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Degradation Rate of Mitochondrial Proteins in Arabidopsis thaliana Cells

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Outgoing claims: the papers this work cites, builds on, or argues with.

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Probability-based protein identification by searching sequence databases using mass spectrometry data
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Basic Local Alignment Search Tool
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AtGRP2, a cold-induced nucleo-cytoplasmic RNA-binding protein, has a role in flower and seed development
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Functional and composition differences between mitochondrial complex II in Arabidopsis and rice are correlated with the complex genetic history of the enzyme
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Photoinhibition of photosystem II under environmental stress
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Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation
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Mitochondrial shaping cuts
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Protein quality control in organelles — AAA/FtsH story
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Mitochondrial complex III deficiencies in the newborn infant
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The multiplicity of dehydrogenases in the electron transport chain of plant mitochondria
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Succinate dehydrogenase: the complex roles of a simple enzyme
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The dynamic state of protein turnover: It's about time
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Mitochondrial quality control: an integrated network of pathways
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Protein degradation – an alternative respiratory substrate for stressed plants
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Subunit VIa of yeast cytochrome c oxidase is not necessary for assembly of the enzyme complex but modulates the enzyme activity. Isolation and characterization of the nuclear-coded gene.
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A Vacuolar-type ATPase, Partially Purified from Potassium Transporting Plasma Membranes of Tobacco Hornworm Midgut
inferredcites →https://doi.org/10.1016/s0891-5849(00)00305-1openalex-snapshot
Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
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Autophagic pathways in Parkinson disease and related disorders
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Proteome Scale Turnover Analysis in Live Animals Using Stable Isotope Metabolic Labeling
inferredcites →https://doi.org/10.1021/ac800080vopenalex-snapshot
Quantitative Analysis of Isotope Distributions In Proteomic Mass Spectrometry Using Least-Squares Fourier Transform Convolution
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Systems-wide Proteomic Analysis in Mammalian Cells Reveals Conserved, Functional Protein Turnover
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Proteome Turnover in the Green Alga Ostreococcus tauri by Time Course 15N Metabolic Labeling Mass Spectrometry
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The Arabidopsis F-box protein TIR1 is an auxin receptor
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ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light
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Accumulation of Newly Synthesized F1 in Vivo in Arabidopsis Mitochondria Provides Evidence for Modular Assembly of the Plant F1Fo ATP Synthase
inferredcites →https://doi.org/10.1074/jbc.m112.432070openalex-snapshot
Subcomplexes of Ancestral Respiratory Complex I Subunits Rapidly Turn Over in Vivo as Productive Assembly Intermediates in Arabidopsis*
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Tandem Phosphorylation of Ser-911 and Thr-912 at the C Terminus of Yeast Plasma Membrane H+-ATPase Leads to Glucose-dependent Activation
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A Quantitative Spatial Proteomics Analysis of Proteome Turnover in Human Cells
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Protein Turnover Quantification in a Multilabeling Approach: From Data Calculation to Evaluation
inferredcites →https://doi.org/10.1074/mcp.m112.021162openalex-snapshot
Metabolic Labeling Reveals Proteome Dynamics of Mouse Mitochondria
inferredcites →https://doi.org/10.1074/mcp.m200046-mcp200openalex-snapshot
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inferredcites →https://doi.org/10.1074/mcp.m600347-mcp200openalex-snapshot
Comparison of Full Versus Partial Metabolic Labeling for Quantitative Proteomics Analysis in Arabidopsis thaliana
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Proteome Dynamics: Revisiting Turnover with a Global Perspective
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2004 SPRING MEETING OF THE WPSA UK BRANCH PAPERS
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Combining Experimental and Predicted Datasets for Determination of the Subcellular Location of Proteins in Arabidopsis
inferredcites →https://doi.org/10.1104/pp.108.130013openalex-snapshot
Autophagy Plays a Role in Chloroplast Degradation during Senescence in Individually Darkened Leaves
inferredcites →https://doi.org/10.1104/pp.111.182352openalex-snapshot
Defining theProtein Complex Proteomeof Plant Mitochondria
