Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo

No abstract is available for this paper.

• Publication year

  1982

• Venue

  Journal of Bacteriology

• Publication date

  1982-03-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1128/jb.149.3.1082-1088.1982PMID 6460751PMCID PMC216498
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Identity of the B56.5 protein, the A-protein, and the groE gene product of Escherichia coli

  1981cited by this paper
• Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis.

  1981cited by this paper
• Role of the host cell in bacteriophage T4 development. I. Characterization of host mutants that block T4 head assembly

  1980cited by this paper
• Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly.

  1979cited by this paper
• Purification and properties of groE, a host protein involved in bacteriophage assembly.

  1979cited by this paper
• Early intermediates in bacteriophage lambda prohead assembly.

  1979cited by this paper
• Identification of a host protein necessary for bacteriophage morphogenesis (the groE gene product).

  1978cited by this paper
• Role of the host in virus assembly: cloning of the Escherichia coli groE gene and identification of its protein product.

  1978cited by this paper
• High resolution two-dimensional electrophoresis of proteins.

  1975cited by this paper
• Bacterial mutants which block phage assembly.

  1974cited by this paper
• Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). I. Initial characterization.

  1973cited by this paper
• Host participation in bacteriophage lambda head assembly.

  1973cited by this paper
• Properties of a mutant of Escherichia coli defective in bacteriophage λ head formation (groE)

  1973cited by this paper
• Cleavage of head and tail proteins during bacteriophage T5 assembly: selective host involvement in the cleavage of a tail protein.

  1973cited by this paper
• Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). II. The propagation of phage lambda.

  1973cited by this paper
• Involvement of a bacterial factor in morphogenesis of bacteriophage capsid.

  1972cited by this paper
• Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly.

  1972cited by this paper

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  2009cites this paper
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  2009cites this paper
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• The Roles of GroES as aCo-Chaperone

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  2001cites this paper
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  2000cites this paper
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  2000cites this paper
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  1999cites this paper
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  1999cites this paper
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  1998cites this paper
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  1998cites this paper
• Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus actinomycetemcomitans

  1998cites this paper
• Cloning, characterization and functional analysis of groESL operon from thermophilic cyanobacterium Synechococcus vulcanus.

  1997cites this paper
• Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage.

  1997cites this paper
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  1996cites this paper
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  1996cites this paper
• In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coli

  1996cites this paper
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  1996cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
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  1995cites this paper
• Protein translocation in Escherichia coli.

  1994cites this paper
• Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli

  1994cites this paper
• Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES

  1994cites this paper
• Subcellular localization and chaperone activities of Borrelia burgdorferi Hsp60 and Hsp70

  1994cites this paper
• A novel strong promoter of the groEx operon of symbiotic bacteria in Amoeba proteus.

  1994cites this paper
• Prediction of an inter-residue interaction in the chaperonin GroEL from multiple sequence alignment is confirmed by double-mutant cycle analysis.

  1994cites this paper
• On the role of groES in the chaperonin-assisted folding reaction. Three case studies.

  1994cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1993cites this paper
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  1992cites this paper
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  1992cites this paper
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  1992cites this paper
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  1991cites this paper
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  1991cites this paper
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  1991cites this paper
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  1991cites this paper
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  1991cites this paper
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  1991cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1990cites this paper
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  1989cites this paper
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  1988cites this paper
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  1988cites this paper
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  1986cites this paper
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  1986cites this paper
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  1985cites this paper
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  1985cites this paper
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  1984cites this paper
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  1984cites this paper
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  1984cites this paper