Mass spectrometrical analysis of bilin-binding protein from the wing of Hebomoia glaucippe (Linnaeus, 1758) (Lepidoptera: Pieridae)
Author:
Affiliation:
1. Department of Pediatrics; Medical University of Vienna; Vienna; Austria
2. Naturhistorisches Museum Wien; Vienna; Austria
Publisher
Wiley
Subject
Clinical Biochemistry,Biochemistry,Analytical Chemistry
Reference37 articles.
1. Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae
2. The Complete Amino-Acid Sequence of the Bilin-Binding Protein fromPieris brassicaeand its Similarity to a Family of Serum Transport Proteins Like the Retinol-Binding Proteins
3. Developmental profiles of 5-aminolevulinate, porphobilinogen and porphobilinogen synthase activity in Pieris brassicae related to the synthesis of the bilin-binding protein
4. Species-specific coordinated gene expression and trans-regulation of larval color pattern in three swallowtail butterflies
5. Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution
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1. Transcriptomic and Proteomic Analysis of Arion vulgaris—Proteins for Probably Successful Survival Strategies?;PLOS ONE;2016-03-17
2. Comparative transcriptome analyses on silk glands of six silkmoths imply the genetic basis of silk structure and coloration;BMC Genomics;2015-03-17
3. Radiation protection from whole-body gamma irradiation (6.7 Gy): behavioural effects and brain protein-level changes by an aminothiol compound GL2011 in the Wistar rat;Amino Acids;2014-03-29
4. Mass spectrometry and 3-nitrotyrosine: Strategies, controversies, and our current perspective;Mass Spectrometry Reviews;2013-10-24
5. Peptide toxin glacontryphan-M is present in the wings of the butterfly Hebomoia glaucippe (Linnaeus, 1758) (Lepidoptera: Pieridae);Proceedings of the National Academy of Sciences;2012-10-15
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