Hepatitis C virus glycoprotein folding: disulfide bond formation and association with calnexin (Q27480329)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8551615%20AND%20SRC:MED&resulttype=core&format=json

14 October 2019

title

Hepatitis C virus glycoprotein folding: disulfide bond formation and association with calnexin (English)

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14 October 2019

1 reference

1 reference

2

C M Rice

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14 October 2019

author name string

J Dubuisson

series ordinal

1

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14 October 2019

publication date

1 February 1996

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14 October 2019

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14 October 2019

volume

70

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14 October 2019

issue

2

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14 October 2019

page(s)

778-786

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Characterization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia viruses

14 October 2019

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21 March 2017

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21 March 2017

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21 March 2017

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21 March 2017

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21 March 2017

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21 March 2017

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Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)

21 March 2017

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Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

21 March 2017

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Retention of unassembled components of integral membrane proteins by calnexin

21 March 2017

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21 March 2017

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7 April 2017

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A second hepatitis C virus-encoded proteinase

7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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7 April 2017

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Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90).

7 April 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide

29 September 2017

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29 September 2017

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Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum

29 September 2017

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Molecular genetics of pestiviruses

29 September 2017

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Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum

29 September 2017

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Vaccinia Virus Replication I. Requirement for the Host-Cell Nucleus

29 September 2017

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Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells

29 September 2017

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Association of folding intermediates of glycoproteins with calnexin during protein maturation

2 June 2018

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=189879

Complex processing and protein:protein interactions in the E2:NS2 region of HCV.

2 June 2018

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Characterization of monoclonal antibodies to bovine viral diarrhoea virus: evidence of a neutralizing activity against gp48 in the presence of goat anti-mouse immunoglobulin serum

2 June 2018

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The p88 molecular chaperone is identical to the endoplasmic reticulum membrane protein, calnexin

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The hepatitis C virus encodes a serine protease involved in processing of the putative nonstructural proteins from the viral polyprotein precursor

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Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme

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12 December 2020

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

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Hormonal regulation of thyroglobulin export from the endoplasmic reticulum of cultured thyrocytes

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Identifiers

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14 October 2019

PubMed publication ID

8551615

1 reference