The complement of family M1 aminopeptidases of Haemonchus contortus — Biotechnological implications-Reference-Cited by-同舟云学术

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The complement of family M1 aminopeptidases of Haemonchus contortus — Biotechnological implications

Published:2016-03 Issue:2 Volume:34 Page:65-76
ISSN:0734-9750
Container-title:Biotechnology Advances
language:en
Short-container-title:Biotechnology Advances

Author:

Mohandas Namitha,Young Neil D.,Jabbar Abdul,Korhonen Pasi K.,Koehler Anson V.,Hall Ross S.,Hu Min,Hofmann Andreas,Gasser Robin B.

Funder

Australian Research Council

National Health and Medical Research Council

Victorian Life Sciences Computation Initiative

Publisher

Elsevier BV

Subject

Biotechnology,Bioengineering,Applied Microbiology and Biotechnology

Reference75 articles.

1. Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site;Addlagatta;Proc. Natl. Acad. Sci. U. S. A.,2006

2. Collaboration within the M1 aminopeptidase family promotes reproductive success in Caenorhabditis elegans;Althoff;Dev. Genes Evol.,2014

3. The Anopheles-midgut APN1 structure reveals a new malaria transmission-blocking vaccine epitope;Atkinson;Nat. Struct. Mol. Biol.,2015

4. Molecular cloning and functional expression of a Caenorhabditis elegans aminopeptidase structurally related to mammalian leukotriene A4 hydrolases;Baset;J. Biol. Chem.,1998

5. A glutathione peroxidase, intracellular peptidases and the TOR complexes regulate peptide transporter PEPT-1 in C. elegans;Benner;PLoS One,2011

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