Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity (541 views)
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2012; 7: 2361-2371.
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Paper type: Journal Article,
Impact factor: 3.463, 5-year impact factor: 4.027
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870331075&partnerID=40&md5=9fa398d8e04f2028cd2717dd16c2c95d
Keywords: Complementary-Peptide, Porin, Rational Design, Activating Protein I, Cell Protein, Complementary Dna, Immunoglobulin Enhancer Binding Protein, Interleukin 6, Mitogen Activated Protein Kinase, Polypeptide Antibiotic Agent, Tumor Necrosis Factor Alpha, Unclassified Drug, Antibacterial Activity, Article, Bacterium Identification, Binding Affinity, Binding Site, Controlled Study, Cytokine Production, Disease Association, Drug Determination, Drug Protein Binding, Drug Synthesis, Enzyme Linked Immunosorbent Assay, Feedback System, Gel Filtration, Haemophilus Infection, Haemophilus Influenzae Type B, Molecular Dynamics, Molecular Pathology, Nonhuman, Protein Function, Protein Secretion, Signal Transduction, Algorithms, Bacterial Proteins, Catalytic Domain, Chromatography, Map Kinase Signaling System, Models, Biological, Nf-Kappa B, Salmonella Typhimurium, Transcription Factor Ap-1, Tumor Necrosis Factor-Alpha, U937 Cells, Bacteria (microorganisms), Haemophilus Influenzae Serotype B,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, CIRPeB and IBB CNR, University of Naples 'Federico II', Napoli, Italy
Department of Experimental Medicine, II University of Naples, Napoli, Italy
References:
Not available.
Int J Nanomed (ISSN: 1178-2013, 1176-9114, 1178-2013electronic), 2012; 7: 2361-2371.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.463, 5-year impact factor: 4.027
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870331075&partnerID=40&md5=9fa398d8e04f2028cd2717dd16c2c95d
Keywords: Complementary-Peptide, Porin, Rational Design, Activating Protein I, Cell Protein, Complementary Dna, Immunoglobulin Enhancer Binding Protein, Interleukin 6, Mitogen Activated Protein Kinase, Polypeptide Antibiotic Agent, Tumor Necrosis Factor Alpha, Unclassified Drug, Antibacterial Activity, Article, Bacterium Identification, Binding Affinity, Binding Site, Controlled Study, Cytokine Production, Disease Association, Drug Determination, Drug Protein Binding, Drug Synthesis, Enzyme Linked Immunosorbent Assay, Feedback System, Gel Filtration, Haemophilus Infection, Haemophilus Influenzae Type B, Molecular Dynamics, Molecular Pathology, Nonhuman, Protein Function, Protein Secretion, Signal Transduction, Algorithms, Bacterial Proteins, Catalytic Domain, Chromatography, Map Kinase Signaling System, Models, Biological, Nf-Kappa B, Salmonella Typhimurium, Transcription Factor Ap-1, Tumor Necrosis Factor-Alpha, U937 Cells, Bacteria (microorganisms), Haemophilus Influenzae Serotype B,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, CIRPeB and IBB CNR, University of Naples 'Federico II', Napoli, Italy
Department of Experimental Medicine, II University of Naples, Napoli, Italy
References:
Not available.
Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity
Haemophilus influenzae type b (Hib) is one of the leading causes of invasive bacterial infection in young children. It is characterized by inflammation that is mainly mediated by cytokines and chemokines. One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. A synthetic peptide corresponding to loop L7 of the porin activates JNK and p38 mitogen-activated protein kinase (MAPK) pathways. We report a novel use of the complementary peptide approach to design a peptide that is able to bind selectively to the protein P2, thereby reducing its activity. This work provides insights into essential molecular details of P2 that may affect the pathogenesis of Hib infections where interruption of the signaling cascade could represent an attractive therapeutic strategy.
Haemophilus influenzae type b (Hib) is one of the leading causes of invasive bacterial infection in young children. It is characterized by inflammation that is mainly mediated by cytokines and chemokines. One of the most abundant components of the Hib outer membrane is the P2 porin, which has been shown to induce the release of several inflammatory cytokines. A synthetic peptide corresponding to loop L7 of the porin activates JNK and p38 mitogen-activated protein kinase (MAPK) pathways. We report a novel use of the complementary peptide approach to design a peptide that is able to bind selectively to the protein P2, thereby reducing its activity. This work provides insights into essential molecular details of P2 that may affect the pathogenesis of Hib infections where interruption of the signaling cascade could represent an attractive therapeutic strategy.
Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity
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Peptides complementary to the active loop of porin P2 from Haemophilus influenzae modulate its activity
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Impact Factor: 3.617
View Export to BibTeX Export to EndNote
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Impact Factor: 4.278
View Export to BibTeX Export to EndNote
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Impact Factor: 2.013
View Export to BibTeX Export to EndNote
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Impact Factor: 4.622
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 7.258
View Export to BibTeX Export to EndNote
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Impact Factor: 2.15
View Export to BibTeX Export to EndNote
21 Records (21 excluding Abstracts).
Total impact factor: 69.629 (69.629 excluding Abstracts).
Total 5 year impact factor: 69.193 (69.193 excluding Abstracts).
Total impact factor: 69.629 (69.629 excluding Abstracts).
Total 5 year impact factor: 69.193 (69.193 excluding Abstracts).
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