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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Aspartyl aminopeptidase

aspartyl aminopeptidase, Dnpep
Top mentioned proteins: aminopeptidase, Angiotensin II, ACID, Renin, fibrillin-1
Papers on aspartyl aminopeptidase
Chloride channel ClC-5 binds to aspartyl aminopeptidase to regulate renal albumin endocytosis.
New
Poronnik et al., Brisbane, Australia. In Am J Physiol Renal Physiol, May 2015
We have identified a novel ClC-5 binding partner, cytosolic aspartyl aminopeptidase (DNPEP; EC 3.4.11.21), that catalyzes the release of N-terminal aspartate/glutamate residues.
STE20/SPS1-related proline/alanine-rich kinase (SPAK) is critical for sodium reabsorption in isolated, perfused thick ascending limb.
New
Huang et al., Dallas, United States. In Am J Physiol Renal Physiol, Apr 2015
The mRNA levels of related OSR1 kinase and SPAK protease Dnpep in SPAK-KO tubules were not significantly different from WT tubules.
Short forms of Ste20-related proline/alanine-rich kinase (SPAK) in the kidney are created by aspartyl aminopeptidase (Dnpep)-mediated proteolytic cleavage.
Delpire et al., Baltimore, United States. In J Biol Chem, 2014
Ion exchange and size exclusion chromatography combined with mass spectrometry identified the protease as aspartyl aminopeptidase.
Identification and characterization of novel inhibitors of Mammalian aspartyl aminopeptidase.
Kiser et al., Philippines. In Mol Pharmacol, 2014
Aspartyl aminopeptidase (DNPEP) has been implicated in the control of angiotensin signaling and endosome trafficking, but its precise biologic roles remain incompletely defined.
Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa.
Kim et al., Suwŏn, South Korea. In Biochem Biophys Res Commun, 2014
Kinetic studies of Pseudomonas aeruginosa aspartyl aminopeptidase (PaAP) which belongs to peptidase family M18 in clan MH revealed that its peptidase activity is dependent on Co(2+) rather than Zn(2+): the kcat (s(-1)) values of PaAP were 0.006, 5.10 and 0.43 in no-metal, Co(2+), and Zn(2+)conditions, respectively.
Identification of Potent and Selective Inhibitors of the Plasmodium falciparum M18 Aspartyl Aminopeptidase (PfM18AAP) of Human Malaria via High-Throughput Screening.
Hodder et al., Jupiter, United States. In J Biomol Screen, 2014
The target of this study, the PfM18 aspartyl aminopeptidase (PfM18AAP), is the only AAP present in the genome of the malaria parasite Plasmodium falciparum.
Inhibitors of the Plasmodium falciparum M17 Leucine Aminopeptidase
Review
Dalton et al., Bethesda, United States. In Unknown Journal, 2014
For survival, the Plasmodium falciparum (Pf) malaria parasite requires the action of a number of metallo-aminopeptidases, including PfM1MAA (membrane alanine aminopeptidase), PfM17LAP (leucine aminopeptidase), and PfM18AAP (aspartyl aminopeptidase).
Clinical impact of aspartyl aminopeptidase expression and activity in colorectal cancer.
López et al., Leioa, Spain. In Transl Res, 2013
Aspartyl aminopeptidase (ASP; EC 3.4.11.21) is a widely distributed and abundant cytosolic enzyme that regulates bioactive peptides such as angiotensin II.
Inhibitors of the Plasmodium falciparum M18 Aspartyl Aminopeptidase
Review
Gardiner et al., Bethesda, United States. In Unknown Journal, 2013
For survival, the Plasmodium falciparum (Pf) malaria parasite requires the action of a number of metallo-aminopeptidases that each display restricted amino acid specificities, including PfM1MAA (membrane alanine aminopeptidase), PfM17LAP (leucine aminopeptidase), and PfM18AAP (aspartyl aminopeptidase), which are thought to act in concert to degrade host erythrocyte hemoglobin that the parasite uses as a source of amino acid building blocks for the synthesis of its own proteins.
Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutants.
Wang et al., Beijing, China. In Mol Biol Cell, 2013
In this study, we identified the C. elegans aspartyl aminopeptidase DNPP-1, loss of which suppresses the sorting and recycling defects in tat-1 mutants without reversing the PS asymmetry defect.
Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
Yue et al., Oxford, United Kingdom. In Bmc Struct Biol, 2011
BACKGROUND: Aspartyl aminopeptidase (DNPEP), with specificity towards an acidic amino acid at the N-terminus, is the only mammalian member among the poorly understood M18 peptidases.
Chondrocyte-specific microRNA-140 regulates endochondral bone development and targets Dnpep to modulate bone morphogenetic protein signaling.
GeneRIF
Kobayashi et al., Tokyo, Japan. In Mol Cell Biol, 2011
Results demonstrate that Mir140 is essential for normal endochondral bone development and suggest that the reduced BMP signaling caused by Dnpep upregulation plays a causal role in the skeletal defects of Mir140-null mice.
Aminopeptidases of malaria parasites: new targets for chemotherapy.
Review
Gardiner et al., Australia. In Infect Disord Drug Targets, 2010
P. falciparum appears to encode for at least nine aminopeptidases, two neutral aminopeptidases, one aspartyl aminopeptidase, one aminopeptidase P, one prolyl aminopeptidase and four methionine aminopeptidases.
Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals.
Prieto et al., Jaén, Spain. In Endocrinol Nutr, 2008
Angiotensin I, through the action of aspartyl aminopeptidase, is converted into angiotensin 2-10, which may counteract the hypertensive actions of angiotensin II.
Brain aminopeptidases and hypertension.
Review
Ramírez et al., Jaén, Spain. In J Renin Angiotensin Aldosterone Syst, 2006
Brain aspartyl aminopeptidase, which converts angiotensin I to angiotensin 2-10, is also a possible target for antihypertensive therapy because of its potential role in BP control.
Dietary fatty acid composition affects aminopeptidase activities in the testes of mice.
GeneRIF
Ramirez et al., Jaén, Spain. In Int J Androl, 2002
dietary fatty acids affect activity in mouse testis
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