14 research outputs found
Orbital-weight redistribution triggered by spin order in the pnictides
The one-particle spectral function and its orbital composition are
investigated in a three-orbital model for the undoped parent compounds of the
iron-based superconductors. In the realistic parameter regime, where results
best fit experimental data, it is observed that the magnetization in the xz and
yz orbitals are markedly different and the Fermi surface presents mostly xz
character, as recently observed in photoemission experiments [T. Shimojima et
al., Phys. Rev. Lett. 104, 057002 (2010)]. Since the ferro-orbital order in
this regime is at most a few percent, these results are mainly driven by the
magnetic order. An analogous analysis for a five-orbital model leads to similar
conclusions.Comment: published versio
Distinguishing and electron pairing symmetries by neutron spin resonance in superconducting NaFeCoAs
A determination of the superconducting (SC) electron pairing symmetry forms
the basis for establishing a microscopic mechansim for superconductivity. For
iron pnictide superconductors, the -pairing symmetry theory predicts the
presence of a sharp neutron spin resonance at an energy below the sum of hole
and electron SC gap energies () below . On the other hand,
the -pairing symmetry expects a broad spin excitation enhancement at an
energy above below . Although the resonance has been observed in
iron pnictide superconductors at an energy below consistent with the
-pairing symmetry, the mode has also be interpreted as arising from the
-pairing symmetry with due to its broad energy width and
the large uncertainty in determining the SC gaps. Here we use inelastic neutron
scattering to reveal a sharp resonance at E=7 meV in SC
NaFeCoAs ( K). On warming towards , the mode
energy hardly softens while its energy width increases rapidly. By comparing
with calculated spin-excitations spectra within the and
-pairing symmetries, we conclude that the ground-state resonance in
NaFeCoAs is only consistent with the -pairing, and
is inconsistent with the -pairing symmetry.Comment: 9 pages, 8 figures. submitted to PR
JMJD1C Regulates Megakaryopoiesis in In Vitro Models through the Actin Network
The histone demethylase JMJD1C is associated with human platelet counts. The JMJD1C knockout in zebrafish and mice leads to the ablation of megakaryocyte–erythroid lineage anemia. However, the specific expression, function, and mechanism of JMJD1C in megakaryopoiesis remain unknown. Here, we used cell line models, cord blood cells, and thrombocytopenia samples, to detect the JMJD1C expression. ShRNA of JMJD1C and a specific peptide agonist of JMJD1C, SAH-JZ3, were used to explore the JMJD1C function in the cell line models. The actin ratio in megakaryopoiesis for the JMJDC modulation was also measured. Mass spectrometry was used to identify the JMJD1C-interacting proteins. We first show the JMJD1C expression difference in the PMA-induced cell line models, the thrombopoietin (TPO)-induced megakaryocyte differentiation of the cord blood cells, and also the thrombocytopenia patients, compared to the normal controls. The ShRNA of JMJD1C and SAH-JZ3 showed different effects, which were consistent with the expression of JMJD1C in the cell line models. The effort to find the underlying mechanism of JMJD1C in megakaryopoiesis, led to the discovery that SAH-JZ3 decreases F-actin in K562 cells and increases F-actin in MEG-01 cells. We further performed mass spectrometry to identify the potential JMJD1C-interacting proteins and found that the important Ran GTPase interacts with JMJD1C. To sum up, JMJD1C probably regulates megakaryopoiesis by influencing the actin network