An overview on HMGB1 inhibitors as potential therapeutic agents in HMGB1-related pathologies (554 views)
Pharmacol Ther (ISSN: 0163-7258, 0163-7258linking), 2014 Mar; 141(3): 347-357.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T , Review,
Impact factor: 9.723, 5-year impact factor: 8.843
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84892171140&partnerID=40&md5=ba1bf8ece36a3642f2dbd93959da89b1
Keywords: Dna-Based Inhibitors, Hmgb1, Hmgb1-Receptors, Peptide Protein Inhibitors, Small-Molecule Inhibitors, Advanced Glycation End Product Receptor, Curved Dna, Gabexate Mesilate, Glycyrrhizic Acid, High Mobility Group B1 Protein, High Mobility Group Inhibitor, Oligonucleotide, Unclassified Drug, Antibody Specificity, Competitive Inhibition, Drug Identification, Drug Interaction, Drug Targeting, Human, Nonhuman, Pathology, Priority Journal, Review, Ethyl Pyruvate, High-Mobility Group Box, Interleukin, Ischemia-Reperfusion, Lipopolysaccharide, Oligodeoxyribonucleotide, Peptide Nucleic Acid, Receptor For Advanced Glycation End Products, Toll-Like Receptor, Tumor Necrosis Factor, Animals, Autoimmune Diseases, Drug Design, Hmgb1 Protein, Inflammation, Molecular Targeted Therapy, Immunologic, Signal Transduction, Autoimmune Diseases Drug Therapy Physiopathology , Hmgb1 Protein Antagonists, Inhibitors Metabolism , Inflammation Drug Therapy Physiopathology , Immunologic Metabolism , Signal Transduction Drug Effects , I R , Lps , Pna , Rage , Tlr , Tnf , Ischemia–reperfusion,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Napoli Federico II, Complesso Universitario di Monte sant'Angelo, via Cintia 21, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini - CNR, via Mezzocannone 16, I-80134 Napoli, Italy
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Pharmacol Ther (ISSN: 0163-7258, 0163-7258linking), 2014 Mar; 141(3): 347-357.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T , Review,
Impact factor: 9.723, 5-year impact factor: 8.843
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84892171140&partnerID=40&md5=ba1bf8ece36a3642f2dbd93959da89b1
Keywords: Dna-Based Inhibitors, Hmgb1, Hmgb1-Receptors, Peptide Protein Inhibitors, Small-Molecule Inhibitors, Advanced Glycation End Product Receptor, Curved Dna, Gabexate Mesilate, Glycyrrhizic Acid, High Mobility Group B1 Protein, High Mobility Group Inhibitor, Oligonucleotide, Unclassified Drug, Antibody Specificity, Competitive Inhibition, Drug Identification, Drug Interaction, Drug Targeting, Human, Nonhuman, Pathology, Priority Journal, Review, Ethyl Pyruvate, High-Mobility Group Box, Interleukin, Ischemia-Reperfusion, Lipopolysaccharide, Oligodeoxyribonucleotide, Peptide Nucleic Acid, Receptor For Advanced Glycation End Products, Toll-Like Receptor, Tumor Necrosis Factor, Animals, Autoimmune Diseases, Drug Design, Hmgb1 Protein, Inflammation, Molecular Targeted Therapy, Immunologic, Signal Transduction, Autoimmune Diseases Drug Therapy Physiopathology , Hmgb1 Protein Antagonists, Inhibitors Metabolism , Inflammation Drug Therapy Physiopathology , Immunologic Metabolism , Signal Transduction Drug Effects , I R , Lps , Pna , Rage , Tlr , Tnf , Ischemia–reperfusion,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università di Napoli Federico II, Complesso Universitario di Monte sant'Angelo, via Cintia 21, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini - CNR, via Mezzocannone 16, I-80134 Napoli, Italy
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An overview on HMGB1 inhibitors as potential therapeutic agents in HMGB1-related pathologies
