(Q40292429)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16616288%20AND%20SRC:MED&resulttype=core&format=json

19 January 2020

title

Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex (English)

1 reference

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19 January 2020

6

1 reference

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19 January 2020

2

Per Johan Klasse

1 reference

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19 January 2020

5

John P Moore

1 reference

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19 January 2020

author name string

Carolina Herrera

series ordinal

1

1 reference

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19 January 2020

Christopher W Kibler

series ordinal

3

1 reference

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19 January 2020

Elizabeth Michael

series ordinal

4

1 reference

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19 January 2020

language of work or name

English

0 references

publication date

17 April 2006

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19 January 2020

1 reference

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19 January 2020

volume

351

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19 January 2020

issue

1

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19 January 2020

page(s)

121-132

1 reference

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A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure

19 January 2020

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Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), Is the primary determinant of SU content of purified human immunodeficiency virus type 1 and simian immunodeficiency virus

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Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage.

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Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum

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Heterogeneity of envelope molecules expressed on primary human immunodeficiency virus type 1 particles as probed by the binding of neutralizing and nonneutralizing antibodies

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Oligomeric and conformational properties of a proteolytically mature, disulfide-stabilized human immunodeficiency virus type 1 gp140 envelope glycoprotein

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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