L. Serrano

4.3k total citations · 1 hit paper
18 papers, 3.2k citations indexed

About

L. Serrano is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, L. Serrano has authored 18 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 8 papers in Materials Chemistry and 3 papers in Cell Biology. Recurrent topics in L. Serrano's work include Protein Structure and Dynamics (11 papers), Enzyme Structure and Function (8 papers) and RNA and protein synthesis mechanisms (6 papers). L. Serrano is often cited by papers focused on Protein Structure and Dynamics (11 papers), Enzyme Structure and Function (8 papers) and RNA and protein synthesis mechanisms (6 papers). L. Serrano collaborates with scholars based in Germany, United Kingdom and Spain. L. Serrano's co-authors include François Stricher, Joost Schymkowitz, Françoise Rousseau-Hans, Jean‐Paul Borg, Ana Rosa Viguera, Mark Bycroft, Emmanuel Lacroix, A.R. Fersht, Alan R. Fersht and James T. Kellis and has published in prestigious journals such as Nature, Nucleic Acids Research and Bioinformatics.

In The Last Decade

L. Serrano

17 papers receiving 3.2k citations

Hit Papers

The FoldX web server: an online force field 2005 2026 2012 2019 2005 500 1000 1.5k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. The FoldX web server: an online force field
    2005 1.9k citations Joost Schymkowitz, Jean‐Paul Borg et al. Nucleic Acids Research profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L. Serrano Germany 12 2.6k 726 337 254 215 18 3.2k
H.T. Wright United States 26 2.0k 0.8× 563 0.8× 201 0.6× 296 1.2× 135 0.6× 61 3.0k
Meytal Landau Israel 31 3.2k 1.2× 509 0.7× 408 1.2× 338 1.3× 145 0.7× 76 4.7k
Kevin J. Lumb United States 29 2.2k 0.9× 656 0.9× 179 0.5× 247 1.0× 171 0.8× 51 2.9k
John Ionides United Kingdom 6 2.3k 0.9× 466 0.6× 268 0.8× 281 1.1× 129 0.6× 9 2.9k
Rasmus H. Fogh United Kingdom 16 2.8k 1.1× 606 0.8× 355 1.1× 335 1.3× 164 0.8× 27 3.6k
Achim Brinker United States 20 3.0k 1.1× 419 0.6× 204 0.6× 359 1.4× 168 0.8× 31 3.6k
Yifan Song China 18 2.3k 0.9× 633 0.9× 237 0.7× 176 0.7× 260 1.2× 46 3.0k
F. Niesen United Kingdom 19 2.7k 1.0× 443 0.6× 261 0.8× 401 1.6× 219 1.0× 25 3.5k
David E. Anderson United States 23 2.5k 1.0× 729 1.0× 530 1.6× 310 1.2× 210 1.0× 43 3.4k
Michał J. Gajda Germany 12 2.0k 0.8× 732 1.0× 223 0.7× 244 1.0× 90 0.4× 21 2.7k

Countries citing papers authored by L. Serrano

Since Specialization
Citations

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

Fields of papers citing papers by L. Serrano

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L. Serrano

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

All Works

18 of 18 papers shown
1.
2.
Encinar, José Antonio, Gregorio Fernández‐Ballester, Ignacio E. Sánchez, et al.. (2009). ADAN: a database for prediction of protein–protein interaction of modular domains mediated by linear motifs. Bioinformatics. 25(18). 2418–2424. 27 indexed citations
3.
Broglia, Ricardo A., L. Serrano, & Guido Tiana. (2007). Protein folding and drug design : Varenna on Lake Como, Villa Monastero, 4-14 July 2006. 2 indexed citations
4.
Serrano, L.. (2005). Modular Protein Domains Edited by G. Cesareni, M. Gimona, M. Sudol and M. Yaffe. Nature Cell Biology. 651–652. 1 indexed citations
5.
Schymkowitz, Joost, et al.. (2005). The FoldX web server: an online force field. Nucleic Acids Research. 33(Web Server). W382–W388. 1921 indexed citations breakdown →
6.
Sloot, Almer M. van der, Margaret M. Mullally, Gregorio Fernández‐Ballester, L. Serrano, & Wim J. Quax. (2004). Stabilization of TRAIL, an all- -sheet multimeric protein, using computational redesign. Protein Engineering Design and Selection. 17(9). 673–680. 30 indexed citations
7.
8.
Rischel, Christian, et al.. (2003). Mean first-passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding. Europhysics Letters (EPL). 61(4). 561–566. 8 indexed citations
9.
Westerholm‐Parvinen, Ann, Isabelle Vernos, & L. Serrano. (2000). Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization. FEBS Letters. 486(3). 285–290. 21 indexed citations
10.
Villegas, Sandra, José C. Martínez, Nico A. J. van Nuland, et al.. (2000). Thermodynamic analysis of helix‐engineered forms of the activation domain of human procarboxypeptidase A2. European Journal of Biochemistry. 267(19). 5891–5899. 11 indexed citations
11.
Taddei, Niccolò, Monica Bucciantini, Cristina Capanni, et al.. (2000). Stabilisation of α-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. Journal of Molecular Biology. 300(3). 633–647. 48 indexed citations
12.
Lacroix, Emmanuel, Ana Rosa Viguera, & L. Serrano. (1998). Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters 1 1Edited by A. R. Fersht. Journal of Molecular Biology. 284(1). 173–191. 384 indexed citations
13.
Blanco, Francisco J., Ángel R. Ortíz, & L. Serrano. (1997). Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragment. PubMed. 2(2). 123–133. 32 indexed citations
14.
Serrano, L., et al.. (1997). Effect of plant extracts on the pepper weevil (Anthonomus eugenii Cano): preliminary results in El Salvador.. 8(1). 99–107. 3 indexed citations
15.
Villegas, Sandra, Ana Rosa Viguera, Francesc Avilés, & L. Serrano. (1996). Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory. PubMed. 1(1). 29–34. 80 indexed citations
16.
Viguera, Ana Rosa & L. Serrano. (1995). Side-chain interactions between sulfur-containing amino acids and phenyalanine in .alpha.-helixes. Biochemistry. 34(27). 8771–8779. 133 indexed citations
17.
Serrano, L., Mark Bycroft, & A.R. Fersht. (1991). Aromatic-aromatic interactions and protein stability. Journal of Molecular Biology. 218(2). 465–475. 297 indexed citations
18.
Bycroft, Mark, Andreas Matouschek, James T. Kellis, L. Serrano, & Alan R. Fersht. (1990). Detection and characterization of a folding intermediate in barnase by NMR. Nature. 346(6283). 488–490. 189 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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