Electron microscopy of the complexes of ribulose-1,5-bisphosphate carboxylase (Rubisco) and Rubisco subunit-binding protein from pea leaves (Q68007504)

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20 September 2019

title

Electron microscopy of the complexes of ribulose-1,5-bisphosphate carboxylase (Rubisco) and Rubisco subunit-binding protein from pea leaves (English)

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20 September 2019

author name string

Tsuprun VL

1

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20 September 2019

Boekema EJ

2

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20 September 2019

Samsonidze TG

3

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20 September 2019

Pushkin AV

4

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20 September 2019

language of work or name

English

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publication date

1 September 1991

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20 September 2019

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20 September 2019

volume

289

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20 September 2019

issue

2

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20 September 2019

page(s)

205-209

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Ribulose-1,5-bisphosphate carboxylase-oxygenase

20 September 2019

cites work

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Ribulose bisphosphate carboxylase: a two-layered, square-shaped molecule of symmetry 422.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Structure of D-ribulose-l,5-bisphosphate carboxylase/oxygenase from Alcaligenes eutrophyus H16.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

The Rubisco subunit binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Assembly of Rubisco from native subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Proteins as molecular chaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

21 January 2018

The heat-shock response

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

21 January 2018

The heat-shock proteins

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2891%2981070-O

10.1016/0014-5793(91)81070-O

21 January 2018

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1915848%20AND%20SRC:MED&resulttype=core&format=json

20 September 2019

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