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Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Provitera Paxton
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
(*)
Provitera Paxton:
Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Taschenbuch

2008, ISBN: 3639025989

ID: 9734094223

[EAN: 9783639025989], Neubuch, [PU: Vdm Verlag Okt 2008], This item is printed on demand - Print on Demand Titel. - HIV has taken the lives of over twenty million people with an additional forty million people currently infected. During the viral life-cycle, an HIV protein, Gag, assembles at the host membrane, specifically at lipid raft regions, at very high concentrations leading to viral particle budding. During a subsequent phase, maturation, Gag is processed into four proteins, matrix (MA), capsid (CA), nucleocapsid (NC) and p6. CA, the major dimerazation domain within Gag, forms the viral core that encapsulates the viral RNA and accessory proteins. Interestingly, within CA is a 20 amino acid stretch of conserved residues, the Major Homology Region (MHR), which form a tightly packed amphipathic helix. Here we have analyzed the membrane binding of the closely related EIAV MA, myristoylated HIV-1 Gag, an MHR deletion mutant of HIV-1 Gag, and a non-myristoylated form of HIV-1 Gag to determine the roles of the multiple exposure faces of MA, myristoylation, and the MHR and the viral particle assembly sequence of HIV-1. Furthermore, we looked at the MHR as a possible drug target by membrane and RNA binding along with aggregate dissociation in the presence of a peptide form of the MHR. 168 pp. Englisch

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Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Provitera Paxton
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ISBN: 9783639025989

ID: d08599e3290731116b2a2f5775e8f4b6

Studies on Gag Membrane Binding and HIV-1 Viral Assembly HIV has taken the lives of over twenty million people with an additional forty million people currently infected. During the viral life-cycle, an HIV protein, Gag, assembles at the host membrane, specifically at lipid raft regions, at very high concentrations leading to viral particle budding. During a subsequent phase, maturation, Gag is processed into four proteins, matrix (MA), capsid (CA), nucleocapsid (NC) and p6. CA, the major dimerazation domain within Gag, forms the viral core that encapsulates the viral RNA and accessory proteins. Interestingly, within CA is a 20 amino acid stretch of conserved residues, the Major Homology Region (MHR), which form a tightly packed amphipathic helix. Here we have analyzed the membrane binding of the closely related EIAV MA, myristoylated HIV-1 Gag, an MHR deletion mutant of HIV-1 Gag, and a non-myristoylated form of HIV-1 Gag to determine the roles of the multiple exposure faces of MA, myristoylation, and the MHR and the viral particle assembly sequence of HIV-1. Furthermore, we looked at the MHR as a possible drug target by membrane and RNA binding along with aggregate dissociation in the presence of a peptide form of the MHR. Bücher / Fremdsprachige Bücher / Englische Bücher 978-3-639-02598-9, VDM Verlag

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Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Provitera, Paxton
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Provitera, Paxton:
Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Taschenbuch

2008, ISBN: 9783639025989

[ED: Taschenbuch / Paperback], [PU: VDM Verlag Dr. Müller], HIV has taken the lives of over twenty million people with an additional forty million people currently infected. During the viral life-cycle, an HIV protein, Gag, assembles at the host membrane, specifically at lipid raft regions, at very high concentrations leading to viral particle budding. During a subsequent phase, maturation, Gag is processed into four proteins, matrix (MA), capsid (CA), nucleocapsid (NC) and p6. CA, the major dimerazation domain within Gag, forms the viral core that encapsulates the viral RNA and accessory proteins. Interestingly, within CA is a 20 amino acid stretch of conserved residues, the Major Homology Region (MHR), which form a tightly packed amphipathic helix. Here we have analyzed the membrane binding of the closely related EIAV MA, myristoylated HIV-1 Gag, an MHR deletion mutant of HIV-1 Gag, and a non-myristoylated form of HIV-1 Gag to determine the roles of the multiple exposure faces of MA, myristoylation, and the MHR and the viral particle assembly sequence of HIV-1. Furthermore, we looked at the MHR as a possible drug target by membrane and RNA binding along with aggregate dissociation in the presence of a peptide form of the MHR., [SC: 0.00], Neuware, gewerbliches Angebot, [GW: 235g]

