Directed Proteomic Analysis of the Human Nucleolus

@article{Andersen2002DirectedPA,
  title={Directed Proteomic Analysis of the Human Nucleolus},
  author={Jens S. Andersen and Carol E. Lyon and Archa H Fox and Anthony Kar Lun Leung and Yun Wah Lam and Hanno Steen and Matthias Mann and Angus I. Lamond},
  journal={Current Biology},
  year={2002},
  volume={12},
  pages={1-11}
}
BACKGROUND The nucleolus is a subnuclear organelle containing the ribosomal RNA gene clusters and ribosome biogenesis factors. Recent studies suggest it may also have roles in RNA transport, RNA modification, and cell cycle regulation. Despite over 150 years of research into nucleoli, many aspects of their structure and function remain uncharacterized. RESULTS We report a proteomic analysis of human nucleoli. Using a combination of mass spectrometry (MS) and sequence database searches… Expand
Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions.
TLDR
The first proteomic analysis of plant (Arabidopsis thaliana) nucleoli is described, in which 217 proteins are identified, allowing a direct comparison of the proteomes of an important nuclear structure between two widely divergent species: human and Arabidopsis. Expand
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The data establish a quantitative proteomic approach for the temporal characterization of protein flux through cellular organelles and demonstrate that the nucleolar proteome changes significantly over time in response to changes in cellular growth conditions. Expand
Bioinformatic analysis of the nucleolus.
TLDR
This review focuses on how to apply the derived knowledge of this newly recognized nucleolar proteome, such as their amino acid/peptide composition and their homologies across species, to explore the function and dynamics of the nucleolus. Expand
The dynamics of the nucleolus.
  • A. Leung, A. Lamond
  • Biology, Medicine
  • Critical reviews in eukaryotic gene expression
  • 2003
TLDR
This review focuses on nucleolar dynamics, studied at each of the single protein, collective proteome, and subnucleolar organization levels. Expand
Functional proteomic analysis of human nucleolus.
TLDR
A proteomic analysis was carried out to draw up a list of proteins present within nucleoli of HeLa cells, allowing the identification of 213 different nucleolar proteins, which reinforces the plurifunctional nature of nucleoli and provides convincing evidence that nucleoli may play a central role in the control of gene expression. Expand
[Advances in the study of the nucleolus].
TLDR
Recent advances in the study of the nucleolus are summarized, including new discoveries of its structure, function, genomics/proteomics as well as its origin and evolution, and several of the important unresolved issues are highlighted. Expand
Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
TLDR
Ribosomal proteins are expressed at high levels beyond that required for the typical rate of ribosome-subunit production and accumulate in the nucleolus more quickly than all other nucleolar components, thereby providing a mechanism for mammalian cells to ensure that ribosomal protein levels are never rate limiting for the efficient assembly of Ribosome subunits. Expand
The Nucleolus Takes Control of Protein Trafficking Under Cellular Stress.
TLDR
The role of Nucleolin and Nucleophosmin, two major components of the nucleolus, in response to genotoxic stress are focused on. Expand
Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder
TLDR
This study provides the first proteome-wide analysis of intrinsic protein disorder for the human nucleolus and shows that nucleolar proteins in general, and mitotic chromosome proteins in particular, have significantly higher intrinsic disorder level compared to cytosolic proteins. Expand
Proteomic characterization of the nucleolar linker histone H1 interaction network.
TLDR
It is concluded that H1 organizes and maintains an extensive protein-protein interaction network in the nucleolus required for nucleolar structure and integrity. Expand
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