Table1_Noisy condition and three-point shot performance in skilled basketball players: the limited effect of self-talk.xlsx

In modern basketball, the three-point shot plays an important tactical role. Basketball players often face the distraction from audience and opponents, necessitating psychological skill to maintain their performance. The study examined the effects of self-talk interventions on the three-point shot performance under quiet and noisy conditions. It involved 42 national second-level basketball players and used a 2 (Condition: quiet condition, noisy condition) × 3 (Intervention: control group, motivational self-talk, instructional self-talk) mixed design to investigate the performance of the static and dynamic three-point shots tasks. The results revealed that the static three-point shot score was significantly lower in noisy condition compared to quiet condition (p = 0.016), while the main effect of Intervention and the interaction effect of Condition × Intervention were not significant. Post-hoc analysis indicated that only the control group showed significantly lower scores in the noisy condition (p = 0.043). For the dynamic three-point shots performance, there were no significant main effects of Intervention or Condition, nor any significant interaction effect between Condition and Intervention. In conclusion, noise distraction negatively affects the static three-point shots task, and although self-talk interventions can mitigate such negative effects, their effectiveness is limited for dynamic three-point shots task with high physical demands.</p

Novel dynamic event-triggered consensus control of multiagent systems with Markovian switching topologies under DoS attacks

This article focuses on the issue of novel dynamic event-triggered consensus control of multiagent systems (MASs) with denial-of-service (DoS) attacks. Different from the conventional Markovian switching topologies, the generally uncertain semi-Markovian (GUSM) switching topologies with partially unknown elements and time-dependent uncertainties are constructed for the leader-following MASs by considering the equipment performance and external uncertain environment influence. To save communication resources, the novel dynamic memory event-triggered strategy (DMETS) is presented to decrease the frequency of communication between agents. Some secure consensus control criteria are established for the MASs with GUSM switching topologies and DoS attacks due to the potential system communication disruption caused by attackers. Finally, two physical system examples are designed to prove the effectiveness of the presented method.</p

The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions

<div><p>Eukaryotic cells extend a variety of surface protrusions to direct cell motility. Formation of protrusions is mediated by coordinated actions between the plasma membrane and the underlying actin cytoskeleton. Here, we found that the single calponin homology (CH) domain-containing protein CHDP-1 induces the formation of cell protrusions in <i>C</i>. <i>elegans</i>. CHDP-1 is anchored to the cortex through its amphipathic helix. CHDP-1 associates through its CH domain with the small GTPase Rac1/CED-10, which is a key regulator of the actin cytoskeleton. CHDP-1 preferentially binds to the GTP-bound active form of the CED-10 protein and preserves the membrane localization of GTP-CED-10. Hence, by coupling membrane expansion to Rac1-mediated actin dynamics, CHDP-1 promotes the formation of cellular protrusions <i>in vivo</i>.</p></div

CHDP-1 promotes the membrane localization of CED-10.

<p>(A) Immunoprecipitation assay of FLAG-tagged CHDP-1 with Myc-tagged CED-10 (G12V), which mimics active GTP-bound CED-10, and Myc-tagged CED-10 (T17N), which mimics inactive GDP-bound CED-10. CHDP-1 binds more strongly to the G12V variant than the T17N variant. (B) Quantification of the relative level of binding between FLAG-CHDP-1 and CED-10 (G12V) or FLAG-CHDP-1 and CED-10 (T17N). ***p < 0.001. (C) The membrane localization of CED-10 is defective in <i>chdp-1(xd27)</i> mutant animals. (D) Quantification of the CED-10 localization defect in wild type and <i>chdp-1(xd27)</i> animals. n ≥ 50. (E) The membrane localization of GFP::CHDP-1 is not altered in <i>ced-10(n1993)</i> mutants. (F) In a cell fractionation assay, the amount of GFP::CED-10 on the plasma membrane is decreased in <i>chdp-1(xd27)</i> mutants. (G) A GST-fused CRIB domain of PAK binds active GTP-CED-10. The amount of GFP tagged CED-10 pulled down by CRIB is decreased in <i>chdp-1(xd27)</i> animals. (H) Quantification of the amount of GFP-CED-10 pulled down by GST-CRIB in wild type and <i>chdp-1(xd27)</i>. (I) The extensive ectopic cell protrusion is significantly reduced in <i>ced-10(xd33)</i>, <i>ced-10(n1933)</i> and <i>ced-10(n3246)</i> animals. (J) The co-distribution of RFP::CHDP-1 and GFP::CED-10 on ectopic PLM protrusions. (K) The co-distribution of mCherry::actin and GFP::CED-10 on ectopic PLM protrusions. Data are presented as mean ± SD; ***p < 0.001, **p < 0.01, *p < 0.05.</p

<i>chdp-1</i> is required for cell protrusion.

