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Items: 1 to 20 of 98

1.

A conserved tetrameric interaction of cry toxin helix α3 suggests a functional role for toxin oligomerization.

Lin X, Parthasarathy K, Surya W, Zhang T, Mu Y, Torres J.

Biochim Biophys Acta. 2014 Jul;1838(7):1777-84. doi: 10.1016/j.bbamem.2014.03.006. Epub 2014 Mar 20.

2.

Pore formation by Cry toxins.

Soberón M, Pardo L, Muñóz-Garay C, Sánchez J, Gómez I, Porta H, Bravo A.

Adv Exp Med Biol. 2010;677:127-42. Review.

PMID:
20687486
3.

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.

4.

A trimeric building block model for Cry toxins in vitro ion channel formation.

Torres J, Lin X, Boonserm P.

Biochim Biophys Acta. 2008 Feb;1778(2):392-7. Epub 2007 Nov 7.

5.

Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications.

Boonserm P, Davis P, Ellar DJ, Li J.

J Mol Biol. 2005 Apr 29;348(2):363-82.

PMID:
15811374
6.

Importance of polarity of the α4-α5 loop residue-Asn(166) in the pore-forming domain of the Bacillus thuringiensis Cry4Ba toxin: implications for ion permeation and pore opening.

Juntadech T, Kanintronkul Y, Kanchanawarin C, Katzenmeier G, Angsuthanasombat C.

Biochim Biophys Acta. 2014 Jan;1838(1 Pt B):319-27. doi: 10.1016/j.bbamem.2013.10.002. Epub 2013 Oct 10.

7.

Crystal structure of Bacillus thuringiensis Cry8Ea1: An insecticidal toxin toxic to underground pests, the larvae of Holotrichia parallela.

Guo S, Ye S, Liu Y, Wei L, Xue J, Wu H, Song F, Zhang J, Wu X, Huang D, Rao Z.

J Struct Biol. 2009 Nov;168(2):259-66. doi: 10.1016/j.jsb.2009.07.004. Epub 2009 Jul 8.

PMID:
19591941
9.

Oligomerization is a key step in Cyt1Aa membrane insertion and toxicity but not necessary to synergize Cry11Aa toxicity in Aedes aegypti larvae.

López-Diaz JA, Cantón PE, Gill SS, Soberón M, Bravo A.

Environ Microbiol. 2013 Nov;15(11):3030-9. doi: 10.1111/1462-2920.12263. Epub 2013 Sep 24.

10.

Unfolding events in the water-soluble monomeric Cry1Ab toxin during transition to oligomeric pre-pore and membrane-inserted pore channel.

Rausell C, Pardo-López L, Sánchez J, Muñoz-Garay C, Morera C, Soberón M, Bravo A.

J Biol Chem. 2004 Dec 31;279(53):55168-75. Epub 2004 Oct 21.

11.

Structural and functional studies of alpha-helix 5 region from Bacillus thuringiensis Cry1Ab delta-endotoxin.

Nuñez-Valdez M, Sánchez J, Lina L, Güereca L, Bravo A.

Biochim Biophys Acta. 2001 Mar 9;1546(1):122-31.

PMID:
11257515
12.

Structural changes of the Cry1Ac oligomeric pre-pore from bacillus thuringiensis induced by N-acetylgalactosamine facilitates toxin membrane insertion.

Pardo-López L, Gómez I, Rausell C, Sanchez J, Soberón M, Bravo A.

Biochemistry. 2006 Aug 29;45(34):10329-36.

PMID:
16922508
13.

Homology modeling of Cry10Aa toxin from B. thuringiensis israelensis and B. thuringiensis subsp. LDC-9.

Mahalakshmi A, Shenbagarathai R.

J Biomol Struct Dyn. 2010 Dec;28(3):363-78.

PMID:
20919752
14.

Bacillus thuringiensis Cry1Ab mutants affecting oligomer formation are non-toxic to Manduca sexta larvae.

Jiménez-Juárez N, Muñoz-Garay C, Gómez I, Saab-Rincon G, Damian-Almazo JY, Gill SS, Soberón M, Bravo A.

J Biol Chem. 2007 Jul 20;282(29):21222-9. Epub 2007 May 30. Erratum in: J Biol Chem. 2013 Mar 22;288(12). doi:10.1074/jbc.A113.701314.

15.

Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin.

Arenas I, Bravo A, Soberón M, Gómez I.

J Biol Chem. 2010 Apr 23;285(17):12497-503. doi: 10.1074/jbc.M109.085266. Epub 2010 Feb 22.

16.

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.

17.

Tryptophan spectroscopy studies and black lipid bilayer analysis indicate that the oligomeric structure of Cry1Ab toxin from Bacillus thuringiensis is the membrane-insertion intermediate.

Rausell C, Muñoz-Garay C, Miranda-CassoLuengo R, Gómez I, Rudiño-Piñera E, Soberón M, Bravo A.

Biochemistry. 2004 Jan 13;43(1):166-74.

PMID:
14705942
18.
19.

Structural and functional analysis of the pre-pore and membrane-inserted pore of Cry1Ab toxin.

Pardo-López L, Gómez I, Muñoz-Garay C, Jiménez-Juarez N, Soberón M, Bravo A.

J Invertebr Pathol. 2006 Jul;92(3):172-7. Epub 2006 Jun 14. Review.

PMID:
16777138
20.

Structure and distribution of the Bacillus thuringiensis Cry4Ba toxin in lipid membranes.

Puntheeranurak T, Stroh C, Zhu R, Angsuthanasombat C, Hinterdorfer P.

Ultramicroscopy. 2005 Nov;105(1-4):115-24. Epub 2005 Aug 8.

PMID:
16125846

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