On the morning of November 1, at Yeoido KBS HallKBS WORLD Radio filmed K-pop stars making their way to attend rehearsals for Music Bank.

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[Economy] :
Finance Minister Choi Sang-mok said Thursday that he expects Donald Trump’s reelection to have a “considerable” impact on the South Korean economy.  The minister made the remarks Wednesday in Seoul during a meeting of ministers concerned with the economy, the morning after Donald Trump won the U.S. ...

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My role as a stable isotope research assistant  British Geological Survey

Laboratory life: my work experience week at BGS  British Geological Survey

Mycobacterium tuberculosis can reside and persist in deep tissues; latent tuberculosis can evade immune detection and has a unique mechanism to convert it into active disease through reactivation. M. tuberculosis Rv1421 (MtRv1421) is a hypothetical protein that has been proposed to be involved in nucleotide binding-related metabolism in cell-growth and cell-division processes. However, due to a lack of structural information, the detailed function of MtRv1421 remains unclear. In this study, a truncated N-terminal domain (NTD) of MtRv1421, which contains a Walker A/B-like motif, was purified and crystallized using PEG 400 as a precipitant. The crystal of MtRv1421-NTD diffracted to a resolution of 1.7 Å and was considered to belong to either the C-centered monoclinic space group C2 or the I-centered orthorhombic space group I222, with unit-cell parameters a = 124.01, b = 58.55, c = 84.87 Å, β = 133.12° or a = 58.53, b = 84.86, c = 90.52 Å, respectively. The asymmetric units of the C2 or I222 crystals contained two or one monomers, respectively. In terms of the binding ability of MtRv1421-NTD to various ligands, uridine diphosphate (UDP) and UDP-N-acetylglucosamine significantly increased the melting temperature of MtRv1421-NTD, which indicates structural stabilization through the binding of these ligands. Altogether, the results reveal that a UDP moiety may be required for the interaction of MtRv1421-NTD as a nucleotide-binding protein with its ligand.

Plasmodium vivax is a major cause of malaria, which poses an increased health burden on approximately one third of the world's population due to climate change. Primaquine, the preferred treatment for P. vivax malaria, is contraindicated in individuals with glucose-6-phosphate dehydrogenase (G6PD) deficiency, a common genetic cause of hemolytic anemia, that affects ∼2.5% of the world's population and ∼8% of the population in areas of the world where P. vivax malaria is endemic. The Seattle Structural Genomics Center for Infectious Disease (SSGCID) conducted a structure–function analysis of P. vivax N-myristoyltransferase (PvNMT) as part of efforts to develop alternative malaria drugs. PvNMT catalyzes the attachment of myristate to the N-terminal glycine of many proteins, and this critical post-translational modification is required for the survival of P. vivax. The first step is the formation of a PvNMT–myristoyl–CoA binary complex that can bind to peptides. Understanding how inhibitors prevent protein binding will facilitate the development of PvNMT as a viable drug target. NMTs are secreted in all life stages of malarial parasites, making them attractive targets, unlike current antimalarials that are only effective during the plasmodial erythrocytic stages. The 2.3 Å resolution crystal structure of the ternary complex of PvNMT with myristoyl-CoA and a novel inhibitor is reported. One asymmetric unit contains two monomers. The structure reveals notable differences between the PvNMT and human enzymes and similarities to other plasmodial NMTs that can be exploited to develop new antimalarials.

A confiscated package of street drugs was characterized by the usual mass spectral (MS) and FT–IR analyses. The confiscated powder material was highly crystalline and was found to consist of two very different species, accidentally of sizes convenient for X-ray diffraction. Thus, one each was selected and redundant com­plete sets of data were collected at 100 K using Cu Kα radiation. The selected crystals contained: (a) 1,2-diphenyl-2-(pyrrolidin-1-yl)ethanone hy­dro­chloride hemihydrate or 1-(2-oxo-1,2-di­phenyl­eth­yl)pyrrolidin-1-ium chloride hemihydrate, C18H20NO+·Cl−·0.5H2O, (I), a synthetic cathinone called `α-D2PV', and (b) the sugar myo-inositol, C6H12O6, (II), probably the only instance in which the drug and its diluent have been fully characterized from a single confiscated sample. Moreover, the structural details of both are rather attractive showing: (i) inter­esting hydrogen bonding observed in pairwise inter­actions by the drug mol­ecules, mediated by the chloride counter-anions and the waters of crystallization, and (ii) π–π inter­actions in the case of the phenyl rings of the drug which are of two different types, namely, π–π stacking and edge-to-π. Finally, the inositol crystallizes with Z' = 2 and the resulting diastereoisomers were examined by overlay techniques.

