K-point longitudinal acoustic phonons are responsible for ultrafast intervalley scattering in monolayer MoSe2

In transition metal dichalcogenides, valley depolarization through intervalley carrier scattering by zone-edge phonons is often unavoidable. Although valley depolarization processes related to various acoustic phonons have been suggested, their optical verification is still vague due to nearly degenerate phonon frequencies on acoustic phonon branches at zone-edge momentums. Here we report an unambiguous phonon momentum determination of the longitudinal acoustic (LA) phonons at the K point, which are responsible for the ultrafast valley depolarization in monolayer MoSe2. Using sub-10-fs-resolution pump-probe spectroscopy, we observed coherent phonons signals at both even and odd-orders of zone-edge LA mode involved in intervalley carrier scattering process. Our phonon-symmetry analysis and first-principles calculations reveal that only the LA phonon at the K point, as opposed to the M point, can produce experimental odd-order LA phonon signals from its nonlinear optical modulation. This work will provide momentum-resolved descriptions of phonon-carrier intervalley scattering processes in valleytronic materials.journal articl

Observation of B+ → χc0K+

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細孔中の海水がコンクリートのスケーリングに及ぼす影響

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Transcript abundance of microvilli associated-like proteins compared between unfed and blood fed sand flies

<p><b>Copyright information:</b></p><p>Taken from "Exploring the midgut transcriptome of comparative analysis of expression profiles of sugar-fed, blood-fed and -infected sandflies"</p><p>http://www.biomedcentral.com/1471-2164/8/300</p><p>BMC Genomics 2007;8():300-300.</p><p>Published online 30 Aug 2007</p><p>PMCID:PMC2034597.</p><p></p> A, C, E: ,,transcript fold over control (reference transcript = alpha tubulin) in unfed and blood fed midgut. B, C, F: ,,semi-quantitative PCR amplified transcripts separated by agarose electrophoresis

Phylogenetic analysis of trypsins from (Ce), (Rn), (Mm), (Hs), (Bg), (Ag), (As), (Aa), (Dm), (Cs), and (Pp)

<p><b>Copyright information:</b></p><p>Taken from "Exploring the midgut transcriptome of comparative analysis of expression profiles of sugar-fed, blood-fed and -infected sandflies"</p><p>http://www.biomedcentral.com/1471-2164/8/300</p><p>BMC Genomics 2007;8():300-300.</p><p>Published online 30 Aug 2007</p><p>PMCID:PMC2034597.</p><p></p> The accession number of the sequence used is in parentheses and node support indicated by the bootstrap values

Multiple sequence alignment of the four putative microvilli associated-like proteins found in the midgut of

<p><b>Copyright information:</b></p><p>Taken from "Exploring the midgut transcriptome of comparative analysis of expression profiles of sugar-fed, blood-fed and -infected sandflies"</p><p>http://www.biomedcentral.com/1471-2164/8/300</p><p>BMC Genomics 2007;8():300-300.</p><p>Published online 30 Aug 2007</p><p>PMCID:PMC2034597.</p><p></p> Predicted signal peptide sequence is underlined and the accession numbers given in parentheses

Small GTPase Cdc42, WASP, and scaffold proteins for higher-order assembly of the F-BAR domain protein

The higher-order assembly of Bin-amphiphysin-Rvs (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, into lattice on the membrane is essential for the formation of subcellular structures. However, the regulation of their ordered assembly has not been elucidated. Here, we show that the higher ordered assembly of growth-arrested specific 7 (GAS7), an F-BAR domain protein, is regulated by the multivalent scaffold proteins of Wiskott-Aldrich syndrome protein (WASP)/neural WASP, that commonly binds to the BAR domain superfamily proteins, together with WISH, Nck, the activated small guanosine triphosphatase Cdc42, and a membrane-anchored phagocytic receptor. The assembly kinetics by fluorescence resonance energy transfer monitoring indicated that the GAS7 assembly on liposomes started within seconds and was further increased by the presence of these proteins. The regulated GAS7 assembly was abolished by Wiskott-Aldrich syndrome mutations both in vitro and in cellular phagocytosis. Therefore, Cdc42 and the scaffold proteins that commonly bind to the BAR domain superfamily proteins promoted GAS7 assembly.journal articl