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Items: 13

1.

Identification of a pore-forming protein from sea anemone Anthopleura dowii Verrill (1869) venom by mass spectrometry.

Ramírez-Carreto S, Pérez-García EI, Salazar-García SI, Bernáldez-Sarabia J, Licea-Navarro A, Rudiño-Piñera E, Pérez-Martínez L, Pedraza-Alva G, Rodríguez-Almazán C.

J Venom Anim Toxins Incl Trop Dis. 2019 Feb 11;25:e147418. doi: 10.1590/1678-9199-JVATITD-1474-18. eCollection 2019.

2.

Sequencing and de novo transcriptome assembly of Anthopleura dowii Verrill (1869), from Mexico.

Ayala-Sumuano JT, Licea-Navarro A, Rudiño-Piñera E, Rodríguez E, Rodríguez-Almazán C.

Genom Data. 2016 Dec 5;11:92-94. doi: 10.1016/j.gdata.2016.11.022. eCollection 2017 Mar.

3.

X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.

Serrano-Posada H, Centeno-Leija S, Rojas-Trejo SP, Rodríguez-Almazán C, Stojanoff V, Rudiño-Piñera E.

Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2396-411. doi: 10.1107/S1399004715018714. Epub 2015 Nov 26.

4.

Evolution of Bacillus thuringiensis Cry toxins insecticidal activity.

Bravo A, Gómez I, Porta H, García-Gómez BI, Rodriguez-Almazan C, Pardo L, Soberón M.

Microb Biotechnol. 2013 Jan;6(1):17-26. doi: 10.1111/j.1751-7915.2012.00342.x. Epub 2012 Mar 29. Review.

5.

Cadherin binding is not a limiting step for Bacillus thuringiensis subsp. israelensis Cry4Ba toxicity to Aedes aegypti larvae.

Rodríguez-Almazán C, Reyes EZ, Zúñiga-Navarrete F, Muñoz-Garay C, Gómez I, Evans AM, Likitvivatanavong S, Bravo A, Gill SS, Soberón M.

Biochem J. 2012 May 1;443(3):711-7. doi: 10.1042/BJ20111579.

6.

Dominant negative phenotype of Bacillus thuringiensis Cry1Ab, Cry11Aa and Cry4Ba mutants suggest hetero-oligomer formation among different Cry toxins.

Carmona D, Rodríguez-Almazán C, Muñoz-Garay C, Portugal L, Pérez C, de Maagd RA, Bakker P, Soberón M, Bravo A.

PLoS One. 2011;6(5):e19952. doi: 10.1371/journal.pone.0019952. Epub 2011 May 16.

7.

The amino- and carboxyl-terminal fragments of the Bacillus thuringensis Cyt1Aa toxin have differential roles in toxin oligomerization and pore formation.

Rodriguez-Almazan C, Ruiz de Escudero I, Cantón PE, Muñoz-Garay C, Pérez C, Gill SS, Soberón M, Bravo A.

Biochemistry. 2011 Jan 25;50(3):388-96. Epub 2010 Dec 29.

8.

Oligomerization of Cry11Aa from Bacillus thuringiensis has an important role in toxicity against Aedes aegypti.

Muñoz-Garay C, Rodríguez-Almazán C, Aguilar JN, Portugal L, Gómez I, Saab-Rincon G, Soberón M, Bravo A.

Appl Environ Microbiol. 2009 Dec;75(23):7548-50. doi: 10.1128/AEM.01303-09. Epub 2009 Oct 9. Erratum in: Appl Environ Microbiol. 2013 Mar;79(5):1762.

9.

Domain II loop 3 of Bacillus thuringiensis Cry1Ab toxin is involved in a "ping pong" binding mechanism with Manduca sexta aminopeptidase-N and cadherin receptors.

Pacheco S, Gómez I, Arenas I, Saab-Rincon G, Rodríguez-Almazán C, Gill SS, Bravo A, Soberón M.

J Biol Chem. 2009 Nov 20;284(47):32750-7. doi: 10.1074/jbc.M109.024968. Epub 2009 Oct 6.

10.

Dominant negative mutants of Bacillus thuringiensis Cry1Ab toxin function as anti-toxins: demonstration of the role of oligomerization in toxicity.

Rodríguez-Almazán C, Zavala LE, Muñoz-Garay C, Jiménez-Juárez N, Pacheco S, Masson L, Soberón M, Bravo A.

PLoS One. 2009;4(5):e5545. doi: 10.1371/journal.pone.0005545. Epub 2009 May 14.

11.

Strategies to improve the insecticidal activity of Cry toxins from Bacillus thuringiensis.

Pardo-López L, Muñoz-Garay C, Porta H, Rodríguez-Almazán C, Soberón M, Bravo A.

Peptides. 2009 Mar;30(3):589-95. doi: 10.1016/j.peptides.2008.07.027. Epub 2008 Aug 19. Review.

12.

Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface.

Rodríguez-Almazán C, Arreola R, Rodríguez-Larrea D, Aguirre-López B, de Gómez-Puyou MT, Pérez-Montfort R, Costas M, Gómez-Puyou A, Torres-Larios A.

J Biol Chem. 2008 Aug 22;283(34):23254-63. doi: 10.1074/jbc.M802145200. Epub 2008 Jun 18.

13.

The stability and formation of native proteins from unfolded monomers is increased through interactions with unrelated proteins.

Rodríguez-Almazán C, Torner FJ, Costas M, Pérez-Montfort R, de Gómez-Puyou MT, Puyou AG.

PLoS One. 2007 Jun 6;2(6):e497.

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