Affinage

SAG

S-arrestin · UniProt P10523

Length
405 aa
Mass
45.1 kDa
Annotated
2026-06-10
100 papers in source corpus 9 papers cited in narrative 9 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SAG (visual arrestin / arrestin-1) terminates rod phototransduction by binding light-activated, rhodopsin-kinase-phosphorylated rhodopsin and sterically occluding transducin, the second step of a two-step receptor deactivation mechanism (PMID:3040978). Arrestin and transducin share overlapping contact sites on metarhodopsin II, accounting for this competitive, desensitizing mode of inhibition (PMID:10969086). In its basal state arrestin is held inactive by a hydrogen-bonded polar core (Arg175, Asp30, Asp296, Asp303, Arg382); engagement of the phosphorylated receptor C-terminus disrupts this core to trigger a global conformational rearrangement that licenses high-affinity binding, and polar-core mutations bypass the phosphorylation requirement entirely (PMID:10206946). The receptor-bound conformational change centers on the finger loop (residues 67–79), which moves toward the receptor and acts as the activation sensor specifically detecting the active rhodopsin conformation, while the relative N- and C-domain orientation is preserved rather than opening clam-shell-like (PMID:23091036, PMID:33159335); the C-edge loops engage the membrane as an anchor in a phosphate-activation-dependent manner (PMID:28220785). Arrestin binding is coupled to chromophore turnover: its release is thermodynamically linked to all-trans-retinal reduction and chromophore exchange, and persistent all-trans-retinal traps arrestin on photoproducts to block recycling (PMID:1386362, PMID:15591052). Inositol phosphates bind the N-domain basic patch and displace the arrestin C-tail to prime, but not fully activate, the receptor-binding state (PMID:34678158).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 1987 High

    Established that arrestin acts as the second, phosphorylation-dependent step of rhodopsin deactivation, defining its core role in quenching phototransduction.

    Evidence In vitro reconstitution of transducin-driven PDE activation in rod outer segments with purified rhodopsin kinase and arrestin

    PMID:3040978

    Open questions at the time
    • Did not resolve the structural basis of phospho-rhodopsin recognition
    • Competition with transducin inferred functionally, not mapped to shared residues
  2. 1992 High

    Showed that arrestin release is gated by chromophore chemistry, linking desensitization to the rhodopsin recycling cycle rather than to an autonomous off-rate.

    Evidence Biochemical reconstitution with native disc membranes plus retinoids and spectrophotometric monitoring of metarhodopsin species

    PMID:1386362

    Open questions at the time
    • Molecular determinants of arrestin binding to M380 pseudo-photoproducts not defined
    • Kinetic coupling between retinal reduction and arrestin dissociation not quantified
  3. 1999 High

    Defined the polar core as the molecular switch that keeps arrestin inactive and that phospho-receptor binding disrupts, explaining the phosphorylation requirement at the residue level.

    Evidence Site-directed and second-site suppressor mutagenesis with in vitro binding to phospho-light-activated rhodopsin, interpreted with the arrestin crystal structure

    PMID:10206946

    Open questions at the time
    • Conformational steps downstream of polar-core disruption not resolved in this study
    • Did not map the receptor-contacting surfaces directly
  4. 2000 Medium

    Mapped arrestin's rhodopsin-contacting regions and showed they overlap transducin's binding sites, providing the structural rationale for steric competition.

    Evidence Spectrophotometric peptide competition (extra-MII) assays with synthetic arrestin peptides on disc membranes

    PMID:10969086

    Open questions at the time
    • Peptide competition gives indirect mapping, not validated in the intact protein
    • Single-lab data without orthogonal structural confirmation
  5. 2004 High

    Demonstrated thermodynamic coupling between arrestin release and retinal release and identified interface residues buried on binding, integrating desensitization with photoproduct decay.

    Evidence Site-directed bimane fluorescence labeling of arrestin mutants with EPR and retinal-release kinetics on purified proteins and disc membranes

    PMID:15591052

    Open questions at the time
    • Whether buried sites contact rhodopsin or phospholipid not fully distinguished
    • Identity of the post-Meta II decay product only tentatively assigned
  6. 2012 High

    Resolved the receptor-bound conformational change, showing finger-loop movement without clam-shell domain reorientation and overturning a prevailing activation model.

