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  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Doi.org Make Money
  6. Keywords
  7. Topics
  8. Schema
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We began analyzing https://jnanobiotechnology.biomedcentral.com/articles/10.1186/s12951-025-03171-x, but it redirected us to https://jnanobiotechnology.biomedcentral.com/articles/10.1186/s12951-025-03171-x. The analysis below is for the second page.

Title[redir]:
Resetting the Hsc70-mediated lysosomal degradation of PD-L1 via a supramolecular meso peptide for the restoration of acquired anti-tumor T cell immunity | Journal of Nanobiotechnology | Full Text
Description:
The reduction of cellular PD-L1 abundance through lysosomal degradation is recognized as essential for effective and sustained targeting of PD-L1-dependent immune evasion in cancer. While Hsc70 can interact with PD-L1 to promote its lysosomal degradation, the overexpression of CMTM6 competitively inhibits this interaction, leading to the blockade of PD-L1 lysosomal degradation. To overcome this issue, a meso chimeric peptide PEPPDL1 was designed to specifically bind the PD-1 binding domain of PD-L1 instead of the Hsc70/CMTM6 binding domain, while also binding to Hsc70 to facilitate the dragging of PD-L1 into Hsc70-mediated chaperone-mediated autophagy (CMA), thereby achieving lysosomal degradation. In order to enable internalization into tumor cells, supramolecular engineering techniques were employed through terminal modification involving sulfydryl and monovalent gold ion (Au(I)), both facilitating self-assembly of modified PEPPDL1 into supramolecular nanospheres termed CTAC-PDL1 driven by aurophilic interaction. Furthermore, based on bioinformatics analysis of mRNA expression data from 30 types of tumors obtained from TCGA database, malignant melanoma was identified as the most suitable indication for CTAC-PDL1 due to its specific characteristics of tumor immune. As expected, CTAC-PDL1 effectively reactivated Hsc70-mediated lysosomal degradation of PD-L1 and consequently restored anti-tumor T cell immunity in a B16F10-derived mouse model of malignant melanoma while maintaining a favorable safety profile. Overall, this work not only presents an alternative approach for targeting PD-L1-dependent cancer immune evasion, but also provides a modularized strategy for discovering specific regulators for target proteins in various diseases.

Matching Content Categories {📚}

  • Science
  • Education
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Content Management System {📝}

What CMS is doi.org built with?

Custom-built

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🚀 Good Traffic: 50k - 100k visitors per month


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Keywords {🔍}

pdl, ctacpdl, fig, pubmed, degradation, article, cells, peppdl, google, scholar, hsc, tumor, expression, cas, cell, lysosomal, analysis, cancer, binding, immune, figure, treatment, melanoma, protein, central, yan, antibody, wang, peptide, skcm, antitumor, liu, interaction, lamp, monoclonal, data, supramolecular, cmtm, tumors, membrane, results, control, mice, resistance, group, intracellular, clinical, vivo, performed, compared,

Topics {✒️}

natural killer/t-cell lymphoma d-peptides-functionalized ultra-small nanoparticles failed anti-pd-1/pd-l1 treatment bionic nano-band-aid constructed pd-l1-dependent immune evasion d-enantiomeric pd-l1-binding motif ctac-pdl1-derived pd-l1 degradation half-turn α-helix conformation hsc70-mediated chaperone-mediated autophagy ctac-pdl1-induced pd-l1 degradation pd-l1 knockout coad anti-pd-l1 antibody specifically cell growth-promoting activity anti-pd-1/pd-l1 therapy [46 anti-pd-1/pd-l1 therapy anti-pd-1/pd-l1 therapy [49 t-sne plots showing l-enantiomeric hsc70-binding motif electronic supplementary material additional information publisher reduced cmtm6-mediated pd-l1 anti-pd-l1 therapy demonstrated hsc70/lamp2-derived lysosomal degradation gsh-concentration-dependent cargo release strongest pd-l1-related correlation peppdl1/pd-l1/hsc70 complex rewiring chaperone-mediated autophagy ctac-pdl1 degraded pd-l1 stimuli-responsive clustered nanohybrids reactivates t-cell immunity anti-tumor action resulting optimal peppdl1/pd-l1 conformation cellular pd-l1 abundance targeting glycosylated pd-l1 regulates chaperone-mediated autophagy cell-mediated tumor regression ctac-pdl1-treated b16f10 cell predicted peppdl1/pd-l1 conformation pro-apoptotic oral nanotherapeutic d-peptide drug delivery hierarchical peptide–lanthanide framework cma-mediated lysosomal degradation hsc70-mediated lysosomal degradation mediate cma-mediated degradation pd-l1 monoclonal antibody anti-pd-l1 therapy hsc70-mediated cma pathway single-cell rna sequencing pd-1/pd-l1 pathway endogenous pd-l1 protein

