@article{
 title = {Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity.},
 type = {article},
 year = {1999},
 identifiers = {[object Object]},
 keywords = {Acetylgalactosamine,Acetylgalactosamine: metabolism,Animals,Antigens, CD13,Antigens, CD13: metabolism,Bacillus thuringiensis,Bacillus thuringiensis: metabolism,Bacterial Proteins,Bacterial Proteins: chemistry,Bacterial Proteins: metabolism,Bacterial Proteins: toxicity,Bacterial Toxins,Binding, Competitive,Endotoxins,Endotoxins: chemistry,Endotoxins: metabolism,Endotoxins: toxicity,Hemolysin Proteins,Manduca,Manduca: metabolism,Microvilli,Microvilli: metabolism,Models, Molecular,Mutagenesis,Protein Binding,Protein Structure, Tertiary,Surface Plasmon Resonance,Time Factors},
 pages = {373-6},
 volume = {462},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/10622728},
 month = {12},
 day = {3},
 id = {4e96fd2a-7715-3701-bdd1-f025a1bb933a},
 created = {2012-02-08T16:01:02.000Z},
 file_attached = {true},
 profile_id = {1a467167-0a41-3583-a6a3-034c31031332},
 group_id = {0e532975-1a47-38a4-ace8-4fe5968bcd72},
 last_modified = {2012-02-08T16:16:23.000Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 abstract = {Bacillus thuringiensis Cry1Ac delta-endotoxin specifically binds a 115-kDa aminopeptidase-N purified from Manduca sexta midgut. Cry1Ac domain III mutations were constructed around a putative sugar-binding pocket and binding to purified aminopeptidase-N and brush border membrane vesicles (BBMV) was compared to toxicity. Q509A, R511A, Y513A, and 509-511 (QNR-AAA) eliminated aminopeptidase-N binding and reduced binding to BBMV. However, toxicity decreased no more than two-fold, indicating activity is not directly correlated with aminopeptidase-N binding. Analysis of toxin binding to aminopeptidase-N in M. sexta is therefore insufficient for predicting toxicity. Mutants retained binding, however, to another BBMV site, suggesting alternative receptors may compensate in vivo.},
 bibtype = {article},
 author = {Jenkins, J L and Lee, M K and Sangadala, S and Adang, M J and Dean, D H},
 journal = {FEBS letters},
 number = {3}
}

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Cry1Ac domain III mutations were constructed around a putative sugar-binding pocket and binding to purified aminopeptidase-N and brush border membrane vesicles (BBMV) was compared to toxicity. Q509A, R511A, Y513A, and 509-511 (QNR-AAA) eliminated aminopeptidase-N binding and reduced binding to BBMV. However, toxicity decreased no more than two-fold, indicating activity is not directly correlated with aminopeptidase-N binding. Analysis of toxin binding to aminopeptidase-N in M. sexta is therefore insufficient for predicting toxicity. Mutants retained binding, however, to another BBMV site, suggesting alternative receptors may compensate in vivo.","bibtype":"article","author":"Jenkins, J L and Lee, M K and Sangadala, S and Adang, M J and Dean, D H","journal":"FEBS letters","number":"3","bibtex":"@article{\n title = {Binding of Bacillus thuringiensis Cry1Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity.