New Insight to Structure-Function Relationship of GalNAc Mediated Primary Interaction between Insecticidal Cry1Ac Toxin and HaALP Receptor of Helicoverpa armigera

Automation of the CHARMM General Force Field (CGenFF) I: Bond Perception and Atom Typing

(2012) K. Vanommeslaeghe et al.   Journal of Chemical Information and Modeling

Role of Alkaline Phosphatase fromManduca sextain the Mechanism of Action ofBacillus thuringiensisCry1Ab Toxin

(2010) Iván Arenas et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

CPHmodels-3.0—remote homology modeling using structure-guided sequence profiles

(2010) Morten Nielsen et al.   NUCLEIC ACIDS RESEARCH

Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens

(2009) Omaththage P. Perera et al.   INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY

Domain II Loop 3 ofBacillus thuringiensisCry1Ab Toxin Is Involved in a “Ping Pong” Binding Mechanism with Manduca sexta Aminopeptidase-N and Cadherin Receptors

(2009) Sabino Pacheco et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Homodimeric Alkaline Phosphatase Located atHelicoverpa armigeraMidgut, a Putative Receptor of Cry1Ac Contains α-GalNAc in Terminal Glycan Structure as Interactive Epitope†

(2009) Anindya Sarkar et al.   JOURNAL OF PROTEOME RESEARCH