The title compound, 3-[(benzo-1,3-dioxol-5-yl)amino]-4-meth­oxy­cyclo­but-3-ene-1,2-dione, C12H9NO5 (3), is a precursor to an anti­mycobacterial squaramide. Block-shaped crystals of a monoclinic form (3-I, space group P21/c, Z = 8, Z' = 2) and needle-shaped crystals of a triclinic form (3-II, space group P-1, Z = 4, Z' = 2) were found to crystallize concomitantly. In both crystal forms, R22(10) dimers assemble through N—H⋯O=C hydrogen bonds. These dimers are formed from crystallographically unique mol­ecules in 3-I, but exhibit crystallographic Ci symmetry in 3-II. Twinning by pseudomerohedry was encountered in the crystals of 3-II. The conformations of 3 in the solid forms 3-I and 3-II are different from one another but are similar for the unique mol­ecules in each polymorph. Density functional theory (DFT) calculations on the free mol­ecule of 3 indicate that a nearly planar conformation is preferred.

Low-molecular-weight (LMW) thiols are involved in many processes in all organisms, playing a protective role against reactive species, heavy metals, toxins and antibiotics. Actinobacteria, such as Mycobacterium tuberculosis, use the LMW thiol mycothiol (MSH) to buffer the intracellular redox environment. The NADPH-dependent FAD-containing oxidoreductase mycothiol disulfide reductase (Mtr) is known to reduce oxidized mycothiol disulfide (MSSM) to MSH, which is crucial to maintain the cellular redox balance. In this work, the first crystal structures of Mtr are presented, expanding the structural knowledge and understanding of LMW thiol reductases. The structural analyses and docking calculations provide insight into the nature of Mtrs, with regard to the binding and reduction of the MSSM substrate, in the context of related oxidoreductases. The putative binding site for MSSM suggests a similar binding to that described for the homologous glutathione reductase and its respective substrate glutathione disulfide, but with distinct structural differences shaped to fit the bulkier MSSM substrate, assigning Mtrs as uniquely functioning reductases. As MSH has been acknowledged as an attractive antitubercular target, the structural findings presented in this work may contribute towards future antituberculosis drug development.

The Mycobacterium tuberculosis trifunctional enzyme (MtTFE) is an α2β2 tetrameric enzyme in which the α-chain harbors the 2E-enoyl-CoA hydratase (ECH) and 3S-hydroxyacyl-CoA dehydrogenase (HAD) active sites, and the β-chain provides the 3-ketoacyl-CoA thiolase (KAT) active site. Linear, medium-chain and long-chain 2E-enoyl-CoA molecules are the preferred substrates of MtTFE. Previous crystallographic binding and modeling studies identified binding sites for the acyl-CoA substrates at the three active sites, as well as the NAD binding pocket at the HAD active site. These studies also identified three additional CoA binding sites on the surface of MtTFE that are different from the active sites. It has been proposed that one of these additional sites could be of functional relevance for the substrate channeling (by surface crawling) of reaction intermediates between the three active sites. Here, 226 fragments were screened in a crystallographic fragment-binding study of MtTFE crystals, resulting in the structures of 16 MtTFE–fragment complexes. Analysis of the 121 fragment-binding events shows that the ECH active site is the `binding hotspot' for the tested fragments, with 41 binding events. The mode of binding of the fragments bound at the active sites provides additional insight into how the long-chain acyl moiety of the substrates can be accommodated at their proposed binding pockets. In addition, the 20 fragment-binding events between the active sites identify potential transient binding sites of reaction intermediates relevant to the possible channeling of substrates between these active sites. These results provide a basis for further studies to understand the functional relevance of the latter binding sites and to identify substrates for which channeling is crucial.

