Query：
学者姓名：徐芃
Refining：
Year
Type
Indexed by
Source
Complex
Co-
Language
Clean All
Abstract ：
Using copper-ionophores to translocate extracellular copper into mitochondria is a clinically validated anticancer strategy that has been identified as a new type of regulated cell death termed "cuproptosis." This study reports a mitochondria-targeting Cu(I) complex, Cu(I)Br(PPh3)(3) (CBP), consisting of a cuprous ion coordinated by three triphenylphosphine moieties and a Br atom. CBP exhibited antitumor and antimetastatic efficacy in vitro and in vivo by specifically targeting mitochondria instigating mitochondrial dysfunction. The cytotoxicity of CBP could only be reversed by a copper chelator rather than inhibitors of the known cell death, indicating copper-dependent cytotoxicity. Furthermore, CBP induced the oligomerization of lipoylated proteins and the loss of Fe-S cluster proteins, consistent with characteristic features of cuproptosis. Additionally, CBP induced remarkable intracellular generation of reactive oxygen species (ROS) through a Fenton-like reaction, indicating a complex antitumor mechanism. This is a proof-of-concept study exploiting the antitumor activity and mechanism of the Cu(I)-based mitochondria-targeting therapy.
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Xu, Siyu , Hao, Yashuai , Xu, Xinyi et al. Antitumor Activity and Mechanistic Insights of a Mitochondria-Targeting Cu(I) Complex [J]. | JOURNAL OF MEDICINAL CHEMISTRY , 2024 , 67 (10) : 7911-7920 . |
| MLA | Xu, Siyu et al. "Antitumor Activity and Mechanistic Insights of a Mitochondria-Targeting Cu(I) Complex" . | JOURNAL OF MEDICINAL CHEMISTRY 67 . 10 (2024) : 7911-7920 . |
| APA | Xu, Siyu , Hao, Yashuai , Xu, Xinyi , Huang, Lu , Liang, Yuqiong , Liao, Jia et al. Antitumor Activity and Mechanistic Insights of a Mitochondria-Targeting Cu(I) Complex . | JOURNAL OF MEDICINAL CHEMISTRY , 2024 , 67 (10) , 7911-7920 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Bacterial infections of plants are widespread and highly virulent, causing serious economic losses in agricultural production worldwide. These infections become particularly prevalent during rainy weather, characterized by high humidity and low light intensity (about 2-10% of a sunny day). Here we identified a class of photosensitizers that were effective in inhibiting plant bacterial infections under rainy weather with dim light. One of these compounds, compound 1, demonstrated exceptional efficacy by eliminating more than 4 logs (99.99%) of either Xanthomonas perforans or Xanthomonas citri subsp. citri (Xcc) strain at a concentration of 6.25 mu M under rainy weather conditions with a light exposure of 28.51 J/cm2. For Clavibacter michiganensis (Cm), compound 1 demonstrated a comparable bactericidal effect at a lower concentration of 3.13 mu M. Furthermore, compound 1 was effective in controlling plant leaf infections during rainy weather. Moreover, compound 1 exhibited a potent inhibitory effect on the biofilms pertinent to tomato spot disease and citrus canker under natural illumination on rainy days. Additionally, compound 1 displayed remarkable resilience to rain-wash on plant leaves, retaining 41.20% of its initial concentration following exposure to three simulated rain events. These findings provide a new strategy for plant pathogen disease management highlight its feasibility even during rainy weather.