<p>(A) Schematic drawing of the BDU-PLM connection. (B) The BDU interneuron connects to the PLM sensory neuron in wild type. The BDU and PLM neurites are indicated by white arrows. The BDU-PLM connecting point is indicated by the white arrowhead. (C) In <i>chdp-1(xd27)</i> mutants, the BDU-PLM connection is disrupted. (D) Time-lapse images of P<i>unc-86</i>::Myr::GFP in wild type showing the dynamic movements of the BDU and PLM growth cones, which are lacking in <i>chdp-1(xd27)</i> animals (E). All scale bars represent 10 μm. (F) BDU and (G) PLM neurite extension during the embryonic stage. (H) Quantification of BDU and PLM length at the embryonic and mid-L4 stages in wild type and <i>chdp-1(xd27)</i> mutants. ***p < 0.001; NS, not significant. (I) PLM neurite extension curve in wild-type and <i>chdp-1(xd27)</i> animals.</p

CHDP-1 associates with CED-10.

<p>(A) CED-10 localizes to the cell cortex. (B-C) GFP::CED-10 co-localizes with RFP::CHDP-1 at the periphery (C) and in protrusions (D) of the PLM cell. Asterisks label the nucleus within the cell body. (D-E) Myc-tagged CED-10 and Flag-tagged CHDP-1 co-precipitate each other. (F) Protein-protein interactions between truncated CHDP-1 and CED-10 fragments in immunoprecipitation assays. FL: full length CHDP-1, FN: N-terminal region, CH: CH domain, FC: C-terminal region. (G) The BDU-PLM connection is not formed in <i>ced-10(xd33)</i> mutants. (H) Membrane protrusion is greatly reduced in <i>ced-10(xd33)</i> mutants. (I) Quantification of the BDU-PLM disconnection defect in <i>ced-10(xd33)</i>, <i>ced-10(n1993)</i>, <i>ced-10(n3246)</i>, and <i>ced-10(xd33)/ced-10(ced-10(n3246)</i> animals. n ≥ 100. ***p < 0.001; **p < 0.01; *p < 0.05.</p

<i>chdp-1</i> promotes cell protrusion.

<p>(A) The PLM cell body displays a spindle-like cell shape in wild type. (B-C) Ectopic cell protrusions (arrowheads) appear on PLM cells (outlined by yellow dashed lines) when <i>chdp-1</i> is over-expressed (<i>OE chdp-1</i>). PLM is labeled by P<i>unc-86</i>::Myr::GFP. (D) Quantification of PLM cells in wild type and <i>chdp-1</i> overexpression animals with ectopic protrusions. (E) GFP::CHDP-1 co-localizes with the plasma membrane marker Myr::mCherry on ectopic protrusions. (F) Some protrusions contain actin (arrows) and some do not (arrowheads). (G) Quantification of protrusion size with or without actin. n ≥ 30. (H-I) The stress-fiber-like structures (H) disappear in <i>chdp-1</i> overexpression animals (<i>OE chdp-1</i>) (I). On the confocal images, asterisks label the nuclei within cell bodies. Data are presented as mean ± SD; ***p < 0.001.</p

CHDP-1 does not associate with actin.

<p>(A) FLAG-tagged CHDP-1 binds to Myc-tagged CHDP-1 in an immunoprecipitation assay. (B) Protein-protein interactions between truncated CHDP-1 fragments in immunoprecipitation assays. FL: full length CHDP-1, FN: N-terminal region, CH: CH domain, FC: C-terminal region. (C) Myc-tagged ACT-1 does not bind to Flag-tagged CHDP-1. (D) Coomassie blue staining of mCherry::CHDP-1, which was purified and resolved on an SDS-PAGE gel. (E) CHDP-1 does not co-sediment with F-actin.</p

<i>chdp-1</i> functions cell-autonomously.

<p>(A) The C10G11.7 gene (<i>chdp-1</i>) encodes a single CH domain-containing protein. The molecular lesions in <i>xd27</i> and <i>tm4947</i> are indicated. P1 and P2: proline-rich regions. Helix: amphipathic helix. (B-C) Quantification of BDU (B) and PLM (C) cell protrusion size using P<i>unc-86</i>::Myr::GFP in wild type, <i>chdp-1(xd27)</i>, <i>chdp-1(tm4947)</i>, and the corresponding <i>chdp-1</i> rescuing strains. n ≥ 30. (D-E) <i>chdp-1</i> gene expression in an embryo (D) and an adult animal (E) revealed by P<i>chdp-1</i>::GFP. In the adult, the BDU and PLM cell bodies are boxed. (F) Rescue of the BDU-PLM disconnection phenotype by tissue-specific expression of <i>chdp-1</i> using different promoters: P<i>unc-53</i> in BDU; P<i>mec-7</i> in PLM; P<i>chdp-1</i> in both BDU and PLM cells; P<i>hyp-7</i> in epidermal cells; P<i>myo-3</i> in muscle cells. n ≥ 100. For all quantification analyses, error bars represent the standard error of the mean (SEM); ***p < 0.001; **p < 0.01; *p < 0.05; NS, not significant.</p

Operating condition for Quantitative HPLC.

a<p>0.05% (v/v) trifluoroacetic acid/water;</p>b<p>pure acetonitrile.</p