Carlos Amero Tello
Doctorado en Biofísica, Ohio State University, EUA (2008)
Profesor: Titular C
SNI: Nivel II
Líneas de Investigación: Bioquímica y Resonancia Magnética Nuclear
Cuerpo Académico: UAEMOR-CA-160 Dinámica de Proteínas
Consolidado
LGAC : Dinámica de proteínas, reconocimiento molecular y agregación
Laboratorio de Bioquímica y Resonancia Magnetica Nuclear
carlosamero@uaem.mx | www.labrmn.com | Teléfono: +52 777 329 7997 Ext.6043
ORCID: 0000-0001-6300-0241| ResearcherID: C-6952-2011| Google Académico
2022
37. Meunier-Carmenate, Y., Valdés-García, G., Maya-Martinez, R., French-Pacheco, L., Fernández-Silva, A., González-Onofre, Y., Millan-Pacheco, C., Pastor, N.*, & Amero, C.* (2023). Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains. Biochemistry, 62(5), 1000–1011. https://doi.org/10.1021/acs.biochem.2c00704
36. Meunier-Carmenate, Y., Valdés-García, G., Maya-Martinez, R., French-Pacheco, L., Fernández-Silva, A., González-Onofre, Y., Millan-Pacheco, C., Pastor, N.*, & Amero, C*. (2023). Unfolding and Aggregation Pathways of Variable Domains from Immunoglobulin Light Chains. Biochemistry, 62(5), 1000–1011. DOI: 10.1021/acs.biochem.2c00704
35. Fernández-Silva, A., Lledías, F., Rodríguez-López, J., Olivares, J. E., French-Pacheco, L., Treviño, M., Amero, C.*, & Díaz-Camino, C. (2022). The Common Bean Small Heat Shock Protein Nodulin 22 from Phaseolus vulgaris L. Assembles into Functional High-Molecular-Weight Oligomers. Molecules, 27(24), 8681. DOI: 10.3390/molecules27248681
34. Ramirez-Bello, V.; Martinez-Seoane, J.; Fernández-Silva, A.; Amero, C.* Zinc and Copper Ions Induce Aggregation of Human β-Crystallins. Molecules 2022, 27 (9), 2970. DOI: 10.3390/molecules27092970
2020
33. Cárdenas, R.; Martínez-Seoane, J.; Amero, C.* Combining Experimental Data and Computational Methods for the Non-Computer Specialist. Molecules 2020, 25 (20), 4783 DOI: 10.3390/molecules2520478
32. UnnikrishnanA.; Amero, C.; Yadav, K.; Stachowski, K.; Potter, D.; Foster, M.*; (2020) DNA Binding Induces a cis to trans Switch in Cre Recombinase to Enable Intasome Assembly, Proceedings of the National Academy of Sciences 117 (40), 24849-24858, https://doi.org/10.1101/2020.05.24.113654
31. Fernández-Silva, A., French-Pacheco, L., Rivillas-Acevedo, L.*, & Amero, C.* (2020). Aggregation pathways of human γ D crystallin induced by metal ions revealed by time dependent methods. PeerJ, 8, e9178. https://doi.org/10.7717/peerj.9178
ARTÍCULOS EN REVISTAS INDEXADAS
2020
33. Cárdenas, R.; Martínez-Seoane, J.; Amero, C.* Combining Experimental Data and Computational Methods for the Non-Computer Specialist. Molecules 2020, 25 (20), 4783 DOI: 10.3390/molecules2520478
32. UnnikrishnanA.; Amero, C.; Yadav, K.; Stachowski, K.; Potter, D.; Foster, M.*; (2020) DNA Binding Induces a cis to trans Switch in Cre Recombinase to Enable Intasome Assembly, Proceedings of the National Academy of Sciences 117 (40), 24849-24858, https://doi.org/10.1101/2020.05.24.113654
