WHY MASSACHUSETTS SHOULD NOT RELEGATE PARENTS TO “LEGAL STRANGERS”1: A SURVEY OF THE MYRIAD INTERPRETATIONS OF THE ICPC

The Interstate Compact on the Placement of Children (ICPC) is a well-intentioned statute that has led to anomalous and irrational results in courts across the country. The ICPC’s aim is to ensure that foster care placements by state agencies of children across state lines preliminary to adoption or placement in foster care are in the child’s best interests. However, certain courts have drastically expanded the ICPC’s reach to cover parental foster care placements. This Article discusses the split in case law, the reasons for limiting the ICPC in Massachusetts, and options for nervous courts, attorneys, and state agencies when sending a child across state lines. Ultimately, this Article argues that the ICPC is not the mechanism to utilize when placing a child with his or her parent across state lines

YOU’RE OBJECTING TO ME?: CHALLENGING JUDICIAL QUESTIONING

This Article examines the often seen and routinely unchallenged practice of judicial questioning. Part I covers the fundamental concept of judicial impartiality and the power of judges to question witnesses. Part II illustrates varied examples from both civil and criminal trials where judges crossed (or may have crossed) the line in questioning witnesses. Part III considers what trial counsel should do in the face of improper judicial questioning. Part IV explains how the failure to object to questioning significantly diminishes the likelihood of success on appeal. In the Conclusion, the Authors urge counsel to object whenever a judge’s questions appear likely to endanger their clients’ rights

Electrophysiological correlates of high-level perception during spatial navigation

We studied the electrophysiological basis of object recognition by recording scalp\ud electroencephalograms while participants played a virtual-reality taxi driver game.\ud Participants searched for passengers and stores during virtual navigation in simulated\ud towns. We compared oscillatory brain activity in response to store views that were targets or\ud nontargets (during store search) or neutral (during passenger search). Even though store\ud category was solely defined by task context (rather than by sensory cues), frontal ...\ud \u

Change in adiposity is associated with change in glycoprotein acetyls but not hsCRP in adolescents with severe obesity.

BACKGROUND Obesity-associated chronic inflammation mediates the development of adverse cardiometabolic outcomes. There are sparse data on associations between severe obesity and inflammatory biomarkers in adolescence; most are cross-sectional and limited to acute phase reactants. Here, we investigate associations between adiposity measures and inflammatory biomarkers in children and adolescents with severe obesity both cross-sectionally and longitudinally. METHODS From the Childhood Overweight Biorepository of Australia (COBRA) study, a total of n = 262 participants, mean age 11.5 years (SD 3.5) with obesity had measures of adiposity (body mass index, BMI; % above the 95th BMI-centile, %>95th BMI-centile; waist circumference, WC; waist/height ratio, WtH; % total body fat, %BF; % truncal body fat, %TF) and inflammation biomarkers (glycoprotein acetyls, GlycA; high-sensitivity C-Reactive Protein, hsCRP; white blood cell count, WBC; and neutrophil/lymphocyte ratio, NLR) assessed at baseline. Ninety-eight individuals at mean age of 15.9 years (3.7) participated in a follow-up study 5.6 (2.1) years later. Sixty-two individuals had longitudinal data. Linear regression models, adjusted for age and sex for cross-sectional analyses were applied. To estimate longitudinal associations between change in adiposity measures with inflammation biomarkers, models were adjusted for baseline measures of adiposity and inflammation. RESULTS All adiposity measures were cross-sectionally associated with GlycA, hsCRP and WBC at both time points. Change in BMI, %>95th BMI-centile, WC, WtH and %TF were associated with concomitant change in GlycA and WBC, but not in hsCRP and NLR. CONCLUSION GlycA and WBC but not hsCRP and NLR may be useful in assessing adiposity-related severity of chronic inflammation over time

KELT-8b: A highly inflated transiting hot Jupiter and a new technique for extracting high-precision radial velocities from noisy spectra

