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Related Concept Videos

DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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.
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Biological Effects of Radiation02:59

Biological Effects of Radiation

All radioactive nuclides emit high-energy particles or electromagnetic waves. When this radiation encounters living cells, it can cause heating, break chemical bonds, or ionize molecules. The most serious biological damage results when these radioactive emissions fragment or ionize molecules. For example, α and β particles emitted from nuclear decay reactions possess much higher energies than ordinary chemical bond energies. When these particles strike and penetrate matter, they produce ions...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: Jul 2, 2026

Preparation of Peripheral Blood Mononuclear Cell Pellets and Plasma from a Single Blood Draw at Clinical Trial Sites for Biomarker Analysis
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Preparation of Peripheral Blood Mononuclear Cell Pellets and Plasma from a Single Blood Draw at Clinical Trial Sites for Biomarker Analysis

Published on: March 20, 2021

Specific ATM-mediated phosphorylation dependent on radiation quality.

Mary K Whalen1, Sukhleen K Gurai, Hengameh Zahed-Kargaran

  • 1Lawrence Berkeley National Laboratory, Life Sciences Division, Berkeley, California 94720, USA.

Radiation Research
|September 4, 2008
PubMed
Summary

High- and low-LET radiation trigger different cellular repair responses. While gamma-H2AX increased with high-LET radiation, ATM-dependent pATF2 and pSMC1 levels decreased, indicating distinct DNA repair signaling.

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Measuring DNA Damage and Repair in Mouse Splenocytes After Chronic In Vivo Exposure to Very Low Doses of Beta- and Gamma-Radiation
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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Last Updated: Jul 2, 2026

Preparation of Peripheral Blood Mononuclear Cell Pellets and Plasma from a Single Blood Draw at Clinical Trial Sites for Biomarker Analysis
07:40

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Published on: March 20, 2021

Measuring DNA Damage and Repair in Mouse Splenocytes After Chronic In Vivo Exposure to Very Low Doses of Beta- and Gamma-Radiation
11:24

Measuring DNA Damage and Repair in Mouse Splenocytes After Chronic In Vivo Exposure to Very Low Doses of Beta- and Gamma-Radiation

Published on: July 3, 2015

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Cellular and Molecular Biology
  • Radiation Biology
  • Biophysics

Background:

  • Cellular responses to radiation are critical for understanding biological effects.
  • Different radiation types (e.g., high- vs. low-LET) can elicit distinct biological outcomes.
  • Phospho-proteins like gamma-H2AX, pATF2, and pSMC1 are key markers of DNA damage response and repair.

Purpose of the Study:

  • To investigate if physical differences between high- and low-linear energy transfer (LET) radiation are reflected in cellular phospho-protein profiles.
  • To compare the kinetics of gamma-H2AX, pATF2, and pSMC1 after X-ray (low-LET) and iron-ion (high-LET) exposure.
  • To elucidate the role of ATM in response to different radiation types.

Main Methods:

  • Utilized flow cytometry to quantify total phospho-protein levels (gamma-H2AX, pATF2, pSMC1) over time post-irradiation.
  • Exposed cells to X-rays (low-LET) and iron ions (high-LET) at equivalent doses.
  • Quantified phospho-protein foci to assess cellular response localization and intensity.

Main Results:

  • Observed greater induction and persistence of gamma-H2AX after high-LET (iron-ion) exposure compared to low-LET (X-ray) exposure.
  • Found markedly lower induction levels of pATF2 and pSMC1 after high-LET exposure compared to low-LET exposure.
  • Quantification of foci revealed fewer cells with pATF2 and pSMC1 foci, and fewer foci per cell, after high-LET exposure.

Conclusions:

  • High- and low-LET radiation induce differential cellular responses, particularly in ATM-dependent signaling pathways.
  • The ATM kinase appears to respond differently to double-strand breaks (DSBs) induced by high-LET versus low-LET radiation.
  • These findings highlight distinct molecular mechanisms underlying cellular responses to varying radiation qualities.