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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Proteomics01:33

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Decoding protein networks during virus entry by quantitative proteomics.

Gisa Gerold1, Janina Bruening1, Thomas Pietschmann2

  • 1Insitute for Experimental Virology, TWINCORE, Centre for Experimental and Clinical Infection Research, A joint Venture Between the Medical School Hannover and the Helmholtz Centre for Infection Research, 30652 Hannover, Germany.

Virus Research
|September 15, 2015
PubMed
Summary
This summary is machine-generated.

Understanding virus entry into host cells requires studying protein-protein interactions. Quantitative proteomics offers advanced methods to map these functional virus entry networks, aiding future research.

Keywords:
Protein interaction networksProtein–protein interactionsQuantitative proteomicsVirus entry

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Area of Science:

  • Virology
  • Biochemistry
  • Proteomics

Background:

  • Virus entry into host cells depends on complex interactions between viral and host proteins.
  • These protein-protein interactions are dynamic, often involving multiprotein complexes crucial for viral binding and uptake.

Purpose of the Study:

  • To review protein interactions during virus entry.
  • To compare classical biochemical methods with advanced quantitative proteomics techniques for studying these interactions.

Main Methods:

  • Review of existing literature on virus entry mechanisms.
  • Comparison of traditional biochemical assays with mass spectrometry-based quantitative proteomics.
  • Highlighting the application of proteomics in mapping virus entry networks.

Main Results:

  • Quantitative proteomics enables reliable protein quantitation from limited samples.
  • Proteomics provides insights into post-translational modifications and protein interactions.
  • Advanced proteomics methods are valuable for mapping functional virus entry networks.

Conclusions:

  • Quantitative proteomics is an indispensable tool for virologists studying virus entry.
  • This methodology offers significant benefits for resolving complex questions in virus entry research.
  • The review emphasizes the power of proteomics in elucidating dynamic viral-host interactions.