Keyword ：
Biofilm Biofilm Photosensitizer Photosensitizer Plant bacterial infection Plant bacterial infection Rain fastness Rain fastness
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Wang, Guodong , Li, Jiahui , Zhang, Wei et al. A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light [J]. | DYES AND PIGMENTS , 2024 , 225 . |
| MLA | Wang, Guodong et al. "A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light" . | DYES AND PIGMENTS 225 (2024) . |
| APA | Wang, Guodong , Li, Jiahui , Zhang, Wei , Jiang, Libin , Mai, Yuhan , Chen, Jingyi et al. A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light . | DYES AND PIGMENTS , 2024 , 225 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Because of the high similarity in structure and sequence, it is challenging to distinguish the S1 pocket among serine proteases, primarily due to the only variability at residue 190 (A190 and S190). Peptide or protein-based inhibitors typically target the negatively charged S1 pocket using lysine or arginine as the P1 residue, yet neither discriminates between the two S1 pocket variants. This study introduces two arginine analogues, L-4-guanidinophenylalanine (12) and L-3-(N-amidino-4-piperidyl)alanine (16), as novel P1 residues in peptide inhibitors. 16 notably enhances affinities across all tested proteases, whereas 12 specifically improved affinities towards proteases possessing S190 in the S1 pocket. By crystallography and molecular dynamics simulations, we discovered a novel mechanism involving a water exchange channel at the bottom of the S1 pocket, modulated by the variation of residue 190. Additionally, the specificity of 12 towards the S190-presenting S1 pocket is dependent on this water channel. This study not only introduces novel P1 residues to engineer inhibitory potency and specificity of peptide inhibitors targeting serine proteases, but also unveils a water-mediated molecular mechanism of targeting serine proteases. © 2024 Elsevier Inc.
Keyword ：
P1 residue P1 residue Peptide inhibitors Peptide inhibitors S1 pocket S1 pocket Serine protease Serine protease Specificity Specificity
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Lin, H. , Xu, M. , Jiang, L. et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue [J]. | Bioorganic Chemistry , 2024 , 152 . |
| MLA | Lin, H. et al. "Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue" . | Bioorganic Chemistry 152 (2024) . |
| APA | Lin, H. , Xu, M. , Jiang, L. , Yuan, C. , Jiang, C. , Huang, M. et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue . | Bioorganic Chemistry , 2024 , 152 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Human heavy chain ferritin (HFn) protein cage has been explored as a nanocarrier for targeted anticancer drug delivery. Here, we introduced a matrix metalloproteinases (MMPs)-cleavable sequence into the DE loop of HFn, creating an MMP-responsive variant, MR-HFn, for localized and extracellular drug release. The crystal structure of MR-HFn revealed that the addition of the MMPs recognition sequence did not affect the self -assembly of HFn but presented a surface -exposed loop susceptible to MMPs cleavage. Biochemical analysis indicated that this engineered protein cage is responsive to MMPs, enabling the targeted release of encapsulated drugs. To evaluate the therapeutic potential of this engineered protein cage, monosubstituted beta -carboxy phthalocyanine zinc (CPZ), a type of photosensitizer, was loaded inside this protein cage. The prepared CPZ@MR-HFn showed higher uptake and stronger phototoxicity in MMPs overexpressed tumor cells, as well as enhanced penetration into multicellular tumor spheroids compared with its counterpart CPZ@HFn in vitro. In vivo, CPZ@MR-HFn displayed a higher tumor inhibitory rate than CPZ@HFn under illumination. These results indicated that MR-HFn is a promising nanocarrier for anticancer drug delivery and the MMP-responsive strategy here can also be adapted for other stimuli.