31. Fernández-Silva, A., French-Pacheco, L., Rivillas-Acevedo, L.*, & Amero, C.* (2020). Aggregation pathways of human γ D crystallin induced by metal ions revealed by time dependent methods. PeerJ, 8, e9178. https://doi.org/10.7717/peerj.9178
30. Pelaez-Aguilar, A. E., Valdés-García, G., French-Pacheco, L., Pastor, N., Amero, C., & Rivillas-Acevedo, L.* (2020). Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G. ACS Omega, 5(13), 7085–7095. https://doi.org/10.1021/acsomega.9b03220
2019
29. Rudiño-Piñera, E.; Peláez-Aguilar, Á. E.; Amero, C.; Díaz-Vilchis, A.* Crystal Structure of 6aJL2-R24G Light Chain Variable Domain: Does Crystal Packing Explain Amyloid Fibril Formation? Biochem. Biophys. Reports 2019, 20, 100682 DOI: 10.1016/j.bbrep.2019.100682
28. Maya-Martinez, R.; French-Pacheco, L.; Valdés-García, G.; Pastor, N.; Amero, C.* Different Dynamics in 6aJL2 Proteins Associated with AL Amyloidosis, a Conformational Disease. Int. J. Mol. Sci. 2019, 20 (17), 4078 DOI: 10.3390/ijms20174078
27. Rodriguez, A.; Pedersen, M. Ø.; Villegas, E.; Rivas‐Santiago, B.; Villegas‐Moreno, J.; Amero, C.; Norton, R. S.; Corzo, G.* Antimicrobial Activity and Structure of a Consensus Human Β‐defensin and Its Comparison to a Novel Putative HBD10. Proteins Struct. Funct. Bioinforma. 2019, prot.25785 DOI: 10.1002/prot.25785
26. Tejera, B.; López, R. E.; Hidalgo, P.; Cárdenas, R.; Ballesteros, G.; Rivillas, L.; French, L.; Amero, C.; Pastor, N.; Santiago, Á.; Groitl, P.; Dobner, T.; Gonzalez, R. A.* The Human Adenovirus Type 5 E1B 55kDa Protein Interacts with RNA Promoting Timely DNA Replication and Viral Late MRNA Metabolism. PLoS One 2019, 14 (4), e0214882 DOI: 10.1371/journal.pone.0214882
2018
25. Velázquez-López, I.; Valdés-García, G.; Romero Romero, S.; Maya Martínez, R.; Leal-Cervantes, A. I.; Costas, M.; Sánchez-López, R.; Amero, C.; Pastor, N.*; Fernández Velasco, D. A.* Localized Conformational Changes Trigger the PH-Induced Fibrillogenesis of an Amyloidogenic λ Light Chain Protein. Biochim. Biophys. Acta - Gen. Subj. 2018, 1862 (7), 1656–1666. DOI: 10.1016/j.bbagen.2018.04.014
24. Krishnarjuna, B.; Villegas-Moreno, J.; Mitchell, M. L.; Csoti, A.; Peigneur, S.; Amero, C.; Pennington, M. W.; Tytgat, J.; Panyi, G.; Norton, R. S.* Synthesis, Folding, Structure and Activity of a Predicted Peptide from the Sea Anemone Oulactis Sp. with an ShKT Fold. Toxicon 2018, 150, 50–59. DOI: 10.1016/j.toxicon.2018.05.006
23. French-Pacheco, L.; Cuevas-Velazquez, C. L.; Rivillas-Acevedo, L.; Covarrubias, A. A.; Amero, C.* Metal-Binding Polymorphism in Late Embryogenesis Abundant Protein AtLEA4-5, an Intrinsically Disordered Protein. PeerJ 2018, 6, e4930. DOI: 10.7717/peerj.4930
2017
22. Macek, P.; Kerfah, R.*; Erba, E. B.; Crublet, E.*; Moriscot, C.; Schoehn, G.; Amero, C.; Boisbouvier, J. Unraveling Self-Assembly Pathways of the 468-kDa Proteolytic Machine TET2. Sci. Adv. 2017, 3 (4), e1601601. DOI: 10.1126/sciadv.1601601
