Analysis of the region for receptor binding and triggering of oligomerization on Bacillus thuringiensis Cry1Aa toxin. (Q39899732)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

title

Analysis of the region for receptor binding and triggering of oligomerization on Bacillus thuringiensis Cry1Aa toxin (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

main subject

Bacillus thuringiensis

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author

Fumiaki Obata

1

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7 February 2020

author name string

Madoka Kitami

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

Yukino Inoue

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

Shogo Atsumi

4

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7 February 2020

Yasutaka Yoshizawa

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

Ryoichi Sato

6

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7 February 2020

language of work or name

English

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publication date

9 September 2009

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7 February 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19740106%20AND%20SRC:MED&resulttype=core&format=json

7 February 2020

volume

276

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7 February 2020

issue

20

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7 February 2020

page(s)

5949-5959

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Beyond the spore--past and future developments of Bacillus thuringiensis as a biopesticide

7 February 2020

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The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis delta-endotoxin are consistent with an "umbrella-like" structure of the pore

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Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin

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Identification of amino acid residues of Bacillus thuringiensis delta-endotoxin CryIAa associated with membrane binding and toxicity to Bombyx mori

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Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts

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Mutations of loop 2 and loop 3 residues in domain II of Bacillus thuringiensis Cry1C delta-endotoxin affect insecticidal specificity and initial binding to Spodoptera littoralis and Aedes aegypti midgut membranes

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Role of two arginine residues in domain II, loop 2 of Cry1Ab and Cry1Ac Bacillus thuringiensis delta-endotoxin in toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase N.

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Mutations at the arginine residues in alpha8 loop of Bacillus thuringiensis delta-endotoxin Cry1Ac affect toxicity and binding to Manduca sexta and Lymantria dispar aminopeptidase N.

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Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins

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Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops alpha-8 and 2 in domain II of Cy1Ab toxin.

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

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Location of the Bombyx mori 175kDa cadherin-like protein-binding site on Bacillus thuringiensis Cry1Aa toxin

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