inferredcites →https://doi.org/10.1105/tpc.012500openalex-snapshot
Enzymes of Glycolysis Are Functionally Associated with the Mitochondrion in Arabidopsis Cells
inferredcites →https://doi.org/10.1105/tpc.110.076075openalex-snapshot
Abscisic Acid Increases Arabidopsis ABI5 Transcription Factor Levels by Promoting KEG E3 Ligase Self-Ubiquitination and Proteasomal Degradation
inferredcites →https://doi.org/10.1111/j.1365-313x.2006.02826.xopenalex-snapshot
The mitochondrial electron transfer flavoprotein complex is essential for survival of Arabidopsis in extended darkness
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Measuring the turnover rates of Arabidopsis proteins using deuterium oxide: an auxin signaling case study
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Deg proteases and their role in protein quality control and processing in different subcellular compartments of the plant cell
inferredcites →https://doi.org/10.1111/j.1399-3054.2011.01541.xopenalex-snapshot
The chloroplast ATP‐dependent Clp protease in vascular plants – new dimensions and future challenges
inferredcites →https://doi.org/10.1111/j.1469-8137.2012.04084.xopenalex-snapshot
Autophagy machinery controls nitrogen remobilization at the whole‐plant level under both limiting and ample nitrate conditions in Arabidopsis
inferredcites →https://doi.org/10.1126/science.1157956openalex-snapshot
Genome-Scale Proteomics Reveals Arabidopsis thaliana Gene Models and Proteome Dynamics
inferredcites →https://doi.org/10.1126/science.1225053openalex-snapshot
Chloroplast Biogenesis Is Regulated by Direct Action of the Ubiquitin-Proteasome System
inferredcites →https://doi.org/10.1126/science.272.5265.1136openalex-snapshot
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
inferredcites →https://doi.org/10.1139/cjpp-77-2-79openalex-snapshot
Pharmacological uses and perspectives of heavy water and deuterated compounds
inferredcites →https://doi.org/10.1146/annurev-biochem-072909-100424openalex-snapshot
Mass Spectrometry–Based Proteomics and Network Biology
inferredcites →https://doi.org/10.1146/annurev.arplant.55.031903.141720openalex-snapshot
ALTERNATIVE NAD(P)H DEHYDROGENASES OF PLANT MITOCHONDRIA
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Proteomic Investigations of Complex I Composition: How to Define a Subunit?

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Detailed Study of Temperature-Related Alterations Throughout the Proteome of Arabidopsis thaliana Seedlings
inferred← citeshttps://doi.org/10.2139/ssrn.4863525openalex-extracted
The Dynamic Shift in Mitochondria from Mature Pollen Grains
inferred← citeshttps://doi.org/10.1002/9781118906583.ch7openalex-snapshot
MITOCHONDRIAL REGULATION AND SIGNALLING IN THE PHOTOSYNTHETIC CELL
inferred← citeshttps://doi.org/10.1002/9781119312994.apr0549openalex-snapshot
Mitochondrial Regulation and Signalling in the Photosynthetic Cell: Principles and Concepts
inferred← citeshttps://doi.org/10.1002/cpz1.114openalex-snapshot
Assessing Protein Synthesis and Degradation Rates in Arabidopsis thaliana Using Amino Acid Analysis
inferred← citeshttps://doi.org/10.1002/jobm.201500315openalex-snapshot
Protein turnover analysis in Salmonella Typhimurium during infection by dynamic SILAC, Topograph, and quantitative proteomics
inferred← citeshttps://doi.org/10.1002/pmic.201300240openalex-snapshot
Quantitative analysis of protein turnover in plants
inferred← citeshttps://doi.org/10.1007/978-1-0716-2784-6_14openalex-snapshot
Relative Protein Lifetime Measurement in Plants Using Tandem Fluorescent Protein Timers
inferred← citeshttps://doi.org/10.1007/s00709-017-1125-9openalex-snapshot
Macroautophagy occurs in distal TMV-uninfected root tip tissue of tomato taking place systemic PCD
inferred← citeshttps://doi.org/10.1007/s11738-016-2155-1openalex-snapshot
Changes in the OXPHOS system in leaf and root mitochondria of Arabidopsis thaliana subjected to long-term sulphur deficiency
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.10.015openalex-snapshot
Distribution and dynamics of OXPHOS complexes in the bacterial cytoplasmic membrane
inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148365openalex-snapshot
Tune instead of destroy: How proteolysis keeps OXPHOS in shape
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114803openalex-snapshot
Temporal alterations of the nascent proteome in response to mitochondrial stress
inferred← citeshttps://doi.org/10.1016/j.cub.2024.12.037openalex-snapshot
The atypical proteome of mitochondria from mature pollen grains
inferred← citeshttps://doi.org/10.1016/j.ibmb.2016.10.005openalex-snapshot
Differential proteomics reveals novel insights into Nosema–honey bee interactions
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Composition of Mitochondrial Complex I during the Critical Node of Seed Aging in Oryza sativa
inferred← citeshttps://doi.org/10.1016/j.jprot.2015.02.011openalex-snapshot
Arabidopsis proteome responses to the smoke-derived growth regulator karrikin
inferred← citeshttps://doi.org/10.1016/j.mito.2014.02.006openalex-snapshot
The life of plant mitochondrial complex I
inferred← citeshttps://doi.org/10.1016/j.mito.2014.04.002openalex-snapshot
Mitochondrial biogenesis in plants during seed germination
inferred← citeshttps://doi.org/10.1016/j.mito.2020.04.011openalex-snapshot
Protein turnover rates in plant mitochondria
inferred← citeshttps://doi.org/10.1016/j.tplants.2013.11.003openalex-snapshot
Why measure enzyme activities in the era of systems biology?