Keyword ：
Human heavy chain ferritin Human heavy chain ferritin Localized extracellular release Localized extracellular release Tumor microenvironment responsive Tumor microenvironment responsive
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Yan, Wen , Li, Hanlin , Ning, Jiamin et al. Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 267 . |
| MLA | Yan, Wen et al. "Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 267 (2024) . |
| APA | Yan, Wen , Li, Hanlin , Ning, Jiamin , Huang, Shuhao , Jiang, Longguang , Xu, Peng et al. Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 267 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Background: Endothelial hyperpermeability-induced vascular dysfunction is a prevalent and significant characteristic in critical illnesses such as sepsis and other conditions marked by acute systemic inflammation. Platelet endothelial cell adhesion molecule-1 (PECAM-1) and Tie2 serve as transmembrane receptors within endothelial cells (ECs), playing pivotal roles not only in maintaining EC-EC junctions but also in influencing vasculogenesis, vessel homeostasis, and vascular remodeling. Objectives: At present, the molecular basis of the PECAM-1-Tie2 interaction remains inadequately elucidated. In the study, recombinant soluble PECAM-1 (sPECAM-1) and Tie2 (sTie2) were expressed by Drosophila S2 and HEK293 expression systems, respectively. The interactions between sPECAM-1 and sTie2 were investigated using the Surface Plasmon Resonance (SPR) and size-exclusion chromatography methods. An immunofluorescence assay was used to detect the binding of sPECAM-1 and sTie2 on endothelial cells. Results: PECAM-1 was found to bind with sTie2 in a sodium and pH-dependent manner as confirmed by the ELISA, the D5-D6 domains of PECAM-1 might play a crucial role in binding with sTie2. Surface Plasmon Resonance (SPR) results showed that the full length of sPECAM-1 has the strongest binding affinity (KD = 48.4 nM) with sTie2, compared to sPECAM-1-D1-D4 and sPECAM-1-D1-D2. This result is consistent with that in the ELISA. In addition, size-exclusion chromatography demonstrated that sPECAM-1, sTie2, and Ang1 can form a ternary complex. Conclusion: In this study, we determined that sPECAM-1 binds to sTie2 in a pH and sodium-dependent manner. The full length of sPECAM-1 has the strongest binding affinity, and the D5-D6 domains in sPECAM-1 play a crucial role in the interaction between sPECAM-1 and sTie2.
Keyword ：
Angiopoietin-1 Angiopoietin-1 Endothelial cell Endothelial cell PECAM-1 PECAM-1 Protein-protein interaction Protein-protein interaction Tie2 Tie2
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Li, Hao , Wang, Rui , Xu, Peng et al. Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation [J]. | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS , 2024 , 735 . |
| MLA | Li, Hao et al. "Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation" . | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 735 (2024) . |
| APA | Li, Hao , Wang, Rui , Xu, Peng , Yuan, Cai , Huang, Mingdong , Jiang, Longguang . Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation . | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS , 2024 , 735 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Urokinase plasminogen activator receptor (uPAR) is a key participant in extracellular proteolysis, tissue remodeling and cell motility. uPAR overexpresses in most solid tumors and several hematologic malignancies, but has low levels on normal tissues, thus is advocated as a molecular target for cancer therapy. One of the obstacles for the evaluation of uPAR targeting agents in preclinical study is the species specificity, where targeting agents for human uPAR usually not bind to murine uPAR. Here, we develop a targeting agent that binds to both murine and human uPAR. This targeting agent is genetically fused to human serum albumin, a commonly used drug carrier, and the final construct is named as uPAR targeting carrier (uPARTC). uPARTC binds specifically to uPAR-overexpressing 293T/huPAR and 293T/muPAR as demonstrated by flow cytometry. A cytotoxic compound, celastrol, is embedded into uPARTC non-covalently. The resulting macromolecular complex show effective proliferation inhibition on both murine and human uPAR overexpressing cells, and exhibit potent antitumor efficacy on hepatoma H22-bearing mice. This work demonstrates that uPARTC is a promising tumor targeting drug carrier, which address the species-specificity challenge of uPAR targeting agents and can be used to load other cytotoxic compounds.
