Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding (Q35872566)

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scientific article published in November 1996

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English	Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding	scientific article published in November 1996

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding (English)

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

molecular chaperones

0 references

1 reference

based on heuristic

inferred from title

author name string

Z Zheng

1

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

E Maidji

2

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

S Tugizov

3

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

L Pereira

4

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

language of work or name

0 references

publication date

1 November 1996

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Journal of Virology

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

70

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

11

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

8029-8040

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=190876

11 July 2018

Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin

1 reference

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11 July 2018

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=190876

11 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=190876

11 July 2018

Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring.

1 reference

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

1 reference

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Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein.

1 reference

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11 July 2018

Calnexin: a membrane-bound chaperone of the endoplasmic reticulum

1 reference

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11 July 2018

Function of human cytomegalovirus glycoprotein B: syncytium formation in cells constitutively expressing gB is blocked by virus-neutralizing antibodies.

1 reference

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Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus

1 reference

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Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum

1 reference

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Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase

1 reference

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The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

1 reference

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Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum

1 reference

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11 July 2018

Mutated forms of human cytomegalovirus glycoprotein B are impaired in inducing syncytium formation.

1 reference

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Conformation-defective herpes simplex virus 1 glycoprotein B activates the promoter of the grp94 gene that codes for the 94-kD stress protein in the endoplasmic reticulum.

1 reference

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Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.

1 reference

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Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms.

1 reference

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Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-Microglobulin

1 reference

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Degradation of CFTR by the ubiquitin-proteasome pathway

1 reference

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Cotranslational folding and calnexin binding during glycoprotein synthesis

1 reference

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Inhibition of invariant chain (Ii)-calnexin interaction results in enhanced degradation of Ii but does not prevent the assembly of alpha beta Ii complexes

1 reference

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Postoligomerization folding of human cytomegalovirus glycoprotein B: identification of folding intermediates and importance of disulfide bonding

1 reference

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Cytomegalovirus-infected cell polypeptides immune-precipitated by sera from children with congenital and perinatal infections

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Congenital cytomegalovirus infection: The relative importance of primary and recurrent maternal infection

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Polymorphism of human cytomegalovirus glycoproteins characterized by monoclonal antibodies

1 reference

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Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F.

1 reference

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Assembly of asparagine-linked oligosaccharides

1 reference

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

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Identification of the human cytomegalovirus glycoprotein B gene and induction of neutralizing antibodies via its expression in recombinant vaccinia virus.

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Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene: primary sequence and predicted protein structure of the wild type and of monoclonal antibody-resistant mutants

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Characterization of two different human cytomegalovirus glycoproteins which are targets for virus neutralizing antibody

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Retinopathy before the diagnosis of AIDS.

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Processing of the gp55-116 envelope glycoprotein complex (gB) of human cytomegalovirus

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Human cytomegalovirus strain Towne glycoprotein B is processed by proteolytic cleavage

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Protein degradation in the endoplasmic reticulum

1 reference

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Sequence requirements for proteolytic processing of glycoprotein B of human cytomegalovirus strain Towne

1 reference

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1 reference

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1 reference

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Transactivation of the grp78 promoter by malfolded proteins, glycosylation block, and calcium ionophore is mediated through a proximal region containing a CCAAT motif which interacts with CTF/NF-I

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Oligomerization of the human cytomegalovirus major envelope glycoprotein complex gB (gp55-116)

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Assembly of conformation-dependent neutralizing domains on glycoprotein B of human cytomegalovirus

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Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90).

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Function of glycoprotein B homologues of the family herpesviridae.

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Cytomegalovirus infection in patients with AIDS

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Multiple infections by cytomegalovirus in patients with acquired immunodeficiency syndrome: documentation by Southern blot hybridization

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Antiviral antibody responses in mothers and their newborn infants with clinical and subclinical congenital cytomegalovirus infections

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The endoplasmic reticulum as a protein-folding compartment

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Constitutive expression of human cytomegalovirus glycoprotein B (gpUL55) with mutagenized carboxy-terminal hydrophobic domains

1 reference

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An empirical approach to protein conformation stability and flexibility

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Cytomegalovirus Infection in a Day-Care Center

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Identifiers

10.1128/JVI.70.11.8029-8040.1996

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

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