
생태, 공간 구조, 선택 압력과 같은 진화적 요인은 계통 발생 구조에 독특한 흔적을 남기며, 이는 계통 발생 분석을 통해 진화적 역학을 연구하기 위한 유용한 도구가 될 수 있음을 시사합니다.


coremsg

생태-공간-구조-및-선택-압력이-계통-발생-구조에-미치는-강력한-영향


생태, 공간 구조 및 선택 압력이 계통 발생 구조에 미치는 강력한 영향


title_rewrite


生態学的動態、空間構造、選択圧は、系統構造に検出可能な形で影響を与え、系統解析を通じて進化過程を研究するための有望なツールとなる可能性がある。


生態学-空間構造-選択圧が系統構造に与える強い影響


生態学、空間構造、選択圧が系統構造に与える強い影響



Ecology, spatial structure, and selection pressure leave distinct, quantifiable signatures in phylogenetic structure, offering a potential method for inferring evolutionary dynamics from phylogenetic data.


how-ecology-spatial-structure-and-selection-pressure-impact-phylogenetic-structure


How Ecology, Spatial Structure, and Selection Pressure Impact Phylogenetic Structure



본 논문에서는 분자 구조의 유사성을 정량화하기 위해 1차원 및 고차원 코호몰로지를 기반으로 하는 새로운 그로모프-하우스도르프 울트라메트릭 접근 방식을 제시합니다. 이 방법은 분자의 루프 및 공동 구조와 같은 국소적인 토폴로지적 특징을 효과적으로 포착하여 기존의 지속적 호몰로지 기술에 비해 더 깊이 있는 정보를 제공합니다.


분자-유사성-정량화를-위한-코호몰로지-기반-그로모프-하우스도르프-거리-접근-방식


분자 유사성 정량화를 위한 코호몰로지 기반 그로모프-하우스도르프 거리 접근 방식



This paper introduces a novel method for quantifying molecular similarity using a cohomology-based Gromov-Hausdorff ultrametric approach, which captures local topological features like loops and voids in molecular structures, offering deeper insights compared to traditional persistent homology techniques.


quantifying-molecular-similarity-using-a-cohomology-based-gromov-hausdorff-ultrametric-approach


Quantifying Molecular Similarity Using a Cohomology-Based Gromov-Hausdorff Ultrametric Approach



광레독스 촉매 작용과 효소 촉매 작용을 결합한 광생물촉매 시스템을 통해 세 가지 라디칼 중간체의 거울상 선택적 삼중 교차 커플링 반응을 달성하여 높은 수율과 거울상 선택성을 가진 키랄 케톤을 합성할 수 있다.


Synergistic photobiocatalysis for enantioselective triple radical sorting - Nature

광촉매-및-효소-촉매-작용의-시너지-효과를-통한-거울상-선택적-삼중-라디칼-분류


광촉매 및 효소 촉매 작용의 시너지 효과를 통한 거울상 선택적 삼중 라디칼 분류



光レドックス触媒と指向性進化したチアミン依存性酵素を組み合わせることで、エナンチオ選択的な三成分ラジカルクロスカップリングを実現する光バイオ触媒システムを開発し、高いエナンチオ選択性で複雑なケトン化合物を合成することに成功した。


エナンチオ選択的な三重ラジカル分類のための相乗的光バイオ触媒作用


沙門氏菌需要利用宿主來源或自身合成的β-丙胺酸來促進細胞內複製和增強毒力，其機制部分是通過β-丙胺酸促進鋅轉運蛋白基因的表達來實現的。


Salmonella is a major foodborne pathogen that can effectively replicate inside host macrophages to establish life-threatening systemic infections. Salmonella must utilize diverse nutrients for growth in nutrient-poor macrophages, but which nutrients are required for intracellular Salmonella growth is largely unknown. Here, we found that either acquisition from the host or de novo synthesis of a nonprotein amino acid, β-alanine, is critical for Salmonella replication inside macrophages. The concentration of β-alanine is decreased in Salmonella -infected macrophages, while the addition of exogenous β-alanine enhances Salmonella replication in macrophages, suggesting that Salmonella can uptake host-derived β-alanine for intracellular growth. Moreover, the expression of panD, the rate-limiting gene required for β-alanine synthesis in Salmonella, is upregulated when Salmonella enters macrophages. Mutation of panD impaired Salmonella replication in macrophages and colonization in the mouse liver and spleen, indicating that de novo synthesis of β-alanine is essential for intracellular Salmonella growth and systemic infection. Additionally, we revealed that β-alanine influences Salmonella intracellular replication and in vivo virulence by increasing expression of the zinc transporter genes znuABC, which in turn facilitates the uptake of the essential micronutrient zinc by Salmonella . Taken together, these findings highlight the important role of β-alanine in the intracellular replication and virulence of Salmonella , and panD is a promising target for controlling systemic Salmonella infection.

### Competing Interest Statement

The authors have declared no competing interest.

Salmonella exploits host- and bacterial-derived β-alanine for replication inside host macrophages

沙門氏菌利用宿主和自身來源的β-丙胺酸在宿主巨噬細胞內複製


살모넬라는 숙주 대식세포 내에서 복제하기 위해 숙주 또는 박테리아 스스로 생성하는 β-alanine을 활용하며, 이는 아연 흡수를 증가시켜 살모넬라의 세포내 복제 및 병원성을 촉진한다.


숙주-대식세포-내에서-복제를-위해-salmonella는-숙주-및-박테리아-유래-β-alanine을-이용한다


숙주 대식세포 내에서 복제를 위해 Salmonella는 숙주 및 박테리아 유래 β-alanine을 이용한다



與 Phactr1/PP1 全酶不同，Neurabin/PP1 全酶的受質特異性主要由與 Neurabin PDZ 結合域的交互作用決定，而不是由去磷酸化位點本身的初級序列決定。


Protein Phosphatase 1 (PP1) relies on association with PP1-interacting proteins (PIPs) to generate substrate-specific PIP/PP1 holoenzymes, but the lack of well-defined substrates has hindered elucidation of the mechanisms involved. We previously demonstrated that the Phactr1 PIP confers sequence specificity on the Phactr1/PP1 holoenzyme by remodelling the PP1 hydrophobic substrate groove. Phactr1 defines a group of “RVxF-ΦΦ-R-W” PIPs that all interact with PP1 in a similar fashion. Here we use a PP1-PIP fusion approach to address sequence specificity and identify substrates of the RVxF-ΦΦ-R-W family PIPs. We show that the four Phactr proteins confer identical sequence specificities on their holoenzymes. We identify the 4E-BP and p70 S6K translational regulators as substrates for the Neurabin/Spinophilin PIPs, implicated in neuronal plasticity, pointing to a role for their holoenzymes in mTORC1-dependent translational control. Biochemical and structural experiments show that in contrast to the Phactrs, substrate recruitment and catalytic efficiency of the PP1-Neurabin and PP1-Spinophilin fusions is primarily determined by substrate interaction with the PDZ domain adjoining their RVxF-ΦΦ-R-W motifs, rather than by recognition of the remodelled PP1 hydrophobic groove. Thus, even PIPs that interact with PP1 in a similar manner use different mechanisms to ensure substrate selectivity.

### Competing Interest Statement

The authors have declared no competing interest.

PDZ-directed substrate recruitment is the primary determinant of specific 4E-BP1 dephosphorylation by PP1-Neurabin

由-pp1-neurabin-介導的-pdz-定向受質募集是特定-4e-bp1-去磷酸化的主要決定因素


由 PP1-Neurabin 介導的 PDZ 定向受質募集是特定 4E-BP1 去磷酸化的主要決定因素
