Francisco Conejero‐Lara

1.5k total citations
61 papers, 1.3k citations indexed

About

Francisco Conejero‐Lara is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Francisco Conejero‐Lara has authored 61 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 20 papers in Materials Chemistry and 16 papers in Physiology. Recurrent topics in Francisco Conejero‐Lara's work include Protein Structure and Dynamics (30 papers), Enzyme Structure and Function (17 papers) and Alzheimer's disease research and treatments (13 papers). Francisco Conejero‐Lara is often cited by papers focused on Protein Structure and Dynamics (30 papers), Enzyme Structure and Function (17 papers) and Alzheimer's disease research and treatments (13 papers). Francisco Conejero‐Lara collaborates with scholars based in Spain, France and United Kingdom. Francisco Conejero‐Lara's co-authors include Bertrand Morel, Ana I. Azuaga, Pedro L. Mateo, Lorena Varela, Salvador Casares, Christopher M. Dobson, Mourad Sadqi, José M. Sánchez‐Ruiz, Chris P. Ponting and Francesc Avilés and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Francisco Conejero‐Lara

60 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Francisco Conejero‐Lara Spain 21 918 298 289 131 98 61 1.3k
Yuji O. Kamatari Japan 24 1.4k 1.5× 184 0.6× 374 1.3× 47 0.4× 42 0.4× 85 1.7k
Cordelia Schiene‐Fischer Germany 29 1.5k 1.7× 287 1.0× 182 0.6× 82 0.6× 153 1.6× 53 2.1k
Luciana Esposito Italy 23 1.1k 1.2× 191 0.6× 437 1.5× 89 0.7× 28 0.3× 74 1.4k
Claus Spitzfaden United Kingdom 18 1.1k 1.2× 190 0.6× 249 0.9× 56 0.4× 60 0.6× 21 1.6k
Jozef Ševčı́k Slovakia 16 891 1.0× 111 0.4× 284 1.0× 42 0.3× 45 0.5× 34 1.3k
Ronald W. Sarver United States 17 701 0.8× 90 0.3× 168 0.6× 26 0.2× 67 0.7× 33 1.1k
Vinod Bhakuni India 19 1.0k 1.1× 94 0.3× 360 1.2× 26 0.2× 88 0.9× 60 1.4k
Laurent Vuillard France 19 763 0.8× 133 0.4× 184 0.6× 36 0.3× 37 0.4× 33 1.2k
Kenji Sasahara Japan 22 914 1.0× 457 1.5× 281 1.0× 125 1.0× 13 0.1× 46 1.3k
J.F. Cutfield New Zealand 22 1.2k 1.3× 110 0.4× 299 1.0× 34 0.3× 102 1.0× 36 1.8k

Countries citing papers authored by Francisco Conejero‐Lara

Since Specialization
Citations

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

Fields of papers citing papers by Francisco Conejero‐Lara

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Francisco Conejero‐Lara. 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 Francisco Conejero‐Lara. The network helps show where Francisco Conejero‐Lara may publish in the future.

