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学者姓名：黄明东
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Abstract ：
The angiopoietin (Ang)-Tie axis, critical for endothelial cell function and vascular development, is a promising therapeutic target for treating vascular disorders and inflammatory conditions like sepsis. This study aimed to enhance the binding affinity of recombinant Ang1 variants to the Tie2 and explore their therapeutic potential. Structural insights from the Ang1-Tie2 complex enabled the identification of key residues within the Ang1 receptor binding domain (RBD) critical for Tie2 interaction. Molecular dynamics simulations revealed that Met436Arg (M436R) and Ala451Asp (A451D) could improve Ang1's Tie2 binding affinity. One variant, Ang1-RBDA451D, demonstrated a 100-fold increase compared to the wild type. Cellular assays revealed that Ang1A451D enhanced Tie2 phosphorylation, promoting endothelial cell migration and tube formation. In vivo, this variant effectively reduced inflammatory cytokines and attenuated organ damage in septic mice. These findings highlight Ang1A451D as a promising therapeutic candidate for vascular diseases, offering notable clinical potential for mitigating sepsis-related vascular dysfunction.
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| GB/T 7714 | Wang, Rui , Li, Hao , Xie, Zhinuo et al. Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice [J]. | SCIENCE ADVANCES , 2025 , 11 (3) . |
| MLA | Wang, Rui et al. "Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice" . | SCIENCE ADVANCES 11 . 3 (2025) . |
| APA | Wang, Rui , Li, Hao , Xie, Zhinuo , Huang, Meijuan , Xu, Peng , Yuan, Cai et al. Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice . | SCIENCE ADVANCES , 2025 , 11 (3) . |
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Vascular thiol isomerases (VTIs) encompass proteins such as protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERp5), ERp46, ERp57, ERp72, thioredoxin-related transmembrane protein 1 (TMX1), and TMX4, and play pivotal functions in platelet aggregation and formation of thrombosis. Investigating vascular thiol isomerases, their substrates implicated in thrombosis, the underlying regulatory mechanisms, and the development of inhibitors targeting these enzymes represents a rapidly advancing frontier within vascular biology. In this review, we summarize the structural characteristics and functional attributes of VTIs, describe the associations between these enzymes and thrombosis, and outline the progress in developing inhibitors of VTIs for potential antithrombotic therapeutic applications.
Keyword ：
Functions Functions Inhibitors Inhibitors Structures Structures Thrombosis Thrombosis Vascular thiol isomerase Vascular thiol isomerase
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| GB/T 7714 | Jiang, Longguang , Yuan, Cai , Flaumenhaft, Robert et al. Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development [J]. | THROMBOSIS JOURNAL , 2025 , 23 (1) . |
| MLA | Jiang, Longguang et al. "Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development" . | THROMBOSIS JOURNAL 23 . 1 (2025) . |
| APA | Jiang, Longguang , Yuan, Cai , Flaumenhaft, Robert , Huang, Mingdong . Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development . | THROMBOSIS JOURNAL , 2025 , 23 (1) . |
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Angiogenesis provides essential nutrients and oxygen to tumors during tumorigenesis, facilitating invasion and metastasis. Consequently, inhibiting tumor angiogenesis is an established strategy in anti-cancer therapy. In this study, we engineered a dual-function nanosystem with both antiangiogenic and photodynamic properties. We transformed the hydrophobic photosensitizer zinc phthalocyanine (PS) into a hydrophilic form via protein renaturation, resulting in a novel photosensitizer: Monocyte-Activating Polypeptide-II (EMAP-II:PS@NPs). Characterization through dynamic light scattering (DLS) and UV-vis spectroscopy showed that these nano- particles exhibited uniform size and stability, and enhanced solubility. We further demonstrated that EMAP-II: PS@NPs effectively target tumor vascular endothelia causing intracellular photodynamic cytotoxicity. Notably, EMAP-II:PS@NPs achieved effective ablation of solid tumors at significantly reduced dosages of drugs compared to conventional therapies, due to their potent apoptotic effects on light-exposed cells. This study highlights the potential of combining anti-angiogenic activity with phototherapy, paving the way for innovative cancer treatment strategies.