    Evidence DEER-EPR distance measurements on spin-labeled arrestin-1 mutant pairs in free and rhodopsin-bound states

    PMID:23091036

    Open questions at the time
    • Functional consequence of the loop-139 displacement not tested
    • Limited to distance pairs sampled
  7. 2017 High

    Identified the C-edge loops as a phosphate-activation-dependent membrane anchor, adding a lipid-interface component to the binding mechanism.

    Evidence Molecular dynamics simulations validated by site-directed fluorescence spectroscopy on arrestin-1 with rhodopsin in membrane

    PMID:28220785

    Open questions at the time
    • Membrane-anchor contribution to overall binding energetics not quantified
    • Single-lab combination of simulation and spectroscopy
  8. 2020 High

    Pinpointed the finger loop as the activation sensor that specifically reads the active receptor conformation, separating activation detection from phosphate sensing.

    Evidence Comprehensive alanine-scanning of finger-loop residues with cell-free translated mutants and in vitro binding to defined rhodopsin forms

    PMID:33159335

    Open questions at the time
    • Structural arrangement of the engaged finger loop in the complex not directly visualized
    • Cooperativity with C-edge and phosphate sensing not dissected
  9. 2021 High

    Showed that inositol phosphates prime arrestin by displacing its C-tail at the N-domain basic patch without disrupting the polar core, distinguishing priming from full activation.

    Evidence X-ray crystallography of bovine arrestin-1 in ligand-free and InsP-bound states

    PMID:34678158

    Open questions at the time
    • Physiological role of InsP priming in vivo not established
    • How priming accelerates subsequent rhodopsin engagement not kinetically defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the priming, phosphate-sensing, finger-loop activation, and membrane-anchoring steps are temporally ordered into a single high-affinity complex in the native rod remains unresolved.
  • No integrated kinetic model coupling InsP priming to receptor engagement
  • In vivo relevance of individual binding elements not tested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060089 molecular transducer activity 2 GO:0098772 molecular function regulator activity 2 GO:0008289 lipid binding 1
Localization
GO:0005886 plasma membrane 1
Pathway
R-HSA-162582 Signal Transduction 2 R-HSA-9709957 Sensory Perception 1
Partners
RHO