Co-authorship network of co-authors of Francisco Conejero‐Lara

This figure shows the co-authorship network connecting the top 25 collaborators of Francisco Conejero‐Lara. A scholar is included among the top collaborators of Francisco Conejero‐Lara 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 Francisco Conejero‐Lara. Francisco Conejero‐Lara 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.
Conejero‐Lara, Francisco, et al.. (2024). Selective Formation of Pd‐DNA Hybrids Using Tailored Palladium‐Mediated Base Pairs: Towards Heteroleptic Pd‐DNA Systems. Angewandte Chemie International Edition. 63(11). e202400261–e202400261. 2 indexed citations
2.
Laumond, Géraldine, et al.. (2022). Exploring Highly Conserved Regions of SARS-CoV-2 Spike S2 Subunit as Targets for Fusion Inhibition Using Chimeric Proteins. International Journal of Molecular Sciences. 23(24). 15511–15511. 2 indexed citations
3.
Contreras‐Montoya, Rafael, Mercedes González, Vaibhav Bhatia, et al.. (2021). Insulin Crystals Grown in Short-Peptide Supramolecular Hydrogels Show Enhanced Thermal Stability and Slower Release Profile. ACS Applied Materials & Interfaces. 13(10). 11672–11682. 27 indexed citations
4.
González‐Vera, Juan A., Francisco Conejero‐Lara, Víctor Blanco, et al.. (2021). In situreal-time monitoring of the mechanism of self-assembly of short peptide supramolecular polymers. Materials Chemistry Frontiers. 5(14). 5452–5462. 26 indexed citations
5.
Morel, Bertrand, et al.. (2021). Conformational flexibility of the conserved hydrophobic pocket of HIV-1 gp41. Implications for the discovery of small-molecule fusion inhibitors. International Journal of Biological Macromolecules. 192. 90–99. 5 indexed citations
6.
Bourdely, Pierre, Carmelo Luci, Nathalie Dereuddre‐Bosquet, et al.. (2017). Sublingual Priming with a HIV gp41-Based Subunit Vaccine Elicits Mucosal Antibodies and Persistent B Memory Responses in Non-Human Primates. Frontiers in Immunology. 8. 63–63. 7 indexed citations
7.
Morel, Bertrand, Salvador Casares, Pedro L. Mateo, et al.. (2016). Molecular and Physicochemical Factors Governing Solubility of the HIV gp41 Ectodomain. Biophysical Journal. 111(4). 700–709. 3 indexed citations
8.
9.
Lacal, Jesús, Carlos Alfonso, Xianxian Liu, et al.. (2010). Identification of a Chemoreceptor for Tricarboxylic Acid Cycle Intermediates. Journal of Biological Chemistry. 285(30). 23126–23136. 83 indexed citations
10.
Morel, Bertrand, Lorena Varela, Ana I. Azuaga, & Francisco Conejero‐Lara. (2010). Environmental Conditions Affect the Kinetics of Nucleation of Amyloid Fibrils and Determine Their Morphology. Biophysical Journal. 99(11). 3801–3810. 101 indexed citations
11.
Candel, Adela M., Eva S. Cobos, Francisco Conejero‐Lara, & José C. Martínez. (2009). Evaluation of folding co-operativity of a chimeric protein based on the molecular recognition between polyproline ligands and SH3 domains. Protein Engineering Design and Selection. 22(10). 597–606. 4 indexed citations
12.
Varela, Lorena, Bertrand Morel, Ana I. Azuaga, & Francisco Conejero‐Lara. (2009). A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state. FEBS Letters. 583(4). 801–806. 19 indexed citations
13.
Casares, Salvador, et al.. (2007). The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3. BMC Structural Biology. 7(1). 22–22. 24 indexed citations
14.
Morel, Bertrand, Salvador Casares, & Francisco Conejero‐Lara. (2005). A Single Mutation Induces Amyloid Aggregation in the α-Spectrin SH3 Domain: Analysis of the Early Stages of Fibril Formation. Journal of Molecular Biology. 356(2). 453–468. 45 indexed citations
15.
Casares, Salvador, et al.. (2003). Structural cooperativity in the SH3 domain studied by site‐directed mutagenesis and amide hydrogen exchange. FEBS Letters. 539(1-3). 125–130. 16 indexed citations
16.
Sadqi, Mourad, et al.. (2002). The temperature dependence of the hydrogen exchange in the SH3 domain of α‐spectrin. FEBS Letters. 527(1-3). 86–90. 10 indexed citations
17.
18.
Azuaga, Ana I., Francisco Conejero‐Lara, Germán Rivas, et al.. (1995). The thermodynamics of association and unfolding of the 205–316 C-terminal fragment of thermolysin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1252(1). 95–102. 8 indexed citations
19.
Conejero‐Lara, Francisco, Pedro L. Mateo, Francesc Avilés, & José M. Sánchez‐Ruiz. (1991). Effect of zinc(2+) on the thermal denaturation of carboxypeptidase B. Biochemistry. 30(8). 2067–2072. 44 indexed citations
20.
Conejero‐Lara, Francisco, et al.. (1991). Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain. European Journal of Biochemistry. 200(3). 663–670. 41 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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