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

Solute carrier family 3

This gene encodes a type II membrane glycoprotein which is one of the components of the renal amino acid transporter which transports neutral and basic amino acids in the renal tubule and intestinal tract. Mutations and deletions in this gene are associated with cystinuria. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, V1a, RPA, Chk1
Papers on SLC3A1
Novel cystine transporter in renal proximal tubule identified as a missing partner of cystinuria-related plasma membrane protein rBAT/SLC3A1.
Kanai et al., Suita, Japan. In Proc Natl Acad Sci U S A, Feb 2016
Among them, the heterodimer of a membrane protein b(0,+)AT/SLC7A9 and its auxiliary subunit rBAT/SLC3A1 is responsible for cystine reabsorption in renal proximal tubules.
Optimization of a cytochrome P450 oxidation system for enhancing protopanaxadiol production in Saccharomyces cerevisiae.
Yuan et al., Tianjin, China. In Biotechnol Bioeng, Feb 2016
Recently, an artificial biosynthetic pathway of protopanaxadiol was built in Saccharomyces cerevisiae by introducing a P. ginseng dammarenediol-II synthase, a P. ginseng cytochrome P450-type protopanaxadiol synthase (PPDS), and a Arabidopsis thaliana NADPH-cytochrome P450 reductase (ATR1).
Structurally distinct Arabidopsis thaliana NLR immune receptors recognize tandem WY domains of an oomycete effector.
Staskawicz et al., Berkeley, United States. In New Phytol, Feb 2016
The Arabidopsis thaliana NLR RPP1 recognizes the tandem WY-domain effector ATR1 from the oomycete Hyaloperonospora arabidopsidis through direct association with C-terminal LRRs.
How should patients with cystine stone disease be evaluated and treated in the twenty-first century?
Osther et al., Fredericia, Denmark. In Urolithiasis, Dec 2015
Today 160 different mutations in the SLC3A1 gene and 116 in the SLC7A9 gene are listed.
Regulation of ATRIP protein abundance by RAD9 in the DNA damage repair pathway.
Ding et al., Nanchang, China. In Cell Mol Biol (noisy-le-grand), 2014
A number of proteins act in concert with ATR to phosphorylate Chk1, including RAD17, the RAD9-RAD1-HUS1 complex, ATR/ATRIP and TopBp1.
Cystinuria: current diagnosis and management.
Giannatos et al., Greece. In Urology, 2014
Two responsible genes have been identified, the SLC3A1 on chromosome 2 and the SLC7A9 on chromosome 19.
Transition-metal-catalyzed laboratory-scale carbon-carbon bond-forming reactions of ethylene.
Sigman et al., Salt Lake City, United States. In Angew Chem Int Ed Engl, 2013
Because of its D2h symmetry, only one insertion outcome is possible.
Clinical, biochemical and molecular characterization of cystinuria in a cohort of 12 patients.
Cardoso et al., Porto, Portugal. In Clin Genet, 2012
In SLC3A1 gene, two large genomic rearrangements and 13 sequence variants are found in cystinuria patients.
Effector recognition and activation of the Arabidopsis thaliana NLR innate immune receptors.
Staskawicz et al., Berkeley, United States. In Cold Spring Harb Symp Quant Biol, 2011
Here, we summarize our recent findings on the Arabidopsis resistance protein RPP1, a member of the TIR-NBS-LRR family of plant NLRs that specifically recognizes the cognate effector protein ATR1.
Cystinuria: an inborn cause of urolithiasis.
Zerres et al., Aachen, Germany. In Orphanet J Rare Dis, 2011
So far, two genes responsible for cystinuria have been identified: SLC3A1 (chromosome 2p21) encodes the heavy subunit rBAT of a renal b(0,+) transporter while SLC7A9 (chromosome 19q12) encodes its interacting light subunit b(0,+)AT.
Potential pharmacologic treatments for cystinuria and for calcium stones associated with hyperuricosuria.
Goldfarb, New York City, United States. In Clin J Am Soc Nephrol, 2011
The drug's safety and effectiveness will be tested in an Slc3a1 knockout mouse that serves as an animal model of cystinuria.
Polyglutamine Atrophin provokes neurodegeneration in Drosophila by repressing fat.
Fanto et al., Milano, Italy. In Embo J, 2011
Polyglutamine Atrophin provokes neurodegeneration in Drosophila by repressing fat.
ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled.
Weller et al., Farmington, United States. In J Virol, 2010
ATRIP may function outside the context of the canonical ATR damage signaling pathway during HSV-1 infection to participate in the viral life cycle.
Neurodegeneration by polyglutamine Atrophin is not rescued by induction of autophagy.
Charroux et al., Milano, Italy. In Cell Death Differ, 2010
Drosophila Atro promote neurodegeneration with autophagic hallmarks both in neuronal photoreceptors and glial cells.
Telomeres avoid end detection by severing the checkpoint signal transduction pathway.
Ferreira et al., Portugal. In Nature, 2010
2), recruit DNA repair proteins (Rad22(RAD52) and Rhp51(RAD51), where the superscript indicates the human orthologue) and checkpoint sensors (RPA, Rad9, Rad26(ATRIP) and Cut5/Rad4(TOPBP1)) to telomeres.
Large rearrangements detected by MLPA, point mutations, and survey of the frequency of mutations within the SLC3A1 and SLC7A9 genes in a cohort of 172 cystinuric Italian patients.
Zelante et al., San Giovanni Rotondo, Italy. In Mol Genet Metab, 2010
Studies identified 6 different alleles in SLC3A1 and 2 in SLC7A9 accounting for a total of 25 copy number changes, 11 in SLC3A1 and 14 in SLC7A9.
Unprotected Drosophila melanogaster telomeres activate the spindle assembly checkpoint.
Cenci et al., Lecce, Italy. In Nat Genet, 2008
The cell cycle arrest elicited by the DDR was alleviated by mutations in mei-41 (encoding ATR), mus304 (ATRIP), grp (Chk1) and rad50 but not by mutations in tefu (ATM).
HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability.
Boulton et al., London, United Kingdom. In Nat Cell Biol, 2007
Here, we show that the human homologue of the Caenorhabditis elegans biological clock protein CLK-2 (HCLK2) associates with the S-phase checkpoint components ATR, ATRIP, claspin and Chk1.
Mismatch repair proteins as sensors of alkylation DNA damage.
Edelmann et al., San Diego, United States. In Cancer Cell, 2006
In a recent issue of Molecular Cell, Yoshioka and coworkers show that MMR complexes (MutSalpha and MutLalpha) are required for the recruitment of ATR-ATRIP to sites of alkylation damage, demonstrating that MMR complexes can function as sensors in DNA damage signal transduction.
TopBP1 activates the ATR-ATRIP complex.
Dunphy et al., Pasadena, United States. In Cell, 2006
Data show that recombinant TopBP1 induces a large increase in the kinase activity of both Xenopus and human ATR-ATRIP.
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