21. Sánchez-Carbente, M. del R.; Batista-García, R. A.; Sánchez-Reyes, A.; Escudero-Garcia, A.; Morales-Herrera, C.; Cuervo-Soto, L. I.; French-Pacheco, L.; Fernández-Silva, A.; Amero, C.; Castillo, E.; Folch-Mallol, J. L.* The First Description of a Hormone-Sensitive Lipase from a Basidiomycete: Structural Insights and Biochemical Characterization Revealed Bjerkandera Adusta Ba EstB as a Novel Esterase. Microbiologyopen 2017, e00463. DOI: 10.1002/mbo3.463
2016
20. Quintanar, L.*; Domínguez-Calva, J. A.; Serebryany, E.; Rivillas-Acevedo, L.; Haase-Pettingell, C.; Amero, C.; King, J. A.* Copper and Zinc Ions Specifically Promote Nonamyloid Aggregation of the Highly Stable Human γ-D Crystallin. ACS Chem. Biol. 2016, 11 (1), 263–272. DOI: 10.1021/acschembio.5b00919
2015
19. Rivillas-Acevedo, L.*; Sánchez-López, C.; Amero, C.; Quintanar, L.* Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes. Inorg. Chem. 2015, 54 (8), 3788–3796. DOI: 10.1021/ic502945k
18. Rivillas-Acevedo, L.; Fernández-Silva, A.; Amero, C.* Function, Structure and Stability of Human Gamma D Crystallins: A Review. In Physical Biology of Proteins and Peptides: Theory, Experiment, and Simulation; 2015; pp 81–98. DOI: 10.1007/978-3-319-21687-4_5
17. Pelaez-Aguilar, A. E.; Rivillas-Acevedo, L.; French-Pacheco, L.; Valdes-Garcia, G.; Maya-Martinez, R.; Pastor, N.; Amero, C.* Inhibition of Light Chain 6aJL2-R24G Amyloid Fiber Formation Associated with Light Chain Amyloidosis. Biochemistry 2015, 54 (32), 4978–4986. DOI: 10.1021/acs.biochem.5b00288
16. Pastor, N.*; Amero, C. Information Flow and Protein Dynamics: The Interplay between Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulations. Front. Plant Sci. 2015, 6 (MAY). DOI: 10.3389/fpls.2015.00306
15. Maya-Martinez, R.; Gil-Rodriguez, P.; Amero, C*. Solution Structure of 6aJL2 and 6aJL2-R24G Amyloidogenics Light Chain Proteins. Biochem. Biophys. Res. Commun. 2015, 456 (2), 695–699. DOI: 10.1016/j.bbrc.2014.12.044
14. Gil-Rodríguez, P.; Amero, C.* 1H, 15N and 13C ; Resonance Assignments for 3rC and 3rCWP: Amyloidogenic Variants of Imunoglobulin λ 3 Light-Chain. Biomol. NMR Assign. 2015, 9 (1), 139–142. DOI: 10.1007/s12104-014-9560-4
2014
13. Rivera-Najera, L. Y.; Saab-Rincón, G.; Battaglia, M.; Amero, C.; Pulido, N. O.; García-Hernández, E.; Solórzano, R. M.; Reyes, J. L.; Covarrubias, A. A. A Group 6 Late Embryogenesis Abundant Protein from Common Bean Is a Disordered Protein with Extended Helical Structure and Oligomer-Forming Properties. J. Biol. Chem. 2014, 289 (46), 31995–32009. DOI: 10.1074/jbc.M114.583369
2012
12. Rodríguez Plaza, J. G.; Villalón Rojas, A.; Herrera, S.; Garza-Ramos, G.; Torres Larios, A.; Amero, C.; Zarraga Granados, G.; Gutiérrez Aguilar, M.; Lara Ortiz, M. T.; Polanco Gonzalez, C.; Uribe Carvajal, S.; Coria, R.; Peña Díaz, A.; Bredesen, D. E.; Castro-Obregon, S.; del Rio, G.* Moonlighting Peptides with Emerging Function. PLoS One 2012, 7 (7). DOI: 10.1371/journal.pone.0040125
