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Valleytronic as a hot topic in recent years focuses on electrons' valley degree of freedom as a quantum information carrier. Here, by combining two-bandk.pmodel with high-throughput density functional theory (DFT) calculations, the valley states of Janus 2H-VSSe monolayer are studied which have spontaneous polarization. Nonvolatile valley polarization state is mainly arises from intrinsic ferromagnetism contributed by V-3d electronic configuration and not the spontaneous out-of-plane dipole moment of VSSe monolayer. The effective Hamiltonian model and DFT calculations both showed that the valley splitting mainly originates from the smaller spin splitting coming from the spin-orbit coupling effect rather than the spin splitting of magnetic exchange field. By using the effective Dirac Hamiltonian and Kubo formula, we further calculated the longitudinal and transversal conductivities and absorption spectra of VSSe monolayer which exhibits an anomalous valley Hall effect and clear valley-selective circular dichroism. Our calculations indicate that the modification of valley and spin splitting related to Berry curvature by applying an external strain is more noticeable than by the change of the magnetic moment orientation and electric field. We found that carriers accumulation with particular spin and valley label can be manipulated by tuning effective Hamiltonian parameters. The coexistence of robust in-plane magnetic ordering and spontaneous valley polarization of 2H-VSSe monolayer supports the possibility of applications in spintronics, valleytronics and optoelectronics devices.
RESUMEN
BACKGROUND: Although several studies have documented an undersupply of dermatologic services in the United States, little is known about the dermatopathology workforce. OBJECTIVE: Objectives included the following: (1) describe the dermatopathology workforce in the United States; (2) identify characteristics associated with academic dermatopathologists; and (3) explore issues surrounding dermatopathology training. METHODS: We conducted a cross-sectional survey of all Fellows of the American Society of Dermatopathology (ASDP) practicing in the United States and its territories. RESULTS: Of 913 ASDP Fellows, 437 (48%) returned a completed questionnaire. Most were male (72%), Caucasian (85%), and had graduated from US/Canadian medical schools (88%). Approximately half (49%) had completed a dermatology residency and a quarter (24%) were in academia. As compared with those in private practice, academic dermatopathologists were more likely to be female (P = .0028), have a medical degree only (P = .0197), and earn $300,000 or less annually (P < .0001). No associations were identified for practice type with either location of medical school (United States/Canada vs other) or year of fellowship graduation (≤1996 vs ≥1997). Although most respondents were satisfied overall with their training, the most common areas identified as inadequate included: coding/billing (47%), biostatistics (38%), pediatric clinical dermatology (27%), and electron microscopy (27%). LIMITATIONS: Moderate response rate and potential recall bias are limitations. CONCLUSIONS: This study of the US dermatopathology workforce provides benchmarks for future studies and strategies for workforce planning.
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Dermatología , Patología , Adulto , Estudios Transversales , Femenino , Humanos , Masculino , Persona de Mediana Edad , Estados Unidos , Recursos HumanosRESUMEN
Supported molybdic acid on nano-Fe3O4@TiO2 (Fe3O4@TiO2@(CH2)3OMoO3H) has been successfully prepared, char-acterized and applied as a catalyst for the synthesis of sulfonamide containing coumarin moieties. The prepared Fe3O4nanoparticles by coprecipitation of Fe2+ and Fe3+ ions were treated with tetraethyl orthotitanate to obtain Fe3O4@TiO2. By anchoring 3-chloropropyltriethoxysilan on Fe3O4@TiO2 followed by reacting with molybdic acid, the desired catalyst was produced. The synthesized catalyst was characterized using XRD, SEM, EDS, FT-IR and VSM analysis. Fe3O4@TiO2@(CH2)3OMoO3H was used as a catalyst for the synthesis of sulfonamide containing coumarin moieties via a three-com-ponent reaction of aryl aldehydes, para-toluenesulfonamide and 4-hydroxycoumarin or 5,7-dihydroxy-4-methylcou-marin. The catalyst recovery test showed the catalyst is highly reusable without losing its activity.
