Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides (704 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 494-502.
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Paper type: Journal Article,
Impact factor: 2.863, 5-year impact factor: 2.675
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-10844289477&partnerID=40&md5=ed8d99643447599d36e22882d829f100
Keywords: Gh Peptides, Hsv-1, Signal Transduction Pathway, Activation Analysis, Cells, Enzyme Kinetics, Signaling, Stress Analysis, Viruses, Cascades, Extracellular Stimuli, Herpes, Mitogen-Activated Protein Kinase (mapk), Polypeptides, Dimer, Glycoprotein, Mitogen Activated Protein Kinase, Mitogen Activated Protein Kinase P38, Peptide Derivative, Stress Activated Protein Kinase, Virus Envelope Protein, Virus Glycoprotein, Animal Cell, Cell Activation, Cell Spreading, Conference Paper, Enzyme Activation, Eukaryote, Herpes Simplex Virus 1, Nonhuman, Peptide Synthesis, Phosphorylation, Virus Adsorption, Amino Acid Sequence, Cercopithecus Aethiops, Herpesvirus 1, Hydrophobicity, Map Kinase Signaling System, Molecular Sequence Data, Peptide Fragments, Vero Cells, Viral Envelope Proteins, Human Herpesvirus 1, Simplexvirus,
Affiliations:
*** IBB - CNR ***
Dipto. di Chim. Biologica and CIRPEB, Universita di Napoli Federico II, Naples, Italy
Dipartimento di Patologia Generale, Seconda Università di Napoli, Naples, Italy
CNR, Universita di Napoli Federico II, Naples, Italy
Dipto. di Medicina Sperimentale, Seconda Università di Napoli, Naples, Italy
References:
Not available.
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 494-502.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.863, 5-year impact factor: 2.675
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-10844289477&partnerID=40&md5=ed8d99643447599d36e22882d829f100
Keywords: Gh Peptides, Hsv-1, Signal Transduction Pathway, Activation Analysis, Cells, Enzyme Kinetics, Signaling, Stress Analysis, Viruses, Cascades, Extracellular Stimuli, Herpes, Mitogen-Activated Protein Kinase (mapk), Polypeptides, Dimer, Glycoprotein, Mitogen Activated Protein Kinase, Mitogen Activated Protein Kinase P38, Peptide Derivative, Stress Activated Protein Kinase, Virus Envelope Protein, Virus Glycoprotein, Animal Cell, Cell Activation, Cell Spreading, Conference Paper, Enzyme Activation, Eukaryote, Herpes Simplex Virus 1, Nonhuman, Peptide Synthesis, Phosphorylation, Virus Adsorption, Amino Acid Sequence, Cercopithecus Aethiops, Herpesvirus 1, Hydrophobicity, Map Kinase Signaling System, Molecular Sequence Data, Peptide Fragments, Vero Cells, Viral Envelope Proteins, Human Herpesvirus 1, Simplexvirus,
Affiliations:
*** IBB - CNR ***
Dipto. di Chim. Biologica and CIRPEB, Universita di Napoli Federico II, Naples, Italy
Dipartimento di Patologia Generale, Seconda Università di Napoli, Naples, Italy
CNR, Universita di Napoli Federico II, Naples, Italy
Dipto. di Medicina Sperimentale, Seconda Università di Napoli, Naples, Italy
References:
Not available.
Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides
Eukaryotic cells respond to extracellular stimuli, such as viruses, by recruiting signal transduction pathways, many of which are mediated through activation of distinct mitogen-activated protein kinase (MAPK) cascades and activation of transductional regulation factors. The best characterized of this pathway are the extracellular signal regulated Kinase (ERK), the c-Jun N-terminal kinase/stress activated protein kinase (JNK/SAPK), and the p38 MAPK cascade. Herpes simplex virus type 1 (HSV-1) encodes at least 11 envelope glycoproteins, which alone or in concert play different roles in viral adsorption, entry, cell-to-cell spread, and immune evasion. Of these proteins, three are designated glycoprotein B (gB), glycoprotein D (gD), and the gH/gL heterodimer, are clearly involved in attachment and entry, and therefore possible candidates in inducing early, cellular activation. Nevertheless, the precise role of each glycoprotein and the cellular factor involved remain elusive. The signal transduction pathways involved, and the outcome of cellular activation on viral entry or postentry events, are still to be elucidated. To better understand the role of signal transduction pathways and phosphorylation events in HSV-1 entry, synthetic peptides modeled on HSV-1 gH were synthesized and tested for MEK1-MEK2/MAPK cascade activation. Our results show a major involvement of the JNK pathway in the intracellular signal transmission after stimulation with gH HSV-1 peptides. (C) 2004 Wiley Periodicals, Inc.
