Host cell entry of vaccinia virus (a poxvirus) proceeds through multiple steps that involve many viral proteins to mediate cell infection. Upon binding to cells, vaccinia virus membrane fuses with host membranes via a viral entry fusion protein complex comprising 11 proteins: A16, A21, A28, F9, G3, G9, H2, J5, L1, L5 and O3. Despite vaccinia virus having two infectious forms, mature and enveloped, that have different membrane layers, both forms require an identical viral entry fusion complex for...
[NMR paper] NMR assignments of vaccinia virus protein A28: an entry-fusion complex component.
NMR assignments of vaccinia virus protein A28: an entry-fusion complex component.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR assignments of vaccinia virus protein A28: an entry-fusion complex component.
Biomol NMR Assign. 2021 Jan 04;:
Authors: Wu D, Lou YC, Chang W, Tzou DM
Abstract
Vaccinia virus (VACV) belonging to the poxvirus family enters the host cell via two different entry pathways; either endocytosis or...
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01-08-2021 03:30 AM
[NMR paper] Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.
Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.
Related Articles Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.
J Mol Biol. 2020 Jun 24;:
Authors: Kwon B, Mandal T, Elkins MR, Oh Y, Cui Q, Hong M
Abstract
HIV-1 entry into cells is mediated by the fusion protein gp41. Cholesterol plays an important...
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06-28-2020 09:39 PM
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
Publication date: February 2018
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1860, Issue 2</br>
Author(s): Mukesh Mahajan, Deepak Chatterjee, Kannaian Bhuvaneswari, Shubhadra Pillay, Surajit Bhattacharjya</br>
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A...
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11-23-2017 08:38 AM
[NMR paper] NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
Biochim Biophys Acta. 2017 Oct 05;:
Authors: Mahajan M, Chatterjee D, Bhuvaneswari K, Pillay S, Bhattacharjya S
Abstract
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV)...
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10-11-2017 10:37 AM
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Abstract Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding 1H,15N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its...
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09-30-2011 08:01 PM
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 06:00 AM
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 05:59 AM
[NMR paper] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
Related Articles Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations
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