Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System (918 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Apr 10; 51(14): 3121-3128.
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Paper type: Journal Article,
Impact factor: 3.377, 5-year impact factor: 3.168
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84859560868&partnerID=40&md5=51ee4d2420684f323b4d435adf61ed88
Keywords: Complex Mechanisms, Ectodomain, Herpes Simplex Virus Type 1, Host Cells, Membrane Fusion, Micellar Environment, Solution Structures, Structure And Orientation, Amino Acids, Biomimetics, Cell Membranes, Glycoproteins, Dodecylphosphorylcholine, Membrane Protein, Unclassified Drug, Article, Crystal Structure, Heteronuclear Single Quantum Coherence, Mutation, Nonhuman, Priority Journal, Protein Domain, Protein Structure, Proton Nuclear Magnetic Resonance, Virus Envelope, Herpesvirus 1, Biomolecular, Peptides, Protein Conformation, Structure-Activity Relationship, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Department of Environmental Sciences, Second University of Naples, Caserta, Italy
Department of Experimental Medicine, Second University of Naples, Napoli, Italy
References:
Not available.
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Apr 10; 51(14): 3121-3128.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.377, 5-year impact factor: 3.168
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84859560868&partnerID=40&md5=51ee4d2420684f323b4d435adf61ed88
Keywords: Complex Mechanisms, Ectodomain, Herpes Simplex Virus Type 1, Host Cells, Membrane Fusion, Micellar Environment, Solution Structures, Structure And Orientation, Amino Acids, Biomimetics, Cell Membranes, Glycoproteins, Dodecylphosphorylcholine, Membrane Protein, Unclassified Drug, Article, Crystal Structure, Heteronuclear Single Quantum Coherence, Mutation, Nonhuman, Priority Journal, Protein Domain, Protein Structure, Proton Nuclear Magnetic Resonance, Virus Envelope, Herpesvirus 1, Biomolecular, Peptides, Protein Conformation, Structure-Activity Relationship, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Napoli, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, Italy
Department of Environmental Sciences, Second University of Naples, Caserta, Italy
Department of Experimental Medicine, Second University of Naples, Napoli, Italy
References:
Not available.
Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System
Glycoprotein H (gH) of the herpes simplex virus type 1 is involved in the complex mechanism of membrane fusion of the viral envelope with host cells. The virus requires four glycoproteins (gB, gD, gH, gL) to execute fusion and the role played by gH remains mysterious. Mutational studies have revealed several regions of gH ectodomain required for fusion and identified the segment from amino acid 625 to 644 as the most fusogenic region. Here, we studied the behavior in a membrane-mimicking DPC micellar environment of a peptide encompassing this region (gH625-644) and determined its NMR solution structure and its orientation within the micelles.
Glycoprotein H (gH) of the herpes simplex virus type 1 is involved in the complex mechanism of membrane fusion of the viral envelope with host cells. The virus requires four glycoproteins (gB, gD, gH, gL) to execute fusion and the role played by gH remains mysterious. Mutational studies have revealed several regions of gH ectodomain required for fusion and identified the segment from amino acid 625 to 644 as the most fusogenic region. Here, we studied the behavior in a membrane-mimicking DPC micellar environment of a peptide encompassing this region (gH625-644) and determined its NMR solution structure and its orientation within the micelles.
Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System
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Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.446
View Export to BibTeX Export to EndNote
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Impact Factor: 3.11
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Browne H, Pedone C, Galdiero M
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Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Sep 5; 280(31): 28632-28643.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, D'Isanto M, Di Niola E, Peluso L, Raieta K, Pedone C, Galdiero M, Benedetti E
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Impact Factor: 2.863
View Export to BibTeX Export to EndNote
18 Records (18 excluding Abstracts).
Total impact factor: 72.979 (72.979 excluding Abstracts).
Total 5 year impact factor: 67.822 (67.822 excluding Abstracts).
Total impact factor: 72.979 (72.979 excluding Abstracts).
Total 5 year impact factor: 67.822 (67.822 excluding Abstracts).
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