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N-acylaminoacyl-peptide hydrolase

APH, OPH, acylpeptide hydrolase, D3F15S2, DNF15S2
This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, APH-1, CAN, Nicastrin, Presenilin-1
Papers using APH antibodies
New mRNAs are preferentially translated during vesicular stomatitis virus infection.
Supplier
Mohr Ian, In PLoS Pathogens, 2007
... Caspase activity was prevented by incubation with 60 µM Q-VD-Oph (Calbiochem) or Z-VAD fmk (Bachem).
Chromatin immunoprecipitation: optimization, quantitative analysis and data normalization.
Supplier
Bryk Mary, In PLoS ONE, 2006
... Seedlings were treated for 48 h at 25°C with or without varying concentrations of APH (Wako Chemicals USA, Inc., Richmond, VA, ...
Chromatin modification of Apaf-1 restricts the apoptotic pathway in mature neurons
Supplier
Deshmukh Mohanish et al., In The Journal of Cell Biology, 1999
... Q-VD-OPH was obtained from MP Biomedicals.
Papers on APH
Expression of recombinant organophosphorus hydrolase in the original producer of the enzyme, Sphingobium fuliginis ATCC 27551.
New
Kawahara et al., Yokohama, Japan. In Biosci Biotechnol Biochem, Feb 2016
UNASSIGNED: The plasmid encoding His-tagged organophosphorus hydrolase (OPH) cloned from Sphingobium fuliginis was modified to be transferred back to this bacterium.
Frequency of Aminoglycoside-Modifying Enzymes and ArmA Among Different Sequence Groups of Acinetobacter baumannii in Iran.
New
Goli et al., Tabrīz, Iran. In Microb Drug Resist, Feb 2016
APH(3'')-VIa-encoding gene was predominant in SG1 (47%), SG2 (62%), and SG6-9 (100%).
Molecular cloning, expression and characterization of acylpeptide hydrolase in the silkworm, Bombyx mori.
New
Zhang et al., Chongqing, China. In Gene, Feb 2016
UNASSIGNED: Acylpeptide hydrolase (APH) can catalyze the release of the N-terminal amino acid from acetylated peptides.
Nicastrin is required for APP but not Notch processing, while Aph-1 is dispensable for processing of both APP and Notch.
New
Xu et al., Knoxville, United States. In J Neurochem, Jan 2016
UNASSIGNED: The γ-secretase complex is composed of at least four components: presenilin (PS1 or PS2), nicastrin (NCT), anterior pharynx-defective 1 (Aph-1), and presenilin enhancer 2 (pen-2).
An atomic structure of human γ-secretase.
New
Impact
Shi et al., Beijing, China. In Nature, Oct 2015
Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
The effects and interactions of APOE and APH-1A polymorphisms in Alzheimer disease.
Gündüz et al., In Turk J Med Sci, 2014
One of the major components of y-secretase complex, anterior pharynx-defective-1 (APH-1), is responsible for the activity of the γ-secretase complex.
Molecular mechanism of intramembrane proteolysis by γ-secretase.
Review
Tomita, Tokyo, Japan. In J Biochem, 2014
It is the catalytic subunit of γ-secretase, which plays critical roles in developmental biology and the molecular etiology of Alzheimer disease, together with three membrane protein cofactors, nicastrin, Aph-1 and Pen-2.
Three-dimensional structure of human γ-secretase.
Impact
Shi et al., Beijing, China. In Nature, 2014
The γ-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a membrane-embedded protease that controls a number of important cellular functions through substrate cleavage.
Toward the structure of presenilin/γ-secretase and presenilin homologs.
Review
Wolfe, Boston, United States. In Biochim Biophys Acta, 2013
Upon assembly with its three protein cofactors (nicastrin, Aph-1 and Pen-2), presenilin undergoes autoproteolysis into two subunits, each of which contributes one of the catalytic aspartates to the active site.
The γ-secretase complex: from structure to function.
Review
Zhang et al., Xiamen, China. In Front Cell Neurosci, 2013
γ-secretase is a high molecular weight complex minimally composed of four components: presenilins (PS), nicastrin, anterior pharynx defective 1 (APH-1), and presenilin enhancer 2 (PEN-2).
Folding and self-assembly of the TatA translocation pore based on a charge zipper mechanism.
Impact
Ulrich et al., Karlsruhe, Germany. In Cell, 2013
Each subunit of TatA consists of a transmembrane segment, an amphiphilic helix (APH), and a C-terminal densely charged region (DCR).
β-arrestin 2 regulates Aβ generation and γ-secretase activity in Alzheimer's disease.
Impact
De Strooper et al., Leuven, Belgium. In Nat Med, 2013
Two GPCRs implicated previously in Alzheimer's disease (GPR3 and the β(2)-adrenergic receptor) mediate their effects on Aβ generation through interaction with β-arrestin 2. β-arrestin 2 physically associates with the Aph-1a subunit of the γ-secretase complex and redistributes the complex toward detergent-resistant membranes, increasing the catalytic activity of the complex.
Prospects for circumventing aminoglycoside kinase mediated antibiotic resistance.
Review
Berghuis et al., Montréal, Canada. In Front Cell Infect Microbiol, 2012
In this review, we present a comprehensive overview of the available APH structures and recent progress in APH inhibitor development, with a focus on the structure-guided strategies.
Synaptic localization of acylpeptide hydrolase in adult rat telencephalon.
GeneRIF
Pancetti et al., Coquimbo, Chile. In Neurosci Lett, 2012
ACPH protein levels are significantly increased at the synapse; ACPH is preferentially located at the pre-synaptic side
Organophosphorus hydrolase as an in vivo catalytic nerve agent bioscavenger.
Review
Reeves et al., College Station, United States. In Drug Test Anal, 2012
A review of the development of organophosphorus hydrolase (OPH) for use as in vivo catalytic bioscavengers is presented here.
Genetic evidence supporting the association of protease and protease inhibitor genes with inflammatory bowel disease: a systematic review.
GeneRIF
Lottaz et al., Leuven, Belgium. In Plos One, 2010
Studies indicate that the cylindromatosis/turban tumor syndrome gene (CYLD) ranked highest, followed by acylaminoacyl-peptidase (APEH), dystroglycan (DAG1), macrophage-stimulating protein (MST1) and ubiquitin-specific peptidase 4 (USP4).
Analysis of the gamma-secretase interactome and validation of its association with tetraspanin-enriched microdomains.
Impact
De Strooper et al., Leuven, Belgium. In Nat Cell Biol, 2009
Gamma-secretase, an aspartyl protease that belongs to the iCLiPs (intramembrane cleaving proteases) family, is a multiprotein complex that consists of presenilin (PS), nicastrin (NCT), Aph-1 and Pen-2 (ref.
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