Eukaryotic TIR (Toll/interleukin-1 receptor protein) domains signal via TIR–TIR interactions, either by self-association or by interaction with other TIR domains. In mammals, TIR domains are found in Toll-like receptors (TLRs) and cytoplasmic adaptor proteins involved in pro-inflammatory signaling. Previous work revealed that the MAL TIR domain (MALTIR) nucleates the assembly of MyD88TIR into crystalline arrays in vitro. A microcrystal electron diffraction (MicroED) structure of the MyD88TIR assembly has previously been solved, revealing a two-stranded higher-order assembly of TIR domains. In this work, it is demonstrated that the TIR domain of TLR2, which is reported to signal as a heterodimer with either TLR1 or TLR6, induces the formation of crystalline higher-order assemblies of MyD88TIR in vitro, whereas TLR1TIR and TLR6TIR do not. Using an improved data-collection protocol, the MicroED structure of TLR2TIR-induced MyD88TIR microcrystals was determined at a higher resolution (2.85 Å) and with higher completeness (89%) compared with the previous structure of the MALTIR-induced MyD88TIR assembly. Both assemblies exhibit conformational differences in several areas that are important for signaling (for example the BB loop and CD loop) compared with their monomeric structures. These data suggest that TLR2TIR and MALTIR interact with MyD88 in an analogous manner during signaling, nucleating MyD88TIR assemblies uni­directionally.

Vancomycin is a glycopeptide antibiotic that for decades has been a mainstay of treatment for persistent bacterial infections. However, the spread of antibiotic resistance threatens its continued utility. In particular, vancomycin-resistant enterococci (VRE) have become a pressing clinical challenge. Vancomycin acts by binding and sequestering the intermediate Lipid II in cell-wall biosynthesis, specifically recognizing a d-alanine-d-alanine dipeptide motif within the Lipid II molecule. VRE achieve resistance by remodeling this motif to either d-alanine-d-lactate or d-alanine-d-serine; the former substitution essentially abolishes recognition by vancomycin of Lipid II, whereas the latter reduces the affinity of the antibiotic by roughly one order of magnitude. The complex of vancomycin bound to d-alanine-d-serine has been crystallized, and its 1.20 Å X-ray crystal structure is presented here. This structure reveals that the d-alanine-d-serine ligand is bound in essentially the same position and same pose as the native d-alanine-d-alanine ligand. The serine-containing ligand appears to be slightly too large to be comfortably accommodated in this way, suggesting one possible contribution to the reduced binding affinity. In addition, two flexible hydroxyl groups – one from the serine side chain of the ligand, and the other from a glucose sugar on the antibiotic – are locked into single conformations in the complex, which is likely to contribute an unfavorable entropic component to the recognition of the serine-containing ligand.

An X-ray absorption spectroscopy (XAS) electrochemical cell was used to collect high-quality XAS measurements of N-truncated Cu:amyloid-β (Cu:Aβ) samples under near-physiological conditions. N-truncated Cu:Aβ peptide complexes contribute to oxidative stress and neurotoxicity in Alzheimer's patients' brains. However, the redox properties of copper in different Aβ peptide sequences are inconsistent. Therefore, the geometry of binding sites for the copper binding in Aβ4–8/12/16 was determined using novel advanced extended X-ray absorption fine structure (EXAFS) analysis. This enables these peptides to perform redox cycles in a manner that might produce toxicity in human brains. Fluorescence XAS measurements were corrected for systematic errors including defective-pixel data, monochromator glitches and dispersion of pixel spectra. Experimental uncertainties at each data point were measured explicitly from the point-wise variance of corrected pixel measurements. The copper-binding environments of Aβ4–8/12/16 were precisely determined by fitting XAS measurements with propagated experimental uncertainties, advanced analysis and hypothesis testing, providing a mechanism to pursue many similarly complex questions in bioscience. The low-temperature XAS measurements here determine that CuII is bound to the first amino acids in the high-affinity amino-terminal copper and nickel (ATCUN) binding motif with an oxygen in a tetragonal pyramid geometry in the Aβ4–8/12/16 peptides. Room-temperature XAS electrochemical-cell measurements observe metal reduction in the Aβ4–16 peptide. Robust investigations of XAS provide structural details of CuII binding with a very different bis-His motif and a water oxygen in a quasi-tetrahedral geometry. Oxidized XAS measurements of Aβ4–12/16 imply that both CuII and CuIII are accommodated in an ATCUN-like binding site. Hypotheses for these CuI, CuII and CuIII geometries were proven and disproven using the novel data and statistical analysis including F tests. Structural parameters were determined with an accuracy some tenfold better than literature claims of past work. A new protocol was also developed using EXAFS data analysis for monitoring radiation damage. This gives a template for advanced analysis of complex biosystems.

