Kyungpook National University

About: Kyungpook National University is a education organization based out in Daegu, South Korea. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 20497 authors who have published 42107 publications receiving 834608 citations.

Observation of electroweak production of same-sign W boson pairs in the two jet and two same-sign lepton final state in proton-proton collisions at s√= 13 TeV

Abstract: The first observation of electroweak production of same-sign W boson pairs in proton-proton collisions is reported The data sample corresponds to an integrated luminosity of 359 fb^(−1) collected at a center-of-mass energy of 13 TeV with the CMS detector at the LHC Events are selected by requiring exactly two leptons (electrons or muons) of the same charge, moderate missing transverse momentum, and two jets with a large rapidity separation and a large dijet mass The observed significance of the signal is 55 standard deviations, where a significance of 57 standard deviations is expected based on the standard model The ratio of measured event yields to that expected from the standard model at leading order is 090 ± 022 A cross section measurement in a fiducial region is reported Bounds are given on the structure of quartic vector boson interactions in the framework of dimension-8 effective field theory operators and on the production of doubly charged Higgs bosons

ERK1 and ERK2 regulate embryonic stem cell self-renewal through phosphorylation of Klf4.

Abstract: Understanding and controlling the mechanism by which stem cells balance self-renewal versus differentiation is of great importance for stem cell therapeutics. Klf4 promotes the self-renewal of embryonic stem cells, but the precise mechanism regulating this role of Klf4 is unclear. We found that ERK1 or ERK2 binds the activation domain of Klf4 and directly phosphorylates Klf4 at Ser123. This phosphorylation suppresses Klf4 activity, inducing embryonic stem cell differentiation. Conversely, inhibition of Klf4 phosphorylation enhances Klf4 activity and suppresses embryonic stem cell differentiation. Notably, phosphorylation of Klf4 by ERKs causes recruitment and binding of the F-box proteins βTrCP1 or βTrCP2 (components of an ubiquitin E3 ligase) to the Klf4 N-terminal domain, which results in Klf4 ubiquitination and degradation. Overall, our data provide a molecular basis for the role of ERK1 and ERK2 in regulating Klf4-mediated mouse embryonic stem cell self-renewal.