Biochemical characterization of digestive membrane‐associated alkaline phosphatase from the velvet bean caterpillarAnticarsia gemmatalis-Reference-Cited by-同舟云学术

Biochemical characterization of digestive membrane‐associated alkaline phosphatase from the velvet bean caterpillarAnticarsia gemmatalis

Published:2019-07 Issue:1 Volume:102 Page:
ISSN:0739-4462
Container-title:Archives of Insect Biochemistry and Physiology
language:en
Short-container-title:Arch. Insect Biochem. Physiol

Author:

da Silva Gabriela¹,Costa Ramos Luís Felipe¹,dos Santos Seckler Henrique¹,Mendonça Gomes Fabio²,Reis Cortines Juliana³,Ramos Isabela⁴,Dinis Anobom Cristiane¹,Alcantara Machado Ednildo²,Perpétua de Oliveira Danielle Maria¹^ORCID

Affiliation:

1. Laboratório de Bioquímica Estrutural de Proteínas, Departamento de Bioquímica, Centro de Ciências Matemáticas e da Natureza, Instituto de QuímicaUniversidade Federal do Rio de JaneiroRio de Janeiro CEP Brazil

2. Laboratório de Bioquímica de Insetos e Parasitos, Instituto de Biofísica Carlos Chagas FilhoUniversidade Federal do Rio de JaneiroRio de Janeiro CEP Brazil

3. Departamento de Virologia, Centro de Ciências da Saúde, Instituto de Microbiologia Paulo de GóesUniversidade Federal do Rio de JaneiroRio de Janeiro CEP Brazil

4. Laboratório de Bioquímica de Insetos, Centro de Ciências da Saúde, Instituto de Bioquímica MédicaUniversidade Federal do Rio de JaneiroRio de Janeiro CEP Brazil

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Publisher

Wiley

Subject

Insect Science,General Medicine,Biochemistry,Physiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/arch.21591

Reference46 articles.

1. Role of Alkaline Phosphatase from Manduca sexta in the Mechanism of Action of Bacillus thuringiensis Cry1Ab Toxin

2. Toxicity and binding studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C and Cry2A proteins in the soybean pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens;Bel Y.;Applied and Enviromental Microbiology,2017

3. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

4. Bacillus thuringiensis: Mechanisms and Use

5. Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains

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