Light–oxygen–voltage (LOV) domains are small photosensory flavoprotein modules that allow the conversion of external stimuli (sunlight) into intra­cellular signals responsible for various cell behaviors (e.g. phototropism and chloro­plast relocation). This ability relies on the light-induced formation of a covalent thio­ether adduct between a flavin chromophore and a reactive cysteine from the protein environment, which triggers a cascade of structural changes that result in the activation of a serine/threonine (Ser/Thr) kinase. Recent developments in time-resolved crystallography may allow the activation cascade of the LOV domain to be observed in real time, which has been elusive. In this study, we report a robust protocol for the production and stable delivery of microcrystals of the LOV domain of phototropin Phot-1 from Chlamydomonas reinhardtii (CrPhotLOV1) with a high-viscosity injector for time-resolved serial synchrotron crystallography (TR-SSX). The detailed process covers all aspects, from sample optimization to data collection, which may serve as a guide for soluble protein preparation for TR-SSX. In addition, we show that the crystals obtained preserve the photoreactivity using infrared spectroscopy. Furthermore, the results of the TR-SSX experiment provide high-resolution insights into structural alterations of CrPhotLOV1 from Δt = 2.5 ms up to Δt = 95 ms post-photoactivation, including resolving the geometry of the thio­ether adduct and the C-terminal region implicated in the signal transduction process.

Identifying and characterizing metal-binding sites (MBS) within macromolecular structures is imperative for elucidating their biological functions. CheckMyMetal (CMM) is a web based tool that facilitates the interactive valid­ation of MBS in structures determined through X-ray crystallography and cryo-electron microscopy (cryo-EM). Recent updates to CMM have significantly enhanced its capability to efficiently handle large datasets generated from cryo-EM structural analyses. In this study, we address various challenges inherent in validating MBS within both X-ray and cryo-EM structures. Specifically, we examine the difficulties associated with accurately identifying metals and modeling their coordination environments by considering the ongoing reproducibility challenges in structural biology and the critical importance of well annotated, high-quality experimental data. CMM employs a sophisticated framework of rules rooted in the valence bond theory for MBS validation. We explore how CMM validation parameters correlate with the resolution of experimentally derived structures of macromolecules and their complexes. Additionally, we showcase the practical utility of CMM by analyzing a representative cryo-EM structure. Through a comprehensive examination of experimental data, we demonstrate the capability of CMM to advance MBS characterization and identify potential instances of metal misassignment.

MltG, a membrane-bound lytic transglycosyl­ase, has roles in terminating glycan polymerization in peptidoglycan and incorporating glycan chains into the cell wall, making it significant in bacterial cell-wall biosynthesis and remodeling. This study provides the first reported MltG structure from Mycobacterium abscessus (maMltG), a superbug that has high antibiotic resistance. Our structural and biochemical analyses revealed that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of maMltG was disclosed using structural analysis and sequence comparison. Overall, this study contributes to our understanding of the transglycosyl­ation reaction of the MltG family, aiding the design of next-generation antibiotics targeting M. abscessus.