Keyword ：
Angiogenesis Angiogenesis Anti-tumor Anti-tumor EMAP-II EMAP-II Phthalocyanine Phthalocyanine
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| GB/T 7714 | Chen, Liyun , Li, Linlin , Zhao, Hailong et al. Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment [J]. | COLLOIDS AND SURFACES B-BIOINTERFACES , 2025 , 248 . |
| MLA | Chen, Liyun et al. "Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment" . | COLLOIDS AND SURFACES B-BIOINTERFACES 248 (2025) . |
| APA | Chen, Liyun , Li, Linlin , Zhao, Hailong , Li, Hao , Li, Jiahui , Li, Chao et al. Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment . | COLLOIDS AND SURFACES B-BIOINTERFACES , 2025 , 248 . |
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Human heavy-chain ferritin (HFn) possesses a stable and uniform cage-like structure, tumor-targeting properties, self-assembly capabilities, and biocompatibility, rendering it an ideal candidate for drug delivery. Here, we developed a dual modified HFn-based nanocage (DFn) that targets the urokinase-type plasminogen activator receptor (uPAR) and, at the same time, is responsive to the tumor microenvironment for controlled extracellular drug release. This DFn was used to co-encapsulate a photosensitizer (CPZ) and a hypoxia-activated prodrug (TPZ), creating the multifunctional nanoparticles C/T@DFn. In vitro cellular assays demonstrated that C/T@DFn significantly outperformed both unmodified HFn-based nanoparticles and its counterpart without the uPARtargeting motif in inhibiting tumor cell survival, proliferation, and migration, and showed enhanced tumor cell spheroids penetration. In vivo studies further demonstrated the improved tumor-specific accumulation and antitumor efficacy of the loaded cargo in the DFn nanocages in comparison with wild-type HFn. This improved therapeutic effect is achieved through receptor-mediated targeting and tumor microenvironment-responsive release of the cargo from the DFn nanocages, resulting in synergistic action of CPZ and TPZ within the tumor tissue. Overall, this study introduces an ideal ferritin-based nanoplatform for the efficient co-delivery of therapeutic agents, offering a promising strategy for targeted tumor therapy.
Keyword ：
Antitumor Antitumor Ferritin nanocage Ferritin nanocage uPAR-targeting uPAR-targeting
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| GB/T 7714 | Li, Hanlin , Qu, Yuhan , Guo, Zhanzhi et al. Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 303 . |
| MLA | Li, Hanlin et al. "Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 303 (2025) . |
| APA | Li, Hanlin , Qu, Yuhan , Guo, Zhanzhi , Chen, Dan , Jiang, Longguang , Xu, Peng et al. Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 303 . |
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Photodynamic therapy (PDT) has gained significant attention as a minimally invasive cancer treatment that induces localized cytotoxicity with limited systemic side effects. When activated by light, typically in the visible or near-infrared spectrum, photosensitizers generate reactive oxygen species (ROS), leading to direct tumor cell death, vascular disruption, and stimulation of antitumor immune responses. This review provides an in-depth overview of the current understanding of PDT's antitumor mechanisms, focusing on ROS-induced cell death, immunogenic cell death, and tumor microenvironment modulation. Additionally, this review provides a critical evaluation of both clinically approved and investigational photosensitizers, detailing their chemical structures, photophysical properties, and therapeutic applications. We also discuss recent advances in combination strategies that integrate PDT with chemotherapy, radiotherapy, or immunotherapy to achieve enhanced therapeutic outcomes. Special emphasis is placed on emerging smart photosensitizers and tumor-targeted delivery systems that respond to microenvironmental stimuli, enhancing therapeutic precision and efficacy.
Keyword ：
antitumor antitumor clinical drugs clinical drugs mechanism mechanism photodynamic therapy photodynamic therapy photosensitizer photosensitizer
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| GB/T 7714 | Chen, Liyun , Lin, Yuxin , Ding, Shangli et al. Recent Advances in Clinically Used and Trialed Photosensitizers for Antitumor Photodynamic Therapy [J]. | MOLECULAR PHARMACEUTICS , 2025 . |
| MLA | Chen, Liyun et al. "Recent Advances in Clinically Used and Trialed Photosensitizers for Antitumor Photodynamic Therapy" . | MOLECULAR PHARMACEUTICS (2025) . |
| APA | Chen, Liyun , Lin, Yuxin , Ding, Shangli , Huang, Mingdong , Jiang, Longguang . Recent Advances in Clinically Used and Trialed Photosensitizers for Antitumor Photodynamic Therapy . | MOLECULAR PHARMACEUTICS , 2025 . |
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Serine proteases, a significant class of enzymes comprising approximately one-third of known human proteases, are ubiquitously present across various organisms. These enzymes typically exhibit highly conserved catalytic domain structures, and their activity is stringently regulated within the body, playing a pivotal role in numerous physiological processes. Dysregulation of serine protease activity can result in severe consequences, including excessive inflammation, heightened risk of thrombosis and cancer, and even mortality. Serine protease inhibitors have emerged as critical regulators, offering a broad range of physiological functions such as maintaining the coagulation-fibrinolysis balance, modulating inflammatory responses, accelerating wound healing, promoting apoptosis, and providing antitumor and antiviral effects. As a result, the development of serine protease inhibitors has become increasingly vital. In recent years, significant progress in the study of serine proteases has led to the pivotal role of various serine protease inhibitors in clinical diagnosis and treatment. This review explores the fundamental mechanisms of serine protease inhibitors, summarizes those that have been successfully integrated into clinical practice, and discusses the challenges encountered in their development along with partial solutions. These advancements lay the groundwork for further refinement and innovation in serine protease inhibitor therapeutics.