Evidence

Reading pass · 9 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1987 Photoactivated rhodopsin is deactivated by a two-step mechanism: rhodopsin kinase phosphorylates light-activated rhodopsin at multiple sites (partially suppressing transducin activation), and then the 48 kDa S-antigen/arrestin binds specifically to phosphorylated rhodopsin to potentiate inhibition, most likely by competing with transducin for binding to phosphorylated rhodopsin. In vitro biochemical assays measuring transducin-mediated phosphodiesterase activation in rod outer segments with purified rhodopsin kinase and arrestin Journal of receptor research High 3040978
1992 Arrestin (SAG) must dissociate from phosphorylated metarhodopsin II to allow rhodopsin recycling; reduction of the photolyzed chromophore all-trans-retinal to all-trans-retinol is essential for arrestin release, chromophore replacement, and phosphate hydrolysis. If all-trans-retinal persists, it forms pseudo-photoproducts (M380) that bind arrestin tightly and block the phototransduction cascade. Biochemical reconstitution with native disc membranes, purified arrestin, rhodopsin kinase, and retinoids; spectrophotometric monitoring of metarhodopsin species The Journal of biological chemistry High 1386362
1999 Visual arrestin maintains an inactive conformation through a hydrogen-bonded 'polar core' network involving residues Arg175, Asp30, Asp296, Asp303, and Arg382. Interaction of the phosphorylated receptor C-terminal segment with arrestin disrupts this polar core, triggering a global conformational rearrangement that enables high-affinity binding to activated rhodopsin. Mutations disrupting polar core residues bypass the requirement for receptor phosphorylation, allowing arrestin to bind activated unphosphorylated rhodopsin. Site-directed mutagenesis combined with in vitro binding assays to phosphorylated light-activated rhodopsin; structure-guided second-site suppressor mutations validated the molecular mechanism; interpreted with the contemporaneous crystal structure of arrestin The Journal of biological chemistry High 10206946
2000 Arrestin contacts rhodopsin via at least three regions: residues 11–30 and 51–70 (N-domain) and residues 231–260 (C-domain), as identified by peptide competition assays. These arrestin peptides also compete with transducin (Gt) binding to metarhodopsin II, indicating that arrestin and transducin share overlapping binding sites on rhodopsin, consistent with the steric competition model of desensitization. Spectrophotometric peptide competition assay (extra-MII monitor) using native disc membranes; sets of synthetic arrestin peptides spanning the full sequence tested for inhibition of arrestin- and transducin-dependent MII stabilization The Journal of biological chemistry Medium 10969086
2004 Arrestin release from rhodopsin and all-trans-retinal release from the opsin are thermodynamically linked events with similar activation energies; arrestin binding slows retinal release approximately 2-fold and abolishes its pH dependence. Fluorescence labeling of arrestin mutants I72C and S251C revealed burial of these sites at the rhodopsin-arrestin or phospholipid-arrestin interface upon binding to phosphorylated light-activated rhodopsin. Arrestin also binds a post-Meta II photodecay product (possibly Meta III), suggesting a role in limiting free retinal accumulation. Site-directed fluorescence labeling of arrestin mutants with monobromobimane; fluorescence, EPR, and biochemical (retinal release kinetics) approaches using purified proteins and disc membranes The Journal of biological chemistry High 15591052
2012 Upon binding to phosphorylated light-activated rhodopsin, the 'finger loop' (residues 67–79) of arrestin-1 moves toward the receptor but does not fully extend. A loop containing residue 139 moves unexpectedly away from the finger loop, facilitating receptor binding. Distal loops at residues 157 and 344 show smaller movements. The relative N- and C-domain orientation remains largely unchanged, contradicting a 'clam-shell' opening model of arrestin activation. Double electron-electron resonance (DEER) EPR spectroscopy using spin-labeled arrestin-1 mutant pairs; distance measurements in free and rhodopsin-bound states Proceedings of the National Academy of Sciences of the United States of America High 23091036
2017 The C-edge loops of arrestin-1 function as a membrane anchor during rhodopsin binding. Activation of arrestin by receptor-attached phosphates is required for C-edge engagement with the membrane. The C-edge adopts distinct conformations and orientations in the pre-complex (phosphate-activated but not yet tightly bound) versus the high-affinity receptor-bound complex. Molecular dynamics simulations combined with site-directed fluorescence spectroscopy experiments on arrestin-1 interacting with rhodopsin in membrane Nature communications High 28220785
2020 Comprehensive mutagenesis of the finger loop in bovine visual arrestin-1 established that the finger loop is the key element of the activation sensor. The majority of finger loop residues are important for binding to light-activated phosphorylated rhodopsin, and six mutations specifically affect binding to the activated (but not phosphorylated-inactive) rhodopsin form, demonstrating that the finger loop specifically detects the active receptor conformation. Comprehensive alanine-scanning mutagenesis of finger loop residues; cell-free translation of radiolabeled arrestin mutants; in vitro binding assays to purified phosphorylated light-activated rhodopsin and other functional rhodopsin forms; tested in context of truncated (pre-activated) arrestin-1 Journal of neurochemistry High 33159335
2021 Inositol phosphates (InsPs) bind to the N-domain basic patch of visual arrestin (Arr1), displacing its C-tail and priming arrestin for interaction with rhodopsin. Crystal structures of bovine Arr1 in ligand-free state (with near-complete C-tail model) and InsP-bound states show that C-tail displacement by InsPs is insufficient to activate arrestin (polar core remains intact), suggesting InsPs prime but do not fully activate Arr1. X-ray crystallography of bovine arrestin-1 (Arr1) in multiple states; structural comparison of ligand-free and InsP-bound forms; C-tail displacement assessed by electron density Structure (London, England : 1993) High 34678158