The title compound, C15H15F3N2O3S, crystallizes in the monoclinic system, space group I2/a, with Z = 8. As expected, the nine-membered heterobicyclic system is virtually planar and the cyclo­hexyl group adopts a chair conformation. There is structural evidence for intra­molecular N—S⋯O chalcogen bonding between the benziso­thia­zolinone S atom and one O atom of the nitro group, approximately aligned along the extension of the covalent N—S bond [N—S⋯O = 162.7 (1)°]. In the crystal, the mol­ecules form centrosymmetric dimers through C—H⋯O weak hydrogen bonding between a C—H group of the electron-deficient benzene ring and the benzo­thia­zolinone carbonyl O atom with an R22(10) motif. In contrast to the previously described N-acyl 7-nitro-5-(tri­fluoro­meth­yl)benzo[d]iso­thia­zol-3(2H)-ones, the title N-cyclo­hexyl­methyl analogue does not inhibit growth of Mycobacterium aurum and Mycobacterium smegmatis in vitro.

This title compound, C20H26O2, was isolated from the benzene fraction of the stem bark of Staudtia kamerunensis Warb. (Myristicaceae) using column chromatography techniques over silica gel. The compound was fully characterized by single-crystal X-ray diffraction, one and two-dimensional NMR spectroscopy, IR and MS spectrometry. The compound has two fused cyclo­hexane rings attached to a benzene ring, with a carb­oxy­lic acid on C-4. This cyclo­hexene ring has a chair conformation while the other adopts a half-chair conformation. The benzene ring is substituted with a propenyl moiety. The structure is characterized by inter­molecular O—H⋯O hydrogen bonds, two C—H⋯O intra­molecular hydrogen bonds and two C—H⋯π inter­actions. The mol­ecular structure confirms previous studies carried out by spectroscopic techniques.

In this work, we showed that the use of ethanol to increase image contrast when imaging cardiac tissue with synchrotron X-ray phase-contrast imaging (X-PCI) leads to heterogeneous tissue shrinkage, which has an impact on the 3D organization of the myocardium.

X-ray absorption spectroscopy (XAS) is a promising technique for determining structural information from sensitive biological samples, but high-accuracy X-ray absorption fine structure (XAFS) requires corrections of systematic errors in experimental data. Low-temperature XAS and room-temperature X-ray absorption spectro-electrochemical (XAS-EC) measurements of N-truncated amyloid-β samples were collected and corrected for systematic effects such as dead time, detector efficiencies, monochromator glitches, self-absorption, radiation damage and noise at higher wavenumber (k). A new protocol was developed using extended X-ray absorption fine structure (EXAFS) data analysis for monitoring radiation damage in real time and post-analysis. The reliability of the structural determinations and consistency were validated using the XAS measurement experimental uncertainty. The correction of detector pixel efficiencies improved the fitting χ2 by 12%. An improvement of about 2.5% of the structural fitting was obtained after dead-time corrections. Normalization allowed the elimination of 90% of the monochromator glitches. The remaining glitches were manually removed. The dispersion of spectra due to self-absorption was corrected. Standard errors of experimental measurements were propagated from pointwise variance of the spectra after systematic corrections. Calculated uncertainties were used in structural refinements for obtaining precise and reliable values of structural parameters including atomic bond lengths and thermal parameters. This has permitted hypothesis testing.

A teen gets a dose of Pfizer's COVID-19 vaccine at Holtz Children's Hospital in Miami on May 18. Nearly 7 million U.S. teens and pre-teens (ages 12 through 17) have received at least one dose of a COVID-19 vaccine, so far, the CDC says.; Credit: Eva Marie Uzcategui/Bloomberg via Getty Images

It's been a little more than a month since adolescents as young as 12 became eligible in the United States to receive the Pfizer vaccine against COVID-19, and nearly all reports have been positive: The vaccine is very effective in this age group, and the vast majority of kids experience mild side effects, if any — the same sore arm or mild flu-like symptoms seen among adults who get the shot.

The Centers for Disease Control and Prevention has recommended that everyone 12-years-old and older get vaccinated against COVID-19, and the rollout is well underway: According to the CDC, nearly 7 million U.S. teens and pre-teens (ages 12 through 17) have received at least one dose of a COVID-19 vaccine, so far.