Keyword ：
Cancer therapy Cancer therapy Celastrol Celastrol Drug carrier Drug carrier HSA HSA uPAR uPAR
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Li, Hanlin , Wang, Zhiyou , Yu, Shujuan et al. Albumin-based drug carrier targeting urokinase receptor for cancer therapy [J]. | INTERNATIONAL JOURNAL OF PHARMACEUTICS , 2023 , 634 . |
| MLA | Li, Hanlin et al. "Albumin-based drug carrier targeting urokinase receptor for cancer therapy" . | INTERNATIONAL JOURNAL OF PHARMACEUTICS 634 (2023) . |
| APA | Li, Hanlin , Wang, Zhiyou , Yu, Shujuan , Chen, Shanli , Zhou, Yang , Qu, Yuhan et al. Albumin-based drug carrier targeting urokinase receptor for cancer therapy . | INTERNATIONAL JOURNAL OF PHARMACEUTICS , 2023 , 634 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Diltiazem and glibenclamide are commonly used hypotensive and antidiabetic drugs. This study reports the discovery of the potential antitumor and antimetastatic effects of these two drugs using a structural dynamics-driven virtual screening targeting urokinase receptor (uPAR). Owing to uPAR's high flexibility, currently resolved crystal structures of uPAR, all in ligand-bound states, provide limited representations of its physiological conformation. To improve the accuracy of screening, we performed a long-timescale molecular dynamics simulation and obtained the representative conformations of apo-uPAR as the targets for our screening. Experimentally, we demonstrated that diltiazem and glibenclamide bound uPAR with KD values in the micromolar range. In addition, both compounds effectively suppressed tumor growth and metastasis in a uPAR-dependent manner in vitro and in vivo. This work not only provides two potent uPAR inhibitors but also reports a proof-of-concept study on the potential off-label antitumor and antimetastatic uses of diltiazem and glibenclamide.
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Zhou, Yang , Song, Meiru , Xie, Daoqing et al. Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor [J]. | JOURNAL OF MEDICINAL CHEMISTRY , 2023 , 66 (8) : 5415-5426 . |
| MLA | Zhou, Yang et al. "Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor" . | JOURNAL OF MEDICINAL CHEMISTRY 66 . 8 (2023) : 5415-5426 . |
| APA | Zhou, Yang , Song, Meiru , Xie, Daoqing , Yan, Shufeng , Xie, Song , Cai, Meiqin et al. Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor . | JOURNAL OF MEDICINAL CHEMISTRY , 2023 , 66 (8) , 5415-5426 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Supramolecular assemblies fabricated by peptide-photosensitizer conjugates have attracted increasing attentions in recent years as drug carriers for chemotherapeutics (CTs). However, these assemblies have been known to suffer from disintegration by serum components leading to off-target drug release, and thereby impairing anti-tumor effects and causing systemic toxicities. To address this problem, this study reports a nano-architectural self-assembly peptide-photosensitizer carrier (NSPC) fabricated by conjugating a phthalocyanine derivative (MCPZnPc) and & epsilon;-poly-L-lysine (EPL). By engineering the core and peripheral interactions, MCPZnPC-EPL (M-E) NSPC firmly encapsulated multiple CTs, creating CT@M-E NSPCs that were highly stable against disintegration in serum. More importantly, CT@M-E NSPCs exhibited controlled release of CTs in tumor tissues. The antitumor effects of CTs were further promoted by the synergism with the reactivated photodynamic effect. Furthermore, M-E NSPC-encapsulation optimized CTs' biodistribution reducing adverse effects in vivo. This study provides a serum-stable supramolecular drug delivery system with photodynamic effect, which is applicable for a broad-range of CTs to promote antitumor effects and ameliorate adverse effects.
