Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
about
Origins and diversity of eukaryotic CO2-concentrating mechanisms: lessons for the futureRubisco activity and regulation as targets for crop improvementCrystal structure of the N-terminal domain of EccA₁ ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis.Structural Insights into the Unusually Strong ATPase Activity of the AAA Domain of the Caenorhabditis elegans Fidgetin-like 1 (FIGL-1) ProteinStructure and Identification of a Pterin Dehydratase-like Protein as a Ribulose-bisphosphate Carboxylase/Oxygenase (RuBisCO) Assembly Factor in the α-CarboxysomeDiscovery of a new motion mechanism of biomotors similar to the earth revolving around the sun without rotation.Structure and mechanism of the primosome protein DnaT-functional structures for homotrimerization, dissociation of ssDNA from the PriB·ssDNA complex, and formation of the DnaT·ssDNA complexStructure of Arabidopsis thaliana Rubisco activaseDegradation of potent Rubisco inhibitor by selective sugar phosphataseMitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin: Metabolic Tools for Enhanced Algal Fitness in the Prominent Order Prymnesiales (Haptophyceae)Cyanobacterial-based approaches to improving photosynthesis in plantsRole of small subunit in mediating assembly of red-type form I Rubisco.Small oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity.Mechanism of one-way traffic of hexameric phi29 DNA packaging motor with four electropositive relaying layers facilitating antiparallel revolution.The ATPase of the phi29 DNA packaging motor is a member of the hexameric AAA+ superfamily.Revolution rather than rotation of AAA+ hexameric phi29 nanomotor for viral dsDNA packaging without coiling.Molecular snapshots of the Pex1/6 AAA+ complex in action.Engineering chloroplasts to improve Rubisco catalysis: prospects for translating improvements into food and fiber crops.Common mechanisms of DNA translocation motors in bacteria and viruses using one-way revolution mechanism without rotationResponses of Nannochloropsis oceanica IMET1 to Long-Term Nitrogen Starvation and Recovery.A pangenomic analysis of the Nannochloropsis organellar genomes reveals novel genetic variations in key metabolic genesA function-based screen for seeking RubisCO active clones from metagenomes: novel enzymes influencing RubisCO activityFairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.Isolation and characterization of the Prochlorococcus carboxysome reveal the presence of the novel shell protein CsoS1D.The nature of the CO2 -concentrating mechanisms in a marine diatom, Thalassiosira pseudonana.Bacterial microcompartments as metabolic modules for plant synthetic biology.Protein oligomerization monitored by fluorescence fluctuation spectroscopy: self-assembly of rubisco activase.Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs.Structural Characterization of a Newly Identified Component of α-Carboxysomes: The AAA+ Domain Protein CsoCbbQ.New approach to develop ultra-high inhibitory drug using the power function of the stoichiometry of the targeted nanomachine or biocomplex.Characterization of the heterooligomeric red-type rubisco activase from red algae.Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases.Optimizing Rubisco and its regulation for greater resource use efficiency.Enhancing C3 photosynthesis: an outlook on feasible interventions for crop improvement.Role of auxiliary proteins in Rubisco biogenesis and function.Rubisco Activases: AAA+ Chaperones Adapted to Enzyme RepairThe Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.The potential for co-evolution of CO2-concentrating mechanisms and Rubisco in diatoms.Regulation of the Calvin-Benson-Bassham cycle in the enigmatic diatoms: biochemical and evolutionary variations on an original theme.
P2860
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P2860
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@ast
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@en
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@nl
type
label
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@ast
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@en
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@nl
prefLabel
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@ast
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@en
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@nl
P2093
P2860
P50
P356
P1433
P1476
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
@en
P2093
Andreas Bracher
Mathias Stotz
Petra Wendler
P2860
P2888
P356
10.1038/NATURE10568
P407
P577
2011-11-02T00:00:00Z
P5875
P6179
1048585431