Meditation-induced near-death experiences: a 3-year longitudinal study

Near-death experiences (NDEs) are life transformational events that are increasingly being subjected to empirical research. However, to date, no study has investigated the phenomenon of a meditation-induced near-death experience (MI-NDE) that is referred to in ancient Buddhist texts. Given that some advanced Buddhist meditators can induce NDEs at a pre-planned point in time, the MI-NDE may make NDEs more empirically accessible and thus advance understanding into the psychology of death-related processes. The present study recruited 12 advanced Buddhist meditators and compared the MI-NDE against two other meditation practices (i.e. that acted as control conditions) in the same participant group. Changes in the content and profundity of the MI-NDE were assessed longitudinally over a 3-year period. Findings demonstrated that compared to the control conditions, the MI-NDE prompted significantly greater pre-post increases in NDE profundity, mystical experiences and non-attachment. Furthermore, participants demonstrated significant increases in NDE profundity across the 3-year study period. Findings from an embedded qualitative analysis (using grounded theory) demonstrated that participants (i) were consciously aware of experiencing NDEs, (ii) retained volitional control over the content and duration of NDEs and (iii) elicited a rich array of non-worldly encounters and spiritual experiences. In addition to providing corroborating evidence in terms of the content of a “regular” (i.e. non-meditation-induced) NDE, novel NDE features identified in the present study indicate that there exist unexplored and/or poorly understood dimensions to NDEs. Furthermore, the study indicates that it would be feasible - including ethically feasible - for future research to recruit advanced meditators in order to assess real-time changes in neurological activity during NDEs

Instability of the rhodium magnetic moment as origin of the metamagnetic phase transition in alpha-FeRh

Based on ab initio total energy calculations we show that two magnetic states of rhodium atoms together with competing ferromagnetic and antiferromagnetic exchange interactions are responsible for a temperature induced metamagnetic phase transition, which experimentally is observed for stoichiometric alpha-FeRh. A first-principle spin-based model allows to reproduce this first-order metamagnetic transition by means of Monte Carlo simulations. Further inclusion of spacial variation of exchange parameters leads to a realistic description of the experimental magneto-volume effects in alpha-FeRh.Comment: 10 pages, 13 figures, accepted for publication in Phys. Rev.

Repetitive N-WASP–Binding Elements of the Enterohemorrhagic Escherichia coli Effector EspFU Synergistically Activate Actin Assembly

Enterohemorrhagic Escherichia coli (EHEC) generate F-actin–rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along with EspFU, a protein that associates indirectly with Tir and contains multiple peptide repeats that stimulate actin polymerization. In vitro, the EspFU repeat region is capable of binding and activating recombinant derivatives of N-WASP, a host actin nucleation-promoting factor. In spite of the identification of these important bacterial and host factors, the underlying mechanisms of how EHEC so potently exploits the native actin assembly machinery have not been clearly defined. Here we show that Tir and EspFU are sufficient for actin pedestal formation in cultured cells. Experimental clustering of Tir-EspFU fusion proteins indicates that the central role of the cytoplasmic portion of Tir is to promote clustering of the repeat region of EspFU. Whereas clustering of a single EspFU repeat is sufficient to bind N-WASP and generate pedestals on cultured cells, multi-repeat EspFU derivatives promote actin assembly more efficiently. Moreover, the EspFU repeats activate a protein complex containing N-WASP and the actin-binding protein WIP in a synergistic fashion in vitro, further suggesting that the repeats cooperate to stimulate actin polymerization in vivo. One explanation for repeat synergy is that simultaneous engagement of multiple N-WASP molecules can enhance its ability to interact with the actin nucleating Arp2/3 complex. These findings define the minimal set of bacterial effectors required for pedestal formation and the elements within those effectors that contribute to actin assembly via N-WASP-Arp2/3–mediated signaling pathways

Emergence of qualia from brain activity or from an interaction of proto-consciousness with the brain: which one is the weirder? Available evidence and a research agenda

This contribution to the science of consciousness aims at comparing how two different theories can explain the emergence of different qualia experiences, meta-awareness, meta-cognition, the placebo effect, out-of-body experiences, cognitive therapy and meditation-induced brain changes, etc. The first theory postulates that qualia experiences derive from specific neural patterns, the second one, that qualia experiences derive from the interaction of a proto-consciousness with the brain\u2019s neural activity. From this comparison it will be possible to judge which one seems to better explain the different qualia experiences and to offer a more promising research agenda

Repetitive N-WASP–Binding Elements of the Enterohemorrhagic Escherichia coli Effector EspFU Synergistically Activate Actin Assembly

Enterohemorrhagic Escherichia coli (EHEC) generate F-actin–rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along with EspFU, a protein that associates indirectly with Tir and contains multiple peptide repeats that stimulate actin polymerization. In vitro, the EspFU repeat region is capable of binding and activating recombinant derivatives of N-WASP, a host actin nucleation-promoting factor. In spite of the identification of these important bacterial and host factors, the underlying mechanisms of how EHEC so potently exploits the native actin assembly machinery have not been clearly defined. Here we show that Tir and EspFU are sufficient for actin pedestal formation in cultured cells. Experimental clustering of Tir-EspFU fusion proteins indicates that the central role of the cytoplasmic portion of Tir is to promote clustering of the repeat region of EspFU. Whereas clustering of a single EspFU repeat is sufficient to bind N-WASP and generate pedestals on cultured cells, multi-repeat EspFU derivatives promote actin assembly more efficiently. Moreover, the EspFU repeats activate a protein complex containing N-WASP and the actin-binding protein WIP in a synergistic fashion in vitro, further suggesting that the repeats cooperate to stimulate actin polymerization in vivo. One explanation for repeat synergy is that simultaneous engagement of multiple N-WASP molecules can enhance its ability to interact with the actin nucleating Arp2/3 complex. These findings define the minimal set of bacterial effectors required for pedestal formation and the elements within those effectors that contribute to actin assembly via N-WASP-Arp2/3–mediated signaling pathways