Keyword ：
challenges challenges clinical application clinical application serine protease serine protease serine protease inhibitor serine protease inhibitor strategies strategies
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| GB/T 7714 | Wei, Yang , Huang, Mingdong , Jiang, Longguang . Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications [J]. | CATALYSTS , 2024 , 14 (11) . |
| MLA | Wei, Yang et al. "Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications" . | CATALYSTS 14 . 11 (2024) . |
| APA | Wei, Yang , Huang, Mingdong , Jiang, Longguang . Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications . | CATALYSTS , 2024 , 14 (11) . |
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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
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| 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 . |
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BACKGROUND:Integrins mediate the adhesion, crawling, and migration of neutrophils during vascular inflammation. Thiol exchange is important in the regulation of integrin functions. ERp72 (endoplasmic reticulum-resident protein 72) is a member of the thiol isomerase family responsible for the catalysis of disulfide rearrangement. However, the role of ERp72 in the regulation of Mac-1 (integrin alpha M beta 2) on neutrophils remains elusive.METHODS:Intravital microscopy of the cremaster microcirculation was performed to determine in vivo neutrophil movement. Static adhesion, flow chamber, and flow cytometry were used to evaluate in vitro integrin functions. Confocal fluorescent microscopy and coimmunoprecipitation were utilized to characterize the interactions between ERp72 and Mac-1 on neutrophil surface. Cell-impermeable probes and mass spectrometry were used to label reactive thiols and identify target disulfide bonds during redox exchange. Biomembrane force probe was performed to quantitatively measure the binding affinity of Mac-1. A murine model of acute lung injury induced by lipopolysaccharide was utilized to evaluate neutrophil-associated vasculopathy.RESULTS:ERp72-deficient neutrophils exhibited increased rolling but decreased adhesion/crawling on inflamed venules in vivo and defective static adhesion in vitro. The defect was due to defective activation of integrin Mac-1 but not LFA-1 (lymphocyte function-associated antigen-1) using blocking or epitope-specific antibodies. ERp72 interacted with Mac-1 in lipid rafts on neutrophil surface leading to the reduction of the C654-C711 disulfide bond in the alpha M subunit that is critical for Mac-1 activation. Recombinant ERp72, via its catalytic motifs, increased the binding affinity of Mac-1 with ICAM-1 (intercellular adhesion molecule-1) and rescued the defective adhesion of ERp72-deficient neutrophils both in vitro and in vivo. Deletion of ERp72 in the bone marrow inhibited neutrophil infiltration, ameliorated tissue damage, and increased survival during murine acute lung injury.CONCLUSIONS:Extracellular ERp72 regulates integrin Mac-1 activity by catalyzing disulfide rearrangement on the alpha M subunit and may be a novel target for the treatment of neutrophil-associated vasculopathy.
Keyword ：
disulfides disulfides ERp72 ERp72 isomerases isomerases macrophage-1 antigen macrophage-1 antigen microscopy microscopy neutrophil infiltration neutrophil infiltration neutrophils neutrophils
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| GB/T 7714 | Li, Yaofeng , Xu, Xulin , Wang, Haoqing Jerry et al. Endoplasmic Reticulum Protein 72 Regulates Integrin Mac-1 Activity to Influence Neutrophil Recruitment [J]. | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY , 2024 , 44 (3) : E82-E98 . |
| MLA | Li, Yaofeng et al. "Endoplasmic Reticulum Protein 72 Regulates Integrin Mac-1 Activity to Influence Neutrophil Recruitment" . | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY 44 . 3 (2024) : E82-E98 . |
| APA | Li, Yaofeng , Xu, Xulin , Wang, Haoqing Jerry , Chen, Yiyao Catherine , Chen, Yaobing , Chiu, Joyce et al. Endoplasmic Reticulum Protein 72 Regulates Integrin Mac-1 Activity to Influence Neutrophil Recruitment . | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY , 2024 , 44 (3) , E82-E98 . |
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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
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| 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 . |
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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.
Keyword ：
P1 residue P1 residue Peptide inhibitors Peptide inhibitors S1 pocket S1 pocket Serine protease Serine protease Specificity Specificity
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| GB/T 7714 | Lin, Haili , Xu, Mingming , Jiang, Longguang et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue [J]. | BIOORGANIC CHEMISTRY , 2024 , 152 . |
| MLA | Lin, Haili et al. "Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue" . | BIOORGANIC CHEMISTRY 152 (2024) . |
| APA | Lin, Haili , Xu, Mingming , Jiang, Longguang , Yuan, Cai , Jiang, Chuan , Huang, Mingdong et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue . | BIOORGANIC CHEMISTRY , 2024 , 152 . |
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