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Origin and evolution of arthropod hemocyanins and related proteins

Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology, 2002
Arthropod hemocyanins are large, multimeric, (n x 6) copper-containing proteins that deliver oxygen in the haemolymph of many chelicerate, crustacean, myriapod, and also possibly some insect species. The arthropod hemocyanins belong to a large protein superfamily that also includes the arthropod phenoloxidases, certain crustacean and insect storage ...
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Proteins toxic to arthropods in the venom of elapid snakes

Journal of Insect Physiology, 1975
It has been found that the lethal action of elapid snake venoms to arthropods (fly larvae and isopods) is due to proteic factors differing from the toxins which are strongly and specifically active on mammals. This conclusion was based on the following: (1) Lack of any correlation between the toxic activity on larvae, isopods, and mice of ten elapid
E, Zlotkin   +4 more
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Heat Shock Proteins and Blood-Feeding in Arthropods

2017
The blood of endothermic vertebrates constitutes the main, or even the only food for many arthropod species. Even though blood is a food rich in nutrients and in most cases sterile, its consumption is associated to many stressing factors. Energetic, thermal, osmotic and oxidative stresses are among the consequences for arthropods of the rapid ingestion
Marcos H. Pereira   +3 more
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Molecular signature of chitin-protein complex in Paleozoic arthropods

Geology, 2011
The conventional geochemical view holds that the chitin and structural protein are not preserved in ancient fossils because they are readily degradable through microbial chitinolysis and proteolysis. Here we show a molecular signature of a relict chitin-protein complex preserved in a Pennsylvanian (310 Ma) scorpion cuticle and a Silurian (417 Ma ...
G. D. Cody   +7 more
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Chito-Protein Matrices in Arthropod Exoskeletons and Peritrophic Matrices

2019
The exoskeleton of an arthropod is formed by layered cuticles that are mainly composed of chitin and associated proteins in form of chito-protein matrices. Some internal organs of an arthropod, such as digestive tract and tracheal system, also contain chitin.
Xiaoming Zhao   +2 more
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A conserved domain in arthropod cuticular proteins binds chitin.

Insect biochemistry and molecular biology, 2001
Many insect cuticular proteins include a 35-36 amino acid motif known as the R&R consensus. The extensive conservation of this region led to the suggestion that it functions to bind chitin. Provocatively, it has no sequence similarity to the well-known cysteine-containing chitin-binding domain found in chitinases and some peritrophic membrane proteins.
J E, Rebers, J H, Willis
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Arthropod adiponectin receptor-like proteins and microbial persistence

Trends in Parasitology
Yingao Guo   +4 more
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