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

scientific article published on 20 March 2014

A conserved tetrameric interaction of cry toxin helix α3 suggests a functional role for toxin oligomerization. is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.BBAMEM.2014.03.006
P698PubMed publication ID24657394
P5875ResearchGate publication ID261033418

P50authorJaume TorresQ52665498
Wahyu SuryaQ56153089
Zhang, TongQ57417211
P2093author name stringXin Lin
Yuguang Mu
Krupakar Parthasarathy
P2860cites workCrystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationQ26778405
P433issue7
P304page(s)1777-1784
P577publication date2014-03-20
P1433published inBiochimica et Biophysica ActaQ864239
P1476titleA conserved tetrameric interaction of cry toxin helix α3 suggests a functional role for toxin oligomerization
P478volume1838

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cites work (P2860)
Q38627789An Intramolecular Salt Bridge in Bacillus thuringiensis Cry4Ba Toxin Is Involved in the Stability of Helix α-3, Which Is Needed for Oligomerization and Insecticidal Activity.
Q55540372Helix α-3 inter-molecular salt bridges and conformational changes are essential for toxicity of Bacillus thuringiensis 3D-Cry toxin family.
Q30365704Molecular approaches to improve the insecticidal activity of Bacillus thuringiensis Cry toxins.
Q40796091Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS.
Q90421925Suppressing a plant-parasitic nematode with fungivorous behavior by fungal transformation of a Bt cry gene

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