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1990 beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science (New York, N.Y.) 1027 2163110
2011 β-Arrestin-mediated receptor trafficking and signal transduction. Trends in pharmacological sciences 590 21680031
2007 Beta-arrestin-biased ligands at seven-transmembrane receptors. Trends in pharmacological sciences 504 17644195
2010 Beyond desensitization: physiological relevance of arrestin-dependent signaling. Pharmacological reviews 301 20427692
2004 The molecular acrobatics of arrestin activation. Trends in pharmacological sciences 277 15102497
2008 Beta-blockers alprenolol and carvedilol stimulate beta-arrestin-mediated EGFR transactivation. Proceedings of the National Academy of Sciences of the United States of America 235 18787115
2007 beta-arrestin-biased agonism at the beta2-adrenergic receptor. The Journal of biological chemistry 219 18086673
2007 Beta-arrestin signaling and regulation of transcription. Journal of cell science 215 17215450
2008 On the origins of arrestin and rhodopsin. BMC evolutionary biology 194 18664266
2018 Catalytic activation of β-arrestin by GPCRs. Nature 171 29720660
2018 Molecular mechanism of GPCR-mediated arrestin activation. Nature 169 29720655
2005 Seven-transmembrane receptor signaling through beta-arrestin. Science's STKE : signal transduction knowledge environment 154 16267056
1999 How does arrestin respond to the phosphorylated state of rhodopsin? The Journal of biological chemistry 153 10206946
2008 How does arrestin assemble MAPKs into a signaling complex? The Journal of biological chemistry 147 19001375
2004 Differential beta-arrestin trafficking and endosomal sorting of somatostatin receptor subtypes. The Journal of biological chemistry 143 15001578
1993 Polypeptide variants of beta-arrestin and arrestin3. The Journal of biological chemistry 137 8340388
2020 How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated Signaling. Cell 130 33296703
1992 The role of arrestin and retinoids in the regeneration pathway of rhodopsin. The Journal of biological chemistry 130 1386362
2015 Emerging Functional Divergence of β-Arrestin Isoforms in GPCR Function. Trends in endocrinology and metabolism: TEM 117 26471844
2003 Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins. The Journal of biological chemistry 116 14530255
2005 Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes. Current opinion in cell biology 109 15780588
2017 Structural basis of arrestin-3 activation and signaling. Nature communications 107 29127291
2017 Arrestin-biased AT1R agonism induces acute catecholamine secretion through TRPC3 coupling. Nature communications 103 28181498
1987 Deactivation of photoactivated rhodopsin by rhodopsin-kinase and arrestin. Journal of receptor research 98 3040978
2001 Beta-arrestin- and dynamin-dependent endocytosis of the AT1 angiotensin receptor. Molecular pharmacology 96 11160859
2010 Morphine-like opiates selectively antagonize receptor-arrestin interactions. The Journal of biological chemistry 90 20189994
2018 Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation. Nature structural & molecular biology 87 29872229
2017 C-edge loops of arrestin function as a membrane anchor. Nature communications 86 28220785
2012 Conformation of receptor-bound visual arrestin. Proceedings of the National Academy of Sciences of the United States of America 84 23091036
2014 Inactivation of SAG/RBX2 E3 ubiquitin ligase suppresses KrasG12D-driven lung tumorigenesis. The Journal of clinical investigation 81 24430184
2012 Functional characterization of SAG/RBX2/ROC2/RNF7, an antioxidant protein and an E3 ubiquitin ligase. Protein & cell 80 23136067
2008 Beta-arrestin-mediated signaling regulates protein synthesis. The Journal of biological chemistry 80 18276584
2008 Physiological and pharmacological implications of beta-arrestin regulation. Pharmacology & therapeutics 80 19100766
2004 Alternative, nonapoptotic programmed cell death: mediation by arrestin 2, ERK2, and Nur77. The Journal of biological chemistry 78 14769794
