Fock space representations of quantum affine algebras and generalized Lascoux-Leclerc-Thibon algorithm

We construct the Fock space representations of classical quantum affine algebras using combinatorics of Young walls. We also show that the crystal graphs of the Fock space representations can be realized as the abstract crystal consisting of proper Young walls. Finally, we give a generalized version of Lascoux-Leclerc-Thibon algorithm for computing the global bases of the basic representations of classical quantum affine algebras.Comment: 70 page

Evolutionary Conserved Motif Finder (ECMFinder) for genome-wide identification of clustered YY1- and CTCF-binding sites

We have developed a new bioinformatics approach called ECMFinder (Evolutionary Conserved Motif Finder). This program searches for a given DNA motif within the entire genome of one species and uses the gene association information of a potential transcription factor-binding site (TFBS) to screen the homologous regions of a second and third species. If multiple species have this potential TFBS in homologous positions, this program recognizes the identified TFBS as an evolutionary conserved motif (ECM). This program outputs a list of ECMs, which can be uploaded as a Custom Track in the UCSC genome browser and can be visualized along with other available data. The feasibility of this approach was tested by searching the genomes of three mammals (human, mouse and cow) with the DNA-binding motifs of YY1 and CTCF. This program successfully identified many clustered YY1- and CTCF-binding sites that are conserved among these species but were previously undetected. In particular, this program identified CTCF-binding sites that are located close to the Dlk1, Magel2 and Cdkn1c imprinted genes. Individual ChIP experiments confirmed the in vivo binding of the YY1 and CTCF proteins to most of these newly discovered binding sites, demonstrating the feasibility and usefulness of ECMFinder

Growth of ultra-uniform graphene using a Ni/W bilayer metal catalyst

We investigated a bilayer catalyst system consisting of polycrystalline Ni and W films for growing mono-layer graphene over large areas. Highly uniform graphene was grown on Ni/W bilayer film with 100% coverage. The graphene grown on Ni/W bilayer film and transferred onto an insulating substrate exhibited average hole and electron mobilities of 727 and 340 cm(2)V(-1)s(-1), respectively. A probable growth mechanism is proposed based on X-ray diffractometry and transmission electron microscopy, which suggests that the reaction between diffused carbon and tungsten atoms results in formation of tungsten carbides. This reaction allows the control of carbon precipitation and prevents the growth of non-uniform multilayer graphene on the Ni surface; this has not been straightforwardly achieved before. These results could be of importance in better understanding mono-layer graphene growth, and suggest a facile fabrication route for electronic applications. (C) 2015 AIP Publishing LLCopen0

Purification and proteomic identification of putative upstream regulators of polo-like kinase-1 from mitotic cell extracts

AbstractPolo-like kinase-1 (Plk1) is phosphorylated on Thr210 for activation during mitosis. Here, we investigated the question of which kinase(s) is the specific upstream kinase of mitotic Plk1. Upstream kinases of Plk1 were purified from mitotic cell extracts through column chromatography procedures, and identified by mass spectrometry. Candidates for Plk1 kinase included p21-activated kinase, aurora A, and mammalian Ste20-like kinases. Immunoprecipitates of these proteins from mitotic cell extracts phosphorylated Plk1 on Thr210. Even if the activity of Aurora A was blocked with a specific inhibitor, Plk1 phosphorylation still occurred, suggesting that function of Plk1 could be controlled by these kinases for proper mitotic progression, as well as by Aurora A in very late G2 phase for the beginning of mitosis.Structured abstractMINT-7996332: PAK1(uniprotkb:Q13153)physically interacts(MI:0915) withPLK1(uniprotkb:P53350) bypull down(MI:0096)MINT-7996345: PAK3(uniprotkb:O75914)physically interacts(MI:0915) withPLK1(uniprotkb:P53350) bypull down(MI:0096