Schema {🗺️}

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         description:The reduction of cellular PD-L1 abundance through lysosomal degradation is recognized as essential for effective and sustained targeting of PD-L1-dependent immune evasion in cancer. While Hsc70 can interact with PD-L1 to promote its lysosomal degradation, the overexpression of CMTM6 competitively inhibits this interaction, leading to the blockade of PD-L1 lysosomal degradation. To overcome this issue, a meso chimeric peptide PEPPDL1 was designed to specifically bind the PD-1 binding domain of PD-L1 instead of the Hsc70/CMTM6 binding domain, while also binding to Hsc70 to facilitate the dragging of PD-L1 into Hsc70-mediated chaperone-mediated autophagy (CMA), thereby achieving lysosomal degradation. In order to enable internalization into tumor cells, supramolecular engineering techniques were employed through terminal modification involving sulfydryl and monovalent gold ion (Au(I)), both facilitating self-assembly of modified PEPPDL1 into supramolecular nanospheres termed CTAC-PDL1 driven by aurophilic interaction. Furthermore, based on bioinformatics analysis of mRNA expression data from 30 types of tumors obtained from TCGA database, malignant melanoma was identified as the most suitable indication for CTAC-PDL1 due to its specific characteristics of tumor immune. As expected, CTAC-PDL1 effectively reactivated Hsc70-mediated lysosomal degradation of PD-L1 and consequently restored anti-tumor T cell immunity in a B16F10-derived mouse model of malignant melanoma while maintaining a favorable safety profile. Overall, this work not only presents an alternative approach for targeting PD-L1-dependent cancer immune evasion, but also provides a modularized strategy for discovering specific regulators for target proteins in various diseases.
         datePublished:2025-02-04T00:00:00Z
         dateModified:2025-02-04T00:00:00Z
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      headline:Resetting the Hsc70-mediated lysosomal degradation of PD-L1 via a supramolecular meso peptide for the restoration of acquired anti-tumor T cell immunity
      description:The reduction of cellular PD-L1 abundance through lysosomal degradation is recognized as essential for effective and sustained targeting of PD-L1-dependent immune evasion in cancer. While Hsc70 can interact with PD-L1 to promote its lysosomal degradation, the overexpression of CMTM6 competitively inhibits this interaction, leading to the blockade of PD-L1 lysosomal degradation. To overcome this issue, a meso chimeric peptide PEPPDL1 was designed to specifically bind the PD-1 binding domain of PD-L1 instead of the Hsc70/CMTM6 binding domain, while also binding to Hsc70 to facilitate the dragging of PD-L1 into Hsc70-mediated chaperone-mediated autophagy (CMA), thereby achieving lysosomal degradation. In order to enable internalization into tumor cells, supramolecular engineering techniques were employed through terminal modification involving sulfydryl and monovalent gold ion (Au(I)), both facilitating self-assembly of modified PEPPDL1 into supramolecular nanospheres termed CTAC-PDL1 driven by aurophilic interaction. Furthermore, based on bioinformatics analysis of mRNA expression data from 30 types of tumors obtained from TCGA database, malignant melanoma was identified as the most suitable indication for CTAC-PDL1 due to its specific characteristics of tumor immune. As expected, CTAC-PDL1 effectively reactivated Hsc70-mediated lysosomal degradation of PD-L1 and consequently restored anti-tumor T cell immunity in a B16F10-derived mouse model of malignant melanoma while maintaining a favorable safety profile. Overall, this work not only presents an alternative approach for targeting PD-L1-dependent cancer immune evasion, but also provides a modularized strategy for discovering specific regulators for target proteins in various diseases.
      datePublished:2025-02-04T00:00:00Z
      dateModified:2025-02-04T00:00:00Z
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         Lysosomal degradation
         Cellular abundance of PD-L1
         Peptide
         Supramolecule
         Tumor immunotherapy
         Biotechnology
         Nanotechnology
         Molecular Medicine
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      email:[email protected]
      name:Leiqing Yao
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            address:
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      name:Department of Medical Oncology, The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an, P.R. China
      name:Department of Medical Oncology, The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an, P.R. China
      name:Department of Medical Oncology, The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an, P.R. China
      name:Department of Medical Oncology, The First Affiliated Hospital of Xi’an Jiaotong University, Xi’an, P.R. China
      name:Department of Infectious Diseases, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, China
      name:National & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, China
      name:Department of Infectious Diseases, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, China
      name:National & Local Joint Engineering Research Center of Biodiagnosis and Biotherapy, The Second Affiliated Hospital of Xi’an Jiaotong University, Xi’an, China

Social Networks {👍}(2)

External Links {🔗}(378)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Prism.js

Emails and Hosting {✉️}

Mail Servers:

  • mx.zoho.eu
  • mx2.zoho.eu
  • mx3.zoho.eu

Name Servers:

  • josh.ns.cloudflare.com
  • zita.ns.cloudflare.com

CDN Services {📦}

  • Crossref

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