We announce the discovery of a highly inflated transiting hot Jupiter discovered by the KELT-North survey. A global analysis including constraints from isochrones indicates that the V = 10.8 host star (HD 343246) is a mildly evolved, G dwarf with $T_{\rm eff} = 5754_{-55}^{+54}$ K, $\log{g} = 4.078_{-0.054}^{+0.049}$, $[Fe/H] = 0.272\pm0.038$, an inferred mass $M_{*}=1.211_{-0.066}^{+0.078}$ M$_{\odot}$, and radius $R_{*}=1.67_{-0.12}^{+0.14}$ R$_{\odot}$. The planetary companion has mass $M_P = 0.867_{-0.061}^{+0.065}$ $M_{J}$, radius $R_P = 1.86_{-0.16}^{+0.18}$ $R_{J}$, surface gravity $\log{g_{P}} = 2.793_{-0.075}^{+0.072}$, and density $\rho_P = 0.167_{-0.038}^{+0.047}$ g cm$^{-3}$. The planet is on a roughly circular orbit with semimajor axis $a = 0.04571_{-0.00084}^{+0.00096}$ AU and eccentricity $e = 0.035_{-0.025}^{+0.050}$. The best-fit linear ephemeris is $T_0 = 2456883.4803 \pm 0.0007$ BJD$_{\rm TDB}$ and $P = 3.24406 \pm 0.00016$ days. This planet is one of the most inflated of all known transiting exoplanets, making it one of the few members of a class of extremely low density, highly-irradiated gas giants. The low stellar $\log{g}$ and large implied radius are supported by stellar density constraints from follow-up light curves, plus an evolutionary and space motion analysis. We also develop a new technique to extract high precision radial velocities from noisy spectra that reduces the observing time needed to confirm transiting planet candidates. This planet boasts deep transits of a bright star, a large inferred atmospheric scale height, and a high equilibrium temperature of $T_{eq}=1675^{+61}_{-55}$ K, assuming zero albedo and perfect heat redistribution, making it one of the best targets for future atmospheric characterization studies.Comment: Submitted to ApJ, feedback is welcom

Characterization and implications of the initial estimated glomerular filtration rate 'dip' upon sodium-glucose cotransporter-2 inhibition with empagliflozin in the EMPA-REG OUTCOME trial

Treatment with sodium-glucose co-transporter-2 inhibitors induces an initial 3-5 ml/min/1.73 m(2) decline in estimated glomerular filtration rate (eGFR). Although considered to be of hemodynamic origin and largely reversible, this 'eGFR dip' may cause concern in clinical practice, which highlights the need to better understand its incidence and clinical implications. In this post hoc analysis of the EMPA-REG OUTCOME trial, 6,668 participants randomized to empagliflozin 10 mg, 25 mg or placebo with eGFR available at baseline and week four were categorized by initial eGFR change into three groups; over 10% decline ('eGFR dipper'), over 0 and up to 10% decline ('eGFR intermediate'), no eGFR decline ('eGFR non-dipper'). Baseline characteristics of 'eGFR intermediate' and 'eGFR non-dipper' were generally comparable. An initial 'eGFR dip' was observed in 28.3% of empagliflozin versus 13.4% of placebo-treated participants; odds ratio 2.7 [95% Confidence Interval 2.3-3.0]. In multivariate logistic regression, diuretic use and higher KDIGO risk category at baseline were independently predictive of an 'eGFR dip' in empagliflozin versus placebo. Safety and beneficial treatment effects with empagliflozin on cardiovascular and kidney outcomes were consistent across subgroups based on these predictive factors. The initial 'eGFR dip' did not have a major impact on the treatment effect of empagliflozin on subsequent cardiovascular death, hospitalization for heart failure, and incident or worsening kidney disease. Thus, patients with type 2 diabetes with more advanced kidney disease and/or on diuretic therapy were more likely to experience an 'eGFR dip' of over 10% with empagliflozin, but reduction in cardiovascular and kidney outcomes was not relevantly modified by such 'eGFR dip.

