(Q33877945)

29 July 2017

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

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29 July 2017

Goloubinoff P

1

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29 July 2017

Christeller JT

series ordinal

2

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29 July 2017

Gatenby AA

series ordinal

3

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29 July 2017

Lorimer GH

series ordinal

4

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29 July 2017

language of work or name

English

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publication date

1 December 1989

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29 July 2017

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29 July 2017

342

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29 July 2017

884-889

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29 July 2017

6252

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https://scigraph.springernature.com/pub.10.1038/342884a0

29 July 2017

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cites work

Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

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7 January 2021

Efficient mapping of protein antigenic determinants

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7 January 2021

A heat shock operon in Coxiella burnetti produces a major antigen homologous to a protein in both mycobacteria and Escherichia coli

1 reference

7 January 2021

A homolog of ribulose bisphosphate carboxylase/oxygenase-binding protein in Chromatium vinosum

1 reference

7 January 2021

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

1 reference

7 January 2021

Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

1 reference

7 January 2021

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1 reference

7 January 2021

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

1 reference

7 January 2021

Host participation in bacteriophage lambda head assembly

1 reference

7 January 2021

Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis

1 reference

7 January 2021

The Rubisco subunit binding protein.

1 reference

7 January 2021

Assembly of Rubisco from native subunits

1 reference

7 January 2021

Imported large subunits of ribulose bisphosphate carboxylase/oxygenase, but not imported beta-ATP synthase subunits, are assembled into holoenzyme in isolated chloroplasts.

1 reference

7 January 2021

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

1 reference

7 January 2021

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

1 reference

7 January 2021

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

1 reference

7 January 2021

Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone

1 reference

7 January 2021

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

1 reference

7 January 2021

Sliding-layer conformational change limited by the quaternary structure of plant RuBisCO.

1 reference

7 January 2021

Crystal structure of the active site of ribulose-bisphosphate carboxylase

1 reference

7 January 2021

Alpha-Lactalbumin: compact state with fluctuating tertiary structure?

1 reference

7 January 2021

‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains

1 reference

7 January 2021

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

1 reference

7 January 2021

Purification and properties of groE, a host protein involved in bacteriophage assembly

1 reference

7 January 2021

Speculations on the functions of the major heat shock and glucose-regulated proteins

1 reference

7 January 2021

Catalysis of protein folding by prolyl isomerase

1 reference

7 January 2021

Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins

1 reference

7 January 2021

The sites for catalysis and activation of ribulosebisphosphate carboxylase share a common domain

1 reference

7 January 2021

Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts

1 reference

7 January 2021

Studies on the assembly of large subunits of ribulose bisphosphate carboxylase in isolated pea chloroplasts

1 reference

7 January 2021

Identifiers

DOI

10.1038/342884A0

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Dimensions Publication ID

29 July 2017

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