inferred← citeshttps://doi.org/10.1016/j.tplants.2014.09.004openalex-snapshot
Shredding the signal: targeting peptide degradation in mitochondria and chloroplasts
inferred← citeshttps://doi.org/10.1016/j.tplants.2017.11.006openalex-snapshot
An In Vivo Perspective of the Role(s) of the Alternative Oxidase Pathway
inferred← citeshttps://doi.org/10.1016/j.tplants.2018.02.010openalex-snapshot
Mitophagy: A Mechanism for Plant Growth and Survival
inferred← citeshttps://doi.org/10.1021/ac403985wopenalex-snapshot
Quantification of Peptide m/z Distributions from 13C-Labeled Cultures with High-Resolution Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.jproteome.5b00990openalex-snapshot
Gaussian Process Modeling of Protein Turnover
inferred← citeshttps://doi.org/10.1038/nplants.2015.17openalex-snapshot
Protein turnover in plant biology
inferred← citeshttps://doi.org/10.1042/bcj20200515openalex-snapshot
Degradation of mitochondrial alternative oxidase in the appendices of Arum maculatum
inferred← citeshttps://doi.org/10.1042/bcj20250120openalex-snapshot
Proteolytic coordination of the OXPHOS Life Cycle
inferred← citeshttps://doi.org/10.1042/bst20220195openalex-snapshot
Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants
inferred← citeshttps://doi.org/10.1074/mcp.m115.049205openalex-snapshot
Drought and Recovery: Independently Regulated Processes Highlighting the Importance of Protein Turnover Dynamics and Translational Regulation in Medicago truncatula
inferred← citeshttps://doi.org/10.1080/15548627.2019.1586258openalex-snapshot
Autophagy accounts for approximately one-third of mitochondrial protein turnover and is protein selective
inferred← citeshttps://doi.org/10.1093/jxb/erae151openalex-snapshot
Experimental approaches to studying translation in plant semi-autonomous organelles
inferred← citeshttps://doi.org/10.1093/jxb/eru495openalex-snapshot
Photosynthetic complex stoichiometry dynamics in higher plants: biogenesis, function, and turnover of ATP synthase and the cytochrome b6f complex
inferred← citeshttps://doi.org/10.1093/jxb/erv298openalex-snapshot
Implications of mutation of organelle genomes for organelle function and evolution
inferred← citeshttps://doi.org/10.1093/plcell/koad128openalex-snapshot
FTSH PROTEASE 3 facilitates Complex I degradation through a direct interaction with the Complex I subunit PSST
inferred← citeshttps://doi.org/10.1093/plcell/koae141openalex-snapshot
Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants
inferred← citeshttps://doi.org/10.1093/plphys/kiab101openalex-snapshot
Mitochondrial redox systems as central hubs in plant metabolism and signaling
inferred← citeshttps://doi.org/10.1093/plphys/kiad108openalex-snapshot
The biogenesis and regulation of the plant oxidative phosphorylation system
inferred← citeshttps://doi.org/10.1093/plphys/kiae056openalex-snapshot
A double-feature mitochondrial proteome exploration show
inferred← citeshttps://doi.org/10.1093/plphys/kiag481openalex-snapshot
Protein turnover in plants—cost of synthesis, repair, and crop engineering opportunities
inferred← citeshttps://doi.org/10.1096/fj.15-272666openalex-snapshot
Respiratory chain protein turnover rates in mice are highly heterogeneous but strikingly conserved across tissues, ages, and treatments
inferred← citeshttps://doi.org/10.1101/2023.02.23.529725openalex-snapshot
FTSH3 facilitates complex I degradation through a direct interaction with the complex I subunit PSST
inferred← citeshttps://doi.org/10.1101/2024.04.30.591943openalex-snapshot
Proteomic Dynamics and Heat Stress Response in Arabidopsis Seedlings
inferred← citeshttps://doi.org/10.1104/pp.114.243014openalex-snapshot
Proteins with High Turnover Rate in Barley Leaves Estimated by Proteome Analysis Combined with in Planta Isotope Labeling
inferred← citeshttps://doi.org/10.1104/pp.114.243741openalex-snapshot
Inducible Repression of Nuclear-Encoded Subunits of the Cytochrome b6f Complex in Tobacco Reveals an Extraordinarily Long Lifetime of the Complex
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Quantifying Protein Synthesis and Degradation in Arabidopsis by Dynamic 13CO2 Labeling and Analysis of Enrichment in Individual Amino Acids in Their Free Pools and in Protein
inferred← citeshttps://doi.org/10.1104/pp.15.00300openalex-snapshot
INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria
inferred← citeshttps://doi.org/10.1104/pp.19.00051openalex-snapshot
Tandem Fluorescent Protein Timers for Noninvasive Relative Protein Lifetime Measurement in Plants
inferred← citeshttps://doi.org/10.1105/tpc.16.00398openalex-snapshot
The Reverse Transcriptase/RNA Maturase Protein MatR Is Required for the Splicing of Various Group II Introns in Brassicaceae Mitochondria
inferred← citeshttps://doi.org/10.1105/tpc.16.00768openalex-snapshot
Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development
inferred← citeshttps://doi.org/10.1105/tpc.19.00535openalex-snapshot
Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications
inferred← citeshttps://doi.org/10.1111/febs.15714openalex-snapshot
Is the NDUFV2 subunit of the hydrophilic complex I domain a key determinant of animal longevity?