Deletion of Complement Factor H–Related Genes CFHR1 and CFHR3 Is Associated with Atypical Hemolytic Uremic Syndrome

Atypical hemolytic uremic syndrome (aHUS) is associated with defective complement regulation. Disease-associated mutations have been described in the genes encoding the complement regulators complement factor H, membrane cofactor protein, factor B, and factor I. In this study, we show in two independent cohorts of aHUS patients that deletion of two closely related genes, complement factor H–related 1 (CFHR1) and complement factor H–related 3 (CFHR3), increases the risk of aHUS. Amplification analysis and sequencing of genomic DNA of three affected individuals revealed a chromosomal deletion of ∼84 kb in the RCA gene cluster, resulting in loss of the genes coding for CFHR1 and CFHR3, but leaving the genomic structure of factor H intact. The CFHR1 and CFHR3 genes are flanked by long homologous repeats with long interspersed nuclear elements (retrotransposons) and we suggest that nonallelic homologous recombination between these repeats results in the loss of the two genes. Impaired protection of erythrocytes from complement activation is observed in the serum of aHUS patients deficient in CFHR1 and CFHR3, thus suggesting a regulatory role for CFHR1 and CFHR3 in complement activation. The identification of CFHR1/CFHR3 deficiency in aHUS patients may lead to the design of new diagnostic approaches, such as enhanced testing for these genes

Oxonium ion scanning mass spectrometry for large-scale plasma glycoproteomics

Protein glycosylation, a complex and heterogeneous post-translational modification that is frequently dysregulated in disease, has been difficult to analyse at scale. Here we report a data-independent acquisition technique for the large-scale mass-spectrometric quantification of glycopeptides in plasma samples. The technique, which we named ‘OxoScan-MS’, identifies oxonium ions as glycopeptide fragments and exploits a sliding-quadrupole dimension to generate comprehensive and untargeted oxonium ion maps of precursor masses assigned to fragment ions from non-enriched plasma samples. By applying OxoScan-MS to quantify 1,002 glycopeptide features in the plasma glycoproteomes from patients with COVID-19 and healthy controls, we found that severe COVID-19 induces differential glycosylation in IgA, haptoglobin, transferrin and other disease-relevant plasma glycoproteins. OxoScan-MS may allow for the quantitative mapping of glycoproteomes at the scale of hundreds to thousands of samples

Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth

Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydroxylation of the small ribosomal subunit protein RPS23. Like OGFOD1, Sud1 catalyzes a single prolyl-hydroxylation of RPS23 in contrast to yeast Tpa1p, where Pro-64 dihydroxylation is observed. RNAi-mediated Sud1 knockdown hinders normal growth in different Drosophila tissues. Growth impairment originates from both reduction of cell size and diminution of the number of cells and correlates with impaired translation efficiency and activation of the unfolded protein response in the endoplasmic reticulum. This is accompanied by phosphorylation of eIF2α and concomitant formation of stress granules, as well as promotion of autophagy and apoptosis. These observations, together with those on enzyme homologs described in the companion articles, reveal conserved biochemical and biological roles for a widely distributed ribosomal oxygenase.Fil: Katz, Maximiliano Javier. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Acevedo, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Loenarz, Christoph. University of Oxford; Reino UnidoFil: Galagovsky, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Liu Yi, Phebee. University Of Oxford; Reino UnidoFil: Pérez, Marcelo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Thalhammer, Armin. University of Oxford; Reino UnidoFil: Sekirnik, Rok. University Of Oxford; Reino UnidoFil: Ge, Wei. University of Oxford; Reino UnidoFil: Melani, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Thomas, Maria Gabriela. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; ArgentinaFil: Simonetta, Sergio Hernan. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; ArgentinaFil: Boccaccio, Graciela Lidia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Schofield, Christoper J. University of Oxford; Reino UnidoFil: Cockman, Matthew E. University of Oxford; Reino UnidoFil: Ratcliffe, Peter J. University of Oxford; Reino UnidoFil: Wappner, Pablo. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentin