ReviewMolecular & cellular proteomics : MCP2010
Proteomics of Saccharomyces cerevisiae Organelles.
Review in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 51 citations in OpenAlex.
- Engineering COInternational journal of molecular sciences · 2025Article
- Qualitative Proteomic Profiling ofFoods (Basel, Switzerland) · 2025Article
- The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria.EMBO reports · 2024Article
- Article
- Genome-scale modeling of yeast metabolism: retrospectives and perspectives.FEMS yeast research · 2022Review
- Current Ethanol Production Requirements for the YeastInternational journal of microbiology · 2022Review
- Wheat omics: Classical breeding to new breeding technologies.Saudi journal of biological sciences · 2021Review
- A subcellular proteome atlas of the yeast Komagataella phaffii.FEMS yeast research · 2020Article
- Quantitative Analyses of the Yeast Oxidative Protein Folding PathwayAntioxidants & redox signaling · 2019Article
- A Protocol to Map the Spatial Proteome Using HyperLOPIT inBio-protocol · 2019Article
- The plasma membrane proteome of Medicago truncatula roots as modified by arbuscular mycorrhizal symbiosis.Mycorrhiza · 2018Article
- Comparison of three methods for mitochondria isolation from the human liver cell line (HepG2).Gastroenterology and hepatology from bed to bench · 2016Article
- Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.PloS one · 2015Article
- The proteomics of lipid droplets: structure, dynamics, and functions of the organelle conserved from bacteria to humans.Journal of lipid research · 2012Review
- Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes.The Journal of biological chemistry · 2011Article
- Online nanoflow reversed phase-strong anion exchange-reversed phase liquid chromatography-tandem mass spectrometry platform for efficient and in-depth proteome sequence analysis of complex organisms.Analytical chemistry · 2011Article
- Proteomic approaches to understanding the role of the cytoskeleton in host-defense mechanisms.Expert review of proteomics · 2011Review
- Defining the plant peroxisomal proteome: from Arabidopsis to rice.Frontiers in plant science · 2011Article
- Opportunities and successes in the search for plasmodesmal proteins.Protoplasma · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Knowledge of the subcellular localization of proteins is indispensable to understand their physiological roles. In the past decade, 18 studies have been performed to analyze the protein content of isolated organelles from Saccharomyces cerevisiae. Here, we integrate the data sets and compare them with other large scale studies on protein localization and abundance. We evaluate the completeness and reliability of the organelle proteomics studies. Reliability depends on the purity of the organelle preparations, which unavoidably contain (small) amounts of contaminants from different locations. Quantitative proteomics methods can be used to distinguish between true organellar constituents and contaminants. Completeness is compromised when loosely or dynamically associated proteins are lost during organelle preparation and also depends on the sensitivity of the analytical methods for protein detection. There is a clear trend in the data from the 18 organelle proteomics studies showing that proteins of low abundance frequently escape detection. Proteins with unknown function or cellular abundance are also infrequently detected, indicating that these proteins may not be expressed under the conditions used. We discuss that the yeast organelle proteomics studies provide powerful lead data for further detailed studies and that methodological advances in organelle preparation and in protein detection may help to improve the completeness and reliability of the data.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.