User:Rua Alhouri/Sandbox 1 - Revision history

Rua Alhouri at 13:32, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 13:32:46 GMT

←Older revision		Revision as of 13:32, 8 December 2015
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	== Influenza virus Glycoproteins==		== Influenza virus Glycoproteins==
-	<Structure load='~~5E2Y~~' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />	+	<Structure load='2HMG' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />

	== Overview of influenza ==		== Overview of influenza ==

Rua Alhouri at 05:23, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 05:23:52 GMT

←Older revision		Revision as of 05:23, 8 December 2015
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	== The M1 protien ==		== The M1 protien ==

-	The M1 protein is one of the major components of the virus by playing an essential role in viral budding. It also forms an intermediate layer between the viral envelope containing the integral membrane proteins and the genomic ribonucleoproteins (RN). The structure of M1 protein has two domain protein with an N-terminal domain containing residues 1–164 and a C-terminal domain with residues 165–252 (Arzt et.al ,2003). The N terminus of M1 has a polybasic sequence at the one side of the molecule, this polybasic sequence sometimes is beta strand and sometimes is alpha helical (Ruigrok et.al, 1999).	+	The M1 protein is one of the major components of the virus by playing an essential role in viral budding. It also forms an intermediate layer between the viral envelope containing the integral membrane proteins and the genomic ribonucleoproteins (RN). The structure of M1 protein has two domain protein with an N-terminal domain containing residues 1–164 and a C-terminal domain with residues 165–252 (Arzt et.al, 2003). The N terminus of M1 has a polybasic sequence at the one side of the molecule, this polybasic sequence sometimes is beta strand and sometimes is alpha helical (Ruigrok et.al, 1999).
-		+
-	The M1 protein ~~function~~ as self ~~polymerisation~~, M1 proteins must bind to both the membrane ~~as well as~~ the viral RNA simultaneously~~. However, even though the M1 protein binds to the viral RNA, the binding is not specific~~. Some other functions include a role in the export by the viral ribonucleoproteins from the host cell nucleus, ~~M1 protein enters~~ the nucleus through its own nuclear localization signal which is needed for the export for the newly formed ribonucleoproteins (Arzt et.al, 2003). ~~There is a protein~~ that involved in this export process, NS2 or NEP for nuclear export protein inhibition of viral transcription, ~~and~~ in the virus assembly and budding~~, which~~ is a form of asexual reproduction that the influenza virus practices (Holsinger et. al 1994).	+	The M1 protein functions as self-polymerization, M1 proteins must bind to both the membrane and the viral RNA simultaneously. Some other functions include: a role in the export by the viral ribonucleoproteins from the host cell nucleus, and entering the nucleus through its own nuclear localization signal, which is needed for the export for the newly formed ribonucleoproteins (Arzt et.al, 2003). The proteins that are involved in this export process are the NS2 or NEP proteins, for nuclear export protein inhibition of viral transcription, as well as partaking in the virus assembly and budding. This is done in the form of asexual reproduction that the influenza virus practices (Holsinger et. al 1994).

	== The M2 protien ==		== The M2 protien ==
-	The structure of the M2 protein consists of a four-helix bundle with a 25-degree tilt. Since the H protein undergoes a conformational change, M2 proteins act as an ion channel by allowing the proton ions to penetrate the viron (Pinto, Lamb 2006). The pumping of the protons will weakens the interaction between the viral matrix proteins and the viral RNA and nucleoproteins. The eight segments of the viral ribonuclease are then released into the cytoplasm and exported to the nucleus. The ability of opening and closing the M2 ion channel depends on the action of single transmembrane domain residue Trp 41. When the pH exceeds pH 7, the channel will be closed, and when the pH is lower than pH 6.5, the channel will be opened. Trp 41 is a key residue in opening and closing ion channel pore (Pinto, Lamb 2006).	+	The structure of the M2 protein consists of a four-helix bundle with a 25-degree tilt. Since the H protein undergoes a conformational change, M2 proteins act as an ion channel by allowing the proton ions to penetrate the viron (Pinto, Lamb 2006). The pumping of the protons will weakens the interaction between the viral matrix proteins and the viral RNA and nucleoproteins. The eight segments of the viral ribonuclease are then released into the cytoplasm and exported to the nucleus. The ability of opening and closing the M2 ion channel depends on the action of single transmembrane domain residue Trp 41. When the pH exceeds pH 7, the channel will be closed, and when the pH is lower than pH 6.5, the channel will be opened. Trp 41 is a key residue in opening and closing ion channel pore (Pinto, Lamb 2006).