HMGB1 (High-Mobility Group Box-1) is a nuclear protein that acts as an architectural chromatin-binding factor involved in the maintenance of nucleosome structure and regulation of gene transcription. It can be released into the extracellular milieu from immune and non-immune cells in response to various stimuli. Extracellular HMGB1 contributes to the pathogenesis of numerous chronic inflammatory and autoimmune diseases, including sepsis, rheumatoid arthritis, atherosclerosis, chronic kidney disease, systemic lupus erythematosus (SLE), as well as cancer pathogenesis. Interaction of released HMGB1 with the cell-surface receptor for advanced glycation end products (RAGE) is one of the main signaling pathways triggering these diseases. It has been also demonstrated that the inhibition of the HMGB1-RAGE interaction represents a promising approach for the modulation of the inflammatory and tumor-facilitating activity of HMGB1. In this review we describe various approaches recently proposed in the literature to inhibit HMGB1 and the related inflammatory processes, especially focusing on the block of RAGE-HMGB1 signaling. Several strategies are based on molecules which mainly interact with RAGE as competitive antagonists of HMGB1. As an alternative, encouraging results have been obtained with HMGB1-targeting, leading to the identification of compounds that directly bind to HMGB1, ranging from small natural or synthetic molecules, such as glycyrrhizin and gabexate mesilate, to HMGB1-specific antibodies, peptides, proteins as well as bent DNA-based duplexes. Future perspectives are discussed in the light of the overall body of knowledge acquired by a large number of research groups operating in different but related fields. (C) 2013 Elsevier Inc. All rights reserved.
HMGB1 (High-Mobility Group Box-1) is a nuclear protein that acts as an architectural chromatin-binding factor involved in the maintenance of nucleosome structure and regulation of gene transcription. It can be released into the extracellular milieu from immune and non-immune cells in response to various stimuli. Extracellular HMGB1 contributes to the pathogenesis of numerous chronic inflammatory and autoimmune diseases, including sepsis, rheumatoid arthritis, atherosclerosis, chronic kidney disease, systemic lupus erythematosus (SLE), as well as cancer pathogenesis. Interaction of released HMGB1 with the cell-surface receptor for advanced glycation end products (RAGE) is one of the main signaling pathways triggering these diseases. It has been also demonstrated that the inhibition of the HMGB1-RAGE interaction represents a promising approach for the modulation of the inflammatory and tumor-facilitating activity of HMGB1. In this review we describe various approaches recently proposed in the literature to inhibit HMGB1 and the related inflammatory processes, especially focusing on the block of RAGE-HMGB1 signaling. Several strategies are based on molecules which mainly interact with RAGE as competitive antagonists of HMGB1. As an alternative, encouraging results have been obtained with HMGB1-targeting, leading to the identification of compounds that directly bind to HMGB1, ranging from small natural or synthetic molecules, such as glycyrrhizin and gabexate mesilate, to HMGB1-specific antibodies, peptides, proteins as well as bent DNA-based duplexes. Future perspectives are discussed in the light of the overall body of knowledge acquired by a large number of research groups operating in different but related fields. (C) 2013 Elsevier Inc. All rights reserved.
An overview on HMGB1 inhibitors as potential therapeutic agents in HMGB1-related pathologies
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An overview on HMGB1 inhibitors as potential therapeutic agents in HMGB1-related pathologies
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Mai A, Rotili D, Tarantino D, Ornaghi P, Tosi F, Vicidomini C, Sbardella G, Nebbioso A, Miceli M, Altucci L, Filetici P
* Small-molecule inhibitors of histone acetyltransferase activity: Identification and biological properties (508 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 16; 49(23): 6897-6907.
Impact Factor: 5.115
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* Small-molecule inhibitors of histone acetyltransferase activity: Identification and biological properties (508 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2006 Nov 16; 49(23): 6897-6907.
Impact Factor: 5.115
View Export to BibTeX Export to EndNote
1 Records (1 excluding Abstracts).
Total impact factor: 5.115 (5.115 excluding Abstracts).
Total 5 year impact factor: 5.504 (5.504 excluding Abstracts).
Total impact factor: 5.115 (5.115 excluding Abstracts).
Total 5 year impact factor: 5.504 (5.504 excluding Abstracts).
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