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Arylsulfatase D

ArsD, arylsulfatase D
The protein encoded by this gene is a member of the sulfatase family. Sulfatases are essential for the correct composition of bone and cartilage matrix. The encoded protein is postranslationally glycosylated and localized to the lysosome. This gene is located within a cluster of similar arylsulfatase genes on chromosome X. A related pseudogene has been identified in the pseudoautosomal region of chromosome Y. [provided by RefSeq, Jul 2011] (from NCBI)
Top mentioned proteins: ATPase, Transcription Factor DP1, HAD, ACID, CAN
Papers on ArsD
Aspects of speech-language abilities are influenced by MECP2 mutation type in girls with Rett syndrome.
Leonard et al., Australia. In Am J Med Genet A, Feb 2015
Cross-sectional data on 766 girls, aged 15 years and under, with genetically confirmed Rett syndrome was obtained from the Australian Rett Syndrome Database (ARSD) (n = 244) and the International Rett Syndrome Phenotype Database (InterRett) (n = 522).
Transcriptional and posttranscriptional regulation of Bacillus sp. CDB3 arsenic-resistance operon ars1.
Zhang et al., Wollongong, Australia. In Peerj, 2014
A hairpin structure formed by internal inverted repeats between arsC and arsD was shown to diminish the expression of the full operon, thereby probably acting as a transcription attenuator.
Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone.
Bhattacharjee et al., Miami, United States. In Biometals, 2014
It receives trivalent As(III) from the intracellular metallochaperone ArsD.
Single nucleotide polymorphism within arylsulfatase D gene (ARSD) is associated with selected kinematic parameters of sperm motility in Holstein-Friesian bulls.
Kaminski et al., In Pol J Vet Sci, 2013
The aim of the study was to find out whether the single nucleotide polymorphism (SNP) within arylsulfatase D (ARSD) gene is associated with kinematic parameters of sperm motility in Holstein-Friesian bulls.
Identification of novel single nucleotide polymorphisms associated with acute respiratory distress syndrome by exome-seq.
Ye et al., Kansas City, United States. In Plos One, 2013
rs78142040 (C>T) occurs within a histone mark (intron 6) of the Arylsulfatase D gene.
Evaluative profiling of arsenic sensing and regulatory systems in the human microbiome project genomes.
Nashiru et al., Daytona Beach, United States. In Microbiol Insights, 2013
We have developed a suite of bioinformatics and visual analytics methods to evaluate the availability (presence or absence) and abundance of functional annotations in a microbial genome for seven Pfam protein families: As(III)-responsive transcriptional repressor (ArsR), anion-transporting ATPase (ArsA), arsenical pump membrane protein (ArsB), arsenate reductase (ArsC), arsenical resistance operon transacting repressor (ArsD), water/glycerol transport protein (aquaporins), and universal stress protein (USP).
The importance of stereochemically active lone pairs for influencing Pb(II) and As(III) protein binding.
Pecoraro et al., Milano, Italy. In Chemistry, 2012
To clarify the requirements for toxic metal binding to metalloregulatory sensor proteins such as As(III) in ArsR/ArsD and Pb(II) in PbrR or replacing Zn(II) in δ-aminolevulinc acid dehydratase (ALAD), we have employed computational and experimental methods examining the binding of these heavy metals to designed peptide models.
Pathways of arsenic uptake and efflux.
Rosen et al., Taiwan. In Curr Top Membr, 2011
The ArsD metallochaperone binds cytosolic As(III) and transfers it to the ArsA subunit of the efflux pump.
Influence of sex and genetic variability on expression of X-linked genes in human monocytes.
Tiret et al., Paris, France. In Genomics, 2011
Few genes exhibited a stronger genetic effect in females than in males (ARSD, DCX, POLA1 and ITM2A).
Genetic mapping of the interface between the ArsD metallochaperone and the ArsA ATPase.
Rosen et al., Detroit, United States. In Mol Microbiol, 2011
The ArsD metallochaperone delivers trivalent metalloids, As(III) or Sb(III), to the ArsA ATPase, the catalytic subunit of the ArsAB As(III) efflux pump.
Bacillus sp. CDB3 isolated from cattle dip-sites possesses two ars gene clusters.
Zhang et al., Wollongong, Australia. In J Environ Sci (china), 2010
The arsD gene from Bacillus species was cloned for the first time and the predict protein differs from the well studied E. coli ArsD by lacking two pairs of C-terminal cysteine residues.
Gene expression profiling identifies ARSD as a new marker of disease progression and the sphingolipid metabolism as a potential novel metabolism in chronic lymphocytic leukemia.
Morra et al., Milano, Italy. In Cancer Biomark, 2010
In addition, this study identified ARSD, a gene belonging to the sphingolipid metabolism, as a new gene significantly overexpressed in UMZAP70(+) compared to MTZAP70(-).
ArsD: an As(III) metallochaperone for the ArsAB As(III)-translocating ATPase.
Rosen et al., Detroit, United States. In J Bioenerg Biomembr, 2007
review of ArsAB and ArsD function
Longterm follow-up in chondrodysplasia punctata, tibia-metacarpal type, demonstrating natural history.
Sheffield et al., Australia. In Am J Med Genet A, 2004
Sterol and very long chain fatty acid profiles, FISH analysis for SHOX gene deletions, blood lymphocyte karyotype, and phytanic acid levels were normal in those tested, and no mutations in arylsulfatase D and E genes were detected.
Mechanisms of metalloregulation of an anion-translocating ATPase.
Shi et al., Detroit, United States. In J Bioenerg Biomembr, 1995
The ars (arsenical resistance) operon cloned from R-factor R773 has five genes that encode two repressor proteins, ArsR and ArsD, and three structural proteins, ArsA, ArsB, and ArsC.
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