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Related Concept Videos

Hypoxia01:23

Hypoxia

Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...
Proteomics01:33

Proteomics

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 proteomics...
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Related Experiment Video

Updated: May 31, 2026

Co-immunoprecipitation Assay Using Endogenous Nuclear Proteins from Cells Cultured Under Hypoxic Conditions
09:17

Co-immunoprecipitation Assay Using Endogenous Nuclear Proteins from Cells Cultured Under Hypoxic Conditions

Published on: August 2, 2018

Hypoxia elicits broad and systematic changes in protein subcellular localization.

Robert Michael Henke1, Ranita Ghosh Dastidar, Ajit Shah

  • 1Department of Molecular and Cell Biology, Center for Systems Biology, University of Texas at Dallas, Richardson, 75080, USA.

American Journal of Physiology. Cell Physiology
|July 15, 2011
PubMed
Summary

Hypoxia alters protein distribution in yeast cells, impacting 203 proteins involved in key cellular functions. This study reveals protein localization as a major mechanism in oxygen signaling, with implications for human hypoxia responses.

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Analysis of Global RNA Synthesis at the Single Cell Level following Hypoxia
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Last Updated: May 31, 2026

Co-immunoprecipitation Assay Using Endogenous Nuclear Proteins from Cells Cultured Under Hypoxic Conditions
09:17

Co-immunoprecipitation Assay Using Endogenous Nuclear Proteins from Cells Cultured Under Hypoxic Conditions

Published on: August 2, 2018

Rapid In Vivo Fixation and Isolation of Translational Complexes from Eukaryotic Cells
14:29

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Published on: December 25, 2021

Analysis of Global RNA Synthesis at the Single Cell Level following Hypoxia
14:53

Analysis of Global RNA Synthesis at the Single Cell Level following Hypoxia

Published on: May 13, 2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic cells rely on oxygen for energy, necessitating robust responses to oxygen level fluctuations.
  • Protein localization and modification are known regulators of protein function, but their role in oxygen signaling at a large scale is understudied.

Purpose of the Study:

  • To investigate the genomewide impact of hypoxia on protein distribution in the model eukaryote Saccharomyces cerevisiae.
  • To determine the contribution of protein localization to oxygen signaling pathways.

Main Methods:

  • Live cell imaging techniques were employed to track protein movements within yeast cells under hypoxic conditions.
  • Analysis of protein redistribution patterns during both hypoxia and reoxygenation phases.

Main Results:

  • Hypoxia induced significant changes in the cellular distribution of 203 yeast proteins, affecting proteins localized to various organelles.
  • Many affected proteins are nuclear components of transcriptional and chromatin remodeling complexes, retained in the cytosol under hypoxia.
  • Protein relocalization upon reoxygenation occurred efficiently, even with inhibited protein synthesis, and hypoxia-induced changes followed a slower time course than reoxygenation-induced changes.

Conclusions:

  • Regulation of protein localization is a widespread and potentially dominant mechanism in eukaryotic oxygen signaling.
  • These findings provide insights into hypoxia responses and may have implications for understanding human cellular responses to oxygen deprivation.