(Q36234085)

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A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle

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Europe PubMed Central

PMC publication ID

12 August 2017

A eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle (English)

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Hepatitis B virus

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

4

object named as

D Ganem

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Jairam R Lingappa

1

object named as

J R Lingappa

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

author name string

R L Martin

2

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

M L Wong

3

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

W J Welch

5

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

V R Lingappa

6

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

language of work or name

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publication date

1 April 1994

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Journal of Cell Biology

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Europe PubMed Central

PMC publication ID

12 August 2017

125

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

1

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

99-111

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

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A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes.

1 reference

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The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

1 reference

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Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Molecular chaperone functions of heat-shock proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Immunoglobulin heavy chain binding protein

1 reference

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Functional messenger RNAs are produced by SP6in vitrotranscription of cloned cDNAs

1 reference

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Efficientin vitrosynthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter

1 reference

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Host participation in bacteriophage lambda head assembly

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). II. The propagation of phage lambda

1 reference

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Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system

1 reference

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

1 reference

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Involvement of heat shock proteins in bacteriophage Mu development

1 reference

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

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The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes

1 reference

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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Expression of hepatitis B viral core region in mammalian cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Assembly of influenza hemagglutinin trimers and its role in intracellular transport

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

The mitochondrial chaperonin hsp60 is required for its own assembly

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

Sequential action of mitochondrial chaperones in protein import into the matrix

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

1 October 2017

The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Assembly of hepadnaviral virions and subviral particles

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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The two mammalian mitochondrial stress proteins, grp 75 and hsp 58, transiently interact with newly synthesized mitochondrial proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Cell-free, de novo synthesis of poliovirus

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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TCP1 complex is a molecular chaperone in tubulin biogenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Characterization of hepatitis B virus capsid particle assembly in Xenopus oocytes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Hepatitis B virus capsid particles are assembled from core-protein dimer precursors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

1 reference

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Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

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Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322

1 reference

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Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product)

1 reference

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1 reference

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Unusually high-level expression of a foreign gene (hepatitis B virus core antigen) in Saccharomyces cerevisiae

1 reference

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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1 reference

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A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2120005

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1 reference

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1 reference

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1 reference

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1 reference

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Molecular Chaperones

1 reference

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/7908022

12 December 2020

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ATCPl-related molecular chaperone from plants refolds phytochrome to its photoreversible form

1 reference

https://pubmed.ncbi.nlm.nih.gov/7908022

12 December 2020

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inferred from PubMed ID database lookup

Synthesis of hepatitis B surface and core antigens in E. coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/7908022

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A stop transfer sequence confers predictable transmembrane orientation to a previously secreted protein in cell-free systems

1 reference

https://pubmed.ncbi.nlm.nih.gov/7908022

12 December 2020

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inferred from PubMed ID database lookup

Electron microscopy of hepatitis B core antigen synthesized in E. coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/7908022

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1083/JCB.125.1.99

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 August 2017

ResearchGate publication ID

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