Amero Tello Carlos

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

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

  • Estudio estructural y funcional de proteínas virales.
  • Caracterización espectroscopica del desplegamiento de la cristalina humana.
  •  Estudios de proteinas y peptidos intrinsicamente despelgadas.
  • Caracterizacion de la formacion de fibras amiloides por proteinas de cadena ligera debida a la temperatura.
  • Caracterizacion de la formacion de fibras amiloides por proteinas de cadena ligera con metales .
  • Caracterización estructural de toxinas y peptidos antimicrobianos.

  1. Cardenas Mena Reinier Felipe 
  2. Ramírez Bello Vanesa Margarita
  3. Meunier Carmenate Yadira Rosa
  4. Castañeda Gutierrez Kimberly
  5. Martínez Seoane Javier Alejandro
  6. Leyva Rodríguez Liliana


Share by: