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cysteine protease, asparaginyl endopeptidase
This gene encodes a cysteine protease that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme may be involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Enzyme activation is triggered by acidic pH and appears to be autocatalytic. Protein expression occurs after monocytes differentiate into dendritic cells. A fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with the majority of solid tumor types. This gene has a pseudogene on chromosome 13. Several alternatively spliced transcript variants have been described, but the biological validity of only two has been determined. These two variants encode the same isoform. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, V1a, HAD, PrP
Papers on cysteine protease
Screening and Characterization of Genes Involved in the Processing of Lipid-Containing Droplets in C. elegans Embryos.
Döring et al., Kiel, Germany. In Genetics, Feb 2016
The genes include cpl-1 (cathepsin L-like cysteine protease), ccz-1 (guanine nucleotide exchange factor subunit), and asm-3 (acid sphingomyelinase), which is closely related to the human Niemann-Pick disease-causing gene, SMPD1.
Highly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity.
Seelig et al., Minneapolis, United States. In Protein Expr Purif, Feb 2016
UNASSIGNED: Streptococcus pyogenes produces the cysteine protease streptopain (SpeB) as a critical virulence factor for pathogenesis.
PIG7 promotes leukemia cell chemosensitivity via lysosomal membrane permeabilization.
Liu et al., Chengdu, China. In Oncotarget, Jan 2016
However, intrinsic antagonism such as serine/cysteine protease inhibitors Spi2A and Cystatin C prevented downstream effectors from triggering leukemia cells, which were only on the "verge of apoptosis".
Natural cysteine protease inhibitors in protozoa: Fifteen years of the chagasin family.
Lima et al., Rio de Janeiro, Brazil. In Biochimie, Dec 2015
UNASSIGNED: Chagasin-type inhibitors comprise natural inhibitors of papain-like cysteine proteases that are distributed among Protist, Bacteria and Archaea.
Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors.
Thatcher et al., Chicago, United States. In Acta Pharm Sin B, Nov 2015
This review provides a general update on strategies for cysteine protease inhibitor design and a focus on cathepsin B and calpain 1 as drug targets for neurodegenerative disorders; the latter focus providing an interesting query for the contemporary assumptions that irreversible, covalent protein modification and low selectivity are anathema to therapeutic safety and efficacy.
[Research progress on ubiquitin-specific protease in antiviral immunity].
Wei-Lin et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, Jun 2015
Ubiquitin-specific protease(USP), which belongs to cysteine protease, is an important member of the deubiquitinating enzyme family(DUB).
Characterization of a Recombinant Cathepsin B-Like Cysteine Peptidase from Diaphorina citri Kuwayama (Hemiptera: Liviidae): A Putative Target for Control of Citrus Huanglongbing.
Soares-Costa et al., São Carlos, Brazil. In Plos One, 2014
The recombinant enzyme was inhibited by the cysteine protease inhibitors E64 (IC50 = 0.014 μM) and CaneCPI-4 (Ki = 0.05 nM) and by the selective cathepsin B inhibitor CA-074 (IC50 = 0.095 nM).
Immune Evasion Mechanisms of Entamoeba histolytica: Progression to Disease.
Chadee et al., Calgary, Canada. In Front Microbiol, 2014
From the parasite, the signature events that lead to disease progression are cysteine protease cleavage of the C-terminus of MUC2 that dissolves the mucus layer followed by Eh binding and cytotoxicity of the mucosal epithelium.
Programmed Cell Death and Caspase Functions During Neural Development.
Miura et al., Tokyo, Japan. In Curr Top Dev Biol, 2014
These findings are mainly derived from genetic studies that prevent cells from dying by apoptosis, which is a major form of PCD and is executed by activation of evolutionarily conserved cysteine protease caspases.
Gingipains from Porphyromonas gingivalis promote the transformation and proliferation of vascular smooth muscle cell phenotypes.
Zhong et al., Ürümqi, China. In Int J Clin Exp Med, 2014
The aim of the present study was to ascertain the effect of Porphyromonas gingivalis cysteine protease gingipain on the proliferation of rat aortic smooth muscle cells (RASMCs).
Mechanism of Trypanosoma brucei gambiense resistance to human serum.
Pays et al., Brussels, Belgium. In Nature, 2013
Two additional features contribute to resistance to TLFs: reduction of sensitivity to APOL1 requiring cysteine protease activity, and TbHpHbR inactivation due to a L210S substitution.
Proteolytic elimination of N-myristoyl modifications by the Shigella virulence factor IpaJ.
Alto et al., Dallas, United States. In Nature, 2013
Here we describe an irreversible mechanism of protein demyristoylation catalysed by invasion plasmid antigen J (IpaJ), a previously uncharacterized Shigella flexneri type III effector protein with cysteine protease activity.
Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser.
Chapman et al., Hamburg, Germany. In Science, 2013
The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host protein degradation, is a promising target to develop new treatments against sleeping sickness, a fatal disease caused by this protozoan parasite.
Legumain: a biomarker for diagnosis and prognosis of human ovarian cancer.
Xiang et al., Tianjin, China. In J Cell Biochem, 2012
Increased legumain expression was validated by real-time PCR and Western blots, correlated positively with an increased malignancy of ovarian tumors.
Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile.
Brandstetter et al., Salzburg, Austria. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
Accepting asparagines and, to lesser extent, aspartic acid in P1, super-activated legumain exhibits a marked pH dependence that is governed by the P1 residue of its substrate and conformationally stabilizing factors such as temperature or ligands
The inflammasome adaptor ASC regulates the function of adaptive immune cells by controlling Dock2-mediated Rac activation and actin polymerization.
Kanneganti et al., Memphis, United States. In Nat Immunol, 2011
The adaptor ASC contributes to innate immunity through the assembly of inflammasome complexes that activate the cysteine protease caspase-1.
Association between serum cathepsin S and mortality in older adults.
Ärnlöv et al., Uppsala, Sweden. In Jama, 2011
CONTEXT: Experimental data suggest that cathepsin S, a cysteine protease, is involved in the complex pathways leading to cardiovascular disease and cancer.
RAC2, AEP, and ICAM1 expression are associated with CNS disease in a mouse model of pre-B childhood acute lymphoblastic leukemia.
Saha et al., Manchester, United Kingdom. In Blood, 2011
We identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion molecule 1 (ICAM1), and ras-related C3 botulinum toxin substrate 2 (RAC2), among others, in an invasive pre-B-cell line that produced leukemia in NOD-SCID mice
Asparagine endopeptidase is required for normal kidney physiology and homeostasis.
Watts et al., Dundee, United Kingdom. In Faseb J, 2011
AEP is required for normal protein catabolism by PTCs, and its loss induces proliferative and other abnormalities in the murine kidney, at least in part through defective regulation of the EGF receptor
Expression of phosphatidylserine-specific phospholipase A(1) mRNA in human THP-1-derived macrophages.
Kohda et al., Japan. In Cell Transplant, 2009
These results suggest that the expression of PS-PLA(1) mRNA in THP-1-derived macrophages is activated via TLR4.
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