	==Influenza treatment ==		==Influenza treatment ==

Rua Alhouri at 05:20, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 05:20:06 GMT

←Older revision		Revision as of 05:20, 8 December 2015
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	== Influenza virus Glycoproteins==		== Influenza virus Glycoproteins==
-	<Structure load='~~2VIU~~' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />	+	<Structure load='5E2Y' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />

	== Overview of influenza ==		== Overview of influenza ==

Rua Alhouri at 05:17, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 05:17:21 GMT

←Older revision		Revision as of 05:17, 8 December 2015
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	<Structure load='2015-12-07 at 11.11.54 PM.jpeg' size='400' frame='true' align='X' caption='schematic diagram of influenza virus depicting the structure of glycoproteins ' scene='Influenza glycoprotiens' />		<Structure load='2015-12-07 at 11.11.54 PM.jpeg' size='400' frame='true' align='X' caption='schematic diagram of influenza virus depicting the structure of glycoproteins ' scene='Influenza glycoprotiens' />
	<scene name='Influenza glycoprotiens'>Influenza glycoprotiens</scene>		<scene name='Influenza glycoprotiens'>Influenza glycoprotiens</scene>
		+
		+	<Structure load='22015-12-07_at_11.58.30_PM.jpeg' size='400' frame='true' align='X' caption='Figure 3. A closer look on the structure of H1 and H2 subunits of Hemagglutinin protein.' scene='H1 and H2' />
		+	<scene name='H1 and H2'>H1 and H2</scene>
		+
		+	<Structure load='2015-12-07_at_11.49.01_PM.jpeg' size='400' frame='true' align='X' caption='Figure 4. The change of Hemagglutinin structure and subunits arrangement due to the drop of PH level. A) the separation of H1 globular protiens due to the drop of pH level. B) the separation of H1 and H2 ' scene='pH induced conformational change' />
		+	<scene name='pH induced conformational change'>pH induced conformational change</scene>

Rua Alhouri at 05:10, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 05:10:34 GMT

←Older revision		Revision as of 05:10, 8 December 2015
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	== Influenza virus Glycoproteins==		== Influenza virus Glycoproteins==
	<Structure load='2VIU' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />		<Structure load='2VIU' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />
-	<Structure load='2015-12-07 at 11.11.54 PM.jpeg' size='400' frame='true' align='X' caption='schematic diagram of influenza virus depicting the structure of glycoproteins ' scene='Influenza glycoprotiens' />	+
	== Overview of influenza ==		== Overview of influenza ==
	The influenza virus is a common virus found in many places around the world and comes in three different subtypes A,B, and C. Influenza A subtype is the most infectious subtype. It causes pandemics with significant mortalities in affected young people for that it has a wide host range including human, pigs, horses, and birds. All the three influenza subtypes contains the same segmental genome and enveloped glycoprotein. The virus is spherically shaped, ranging from 80 to 120 nm in diameter. The viral particles contain 3 proteins on their outer surface, called: H, N, and M2. It also contains a matrix protein M1 below the outer surface. Each protein has a different function that helps the virus to penetrate and enter the animal’s host cell. The virus also contains eight segments of single stranded negative polarity RNA. Once the virus infects the cell, it will travel to the nucleus to replicate its genome, then the viral mRNA will transfer to the cytoplasm to be translated into viral proteins. Once all the viral proteins are formed, they will all aggregate and get released from the host cell (Shors, 2013).		The influenza virus is a common virus found in many places around the world and comes in three different subtypes A,B, and C. Influenza A subtype is the most infectious subtype. It causes pandemics with significant mortalities in affected young people for that it has a wide host range including human, pigs, horses, and birds. All the three influenza subtypes contains the same segmental genome and enveloped glycoprotein. The virus is spherically shaped, ranging from 80 to 120 nm in diameter. The viral particles contain 3 proteins on their outer surface, called: H, N, and M2. It also contains a matrix protein M1 below the outer surface. Each protein has a different function that helps the virus to penetrate and enter the animal’s host cell. The virus also contains eight segments of single stranded negative polarity RNA. Once the virus infects the cell, it will travel to the nucleus to replicate its genome, then the viral mRNA will transfer to the cytoplasm to be translated into viral proteins. Once all the viral proteins are formed, they will all aggregate and get released from the host cell (Shors, 2013).
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	Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035		Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035
		+
		+	== Figures ==
		+	<Structure load='2015-12-07 at 11.11.54 PM.jpeg' size='400' frame='true' align='X' caption='schematic diagram of influenza virus depicting the structure of glycoproteins ' scene='Influenza glycoprotiens' />
		+	<scene name='Influenza glycoprotiens'>Influenza glycoprotiens</scene>