Enterohemorrhagic E. coli Requires N-WASP for Efficient Type III Translocation but Not for EspFU-Mediated Actin Pedestal Formation

Upon infection of mammalian cells, enterohemorrhagic E. coli (EHEC) O157:H7 utilizes a type III secretion system to translocate the effectors Tir and EspFU (aka TccP) that trigger the formation of F-actin-rich ‘pedestals’ beneath bound bacteria. EspFU is localized to the plasma membrane by Tir and binds the nucleation-promoting factor N-WASP, which in turn activates the Arp2/3 actin assembly complex. Although N-WASP has been shown to be required for EHEC pedestal formation, the precise steps in the process that it influences have not been determined. We found that N-WASP and actin assembly promote EHEC-mediated translocation of Tir and EspFU into mammalian host cells. When we utilized the related pathogen enteropathogenic E. coli to enhance type III translocation of EHEC Tir and EspFU, we found surprisingly that actin pedestals were generated on N-WASP-deficient cells. Similar to pedestal formation on wild type cells, Tir and EspFU were the only bacterial effectors required for pedestal formation, and the EspFU sequences required to interact with N-WASP were found to also be essential to stimulate this alternate actin assembly pathway. In the absence of N-WASP, the Arp2/3 complex was both recruited to sites of bacterial attachment and required for actin assembly. Our results indicate that actin assembly facilitates type III translocation, and reveal that EspFU, presumably by recruiting an alternate host factor that can signal to the Arp2/3 complex, exhibits remarkable versatility in its strategies for stimulating actin polymerization

Hydra Mesoglea Proteome Identifies Thrombospondin as a Conserved Component Active in Head Organizer Restriction

Thrombospondins (TSPs) are multidomain glycoproteins with complex matricellular functions in tissue homeostasis and remodeling. We describe a novel role of TSP as a Wnt signaling target in the basal eumetazoan Hydra. Proteome analysis identified Hydra magnipapillata TSP (HmTSP) as a major component of the cnidarian mesoglea. In general, the domain organization of cnidarian TSPs is related to the pentameric TSPs of bilaterians, and in phylogenetic analyses cnidarian TSPs formed a separate clade of high sequence diversity. HmTSP expression in polyps was restricted to the hypostomal tip and tentacle bases that harbor Wnt-regulated organizer tissues. In the hypostome, HmTSP- and Wnt3-expressing cells were identical or in close vicinity to each other, and regions of ectopic tentacle formation induced by pharmacological β-Catenin activation (Alsterpaullone) corresponded to foci of HmTSP expression. Chromatin immunoprecipitation (ChIP) confirmed binding of Hydra TCF to conserved elements in the HmTSP promotor region. Accordingly, β-Catenin knockdown by siRNAs reduced normal HmTSP expression at the head organizer. In contrast, knockdown of HmTSP expression led to increased numbers of ectopic organizers in Alsterpaullone-treated animals, indicating a negative regulatory function. Our data suggest an unexpected role for HmTSP as a feedback inhibitor of Wnt signaling during Hydra body axis patterning and maintenance

Exploring the anomaly in the interaction cross section and matter radius of 23O

New measurements of the interaction cross sections of 22,23O at 900A MeV performed at the GSI, Darmstadt are reported that address the unsolved puzzle of the large cross section previously observed for 23O. The matter radii for these oxygen isotopes extracted through a Glauber model analysis are in good agreement with the new predictions of the ab initio coupled-cluster theory reported here. They are consistent with a 22O+neutron description of 23O as well.Comment: 4 pages, 3 figure

First investigation on the isomeric ratio in multinucleon transfer reactions: Entrance channel effects on the spin distribution

The multinucleon transfer (MNT) reaction approach was successfully employed for the first time to measure the isomeric ratios (IRs) of $^{211}$Po (25/2$^+$) isomer and its (9/2$^+$) ground state at the IGISOL facility using a 945 MeV $^{136}$Xe beam impinged on $^{209}$Bi and $^{\rm nat}$Pb targets. The dominant production of isomers compared to the corresponding ground states was consistently revealed in the $\alpha$-decay spectra. Deduced IR of $^{211}$Po populated through the $^{136}$Xe+$^{\rm nat}$Pb reaction was found to enhance $\approx$1.8-times than observed for $^{136}$Xe+$^{209}$Bi. State-of-the-art Langevin-type model calculations have been utilized to estimate the spin distribution of an MNT residue. The computations qualitatively corroborate with the considerable increase in IRs of $^{211}$Po produced from $^{136}$Xe+$^{\rm nat}$Pb compared to $^{136}$Xe+$^{209}$Bi. Theoretical investigations indicate a weak influence of target spin on IRs. The enhancement of the $^{211}$Po isomer in the $^{136}$Xe+$^{\rm nat}$Pb over $^{136}$Xe+$^{209}$Bi can be attributed to the different proton ($p$)-transfer production routes. Estimations demonstrate an increment in the angular momentum transfer, favorable for isomer production, with increasing projectile energy. Comparative analysis indicates the two entrance channel parameters, projectile mass and $p$-transfer channels, strongly influencing the population of the high-spin isomer of $^{211}$Po (25/2$^+$). This is the first experimental and theoretical investigation on the IRs of nuclei produced via different channels of MNT reactions, with the latter quantitatively underestimating the former by a factor of two.Comment: 5 figure