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Cumarinas/síntesis química , Nanopartículas de Magnetita/química , Sulfonamidas/síntesis química , Catálisis , Fenómenos Magnéticos , Molibdeno/química , Titanio/químicaRESUMEN
Anthrax lethal toxin is the major cause of death in systemic anthrax. Lethal toxin consists of two proteins: protective antigen and LF (lethal factor). Protective antigen binds to a cell-surface receptor and transports LF into the cytosol. LF is a metalloprotease that targets MKKs [MAPK (mitogen-activated protein kinase) kinases]/MEKs [MAPK/ERK (extracellular-signal-regulated kinase) kinases], cleaving them to remove a small N-terminal stretch but leaving the bulk of the protein, including the protein kinase domain, intact. LF-mediated cleavage of MEK1 and MKK6 has been shown to inhibit signalling through their cognate MAPK pathways. However, the precise mechanism by which this proteolytic cleavage inhibits signal transmission has been unclear. Here we show that the C-terminal LF-cleavage products of MEK1, MEK2, MKK3, MKK4, MKK6 and MKK7 are impaired in their ability to bind to their MAPK substrates, suggesting a common mechanism for the LF-induced inhibition of signalling.
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Antígenos Bacterianos , Toxinas Bacterianas/metabolismo , MAP Quinasa Quinasa 4 , Quinasas de Proteína Quinasa Activadas por Mitógenos/metabolismo , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Secuencia de Aminoácidos , Animales , Toxinas Bacterianas/farmacología , Sitios de Unión , Proteínas Quinasas Dependientes de Calcio-Calmodulina/metabolismo , Humanos , Proteínas Quinasas JNK Activadas por Mitógenos , MAP Quinasa Quinasa 1 , MAP Quinasa Quinasa 2 , MAP Quinasa Quinasa 3 , MAP Quinasa Quinasa 6 , MAP Quinasa Quinasa 7 , Sistema de Señalización de MAP Quinasas/efectos de los fármacos , Proteína Quinasa 1 Activada por Mitógenos/metabolismo , Proteína Quinasa 3 Activada por Mitógenos , Quinasas de Proteína Quinasa Activadas por Mitógenos/química , Datos de Secuencia Molecular , Proteínas Tirosina Quinasas/metabolismo , Ratas , Alineación de Secuencia , Proteínas Quinasas p38 Activadas por MitógenosRESUMEN
BACKGROUND: The current trend of heart transplantation in recent years has taken a quantum leap forward. We decided to look back at our experience in this center. OBJECTIVES: Here, we focus on the diagnostic pitfalls and challenges in these biopsies. PATIENTS AND METHODS: Forty two patients based on the standard protocol of heart transplantation group, yielded 63 biopsy samples over a period of 33 months (April 2010 - December 2012). The mean age was 30.4 years (ranging from 16 to 58 years) with 51 males (81%) and 12 females (19%). All the patients were examined periodically and biopsy samples were taken from the right ventricular wall. RESULTS: Rarely fewer than three pieces of myocardial samples were procured. Scar, adipose tissues and blood clots may be seen instead. Quilty effect (nodular endocardial lesions composed of inflammatory cell infiltrates) was seen in 8 cases (12.7%). Other findings not directly related to rejection including early ischemic injury, Quilty effect and post-transplant lymphoproliferative disorders (PTLD) were not encountered. CONCLUSIONS: Specimen inadequacy was not a major problem in our center. It poses a great limitation, because suboptimal specimens sometimes mislead the pathologist. Other findings especially Quilty effect were within the range defined for this finding.
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In this report, a case of blue toe syndrome related to persistent sciatic artery pseudoaneurysm in a 63-year-old woman, which was diagnosed by selective angiography, is presented. The pseudoaneurysm was successfully treated with coil embolization with good clinical results. A persistent sciatic artery is a rare embryological anomaly that occurs when the sciatic artery fails to regress during fetal development. Therefore, thromboembolisms from persistent sciatic artery aneurysm are rare.