},\n type = {article},\n year = {1999},\n identifiers = {[object Object]},\n keywords = {Acetylgalactosamine,Acetylgalactosamine: metabolism,Animals,Antigens, CD13,Antigens, CD13: metabolism,Bacillus thuringiensis,Bacillus thuringiensis: metabolism,Bacterial Proteins,Bacterial Proteins: chemistry,Bacterial Proteins: metabolism,Bacterial Proteins: toxicity,Bacterial Toxins,Binding, Competitive,Endotoxins,Endotoxins: chemistry,Endotoxins: metabolism,Endotoxins: toxicity,Hemolysin Proteins,Manduca,Manduca: metabolism,Microvilli,Microvilli: metabolism,Models, Molecular,Mutagenesis,Protein Binding,Protein Structure, Tertiary,Surface Plasmon Resonance,Time Factors},\n pages = {373-6},\n volume = {462},\n websites = {http://www.ncbi.nlm.nih.gov/pubmed/10622728},\n month = {12},\n day = {3},\n id = {4e96fd2a-7715-3701-bdd1-f025a1bb933a},\n created = {2012-02-08T16:01:02.000Z},\n file_attached = {true},\n profile_id = {1a467167-0a41-3583-a6a3-034c31031332},\n group_id = {0e532975-1a47-38a4-ace8-4fe5968bcd72},\n last_modified = {2012-02-08T16:16:23.000Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n abstract = {Bacillus thuringiensis Cry1Ac delta-endotoxin specifically binds a 115-kDa aminopeptidase-N purified from Manduca sexta midgut. Cry1Ac domain III mutations were constructed around a putative sugar-binding pocket and binding to purified aminopeptidase-N and brush border membrane vesicles (BBMV) was compared to toxicity. Q509A, R511A, Y513A, and 509-511 (QNR-AAA) eliminated aminopeptidase-N binding and reduced binding to BBMV. However, toxicity decreased no more than two-fold, indicating activity is not directly correlated with aminopeptidase-N binding. Analysis of toxin binding to aminopeptidase-N in M. sexta is therefore insufficient for predicting toxicity. Mutants retained binding, however, to another BBMV site, suggesting alternative receptors may compensate in vivo.},\n bibtype = {article},\n author = {Jenkins, J L and Lee, M K and Sangadala, S and Adang, M J and Dean, D H},\n journal = {FEBS letters},\n number = {3}\n}","author_short":["Jenkins, J., L.","Lee, M., K.","Sangadala, S.","Adang, M., J.","Dean, D., H."],"urls":{"Paper":"http://bibbase.org/service/mendeley/1a467167-0a41-3583-a6a3-034c31031332/file/72a3c01c-3957-03ed-3367-2f33ccce8b9b/1999-Binding_of_Bacillus_thuringiensis_Cry1Ac_toxin_to_Manduca_sexta_aminopeptidase-N_receptor_is_not_directly_related_t.pdf.pdf"},"bibbaseid":"jenkins-lee-sangadala-adang-dean-bindingofbacillusthuringiensiscry1actoxintomanducasextaaminopeptidasenreceptorisnotdirectlyrelatedtotoxicity-1999","role":"author","keyword":["Acetylgalactosamine","Acetylgalactosamine: metabolism","Animals","Antigens","CD13","Antigens","CD13: metabolism","Bacillus thuringiensis","Bacillus thuringiensis: metabolism","Bacterial Proteins","Bacterial Proteins: chemistry","Bacterial Proteins: metabolism","Bacterial Proteins: toxicity","Bacterial Toxins","Binding","Competitive","Endotoxins","Endotoxins: chemistry","Endotoxins: metabolism","Endotoxins: toxicity","Hemolysin Proteins","Manduca","Manduca: metabolism","Microvilli","Microvilli: metabolism","Models","Molecular","Mutagenesis","Protein Binding","Protein Structure","Tertiary","Surface Plasmon Resonance","Time Factors"],"downloads":0,"html":""},"search_terms":["binding","bacillus","thuringiensis","cry1ac","toxin","manduca","sexta","aminopeptidase","receptor","directly","related","toxicity","jenkins","lee","sangadala","adang","dean"],"keywords":["acetylgalactosamine","acetylgalactosamine: metabolism","animals","antigens","cd13","antigens","cd13: metabolism","bacillus thuringiensis","bacillus thuringiensis: metabolism","bacterial proteins","bacterial proteins: chemistry","bacterial proteins: metabolism","bacterial proteins: toxicity","bacterial toxins","binding","competitive","endotoxins","endotoxins: chemistry","endotoxins: metabolism","endotoxins: toxicity","hemolysin proteins","manduca","manduca: metabolism","microvilli","microvilli: metabolism","models","molecular","mutagenesis","protein binding","protein structure","tertiary","surface plasmon resonance","time factors"],"authorIDs":[]}