A proposed role for Leishmania major carboxypeptidase in peptide catabolism-Reference-Cited by-同舟云学术

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A proposed role for Leishmania major carboxypeptidase in peptide catabolism

Published:2008-08 Issue:1 Volume:373 Page:25-29
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Isaza Clara E.,Zhong Xuejun,Rosas Lucia E.,White James D.,Chen Rita P.-Y.,Liang George F.-C.,Chan Sunney I.,Satoskar Abhay R.,Chan Michael K.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference28 articles.

1. Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1;Lee;Biosci. Biotechnol. Biochem.,1992

2. Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus;Cheng;Protein Sci.,1999

3. Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus;Arndt;Structure,2002

4. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs;Altschul;Nucleic Acids Res.,1997

5. Structure of neurolysin reveals a deep channel that limits substrate access;Brown;Proc. Natl. Acad. Sci. USA,2001

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4. Potent and selective inhibitors for M32 metallocarboxypeptidases identified from high-throughput screening of anti-kinetoplastid chemical boxes;PLOS Neglected Tropical Diseases;2019-07-22

5. Substrate specificity profiling of M32 metallocarboxypeptidases from Trypanosoma cruzi and Trypanosoma brucei;Molecular and Biochemical Parasitology;2018-01

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