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Mitogen-activated protein kinase (MAPK) cascades control gene expression patterns in response to extracellular stimuli. MAPK/ERK (extracellular-signal-regulated kinase) kinases (MEKs) activate MAPKs by phosphorylating them; activated MAPKs, in turn, phosphorylate target transcription factors, and are deactivated by phosphatases. One mechanism for maintaining signal specificity and efficiency is the interaction of MAPKs with their substrates and regulators through high-affinity docking sites. In the present study, we show that peptides corresponding to the MAPK-docking sites of MEK1, MEK2, Ste7, Elk-1 and MAPK phosphatase (MKP)-2 potently inhibit MEK2 phosphorylation of ERK2, ERK2 phosphorylation of Elk-1, and MKP-1 dephosphorylation of ERK2. Each peptide inhibited multiple reactions; for example, the MEK2 peptide inhibited not only MEK2, but also ERK2 and MKP-1. In addition, these docking-site peptides inhibited MEK2-ERK2 binding. The MAPK-docking site of MEK1 also potently stimulated ERK2-mediated phosphorylation of a target site on the same peptide. Control peptides with mutations of conserved basic and hydrophobic residues of the MAPK-docking site consensus lacked biological activity. We conclude that MEKs, MKPs and the Elk-1 transcription factor compete for binding to the same region of ERK2 via protein-protein interactions that are crucial for kinase/phosphatase activity.
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Sistema de Señalización de MAP Quinasas/fisiología , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Proteínas Tirosina Fosfatasas/metabolismo , Factores de Transcripción/metabolismo , Secuencia de Aminoácidos , Sitios de Unión , Proteínas de Unión al ADN/genética , Proteínas de Unión al ADN/metabolismo , Fosfatasa 1 de Especificidad Dual , MAP Quinasa Quinasa 1 , MAP Quinasa Quinasa 2 , Proteína Quinasa 1 Activada por Mitógenos/genética , Proteína Quinasa 1 Activada por Mitógenos/metabolismo , Quinasas de Proteína Quinasa Activadas por Mitógenos/genética , Quinasas de Proteína Quinasa Activadas por Mitógenos/metabolismo , Proteínas Quinasas Activadas por Mitógenos/genética , Datos de Secuencia Molecular , Péptidos/genética , Péptidos/metabolismo , Fosforilación , Unión Proteica , Proteínas Quinasas/genética , Proteínas Quinasas/metabolismo , Proteína Fosfatasa 1 , Proteínas Serina-Treonina Quinasas/genética , Proteínas Serina-Treonina Quinasas/metabolismo , Proteínas Tirosina Fosfatasas/genética , Proteínas Tirosina Quinasas/genética , Proteínas Tirosina Quinasas/metabolismo , Proteínas Recombinantes de Fusión/metabolismo , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo , Alineación de Secuencia , Factores de Transcripción/genéticaRESUMEN
Specific docking interactions between MAPKs and their activating MAPK kinases (MKKs or MEKs) are crucial for efficient and accurate signal transmission. Here, we report the identification of a MAPK-docking site, or "D-site," in the N terminus of human MKK4/JNKK1. This docking site conforms to the consensus sequence for known D-sites in other MKKs and contains the first of the two cleavage sites for anthrax lethal factor protease that have been found in the N terminus of MKK4. This docking site was both necessary and sufficient for the high affinity binding of the MAPKs JNK1, JNK2, JNK3, p38 alpha, and p38 beta to MKK4. Mutations that altered conserved residues in this docking site reduced JNK/p38 binding. In addition, a peptide version of this docking site, as well as a peptide version of the JNK-binding site of the JIP-1 scaffold protein, inhibited both MKK4/JNK binding and MKK4-mediated phosphorylation of JNK1. These same peptides also inhibited JNK2-mediated phosphorylation of c-Jun and ATF2, suggesting that transcription factors, MKK4, and the JIP scaffold compete for docking to JNK. Finally, the selectivity of the MKK4, MEK1, and MEK2 D-sites for JNK versus ERK was quantified. The MEK1 and MEK2 D-sites displayed a strong selectivity for their cognate MAPK (ERK2) versus a non-cognate MAPK (JNK). In contrast, the MKK4 D-site exhibited only limited selectivity for JNK versus ERK.