(Q81007336)

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Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region

scientific article published on 01 October 2005

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

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Kathryn E Follis

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

Joanne York

2

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

Jack H Nunberg

3

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Europe PubMed Central

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5 January 2020

publication date

1 October 2005

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

341

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5 January 2020

1

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5 January 2020

122-129

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

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Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions.

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Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins

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The packing of α-helices: simple coiled-coils

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Ribonuclease S-peptide as a carrier in fusion proteins.

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Newly discovered coronavirus as the primary cause of severe acute respiratory syndrome.

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Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

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Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors

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The Genome sequence of the SARS-associated coronavirus

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Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein

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Retroviruses pseudotyped with the severe acute respiratory syndrome coronavirus spike protein efficiently infect cells expressing angiotensin-converting enzyme 2.

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Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein

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Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate

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7 January 2021

Coronavirus as a possible cause of severe acute respiratory syndrome

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7 January 2021

Characterization of a novel coronavirus associated with severe acute respiratory syndrome

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Conformational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes

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Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry

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Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

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7 January 2021

The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection

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7 January 2021

Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage

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Synthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein

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Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein

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Structural characterization of the SARS-coronavirus spike S fusion protein core.

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Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion

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The fusion-controlling disulfide bond isomerase in retrovirus Env is triggered by protein destabilization

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based on heuristic

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Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2005.07.005

7 January 2021

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Identifiers

10.1016/J.VIROL.2005.07.005

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16081124%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

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