(Q38850428)

7 September 2017

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title

Role of auxiliary proteins in Rubisco biogenesis and function (English)

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7 September 2017

Manajit Hayer-Hartl

4

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Franz-Ulrich Hartl

series ordinal

3

object named as

F Ulrich Hartl

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7 September 2017

Thomas Hauser

1

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7 September 2017

Leonhard Popilka

series ordinal

2

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7 September 2017

publication date

2 June 2015

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7 September 2017

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7 September 2017

volume

1

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7 September 2017

page(s)

15065

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Structure and function of Rubisco

7 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Primary Production of the Biosphere: Integrating Terrestrial and Oceanic Components

21 January 2018

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https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Ribulose-1,5-bisphosphate carboxylase-oxygenase

21 January 2018

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Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase

21 January 2018

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Biochemistry: Tackling unintelligent design.

21 January 2018

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https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Catalysis and regulation in Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): a historical perspective.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Photorespiration: current status and approaches for metabolic engineering

21 January 2018

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https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Metabolic engineering towards the enhancement of photosynthesis.

21 January 2018

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https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

21 January 2018

Enhancing photosynthesis

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Increasing photosynthetic carbon assimilation in C3 plants to improve crop yield: current and future strategies

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

21 January 2018

Improving photosynthesis

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Rubisco activity and regulation as targets for crop improvement

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Manipulation of Rubisco: the amount, activity, function and regulation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Role of the small subunit in ribulose-1,5-bisphosphate carboxylase/oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Functional incorporation of sorghum small subunit increases the catalytic turnover rate of Rubisco in transgenic rice

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Protein import into chloroplasts--how chaperones feature into the game

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

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/10.1038%2FNPLANTS.2015.65

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Molecular chaperone functions in protein folding and proteostasis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Coupled chaperone action in folding and assembly of hexadecameric Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The complexity of chloroplast chaperonins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Cpn20: siamese twins of the chaperonin world

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure and allostery of the chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Differential effects of co-chaperonin homologs on cpn60 oligomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

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/10.1038%2FNPLANTS.2015.65

GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Overproduction of Anabaena 7120 ribulose-bisphosphate carboxylase/oxygenase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

RbcX can function as a rubisco chaperonin, but is non-essential in Synechococcus PCC7942.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus participates in the final stages of ribulose-1,5-bisphosphate carboxylase/oxygenase assembly in Escherichia coli cells and in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Insights into eukaryotic Rubisco assembly - crystal structures of RbcX chaperones from Arabidopsis thaliana

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Initial characteristics of RbcX proteins from Arabidopsis thaliana

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Subunit interface dynamics in hexadecameric rubisco.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The ribosome as a hub for protein quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Identification of a Hsp70 recognition domain within the rubisco small subunit transit peptide.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Reconstruction of metabolic pathways, protein expression, and homeostasis machineries across maize bundle sheath and mesophyll chloroplasts: large-scale quantitative proteomics using the first maize genome assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

BUNDLE SHEATH DEFECTIVE2, a novel protein required for post-translational regulation of the rbcL gene of maize.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The BSD2 ortholog in Chlamydomonas reinhardtii is a polysome-associated chaperone that co-migrates on sucrose gradients with the rbcL transcript encoding the Rubisco large subunit.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Ribulose-1,5-bis-phosphate carboxylase/oxygenase accumulation factor1 is required for holoenzyme assembly in maize.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure and Identification of a Pterin Dehydratase-like Protein as a Ribulose-bisphosphate Carboxylase/Oxygenase (RuBisCO) Assembly Factor in the α-Carboxysome

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Role of small subunit in mediating assembly of red-type form I Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Regulation of Rubisco activase and its interaction with Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Rubisco regulation: a role for inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

AAA+ proteins: have engine, will work

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The AAA+ superfamily of functionally diverse proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure and function of the AAA+ nucleotide binding pocket

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Structure of green-type Rubisco activase from tobacco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Atomic Resolution X-ray Structure of the Substrate Recognition Domain of Higher Plant Ribulose-bisphosphate Carboxylase/Oxygenase (Rubisco) Activase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Degradation of potent Rubisco inhibitor by selective sugar phosphatase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Metabolite damage and its repair or pre-emption

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Protein oligomerization monitored by fluorescence fluctuation spectroscopy: self-assembly of rubisco activase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Biophysical characterization of higher plant Rubisco activase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco-Rubisco activase interaction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Rubisco, Rubisco activase, and global climate change

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Genomic buffering mitigates the effects of deleterious mutations in bacteria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Stability effects of mutations and protein evolvability

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The effect of chaperonin buffering on protein evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Cumulative impact of chaperone-mediated folding on genome evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

GroEL/ES buffering and compensatory mutations promote protein evolution by stabilizing folding intermediates

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Chaperonin overexpression promotes genetic variation and enzyme evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Evolving improved Synechococcus Rubisco functional expression in Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Opposing effects of folding and assembly chaperones on evolvability of Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Cyanobacterial-based approaches to improving photosynthesis in plants

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

A faster Rubisco with potential to increase photosynthesis in crops

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

T-Coffee: A novel method for fast and accurate multiple sequence alignment

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Dendroscope 3: an interactive tool for rooted phylogenetic trees and networks

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

The age of Rubisco: the evolution of oxygenic photosynthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

Advancing our understanding and capacity to engineer nature's CO2-sequestering enzyme, Rubisco

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Form I Rubiscos from non-green algae are expressed abundantly but not assembled in tobacco chloroplasts

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Rubisco: the enzyme that keeps on giving

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

The 70-kDa heat-shock protein/DnaK chaperone system is required for the productive folding of ribulose-biphosphate carboxylase subunits in Escherichia coli

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

A protein with an inactive pterin-4a-carbinolamine dehydratase domain is required for Rubisco biogenesis in plants

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Improving recombinant Rubisco biogenesis, plant photosynthesis and growth by coexpressing its ancillary RAF1 chaperone

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Erratum: Degradation of potent Rubisco inhibitor by selective sugar phosphatase

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

NanoESI Mass Spectrometry of Rubisco and Rubisco Activase Structures and Their Interactions with Nucleotides and Sugar Phosphates

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

ATP and magnesium promote cotton short-form ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase hexamer formation at low micromolar concentrations

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Characterization of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase activase isoforms reveals hexameric assemblies with increased thermal stability

1 reference

https://api.crossref.org/works/10.1038%2FNPLANTS.2015.65

7 January 2021

Identifiers

DOI

10.1038/NPLANTS.2015.65

1 reference

Dimensions Publication ID

7 September 2017

1049636544

0 references

1 reference