Rua Alhouri at 05:07, 8 December 2015

Rua Alhouri — Tue, 08 Dec 2015 05:07:23 GMT

←Older revision		Revision as of 05:07, 8 December 2015
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	== Influenza virus Glycoproteins==		== Influenza virus Glycoproteins==
	<Structure load='2VIU' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />		<Structure load='2VIU' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />
-		+	<Structure load='2015-12-07 at 11.11.54 PM.jpeg' size='400' frame='true' align='X' caption='schematic diagram of influenza virus depicting the structure of glycoproteins ' scene='Influenza glycoprotiens' />
	== Overview of influenza ==		== Overview of influenza ==
	The influenza virus is a common virus found in many places around the world and comes in three different subtypes A,B, and C. Influenza A subtype is the most infectious subtype. It causes pandemics with significant mortalities in affected young people for that it has a wide host range including human, pigs, horses, and birds. All the three influenza subtypes contains the same segmental genome and enveloped glycoprotein. The virus is spherically shaped, ranging from 80 to 120 nm in diameter. The viral particles contain 3 proteins on their outer surface, called: H, N, and M2. It also contains a matrix protein M1 below the outer surface. Each protein has a different function that helps the virus to penetrate and enter the animal’s host cell. The virus also contains eight segments of single stranded negative polarity RNA. Once the virus infects the cell, it will travel to the nucleus to replicate its genome, then the viral mRNA will transfer to the cytoplasm to be translated into viral proteins. Once all the viral proteins are formed, they will all aggregate and get released from the host cell (Shors, 2013).		The influenza virus is a common virus found in many places around the world and comes in three different subtypes A,B, and C. Influenza A subtype is the most infectious subtype. It causes pandemics with significant mortalities in affected young people for that it has a wide host range including human, pigs, horses, and birds. All the three influenza subtypes contains the same segmental genome and enveloped glycoprotein. The virus is spherically shaped, ranging from 80 to 120 nm in diameter. The viral particles contain 3 proteins on their outer surface, called: H, N, and M2. It also contains a matrix protein M1 below the outer surface. Each protein has a different function that helps the virus to penetrate and enter the animal’s host cell. The virus also contains eight segments of single stranded negative polarity RNA. Once the virus infects the cell, it will travel to the nucleus to replicate its genome, then the viral mRNA will transfer to the cytoplasm to be translated into viral proteins. Once all the viral proteins are formed, they will all aggregate and get released from the host cell (Shors, 2013).

Rua Alhouri at 21:04, 7 December 2015

Rua Alhouri — Mon, 07 Dec 2015 21:04:30 GMT

Rua Alhouri at 21:01, 7 December 2015

Rua Alhouri — Mon, 07 Dec 2015 21:01:16 GMT

←Older revision		Revision as of 21:01, 7 December 2015
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	The H2 portion of H0 is called membrane-spanning anchor and it is directly involved in the fusion mechanism. H2 has a hairpin structure composed by two antiparallel alpha-helices. The C- terminal of H2 is embedded in the viral membrane while the N-terminal end contains 10 hydrophobic amino acid forming the fusion peptide (Proteopedia, 2011).		The H2 portion of H0 is called membrane-spanning anchor and it is directly involved in the fusion mechanism. H2 has a hairpin structure composed by two antiparallel alpha-helices. The C- terminal of H2 is embedded in the viral membrane while the N-terminal end contains 10 hydrophobic amino acid forming the fusion peptide (Proteopedia, 2011).