Still, soon after the FDA authorized the use of Pfizer's vaccine in young people, federal agencies began receiving reports of mild chest pain or other signs of possible heart inflammation (known as myocarditis) in a very small percentage of recently vaccinated teens.

CDC director Rochelle Walensky said at a White House briefing Friday that there have been more than 300 cases of heart inflammation reported among more than 20 million teens and young adults who have received one of the vaccines made by Moderna or Pfizer. She said that in the "vast majority" of cases, the inflammation went away.

An expert advisory committee to the health agency is expected to review the cases in more depth at a meeting Friday.

So, in the meantime, should parents of teens hesitate to have their kids vaccinated against COVID-19? Vaccine experts and the American Academy of Pediatrics say no, don't hesitate. It's good for doctors and patients to be aware that there might be a connection between the mRNA vaccines and heart inflammation, and to report to their pediatrician anything they see in that first week after vaccination. But it is also important, the CDC notes, to recognize that even if this does turn out to be an extremely rare side effect of the vaccine, "most patients who received care responded well to medicine and rest and quickly felt better." And the serious risks of COVID -19 — even for young healthy people — outweigh the risks of any possible side effects from the vaccine. Here are some questions you may have, and what's known:

What exactly is myocarditis?

Myocarditis is an inflammation of the heart muscle, and pericarditis, also being investigated, is an inflammation of the sac around the heart.

Long before the pandemic, thousands of cases of myocarditis were diagnosed in the U.S. and around the world each year, often triggered by the body's immune response to infections. SARS-CoV-2 can trigger it, and so can cold viruses, and staph and strep and HIV. Other causes include toxins and allergies.

Symptoms include chest pain and shortness of breath. It's often mild enough to go unnoticed, but a full-blown case in adults can cause arrhythmias and heart failure that require careful treatment with multiple medications, and several months of strict rest. In a case study of seven teenagers who got myocarditis following vaccination published last week in the journal Pediatrics, all seven got better after routine treatment with anti-inflammatory drugs.

Pediatric cardiologist Dr. Stuart Berger of the Northwestern University Feinberg School of Medicine, a spokesperson for the American Academy of Pediatrics, says vaccine-related myocarditis in teens is not all that worrisome. "Although they appear with some symptoms of chest pain, and maybe some findings on EKGs, all of the cases we've seen have been on the mild end of the spectrum," he says.

So, what's the concern?

Several hundred reports about the inflammation have been filed with the federal government's Vaccine Adverse Event Reporting System (VAERS); that's a repository of reports sent in by health professionals and patients about any health events they spot in the hours or days after vaccinations. Many of the events reported turn out to be coincidental — not caused by a vaccine. The database is just meant as a starting point for further investigation and not proof of cause and effect. But as NPR's Geoff Brumfiel noted this week, "when millions of people are vaccinated within a short period, the total number of these reported events can look big."

That said, anecdotes reported by doctors in medical journals and reports to VAERS suggest that both of the mRNA vaccines authorized for use in the U.S. — the Pfizer and Moderna vaccines — might slightly increase the incidence of myocarditis in young people. In 2003, a report in the New England Journal of Medicine estimated the background incidence of myocarditis to be 1.13 cases in 100,000 children per year.

Paul Offit, professor of pediatrics at the Children's Hospital of Philadelphia and a member of a Food and Drug Administration vaccine advisory committee says there likely is a causal link between the heart inflammation some doctors are seeing in these teens and the second dose of vaccine. "I think it's real," he says, but hastens to add that the effect is exceedingly small – based on the data collected so far, maybe one in 50,000 vaccinees between the ages of 16 and 39. "And the good news is at least so far it looks to be transient and self-resolving."

Still, maybe I should wait to get my teen vaccinated and see how this plays out?

Uhm, no, according to several vaccine experts contacted by NPR. And this is where a little math comes in handy.

"Take a stadium full of 100,000 people between the ages of 16 and 39, which is the subset that appears to be at greater risk," Offit says. "Vaccinate all of them, and two might get myocarditis." But if you don't vaccinate any of the 100,000, he estimates that about 1,300 would eventually get COVID-19. And those numbers are likely to increase this winter.

