tlr4 antagonist lps rs Search Results


tlr4 ligand antagonists  (Mimetics)
86
Mimetics tlr4 ligand antagonists
Divergent modulation of HMGB1 functions through distinct molecular interactions. (A) Interfacial residues of human HMGB1 for interacting with <t>TLR4,</t> RAGE, or TN P2. The binding regions for TLR4 (residues 89–108) and RAGE (residues 150–183) are highlighted in italicized red and blue text, respectively. Key P2-interacting residues are highlighted in non-italicized purple text. (B) Divergent functional outcomes stemming from HMGB1’s interaction with various proteins. HMGB1 engages TLR4 and RAGE receptors, leading to the induction of cytokine/chemokine production and macrophage pyroptosis, respectively. Conversely, some endogenous proteins, such as HP, can bind to HMGB1 to induce anti-inflammatory IL-10. Similarly, TN can sequester HMGB1 to facilitate the endocytosis of HMGB1/TN complexes, and subsequently induce macrophage pyroptosis and immunosuppression. In contrast, a TN-derived P2–1 peptide binds HMGB1 to prevent its interaction with a pro-endocytic receptor, RAGE, thereby suppressing macrophage pyroptosis and HMGB1-mediated pCTS-L upregulation.
Tlr4 Ligand Antagonists, supplied by Mimetics, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tlr4+antagonist+lps+rs/immunomodulatory+specific+tlr4/pmc13194016-228-4-9
Average 86 stars, based on 1 article reviews
tlr4 ligand antagonists - by Bioz Stars, 2026-10
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mta00  (Bio-Techne corporation)
99
Bio-Techne corporation mta00
Divergent modulation of HMGB1 functions through distinct molecular interactions. (A) Interfacial residues of human HMGB1 for interacting with <t>TLR4,</t> RAGE, or TN P2. The binding regions for TLR4 (residues 89–108) and RAGE (residues 150–183) are highlighted in italicized red and blue text, respectively. Key P2-interacting residues are highlighted in non-italicized purple text. (B) Divergent functional outcomes stemming from HMGB1’s interaction with various proteins. HMGB1 engages TLR4 and RAGE receptors, leading to the induction of cytokine/chemokine production and macrophage pyroptosis, respectively. Conversely, some endogenous proteins, such as HP, can bind to HMGB1 to induce anti-inflammatory IL-10. Similarly, TN can sequester HMGB1 to facilitate the endocytosis of HMGB1/TN complexes, and subsequently induce macrophage pyroptosis and immunosuppression. In contrast, a TN-derived P2–1 peptide binds HMGB1 to prevent its interaction with a pro-endocytic receptor, RAGE, thereby suppressing macrophage pyroptosis and HMGB1-mediated pCTS-L upregulation.
Mta00, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tlr4+antagonist+lps+rs/mta00/bio-techne+corporation___mta00
Average 99 stars, based on 1 article reviews
mta00 - by Bioz Stars, 2026-10
99/100 stars
  Buy from Supplier
m6000  (Bio-Techne corporation)
99
Bio-Techne corporation m6000
Divergent modulation of HMGB1 functions through distinct molecular interactions. (A) Interfacial residues of human HMGB1 for interacting with <t>TLR4,</t> RAGE, or TN P2. The binding regions for TLR4 (residues 89–108) and RAGE (residues 150–183) are highlighted in italicized red and blue text, respectively. Key P2-interacting residues are highlighted in non-italicized purple text. (B) Divergent functional outcomes stemming from HMGB1’s interaction with various proteins. HMGB1 engages TLR4 and RAGE receptors, leading to the induction of cytokine/chemokine production and macrophage pyroptosis, respectively. Conversely, some endogenous proteins, such as HP, can bind to HMGB1 to induce anti-inflammatory IL-10. Similarly, TN can sequester HMGB1 to facilitate the endocytosis of HMGB1/TN complexes, and subsequently induce macrophage pyroptosis and immunosuppression. In contrast, a TN-derived P2–1 peptide binds HMGB1 to prevent its interaction with a pro-endocytic receptor, RAGE, thereby suppressing macrophage pyroptosis and HMGB1-mediated pCTS-L upregulation.
M6000, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/tlr4+antagonist+lps+rs/m6000/bio-techne+corporation___m6000
Average 99 stars, based on 1 article reviews
m6000 - by Bioz Stars, 2026-10
99/100 stars
  Buy from Supplier

Image Search Results


Divergent modulation of HMGB1 functions through distinct molecular interactions. (A) Interfacial residues of human HMGB1 for interacting with TLR4, RAGE, or TN P2. The binding regions for TLR4 (residues 89–108) and RAGE (residues 150–183) are highlighted in italicized red and blue text, respectively. Key P2-interacting residues are highlighted in non-italicized purple text. (B) Divergent functional outcomes stemming from HMGB1’s interaction with various proteins. HMGB1 engages TLR4 and RAGE receptors, leading to the induction of cytokine/chemokine production and macrophage pyroptosis, respectively. Conversely, some endogenous proteins, such as HP, can bind to HMGB1 to induce anti-inflammatory IL-10. Similarly, TN can sequester HMGB1 to facilitate the endocytosis of HMGB1/TN complexes, and subsequently induce macrophage pyroptosis and immunosuppression. In contrast, a TN-derived P2–1 peptide binds HMGB1 to prevent its interaction with a pro-endocytic receptor, RAGE, thereby suppressing macrophage pyroptosis and HMGB1-mediated pCTS-L upregulation.

Journal: Frontiers in Immunology

Article Title: Pharmacological intervention of the HMGB1-pCTS-L axis to ameliorate inflammatory diseases

doi: 10.3389/fimmu.2026.1843251

Figure Lengend Snippet: Divergent modulation of HMGB1 functions through distinct molecular interactions. (A) Interfacial residues of human HMGB1 for interacting with TLR4, RAGE, or TN P2. The binding regions for TLR4 (residues 89–108) and RAGE (residues 150–183) are highlighted in italicized red and blue text, respectively. Key P2-interacting residues are highlighted in non-italicized purple text. (B) Divergent functional outcomes stemming from HMGB1’s interaction with various proteins. HMGB1 engages TLR4 and RAGE receptors, leading to the induction of cytokine/chemokine production and macrophage pyroptosis, respectively. Conversely, some endogenous proteins, such as HP, can bind to HMGB1 to induce anti-inflammatory IL-10. Similarly, TN can sequester HMGB1 to facilitate the endocytosis of HMGB1/TN complexes, and subsequently induce macrophage pyroptosis and immunosuppression. In contrast, a TN-derived P2–1 peptide binds HMGB1 to prevent its interaction with a pro-endocytic receptor, RAGE, thereby suppressing macrophage pyroptosis and HMGB1-mediated pCTS-L upregulation.

Article Snippet: Although clinical trials involving TLR4 ligand antagonists (e.g., LPS mimetics, eritoran) ( ) and early cytokines (e.g., TNF) neutralizing mAbs ( , ) failed to improve sepsis survival, it is crucial to distinguish between targeting general TLR4 activation or early cytokines, and specifically interfering with HMGB1/pCTS-L-TLR4 interactions.

Techniques: Binding Assay, Functional Assay, Derivative Assay