-	When H protein attaches to sialic acid residues of the ciliated columnar epithelial cell lining the sinuses and airways, the bound virus is endocytosed by the cell and the virions enter the cell within the endosomal vesicle. Then the endosomal vesicle pH level drops and reaches about 5.5 due to the pumping of protons inside the vesicle by the M2 ions channel. As a result, the H1 protein shifts its position, allowing the H2 protein to become embedded in the host cell membrane. Additionally, the C-terminus embedded in the viral membrane rearranges, bringing the two membranes closer together and facilitation fusion (Wilson et. al 1981). The pH induced conformational changes are partially but not completely reversible. As the pH decrease to 5.5, the three globular heads start to dissociate due to the protonation of relevant H protein residues. the change in pH facilitate the releasing of the fusion peptides. Also at low pH the short and long alpha-helix are separated(Thoennes et.al 2008). The shifting of H1 subunit plays an important role in H mediated membrane fusion , H1 protein helps the membrane attachment and fusion, which results in the release of viral RNA’s into the cytoplasm and then into the cell’s nucleus for RNA replication (Racanilllo, 2009)	+	When H protein attaches to sialic acid residues of the ciliated columnar epithelial cell lining the sinuses and airways, the bound virus is endocytosed by the cell and the virions enter the cell within the endosomal vesicle. Then the endosomal vesicle pH level drops and reaches about 5.5 due to the pumping of protons inside the vesicle by the M2 ions channel. As a result, the H1 protein shifts its position, allowing the H2 protein to become embedded in the host cell membrane. Additionally, the C-terminus embedded in the viral membrane rearranges, bringing the two membranes closer together and facilitation fusion (Wilson et. al 1981). The pH induced conformational changes are partially but not completely reversible. As the pH decrease to 5.5, the three globular heads start to dissociate due to the protonation of relevant H protein residues. the change in pH facilitate the releasing of the fusion peptides. Also at low pH the short and long alpha-helix are separated(Thoennes et.al 2008). The shifting of H1 subunit plays an important role in H mediated membrane fusion , H1 protein helps the membrane attachment and fusion, which results in the release of viral RNA’s into the cytoplasm and then into the cell’s nucleus for RNA replication (Racanilllo, 2009).

	== The Neuraminidase (N) protien ==		== The Neuraminidase (N) protien ==

Rua Alhouri at 20:57, 7 December 2015

Rua Alhouri — Mon, 07 Dec 2015 20:57:11 GMT

←Older revision		Revision as of 20:57, 7 December 2015
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	== Influenza virus Glycoproteins==		== Influenza virus Glycoproteins==
-		+	<Structure load='2VIU' size='400' frame='true' align='X' caption='Influenza Hemagglutinin protein ' scene='Hemagglutinin' />

	== Overview of influenza ==		== Overview of influenza ==
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	Wilson, I., Skehel, J., & Wiley, D. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 289(5796), 366.		Wilson, I., Skehel, J., & Wiley, D. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 289(5796), 366.
	Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035		Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035
-
-	{{STRUCTURE_1dq8\| right\| PDB=1dq8 \| SCENE=Hemagglutinin /1dq8_starting_scene/1 \|CAPTION= Crystal Structure of Hemagglutinin protein, [[2VIU]] }}

Rua Alhouri at 20:45, 7 December 2015

Rua Alhouri — Mon, 07 Dec 2015 20:45:48 GMT

←Older revision		Revision as of 20:45, 7 December 2015
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	Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035		Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035

-	{{STRUCTURE_1dq8\| right\| PDB=1dq8 \| SCENE=~~HMG-CoA_Reductase~~/1dq8_starting_scene/1 \|CAPTION= Crystal Structure of ~~Human HMG-CoA Reductase Catalytic Domain~~, [[~~1dq8~~]] }}	+	{{STRUCTURE_1dq8\| right\| PDB=1dq8 \| SCENE=Hemagglutinin /1dq8_starting_scene/1 \|CAPTION= Crystal Structure of Hemagglutinin protein, [[2VIU]] }}

