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


Aga, aspartylglucosaminidase, glycosylasparaginase
Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme. Alternatively spliced transcript variants have been identified. [provided by RefSeq, Jan 2010] (from NCBI)
Top mentioned proteins: HAD, ACID, CAN, AGE, CTX
Papers on Aga
Analysis of the protective effects of a neuronal Cav2.1 calcium channel in brain injury.
Takahashi et al., Wako, Japan. In Neuroscience, Feb 2016
To examine the relationship between Cav2.1 channel function and brain injury, we induced cryogenic brain damage in homozygous rolling Nagoya (rol/rol), control wild-type (+/+), ω-agatoxin IVA-pretreated +/+ (ω-aga +/+), and ω-agatoxin IVA-post-treated +/+ (ω-aga-post-treated +/+) mice.
Rhesus and Kell Phenotyping of Voluntary Blood Donors: Foundation of a Donor Data Bank.
Khurshid et al., Karāchi, Pakistan. In J Coll Physicians Surg Pak, Oct 2015
PLACE AND DURATION OF STUDY: Blood Bank, The Aga Khan University Hospital, Karachi, in the year 2014.
High-threshold Ca2+ channels behind gamma band activity in the pedunculopontine nucleus (PPN).
Garcia-Rill et al., Buenos Aires, Argentina. In Physiol Rep, Jun 2015
In 50% of cells, the N-type Ca(2+) channel blocker ω-Conotoxin-GVIA (ω-CgTx) reduced gamma oscillation amplitude, while subsequent addition of the P/Q-type blocker ω-Agatoxin-IVA (ω-Aga) blocked the remaining oscillations.
Positive Association of Vitamin E Supplementation with Hemoglobin Levels in Mildly Anemic Healthy Pakistani Adults.
Perwaiz Iqbal et al., Karāchi, Pakistan. In Int J Vitam Nutr Res, 2014
METHOD: In a single-blinded and placebo-controlled randomized trial, 124 mildly anemic subjects from the General Practitioners' Clinics and personnel of the Aga Khan University were randomized into intervention (n = 82) and control (n = 42) group.
Ependymal tumors with oligodendroglioma like clear cells: Experience from a tertiary care hospital in Pakistan.
Ahmed et al., Karāchi, Pakistan. In Surg Neurol Int, 2014
METHODS: It was retrospective cohort conducted at the Department of Neurosurgery, Aga Khan University from 2003 to 2013.
Expanding targets for a metabolic therapy of cancer: L-asparaginase.
Scotti et al., Pavia, Italy. In Recent Pat Anticancer Drug Discov, 2012
[review] Natural killer (NK) cell tumors, subtypes of myeloid leukemias and T-cell lymphomas respond to ASNase; ovarian carcinomas and other solid tumors have been proposed as additional targets for ASNase, with a potential role for glutaminase. activity.
Irreversible inhibitors and activity-based probes as research tools in chemical glycobiology.
Overkleeft et al., Cambridge, United States. In Org Biomol Chem, 2011
Following discussion of some general aspects of the biosynthesis and degradation of N-linked glycoproteins, attention is focused on the enzymes that hydrolyze the protein-carbohydrate linkage, peptide N-glycanase and glycosylasparaginase and their mechanism.
Schizophrenia susceptibility genes directly implicated in the life cycles of pathogens: cytomegalovirus, influenza, herpes simplex, rubella, and Toxoplasma gondii.
Carter, Hastings, United Kingdom. In Schizophr Bull, 2009
For example, aspartylglucosaminidase (AGA), PLA2, SIAT8B, GALNT7, or B3GAT1 metabolize chemical ligands to which the influenza virus, herpes simplex, cytomegalovirus (CMV), rubella, or Toxoplasma gondii bind.
Plasma lysosomal enzyme activities in congenital disorders of glycosylation, galactosemia and fructosemia.
Dimitriou et al., Athens, Greece. In Clin Chim Acta, 2009
Increased AGA plasma activity, although a consistent finding in congenital disorders of glycosylation patients, is not specific to this group of disorders.
Structural basis of aspartylglucosaminuria.
Sakuraba et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2009
The amino acid substitutions in aspartylglucosaminidase responsible for aspartylglucosaminuria were classified and divided in three groups.
Lysosomal metabolism of glycoproteins.
Winchester, London, United Kingdom. In Glycobiology, 2005
The process is initiated by the removal of any core and peripheral fucose, which is a prerequisite for the action of the peptide N-glycanase aspartylglucosaminidase, which hydrolyzes the glycan-peptide bond.
Elevation of plasma aspartylglucosaminidase is a useful marker for the congenital disorders of glycosylation type I (CDG I).
Young et al., London, United Kingdom. In J Inherit Metab Dis, 2004
aspartylglucosaminidase may have a role in development of congenital disorders of glycosylation type I
A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase.
Jalanko et al., Helsinki, Finland. In Hum Mutat, 2004
A new point mutation, c.44T>G, found in a Finnish compound heterozygote causes a L15R AA substitution in the signal sequence of the AGA enzyme, affecting AGA translocation by altering a critical hydrophobic core structure in the signal sequence.
Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta.
Adams, Riverside, United States. In Toxicon, 2004
The omega-agatoxins target neuronal calcium channels, modifying their properties in distinct ways, either through gating modification (omega-Aga-IVA) or by reduction of unitary current (omega-Aga-IIIA).
Angiokeratoma corporis diffusum in a Spanish patient with aspartylglucosaminuria.
Fernández-Herrera et al., Madrid, Spain. In Br J Dermatol, 2002
Aspartylglucosaminuria (AGU) is a rare hereditary disorder mostly affecting the Finnish population, with only a few sporadic patients of non-Finnish origin.
Structural insights into the mechanism of intramolecular proteolysis.
Guo et al., Boston, United States. In Cell, 1999
A variety of proteins, including glycosylasparaginase, have recently been found to activate functions by self-catalyzed peptide bond rearrangements from single-chain precursors.
A mouse model for the human lysosomal disease aspartylglycosaminuria.
Groffen et al., Los Angeles, United States. In Nat Med, 1996
Aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation in humans, is caused by mutations in the gene encoding the lysosomal enzyme glycosylasparaginase (Aga).
Autocatalytic processing of the 20S proteasome.
Baumeister et al., München, Germany. In Nature, 1996
The four currently known Ntn hydrolases (glutamine PRPP amidotransferase, penicillin acylase, the 20S proteasome and aspartylglucosaminidase) are encoded as inactive precursors, and are activated by cleavage of the peptide bond preceding the catalytic residue.
Other lipopeptides.
Ballio et al., In Science, 1995
A sentence reading, "Comparisons with experiments using higher concentrations of carrier protein (1.0 mg/mL) revealed no significant differences in the rate of efficacy of omega-Aga-IVA action" should have been inserted before the last sentence in the legend of figure 1.
Functional expression of a rapidly inactivating neuronal calcium channel.
Horne et al., Stanford, United States. In Nature, 1993
Unlike L-type or P-type channels, doe-1 is not blocked by dihydropyridine antagonists or the peptide toxin omega-Aga-IVA, respectively.
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