inferred← citeshttps://doi.org/10.1111/jipb.12858openalex-snapshot
Phosphorylation at Ser28 stabilizes the Arabidopsis nitrate transporter NRT2.1 in response to nitrate limitation
inferred← citeshttps://doi.org/10.1111/jipb.13087openalex-snapshot
Exploring the diversity of plant proteome
inferred← citeshttps://doi.org/10.1111/mmi.14108openalex-snapshot
Phosphagen kinase function in flagellated spores of the oomycete Phytophthora infestans integrates transcriptional regulation, metabolic dynamics and protein retargeting
inferred← citeshttps://doi.org/10.1111/nph.17756openalex-snapshot
Protein turnover in the developing Triticum aestivum grain
inferred← citeshttps://doi.org/10.1111/pce.12381openalex-snapshot
Relationship between starch degradation and carbon demand for maintenance and growth in A rabidopsis thaliana in different irradiance and temperature regimes
inferred← citeshttps://doi.org/10.1111/pce.70322openalex-snapshot
Metabolic Responses to Salinity Identify a Role for Mitochondrial 2‐Oxoglutarate Dehydrogenase in Wheat Tissue Tolerance
inferred← citeshttps://doi.org/10.1111/ppl.70529openalex-snapshot
Proteomic Analysis Infers Optimized ATP ‐Production in Guard Cell Mitochondria
inferred← citeshttps://doi.org/10.1111/tpj.13111openalex-snapshot
Two NYN domain containing putative nucleases are involved in transcript maturation in Arabidopsis mitochondria
inferred← citeshttps://doi.org/10.1111/tpj.13392openalex-snapshot
Changes in specific protein degradation rates in Arabidopsis thaliana reveal multiple roles of Lon1 in mitochondrial protein homeostasis
inferred← citeshttps://doi.org/10.1111/tpj.14534openalex-snapshot
Single organelle function and organization as estimated from Arabidopsis mitochondrial proteomics
inferred← citeshttps://doi.org/10.1111/tpj.15495openalex-snapshot
Plant mitochondria – past, present and future
inferred← citeshttps://doi.org/10.1146/annurev-arplant-043014-115547openalex-snapshot
Protein Maturation and Proteolysis in Plant Plastids, Mitochondria, and Peroxisomes
inferred← citeshttps://doi.org/10.1371/journal.pone.0091537openalex-snapshot
Analysis of Isotopic Labeling in Peptide Fragments by Tandem Mass Spectrometry
inferred← citeshttps://doi.org/10.21203/rs.3.rs-4351529/v1openalex-snapshot
Unraveling Proteomic Adaptations to Moderate Heat Stress in Arabidopsis thaliana: Insights for Developing Thermotolerant Crops
inferred← citeshttps://doi.org/10.3389/fpls.2020.00948openalex-snapshot
Systematic Review of Plant Ribosome Heterogeneity and Specialization
inferred← citeshttps://doi.org/10.3390/ijms15057624openalex-snapshot
Degradation of Organelles or Specific Organelle Components via Selective Autophagy in Plant Cells
inferred← citeshttps://doi.org/10.3390/ijms25115882openalex-snapshot
Elevated Temperature Effects on Protein Turnover Dynamics in Arabidopsis thaliana Seedlings Revealed by 15N-Stable Isotope Labeling and ProteinTurnover Algorithm
inferred← citeshttps://doi.org/10.70675/1c379a96z0deez4407zbf06z5144fecbf1f1openalex-snapshot
Optimisation de la respiration du nitrate à travers l'organisation de ses acteurs
inferred← citeshttps://doi.org/10.7554/elife.05357openalex-snapshot
Dynamic subcellular localization of a respiratory complex controls bacterial respiration
inferred← citeshttps://doi.org/10.7554/elife.05357.017openalex-snapshot
Author response: Dynamic subcellular localization of a respiratory complex controls bacterial respiration
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