4,301 research outputs found

    Is the exotic X(5568)X(5568) a bound state?

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    Stimulated by the recent observation of the exotic X(5568)X(5568) state by D0 Collaboration, we study the four-quark system usbˉdˉus\bar{b}\bar{d} with quantum numbers JP=0+J^P=0^+ in the framework of chiral quark model. Two structures, diquark-antidiquark and meson-meson, with all possible color configurations are investigated by using Gaussian expansion method. The results show that energies of the tetraquark states with diquark-antiquark structure are too high to the candidate of X(5568)X(5568), and no molecular structure can be formed in our calculations. The calculation is also extended to the four-quark system uscˉdˉus\bar{c}\bar{d} and the same results as that of usbˉdˉus\bar{b}\bar{d} are obtained.Comment: 5 pages, 1 figur

    Analysis of hidden-bottom bb\bar{b}\bar{b} states

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    Motivated by the searching for bbbˉbˉbb\bar{b}\bar{b} states at LHC recently, we calculate the ground-state energies of bbbˉbˉbb\bar{b}\bar{b} states with quantum numbers IJP=00+,01+,02+IJ^P=00^+,01^+,02^+ in a nonrelativistic chiral quark model using the Gaussian expansion method. In our calculations, two structures, meson-meson and diquark-antidiquark, and their coupling, along with all possible color configurations are considered. It is expected that the studies shall be helpful for the experimental searching of fully-heavy exotic tetraquark states.Comment: 7 pages, 1 figur

    Light-meson masses in an unquenched quark model

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    We perform a coupled-channels calculation of the masses of light mesons with the quantum numbers IJP=IJ^{P=-}, (I,J)=0,1(I,J)=0,1, by including qqˉq\bar{q} and (qqˉ)2(q\bar{q})^2 components in a nonrelativistic chiral quark model. The coupling between two- and four-quark configurations is realized through a 3P0^3P_0 quark-pair creation model. With the usual form of this operator, the mass shifts are large and negative, an outcome which raises serious issues of validity for the quenched quark model. Herein, therefore, we introduce some improvements of the 3P0^3P_0 operator in order to reduce the size of the mass shifts. By introducing two simple factors, physically well motivated, the coupling between qqˉq\bar{q} and (qqˉ)2(q\bar{q})^2 components is weakened, producing mass shifts that are around 10-20% of hadron bare masses.Comment: 10 pages, 1 figure, 7 table

    Star-factors of tournaments

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    Let S_m denote the m-vertex simple digraph formed by m-1 edges with a common tail. Let f(m) denote the minimum n such that every n-vertex tournament has a spanning subgraph consisting of n/m disjoint copies of S_m. We prove that m lg m - m lg lg m <= f(m) <= 4m^2 - 6m for sufficiently large m.Comment: 5 pages, 1 figur

    Mga Modulates Bmpr1a Activity by Antagonizing Bs69 in Zebrafish

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    MAX giant associated protein (MGA) is a dual transcriptional factor containing both T-box and bHLHzip DNA binding domains. In vitro studies have shown that MGA functions as a transcriptional repressor or activator to regulate transcription of promotors containing either E-box or T-box binding sites. BS69 (ZMYND11), a multidomain-containing (i.e., PHD, BROMO, PWWP, and MYND) protein, has been shown to selectively recognizes histone variant H3.3 lysine 36 trimethylation (H3.3K36me3), modulates RNA Polymerase II elongation, and functions as RNA splicing regulator. Mutations in MGA or BS69 have been linked to multiple cancers or neural developmental disorders. Here, by TALEN and CRISPR/Cas9-mediated loss of gene function assays, we show that zebrafish Mga and Bs69 are required to maintain proper Bmp signaling during early embryogenesis. We found that Mga protein localized in the cytoplasm modulates Bmpr1a activity by physical association with Zmynd11/Bs69. The Mynd domain of Bs69 specifically binds the kinase domain of Bmpr1a and interferes with its phosphorylation and activation of Smad1/5/8. Mga acts to antagonize Bs69 and facilitate the Bmp signaling pathway by disrupting the Bs69-Bmpr1a association. Functionally, Bmp signaling under control of Mga and Bs69 is required for properly specifying the ventral tailfin cell fate.</p
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