About one in 1,000 children who get COVID-19 have gone on to develop a condition called MIS-C (multisystem inflammatory syndrome in children), says Offit, and most of those kids have had some level of myocarditis. In addition, the new coronavirus has directly caused myocarditis in some children and adults. Which of the two stadiums in Offit's metaphor would have more cases of myocarditis — the vaccinated children or unvaccinated kids — is not known precisely. But Offit says he suspects it would be the unvaccinated group. And there's no doubt that 1,000 unvaccinated children would suffer more COVID-19-related illnesses. "A choice not to get a vaccine is not a choice to avoid myocarditis," he says. "It's a choice to take a different risk — and I would argue a more serious one" — of developing a bad case of COVID-19 or long-COVID or COVID-caused myocarditis.

Are the experts advising their own kids in this age group to get vaccinated?

Yes. "I understand people having concerns," says Dr. Judith Guzman-Cottrill. She's a parent and professor of pediatric infectious diseases at the Oregon Health and Science University, as well as the senior author on a small study that came out this month in the journal Pediatrics. In the report, Guzman-Cottrill and her colleagues analyzed the cases of seven boys around the country who developed myocarditis within four days of receiving the Pfizer-BioNTech vaccine.

She and her family recently faced the vaccination decision for her own 13-year-old daughter — and said a whole-hearted yes to the shot.

Guzman-Cottrill suspects there may turn out to be a slightly increased risk of heart inflammation from vaccination in young people, but she and her co-authors note in the Pediatrics report that a direct cause-and-effect connection — even in these seven cases — has yet to be established. And she's impressed that despite the millions of doses that have so far been delivered to teens, no clear and serious post-vaccination problems have shown up. "The emergency departments and urgent care clinics are not filled with teenagers complaining of chest pain," she says.

She's treated unvaccinated teens who developed severe myocarditis from an infection with the COVID-19 virus, and others who developed COVID-19 pneumonia and respiratory failure. Seeing those teens struggle — teens who lacked the powerful immune protection the vaccine provides — was enough for her to suggest vaccination to her daughter, who got her second vaccination earlier this week.

"She saw it as a pathway back to a normal post pandemic life," Guzman-Cottrill says.

And that's where public health comes in. "We really need a highly vaccinated student body when kids return to the classroom this fall," says Guzman-Cottrill, "so we don't see surges in COVID-19 cases."

Joanne Silberner, a former health policy correspondent for NPR, is a freelance journalist living in Seattle.

This content is from Southern California Public Radio. View the original story at SCPR.org.

A waitress wears a face mask while serving at Langer's Delicatessen-Restaurant in Los Angeles on June 15.; Credit: Frederic J. Brown/AFP via Getty Images

Normal is not easily defined.

The past 15 months, though, have certainly been anything but.

Americans are starting to believe a "sense of normal" is approaching fairly soon, however, according to a new NPR/PBS NewsHour/Marist survey. The poll also found that with the coronavirus receding in this country, mask-wearing is declining and Americans are going out more. But they remain cautious about being in large crowds.

As the country continues to open up, more focus turns to the economy, which cratered during the beginning of the pandemic last year. And Americans are split by race, gender and politics on whether President Biden's ambitious policies are helping or not.

Race, gender, party divides on Biden and the economy

Three months ago, in a similar survey, 49% of adults said the president's policies were strengthening the economy, while 44% said they were weakening it.

Now, that's declined a net of 6 points, as 44% of respondents in the new poll say Biden's policies have strengthened the economy and 45% say the opposite. The percentage who were unsure also jumped 4 points. It's all a little bit of a warning sign for Biden, as he pushes for two large — and expensive — spending packages.

There are significant splits by race and gender:

• Just 39% of whites said Biden's policies have strengthened the economy, but 52% of people of color say they have.
• 54% of independent men say his policies have weakened the economy, while 56% of independent women say they've strengthened it. 
• 45% of white male college grads say Biden has strengthened the economy, but a significantly higher 64% of white women with college degrees said so.

