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Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol

Authors: Christis, C.; Lubsen, N.H.; Lubsen, N.H.; Braakman, I.;

Protein folding includes oligomerization – examples from the endoplasmic reticulum and cytosol

Abstract

A correct three‐dimensional structure is a prerequisite for protein functionality, and therefore for life. Thus, it is not surprising that our cells are packed with proteins that assist protein folding, the process in which the native three‐dimensional structure is formed. In general, plasma membrane and secreted proteins, as well as those residing in compartments along the endocytic and exocytic pathways, fold and oligomerize in the endoplasmic reticulum. The proteins residing in the endoplasmic reticulum are specialized in the folding of this subset of proteins, which renders this compartment a protein‐folding factory. This review focuses on protein folding in the endoplasmic reticulum, and discusses the challenge of oligomer formation in the endoplasmic reticulum as well as the cytosol.

Related Organizations
Keywords

Protein Folding, Polymers, Protein Disulfide-Isomerases, Receptors, Antigen, T-Cell, Endoplasmic Reticulum, Cytosol, Lectins, HSP70 Heat-Shock Proteins, Oxidoreductases Acting on Sulfur Group Donors, Molecular Biology, Glycoproteins, Deoxyribonucleases, Membrane Glycoproteins, Research Programme of Radboud Institute for Molecular Life Sciences, Bio-Molecular Chemistry, DNA-Directed RNA Polymerases, Peptidylprolyl Isomerase, Globins, Protein Transport, Immunoglobulin M, Apoptosis Regulatory Proteins, Dimerization, Molecular Chaperones

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    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    52
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 10%
    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    Top 10%
    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
    Top 10%
Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
52
Top 10%
Top 10%
Top 10%
Green
bronze