Eukaryotic cells respond to extracellular stimuli, such as viruses, by recruiting signal transduction pathways, many of which are mediated through activation of distinct mitogen-activated protein kinase (MAPK) cascades and activation of transductional regulation factors. The best characterized of this pathway are the extracellular signal regulated Kinase (ERK), the c-Jun N-terminal kinase/stress activated protein kinase (JNK/SAPK), and the p38 MAPK cascade. Herpes simplex virus type 1 (HSV-1) encodes at least 11 envelope glycoproteins, which alone or in concert play different roles in viral adsorption, entry, cell-to-cell spread, and immune evasion. Of these proteins, three are designated glycoprotein B (gB), glycoprotein D (gD), and the gH/gL heterodimer, are clearly involved in attachment and entry, and therefore possible candidates in inducing early, cellular activation. Nevertheless, the precise role of each glycoprotein and the cellular factor involved remain elusive. The signal transduction pathways involved, and the outcome of cellular activation on viral entry or postentry events, are still to be elucidated. To better understand the role of signal transduction pathways and phosphorylation events in HSV-1 entry, synthetic peptides modeled on HSV-1 gH were synthesized and tested for MEK1-MEK2/MAPK cascade activation. Our results show a major involvement of the JNK pathway in the intracellular signal transmission after stimulation with gH HSV-1 peptides. (C) 2004 Wiley Periodicals, Inc.
Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides
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Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides
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View Export to BibTeX Export to EndNote
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Impact Factor: 5.155
View Export to BibTeX Export to EndNote
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Impact Factor: 5.52
View Export to BibTeX Export to EndNote
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Impact Factor: 3.379
View Export to BibTeX Export to EndNote
Innocenti A, Scozzafava A, Parkkila S, Puccetti L, De Simone G, Supuran CT
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Impact Factor: 2.531
View Export to BibTeX Export to EndNote
Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S
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Impact Factor: 4.399
View Export to BibTeX Export to EndNote
Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
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Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Impact Factor: 3.664
View Export to BibTeX Export to EndNote
Pailot A, D'Ambrosio K, Corbier C, Talfournier F, Branlant G
* Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (422 views)
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Impact Factor: 4.1
View Export to BibTeX Export to EndNote
Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* A new spot test for sulfhydryl-containing compounds (509 views)
Anal Biochem, 2006 Mar 14; 79(1-2): 610-611.
Impact Factor: 2.305
View Export to BibTeX Export to EndNote
Cappiello M, Alterio V, Amodeo P, Del Corso A, Scaloni A, Pedone C, Moschini R, De Donatis GM, De Simone G, Mura U
* Metal ion substitution in the catalytic site greatly affects the binding of sulfhydryl-containing compounds to leucyl aminopeptidase (998 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2006 Mar 14; 45(10): 3226-3234.
Impact Factor: 3.633
View Export to BibTeX Export to EndNote
Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S-I
* Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex (755 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Oct 7; 280(40): 34278-34287.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Esposito L, Daggett V
* Insight into ribonuclease A domain swapping by molecular dynamics unfolding simulations (626 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2005 Mar 8; 44(9): 3358-3368.
Impact Factor: 3.848
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (437 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
De Capua A, Del Gatto A, Zaccaro L, Saviano G, Carlucci A, Livigni A, Gedressi C, Tancredi T, Pedone C, Saviano M
* A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study (764 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 459-466.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Mansi R, Tesauro D, De Capua A, Fattorusso R, Carac C, Aloj L, Benedetti E, Morelli G
* Peptide-chelating agent conjugate for selective targeting of somatostatin receptor type 1: Synthesis and characterization (515 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 527-534.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
Galdiero M, Vitiello M, Galdiero S
* Eukaryotic cell signaling and transcriptional activation induced by bacterial porins (754 views)
Fems Microbiology Letters (ISSN: 0378-1097), 2003 Sep 12; 226(1): 57-64.
Impact Factor: 1.932
View Export to BibTeX Export to EndNote
Garzillo AM, Colao MC, Buonocore V, Oliva R, Falcigno L, Saviano M, Santoro AM, Zappala R, Bonomo RP, Bianco C, Giardina P, Palmieri G, Sannia G
* Structural and kinetic characterization of native laccases from Pleurotas ostreatus, Rigidoporus lignosus, and Trametes trogii (666 views)
Journal Of Protein Chemistry (ISSN: 0277-8033), 2001 Apr; 20(3): 191-201.
Impact Factor: 1.021
View Export to BibTeX Export to EndNote
Bonomo RP, Boudet AM, Cozzolino R, Rizzarelli E, Santoro AM, Sterjiades R, Zappalà R
A comparative study of two isoforms of laccase secreted by the 'white- rot' fungus Rigidoporus lignosus, exhibiting significant structural and functional differences (439 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 1998 Sep; 71(3-4): 205-211.
Impact Factor: 1.162
View Export to BibTeX Export to EndNote
22 Records (22 excluding Abstracts).
Total impact factor: 75.321 (75.321 excluding Abstracts).
Total 5 year impact factor: 74.785 (74.785 excluding Abstracts).
Total impact factor: 75.321 (75.321 excluding Abstracts).
Total 5 year impact factor: 74.785 (74.785 excluding Abstracts).
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