2018 Structural Basis of Arrestin-Dependent Signal Transduction. Trends in biochemical sciences 72 29636212
2023 Plasma membrane preassociation drives β-arrestin coupling to receptors and activation. Cell 70 37146613
2000 Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin. The Journal of biological chemistry 68 10969086
2004 Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events. The Journal of biological chemistry 67 15591052
2015 β-Arrestin-biased signaling mediates memory reconsolidation. Proceedings of the National Academy of Sciences of the United States of America 63 25831532
2021 Receptor-Arrestin Interactions: The GPCR Perspective. Biomolecules 61 33557162
2017 Understanding the GPCR biased signaling through G protein and arrestin complex structures. Current opinion in structural biology 61 28558341
2014 G Protein and β-arrestin signaling bias at the ghrelin receptor. The Journal of biological chemistry 61 25261469
2014 Arrestin interactions with G protein-coupled receptors. Handbook of experimental pharmacology 60 24292823
2023 Tail engagement of arrestin at the glucagon receptor. Nature 56 37558880
2017 Structural mechanism of arrestin activation. Current opinion in structural biology 56 28600951
2018 Arrestin recruitment to dopamine D2 receptor mediates locomotion but not incentive motivation. Molecular psychiatry 55 30120413
2013 Structural determinants of arrestin functions. Progress in molecular biology and translational science 54 23764050
1999 Expression, purification, and biochemical characterization of SAG, a ring finger redox-sensitive protein. Free radical biology & medicine 52 10443936
2023 Signal transduction at GPCRs: Allosteric activation of the ERK MAPK by β-arrestin. Proceedings of the National Academy of Sciences of the United States of America 51 37844230
2009 Diversity in arrestin function. Cellular and molecular life sciences : CMLS 51 19597700
2008 Beta-arrestin-mediated signaling in the heart. Circulation journal : official journal of the Japanese Circulation Society 47 18838825
2019 Arrestin-β-1 Physically Scaffolds TSH and IGF1 Receptors to Enable Crosstalk. Endocrinology 46 31127272
2020 Allosteric interactions in the parathyroid hormone GPCR-arrestin complex formation. Nature chemical biology 45 32632293
2014 β-Arrestin-1 mediates thyrotropin-enhanced osteoblast differentiation. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 45 24723693
1993 Beta-arrestin and arrestin are recognized by autoantibodies in sera from multiple sclerosis patients. Proceedings of the National Academy of Sciences of the United States of America 45 8475065
2020 SnapShot: β-Arrestin Functions. Cell 44 32888497
2016 β-Arrestin mediates the Frank-Starling mechanism of cardiac contractility. Proceedings of the National Academy of Sciences of the United States of America 44 27911784
2014 Overview of different mechanisms of arrestin-mediated signaling. Current protocols in pharmacology 43 25446289
2013 True arrestins and arrestin-fold proteins: a structure-based appraisal. Progress in molecular biology and translational science 42 23764049
2019 Therapeutic Potential of Targeting ß-Arrestin. Frontiers in pharmacology 40 30894814
2014 Role for β-arrestin in mediating paradoxical β2AR and PAR2 signaling in asthma. Current opinion in pharmacology 40 24907413
2020 Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers. EMBO reports 39 32929862
2013 Progastrin stimulates colonic cell proliferation via CCK2R- and β-arrestin-dependent suppression of BMP2. Gastroenterology 38 23891976
2005 Beta-arrestin goes nuclear. Cell 38 16325568
2018 Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification. Proceedings of the National Academy of Sciences of the United States of America 37 30591558
2018 Arrestin-mediated signaling: Is there a controversy? World journal of biological chemistry 37 30595812
2017 β-arrestin signalling and bias in hormone-responsive GPCRs. Molecular and cellular endocrinology 36 28174117