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(*) Derzeit vergriffen bedeutet, dass dieser Titel momentan auf keiner der angeschlossenen Plattform verfügbar ist.
Studies on Gag Membrane Binding and HIV-1 Viral Assembly
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
(*)
Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Taschenbuch

2008, ISBN: 9783639025989

[ED: Taschenbuch / Paperback], [PU: VDM Verlag Dr. Müller], HIV has taken the lives of over twenty million people with an additional forty million people currently infected. During the viral life-cycle, an HIV protein, Gag, assembles at the host membrane, specifically at lipid raft regions, at very high concentrations leading to viral particle budding. During a subsequent phase, maturation, Gag is processed into four proteins, matrix (MA), capsid (CA), nucleocapsid (NC) and p6. CA, the major dimerazation domain within Gag, forms the viral core that encapsulates the viral RNA and accessory proteins. Interestingly, within CA is a 20 amino acid stretch of conserved residues, the Major Homology Region (MHR), which form a tightly packed amphipathic helix. Here we have analyzed the membrane binding of the closely related EIAV MA, myristoylated HIV-1 Gag, an MHR deletion mutant of HIV-1 Gag, and a non-myristoylated form of HIV-1 Gag to determine the roles of the multiple exposure faces of MA, myristoylation, and the MHR and the viral particle assembly sequence of HIV-1. Furthermore, we looked at the MHR as a possible drug target by membrane and RNA binding along with aggregate dissociation in the presence of a peptide form of the MHR., [SC: 0.00], Neuware, gewerbliches Angebot, [GW: 235g]

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Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Provitera Paxton
Vergriffenes Buch, derzeit bei uns nicht verfügbar.
(*)
Provitera Paxton:
Studies on Gag Membrane Binding and HIV-1 Viral Assembly - Taschenbuch

2008, ISBN: 3639025989

ID: 13788091871

[EAN: 9783639025989], Neubuch, This item is printed on demand for shipment within 3 working days., [PU: VDM Verlag Dr. Müller, Saarbrücken]

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Details zum Buch
Studies on Gag Membrane Binding and HIV-1 Viral Assembly

HIV has taken the lives of over twenty million people with an additional forty million people currently infected. During the viral life-cycle, an HIV protein, Gag, assembles at the host membrane, specifically at lipid raft regions, at very high concentrations leading to viral particle budding. During a subsequent phase, maturation, Gag is processed into four proteins, matrix (MA), capsid (CA), nucleocapsid (NC) and p6. CA, the major dimerazation domain within Gag, forms the viral core that encapsulates the viral RNA and accessory proteins. Interestingly, within CA is a 20 amino acid stretch of conserved residues, the Major Homology Region (MHR), which form a tightly packed amphipathic helix. Here we have analyzed the membrane binding of the closely related EIAV MA, myristoylated HIV-1 Gag, an MHR deletion mutant of HIV-1 Gag, and a non-myristoylated form of HIV-1 Gag to determine the roles of the multiple exposure faces of MA, myristoylation, and the MHR and the viral particle assembly sequence of HIV-1. Furthermore, we looked at the MHR as a possible drug target by membrane and RNA binding along with aggregate dissociation in the presence of a peptide form of the MHR.

Detailangaben zum Buch - Studies on Gag Membrane Binding and HIV-1 Viral Assembly


EAN (ISBN-13): 9783639025989
ISBN (ISBN-10): 3639025989
Taschenbuch
Erscheinungsjahr: 2008
Herausgeber: VDM Verlag
168 Seiten
Gewicht: 0,267 kg
Sprache: eng/Englisch

Buch in der Datenbank seit 07.02.2009 22:54:39
Buch zuletzt gefunden am 13.05.2017 07:29:47
ISBN/EAN: 3639025989

ISBN - alternative Schreibweisen:
3-639-02598-9, 978-3-639-02598-9


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