Moura, Robert Huber, Jean LeGall, Tânia F. Oliveira, Maria João Romão, Peter Hof, Maria Luı́sa Rodrigues and José A. Brito and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Margarida Archer

64 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Margarida Archer Portugal 24 1.1k 623 416 263 173 66 2.1k
Vincent Nivière France 29 973 0.9× 348 0.6× 664 1.6× 295 1.1× 104 0.6× 52 1.9k
Karl Fisher United Kingdom 31 1.3k 1.2× 931 1.5× 506 1.2× 340 1.3× 94 0.5× 84 2.9k
Brian Bennett United States 22 875 0.8× 478 0.8× 399 1.0× 337 1.3× 78 0.5× 88 2.3k
Eberhard Warkentin Germany 27 1.0k 1.0× 1.1k 1.7× 693 1.7× 744 2.8× 144 0.8× 61 2.6k
Bruno Guigliarelli France 32 1.2k 1.1× 719 1.2× 369 0.9× 618 2.3× 75 0.4× 88 2.7k
Brett M. Barney United States 31 641 0.6× 1.3k 2.1× 481 1.2× 377 1.4× 117 0.7× 55 2.3k
Peter‐Leon Hagedoorn Netherlands 33 1.5k 1.4× 646 1.0× 570 1.4× 494 1.9× 136 0.8× 127 3.2k
Pablo J. González Argentina 23 424 0.4× 496 0.8× 350 0.8× 205 0.8× 97 0.6× 61 1.4k
Dennis H. Flint United States 20 1.4k 1.3× 1.1k 1.7× 419 1.0× 397 1.5× 61 0.4× 31 2.6k
Sean J. Elliott United States 31 1.5k 1.4× 986 1.6× 729 1.8× 444 1.7× 97 0.6× 90 3.2k

Countries citing papers authored by Margarida Archer

Since Specialization
Citations

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

Fields of papers citing papers by Margarida Archer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Margarida Archer

This figure shows the co-authorship network connecting the top 25 collaborators of Margarida Archer. A scholar is included among the top collaborators of Margarida Archer 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 Margarida Archer. Margarida Archer 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.
Erramilli, Satchal K., Yu-Jen Wang, Brian Kloss, et al.. (2025). Structural insights into terminal arabinosylation of mycobacterial cell wall arabinan. Nature Communications. 16(1). 3973–3973.
2.
Melo, Manuel N., et al.. (2023). Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids. Pharmaceutics. 15(1). 157–157. 6 indexed citations
3.
Archer, Margarida, et al.. (2022). In vitro neutralisation of Zika virus by an engineered protein targeting the viral envelope fusion loop. Molecular Systems Design & Engineering. 8(4). 516–526. 4 indexed citations
4.
Leandro, Paula, et al.. (2022). Impact of Fluorinated Ionic Liquids on Human Phenylalanine Hydroxylase—A Potential Drug Delivery System. Nanomaterials. 12(6). 893–893. 7 indexed citations
5.
Gonçalves, Juliana, Marta Alenquer, Filipe Ferreira, et al.. (2021). Secretory IgA and T cells targeting SARS-CoV-2 spike protein are transferred to the breastmilk upon mRNA vaccination. Cell Reports Medicine. 2(12). 100468–100468. 34 indexed citations
6.
Tan, Yong Zi, James E. Keener, Ruixiang Blake Zheng, et al.. (2020). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. Nature Communications. 11(1). 3396–3396. 15 indexed citations
7.
Nogły, Przemysław, et al.. (2020). Crystal Structure of Mannose Specific IIA Subunit of Phosphotransferase System from Streptococcus pneumoniae. Molecules. 25(20). 4633–4633. 4 indexed citations
8.
Nogły, Przemysław, Ivan Gushchin, Alina Remeeva, et al.. (2014). X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. Nature Communications. 5(1). 4169–4169. 40 indexed citations
9.
Brito, José A., et al.. (2014). Production, crystallization and preliminary crystallographic analysis ofAllochromatium vinosumthiosulfate dehydrogenase TsdA, an unusual acidophilicc-type cytochrome. Acta Crystallographica Section F Structural Biology Communications. 70(10). 1424–1427. 6 indexed citations
10.
Moraes, Isabel & Margarida Archer. (2014). Methods for the Successful Crystallization of Membrane Proteins. Methods in molecular biology. 1261. 211–230. 8 indexed citations
11.
Brito, José A., Tânia F. Oliveira, Przemysław Nogły, et al.. (2013). An Efficient Strategy for Small-Scale Screening and Production of Archaeal Membrane Transport Proteins in Escherichia coli. PLoS ONE. 8(10). e76913–e76913. 19 indexed citations
12.
Oliveira, Tânia F., Edward Franklin, Amir R. Khan, et al.. (2011). Structural Insights into Dissimilatory Sulfite Reductases: Structure of Desulforubidin from Desulfomicrobium Norvegicum. Frontiers in Microbiology. 2. 71–71. 33 indexed citations
13.
Brito, José A., Filipa L. Sousa, Meike Stelter, et al.. (2009). Structural and Functional Insights into Sulfide:Quinone Oxidoreductase ,. Biochemistry. 48(24). 5613–5622. 114 indexed citations
14.
Stelter, Meike, Ana M. P. Melo, Guðmundur Ó. Hreggviðsson, et al.. (2009). Structure at 1.0 Å resolution of a high-potential iron–sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus. JBIC Journal of Biological Inorganic Chemistry. 15(3). 303–313. 20 indexed citations
15.
Rodrigues, Maria Luı́sa, Margarida Archer, Paulo Martel, et al.. (2005). Crystal structures of the free and sterol-bound forms of β-cinnamomin. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764(1). 110–121. 29 indexed citations
16.
Rodrigues, Mariana Lins, Margarida Archer, Paulo Martel, et al.. (2002). Crystal structure of β-cinnamomin, a toxic protein fromPhytophthora cinnamomi. Acta Crystallographica Section A Foundations of Crystallography. 58(s1). c298–c298. 2 indexed citations
17.
Bonifácio, Maria João, Margarida Archer, Maria Luı́sa Rodrigues, et al.. (2002). Kinetics and Crystal Structure of Catechol-O-Methyltransferase Complex with Co-Substrate and a Novel Inhibitor with Potential Therapeutic Application. Molecular Pharmacology. 62(4). 795–805. 76 indexed citations
18.
Rodrigues, Mariana Lins, Margarida Archer, Maria João Bonifácio, Patrício Soares‐da‐Silva, & M.A. Carrondo. (2001). Crystallization and preliminary crystallographic characterization of catechol-O-methyltransferase in complex with its cosubstrate and an inhibitor. Acta Crystallographica Section D Biological Crystallography. 57(6). 906–908. 7 indexed citations
19.
Archer, Margarida, Robert Huber, Pedro Tavares, et al.. (1995). Crystal Structure of Desulforedoxin fromDesulfovibrio gigasDetermined at 1.8 Å Resolution: A Novel Non-heme Iron Protein Structure. Journal of Molecular Biology. 251(5). 690–702. 70 indexed citations
20.
Romão, Maria João, Margarida Archer, Isabel Moura, et al.. (1993). Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe‐2S] centers. European Journal of Biochemistry. 215(3). 729–732. 23 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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