Keyword ：
Chemotherapeutics Chemotherapeutics Drug delivery system Drug delivery system Peptide-photosensitizer conjugate Peptide-photosensitizer conjugate Serum stability Serum stability Supramolecular assemblies Supramolecular assemblies
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Chen, Jincan , Zhou, Yang , Song, Meiru et al. A Serum-Stable supramolecular drug carrier for chemotherapeutics fabricated by a Peptide-Photosensitizer conjugate [J]. | JOURNAL OF COLLOID AND INTERFACE SCIENCE , 2023 , 646 : 959-969 . |
| MLA | Chen, Jincan et al. "A Serum-Stable supramolecular drug carrier for chemotherapeutics fabricated by a Peptide-Photosensitizer conjugate" . | JOURNAL OF COLLOID AND INTERFACE SCIENCE 646 (2023) : 959-969 . |
| APA | Chen, Jincan , Zhou, Yang , Song, Meiru , Chen, Yijian , Wang, Dong , Huang, Yunmei et al. A Serum-Stable supramolecular drug carrier for chemotherapeutics fabricated by a Peptide-Photosensitizer conjugate . | JOURNAL OF COLLOID AND INTERFACE SCIENCE , 2023 , 646 , 959-969 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
Polyphosphate (PolyP) is a polymer comprised of linear phosphate units connected by phosphate anhydride bonds. PolyP exists in a diverse range of eukaryotes and prokaryotes with varied chain lengths ranging from six to thousands of phosphate units. Upon activation, human platelets and neutrophils release short-chain PolyP, along with other components, to initiate the coagulation pathway. Long-chain PolyP derived from cellular or bacterial organelles exhibits higher proinflammatory and procoagulant effects compared to short-chain PolyP. Notably, PolyP has been identified as a low-hemorrhagic antithrombotic target since neutralizing plasma PolyP suppresses the thrombotic process without impairing the hemostatic functions. As an inorganic polymer without uniform steric configuration, PolyP is typically targeted by cationic polymers or recombinant polyphosphatases rather than conventional antibodies, small-molecule compounds, or peptides. Additionally, because of its procoagulant property, PolyP has been incorporated in wound-dressing materials to facilitate blood hemostasis. This review summarizes current studies on PolyP as a low-hemorrhagic antithrombotic target and the development of hemostatic materials based on PolyP.
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | Chen, Ruoyu , Huang, Mingdong , Xu, Peng . Polyphosphate as an antithrombotic target and hemostatic agent [J]. | JOURNAL OF MATERIALS CHEMISTRY B , 2023 . |
| MLA | Chen, Ruoyu et al. "Polyphosphate as an antithrombotic target and hemostatic agent" . | JOURNAL OF MATERIALS CHEMISTRY B (2023) . |
| APA | Chen, Ruoyu , Huang, Mingdong , Xu, Peng . Polyphosphate as an antithrombotic target and hemostatic agent . | JOURNAL OF MATERIALS CHEMISTRY B , 2023 . |
| Export to | NoteExpress RIS BibTex |
Version ：
Abstract ：
细菌和病毒造成的空气污染对公众健康构成了严重威胁。空气过滤器作为一种去除空气中有害微生物的方法被广泛使用(例如著名的HEPA过滤器)。然而,在已有过滤介质中,捕获的微生物可以保持存活,甚至一些微生物可以通过吸收空气中的水分和灰尘中的营养物质在过滤介质上生长和繁殖。而且,在维护过程中,这些微生物很可能会重新悬浮在空气中从而造成二次空气污染。因此,开发一种可高效杀灭空气中的病原体且具有良好的生物安全性的空气过滤材料在消毒抗菌材料领域的应用十分重要。我们制备了一种含有光敏剂和壳聚糖的抗菌聚对苯二甲酸乙二酯(PET)纤维材料;壳聚糖能与光敏剂的羧基发生静电键合作用。这种双重组分纤维表现出广谱的抗菌活性,甚至包括耐药性细菌。用这种双组分纤维制备的空气过滤材料对细菌表现出了优异的抗菌性能。
Keyword ：
光动力 光动力 壳聚糖 壳聚糖 抗菌 抗菌 空气消毒 空气消毒 聚酯 聚酯
Cite：
Copy from the list or Export to your reference management。
| GB/T 7714 | 林羽欣 , 陈静怡 , 麦宇涵 et al. 一种高效去除空气过滤器中细菌蓄积的聚酯材料 [C] //ASTF 2023（第5届）抗菌科学与技术论坛论文摘要集 . 2023 . |
| MLA | 林羽欣 et al. "一种高效去除空气过滤器中细菌蓄积的聚酯材料" ASTF 2023（第5届）抗菌科学与技术论坛论文摘要集 . (2023) . |
| APA | 林羽欣 , 陈静怡 , 麦宇涵 , 陈李云 , 陈铮 , 王国栋 et al. 一种高效去除空气过滤器中细菌蓄积的聚酯材料 ASTF 2023（第5届）抗菌科学与技术论坛论文摘要集 . (2023) . |
| Export to | NoteExpress RIS BibTex |
Version ：
Export
| Results： |
Selected to |
| Format： |