11. Ayala, I.; Hamelin, O.; Amero, C.; Pessey, O.; Plevin, M. J.; Gans, P.; Boisbouvier, J.* An Optimized Isotopic Labelling Strategy of Isoleucine-γ <inf>2</inf> Methyl Groups for Solution NMR Studies of High Molecular Weight Proteins. Chem. Commun. 2012, 48 (10), 1434–1436. DOI: 10.1039/c1cc12932e
2011
10. Amero, C.; Asunción Durá, M.; Noirclerc-Savoye, M.; Perollier, A.; Gallet, B.; Plevin, M. J.; Vernet, T.; Franzetti, B.; Boisbouvier, J*. A Systematic Mutagenesis-Driven Strategy for Site-Resolved NMR Studies of Supramolecular Assemblies. J. Biomol. NMR 2011, 50 (3), 229–236. DOI: 10.1007/s10858-011-9513-5
2010
9. Gans, P.; Hamelin, O.; Sounier, R.; Ayala, I.; Durá, M. A.; Amero, C.; Noirclerc-Savoye, M.; Franzetti, B.; Plevin, M. J.; Boisbouvier, J.* Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins. Angew. Chemie - Int. Ed. 2010, 49 (11), 1958–1962. DOI: 10.1002/anie.200905660
2009
8. Xu, Y.; Amero, C.; Pulukkunat, D. K.; Gopalan, V.*; Foster, M. P*. Solution Structure of an Archaeal RNase P Binary Protein Complex: Formation of the 30-kDa Complex between Pyrococcus Furiosus RPP21 and RPP29 Is Accompanied by Coupled Protein Folding and Highlights Critical Features for Protein-Protein and Protein-RNA Interactions. J. Mol. Biol. 2009, 393 (5), 1043–1055. DOI: 10.1016/j.jmb.2009.08.068
7. Amero, C.; Schanda, P.; Asunción Durá, M.; Ayala, I.; Marion, D.; Franzetti, B.; Brutscher, B.; Boisbouvier, J.* Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies. J. Am. Chem. Soc. 2009, 131 (10), 3448–3449. DOI: 10.1021/ja809880p
6. Amero, C.; Byerly, D. W.; McElroy, C. A.; Simmons, A.; Foster, M. P.* Ligand-Induced Changes in the Structure and Dynamics of Escherichia Coli Peptide Deformylase. Biochemistry 2009, 48 (32), 7595–7607. DOI: 10.1021/bi900600b
2008
5. Amero, C.; Boomershine, W. P.; Xu, Y.; Foster, M.* Solution Structure of Pyrococcus Furiosus RPP21, a Component of the Archaeal RNase P Holoenzyme, and Interactions with Its RPP29 Protein Partner. Biochemistry 2008, 47 (45), 11704–11710. DOI: 10.1021/bi8015982
4. Amero, C.; Arnold, J. J.; Moustafa, I. M.; Cameron, C. E.*; Foster, M. P.* Identification of the oriI-Binding Site of Poliovirus 3C Protein by Nuclear Magnetic Resonance Spectroscopy. J. Virol. 2008, 82 (9), 4363–4370. DOI: 10.1128/JVI.02087-07
2007
3. Foster, M. P.*; McElroy, C. A.; Amero, C. Solution NMR of Large Molecules and Assemblies. Biochemistry 2007, 46 (2), 331–340. DOI: 10.1021/bi0621314
2002
2. Espinosa, G.; Amero, C.; B. Gammage, R. Measurements of Alpha Particle Energy Using Nuclear Tracks in Solids Methodology. Radiat. Prot. Dosim. 2002, 101 (1–4), 561–564. DOI: 10.1093/oxfordjournals.rpd.a006049
2001
1. Amero, C.; Golzarri, J. I.; Izerrouken, M.; Espinosa, G.* 148Gd, 238U, 239Pu and 244Cm Alpha Particle Energy Analysis Using Tracks in Solids. Radiat. Meas. 2001, 34 (1–6), 341–343. DOI: 10.1016/S1350-4487(01)00180-9