2010 Transduced Tat-SAG fusion protein protects against oxidative stress and brain ischemic insult. Free radical biology & medicine 36 20100567
2019 The structural basis of the arrestin binding to GPCRs. Molecular and cellular endocrinology 35 30703488
2016 β-Arrestin-2 Counters CXCR7-Mediated EGFR Transactivation and Proliferation. Molecular cancer research : MCR 35 26921391
2019 β-Arrestin-2 BRET Biosensors Detect Different β-Arrestin-2 Conformations in Interaction with GPCRs. ACS sensors 33 31849219
2012 Arrestin scaffolds NHERF1 to the P2Y12 receptor to regulate receptor internalization. The Journal of biological chemistry 31 22610101
2024 GPCR-dependent and -independent arrestin signaling. Trends in pharmacological sciences 30 38906769
2016 SAG/Rbx2-Dependent Neddylation Regulates T-Cell Responses. The American journal of pathology 29 27543965
2022 The α-Arrestin ARRDC3 Is an Emerging Multifunctional Adaptor Protein in Cancer. Antioxidants & redox signaling 28 34465145
2022 β-arrestin-1 and β-arrestin-2 Restrain MRGPRX2-Triggered Degranulation and ERK1/2 Activation in Human Skin Mast Cells. Frontiers in allergy 26 35910860
2021 Activation of PTH1R alleviates epididymitis and orchitis through Gq and β-arrestin-1 pathways. Proceedings of the National Academy of Sciences of the United States of America 26 34740971
2014 Arrestin expression in E. coli and purification. Current protocols in pharmacology 26 25446290
2020 The finger loop as an activation sensor in arrestin. Journal of neurochemistry 25 33159335
2019 Calcium-Sensing Receptor Internalization Is β-Arrestin-Dependent and Modulated by Allosteric Ligands. Molecular pharmacology 25 31399503
2019 Arrestin-independent constitutive endocytosis of GPR125/ADGRA3. Annals of the New York Academy of Sciences 25 31659746
2013 Phosphorylation regulates TRPV1 association with β-arrestin-2. The Biochemical journal 25 23360390
2014 β-Arrestin-dependent deactivation of mouse melanopsin. PloS one 24 25401926
2014 Engineered hyperphosphorylation of the β2-adrenoceptor prolongs arrestin-3 binding and induces arrestin internalization. Molecular pharmacology 23 25425623
2022 Selective phosphorylation of threonine residues defines GPR84-arrestin interactions of biased ligands. The Journal of biological chemistry 22 35427647
2016 Structural mechanism of GPCR-arrestin interaction: recent breakthroughs. Archives of pharmacal research 22 26825061
2021 Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure (London, England : 1993) 21 34678158
2015 β-Arrestin 2 Promotes Hepatocyte Apoptosis by Inhibiting Akt Protein. The Journal of biological chemistry 21 26582201
2014 Molecular mechanism of phosphorylation-dependent arrestin activation. Current opinion in structural biology 21 25484000
2017 Arrestin-2 and arrestin-3 differentially modulate locomotor responses and sensitization to amphetamine. Neuropharmacology 20 28419873
2012 β-arrestin-mediated signaling improves the efficacy of therapeutics. Journal of pharmacological sciences 20 22447307
2020 Many faces of the GPCR-arrestin interaction. Archives of pharmacal research 19 32803684
2019 Structural Mechanism of the Arrestin-3/JNK3 Interaction. Structure (London, England : 1993) 19 31080119
2018 Unique Roles of β-Arrestin in GPCR Trafficking Revealed by Photoinducible Dimerizers. Scientific reports 19 29330504
2013 Arrestin pathways as drug targets. Progress in molecular biology and translational science 18 23764065
2021 CXCR7 ameliorates myocardial infarction as a β-arrestin-biased receptor. Scientific reports 17 33564089
2018 A rapid fluorogenic GPCR-β-arrestin interaction assay. Protein science : a publication of the Protein Society 17 29411438
2013 β-Arrestin-kinase scaffolds: turn them on or turn them off? Wiley interdisciplinary reviews. Systems biology and medicine 17 23319470
1999 Phosducin, beta-arrestin and opioid receptor migration. European journal of pharmacology 17 10443588
1992 SAG: a Schwann cell membrane glycoprotein. The Journal of neuroscience : the official journal of the Society for Neuroscience 17 1376775

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