Inflation vs. wages by party

A quarter of Americans rank inflation as the U.S. economy's top concern. That's followed by wages, unemployment, housing costs, labor shortages, gas prices and interest rates.

But there's a sharp political divide on the question. Republicans and independents rank inflation as their top concern, while for Democrats, it was wages. Just 4% of Republicans said wages were their top concern.

Return to "normal"

Americans are growing increasingly optimistic about when life will return to a "sense of normal," as the survey labels it.

In April, three-quarters of Americans said they believe it will take six months or more. Now, it's just half. About a quarter (27%) say it will be less than six months, up from 15% two months ago.

People are also growing more comfortable doing certain things, saying they're:

• dining out at restaurants (78%) and 
• visiting unvaccinated friends and family (75%).

But they are not as comfortable doing others:

• almost 7-in-10 are not going out to bars; 
• about two-thirds are not attending live concerts or sporting events (65%);
• and a majority have also not resumed going to in-person religious services (54%).

COVID-19 vaccines and going back to work

While half say they are concerned about another coronavirus surge, almost 9-in-10 U.S. adults with jobs say they are at least somewhat comfortable returning to work.

Notably, a majority (57%) of those with jobs do not believe employers should require COVID-19 vaccines as a condition to return to in-person work.

More than a quarter of Americans say they will not get vaccinated. The most resistant to getting vaccinated continue to be supporters of former President Donald Trump. Half of them say they won't get the shot, the highest of any group surveyed. Trump has touted the vaccine and got it himself.

Since Centers for Disease Control and Prevention guidelines came out, noting that Americans who have been vaccinated can largely set masks aside, there's been a double-digit decline in those saying they wear a mask even when it's not required.

There's also been a double-digit increase in those saying they generally do not wear a mask. In May, 49% said they wore masks even when it was not required. Now, that's just 36%.

One-in-five said they generally do not wear masks. Two months ago, it was less than one-in-10.

Affordability, not coronavirus, limiting vacations

Speaking of getting back to normal, a majority of Americans say they plan to take a vacation this summer.

But of the significant minority (45%) who say they aren't taking one, almost three times as many cited affordability (35%) as the main reason for not going, as opposed to concerns about COVID-19 (12%).

Methodology: The poll of 1,115 U.S. adults was conducted using live telephone interviewers from June 22 through June 29. Survey questions were available in English or Spanish. The full sample has a margin of error of plus or minus 3.7 percentage points, with larger margins of error for smaller group subsets.

This content is from Southern California Public Radio. View the original story at SCPR.org.

The permit center is in the process of adding QR Codes to the permit hard card.  The following is an explanation about how the code works from Steve Lackey.   By Steve Lackey Along with the use of smartphones and other related devices, QR Codes are becoming quite popular and useful.  Called “Quick Response Codes”, they store [...]

; Credit: Asa Mathat/TED / Asa Mathat

Part 4 of TED Radio Hour episode An SOS From The Ocean

Legendary oceanographer Sylvia Earle has been exploring and working to protect our oceans for more than half a century. Her message has stayed the same: we're taking our oceans for granted.

About Sylvia Earle

Sylvia Earle is an oceanographer, explorer, and author. She is the president of Mission Blue, an organization that aims to establish marine protected areas around the world. She is also a National Geographic Explorer.

Earle has led more than 50 expeditions and clocked more than 7,000 hours underwater. She was captain of the first all-female team to live underwater in 1970--one of many extended underwater stays. In 1979, she walked untethered on the sea floor at a lower depth than any other woman before or since. In the 1980s, she started the companies Deep Ocean Engineering and Deep Ocean Technologies with engineer Graham Hawkes to design undersea vehicles that allow scientists to work at previously inaccessible depths. In the early 1990s, she served as Chief Scientist of the National Oceanographic and Atmospheric Administration. In 2009, she became the recipient of the million dollar TED Prize to continue her work to protect oceans.

Earle received an associate degree from St. Petersburg Jr. College, has a Bachelor of Science and Master of Science degree from Florida State University, and a Doctorate of Psychology from Duke University.

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