←Older revision		Revision as of 21:04, 7 December 2015
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	<references/>		<references/>
	AArzt, S., Petit, I., Burmeister, W. P., Ruigrok, R. W. H., & Baudin, F. (2004). Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2). Virus Research, 99(2), 115-119. doi:http://dx.doi.org/10.1016/j.virusres.2003.10.010		AArzt, S., Petit, I., Burmeister, W. P., Ruigrok, R. W. H., & Baudin, F. (2004). Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2). Virus Research, 99(2), 115-119. doi:http://dx.doi.org/10.1016/j.virusres.2003.10.010
		+
	Gray, C., & Tamm, L. K. (1998). pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Protein Science : A Publication of the Protein Society, 7(11), 2359.		Gray, C., & Tamm, L. K. (1998). pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Protein Science : A Publication of the Protein Society, 7(11), 2359.
		+
	Gürtler, L. (2006). In Kamps B. S., Hoffmann C. and Preiser W. (Eds.), Virology of human influenza Flying publisher.		Gürtler, L. (2006). In Kamps B. S., Hoffmann C. and Preiser W. (Eds.), Virology of human influenza Flying publisher.
		+
	Hemagglutinin (influenza). (2015). Retrieved 11/13, 2015, from https://en.wikipedia.org/wiki/Hemagglutinin_(influenza)		Hemagglutinin (influenza). (2015). Retrieved 11/13, 2015, from https://en.wikipedia.org/wiki/Hemagglutinin_(influenza)
	Holsinger, L., Nichani, D., Pinto, L., & Lamb, R. (1994). Influenza A virus M2 ion channel protein: A structure-function analysis. Journal of Virology, 68(3), 1551.		Holsinger, L., Nichani, D., Pinto, L., & Lamb, R. (1994). Influenza A virus M2 ion channel protein: A structure-function analysis. Journal of Virology, 68(3), 1551.
		+
	Influenza hemagglutinin. (2011). Retrieved 11/13, 2015, from http://proteopedia.org/wiki/index.php/Influenza_hemagglutinin		Influenza hemagglutinin. (2011). Retrieved 11/13, 2015, from http://proteopedia.org/wiki/index.php/Influenza_hemagglutinin
	Avian Influenza Neuraminidase.(2014). Retrieved 11/13, 2015, from		Avian Influenza Neuraminidase.(2014). Retrieved 11/13, 2015, from
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	Hemagglutinin. (2015). Retrieved 11/14, 2015, from http://proteopedia.org/wiki/index.php/Hemagglutinin		Hemagglutinin. (2015). Retrieved 11/14, 2015, from http://proteopedia.org/wiki/index.php/Hemagglutinin
	Pinto, L., & Lamb, R. (2006). The M2 proton channels of a A and B viruses. The Journal of Biological Chemistry, 281(14), 8997.		Pinto, L., & Lamb, R. (2006). The M2 proton channels of a A and B viruses. The Journal of Biological Chemistry, 281(14), 8997.
		+
	Racaniello, V. (2009). Release of influenza viral RNAs into cells. Retrieved 11/14, 2015, from http://www.virology.ws/2009/05/06/release-of-influenza-viral-rnas-into-cells/		Racaniello, V. (2009). Release of influenza viral RNAs into cells. Retrieved 11/14, 2015, from http://www.virology.ws/2009/05/06/release-of-influenza-viral-rnas-into-cells/
		+
	Ruigrok, R. W. H., Barge, A., Durrer, P., Brunner, J., Ma, K., & Whittaker, G. R. (1999). Membrane interaction of influenza virus M1 protein. Virology, 267(2), 289-298. doi:http://dx.doi.org/10.1006/viro.1999.0134		Ruigrok, R. W. H., Barge, A., Durrer, P., Brunner, J., Ma, K., & Whittaker, G. R. (1999). Membrane interaction of influenza virus M1 protein. Virology, 267(2), 289-298. doi:http://dx.doi.org/10.1006/viro.1999.0134
		+
	Shors, T. (2013). Infulenza viruses. Understanding Viruses (2nd ed., pp. 345-290). Burlington, MA: Jones & Bartlett Learning.		Shors, T. (2013). Infulenza viruses. Understanding Viruses (2nd ed., pp. 345-290). Burlington, MA: Jones & Bartlett Learning.
	Wilson, I., Skehel, J., & Wiley, D. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 289(5796), 366.		Wilson, I., Skehel, J., & Wiley, D. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 289(5796), 366.
		+
	Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035		Thoennes, S., Li, Z., Lee, B., Langley, W. A., Skehel, J. J., Russell, R. J., et al. (2008). Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology,370(2), 403-414. doi:http://dx.doi.org/10.1016/j.virol.2007.08.035