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Related Concept Videos

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.
Introduction to Nuclear Reprogramming01:14

Introduction to Nuclear Reprogramming

Nuclear reprogramming is the process of switching gene expression of one cell type to that of another cell type, usually from a differentiated cell state to an undifferentiated cell state. Differentiation occurs during processes such as development and morphogenesis, tissue regeneration, and malignancy. Cells can also be artificially induced to reprogram their gene expression by techniques such as nuclear transfer, induced pluripotency, and cell fusion. Such techniques have many applications in...
Negative Regulator Molecules01:23

Negative Regulator Molecules

Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
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...
Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

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Related Experiment Video

Updated: May 15, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
10:12

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications

Published on: April 21, 2023

Reprogramming cellular events by poly(ADP-ribose)-binding proteins.

Jana Krietsch1,2, Michèle Rouleau1,3, Émilie Pic1

  • 1Centre de recherche du CHUQ - Pavillon CHUL - Cancer Axis, Laval University, Québec, QC, Canada G1V 4G2.

Molecular Aspects of Medicine
|December 27, 2012
PubMed
Summary

Poly(ADP-ribosyl)ation, a key cellular process, involves poly(ADP-ribose) polymerases (PARPs) modifying proteins. Non-covalent binding to these modifications regulates crucial pathways like DNA repair and cell death.

Keywords:
Macro domainPARGPARPPBZPoly(ADP-ribose)WWE

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Last Updated: May 15, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
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Published on: January 31, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Poly(ADP-ribosyl)ation is a posttranslational modification catalyzed by PARPs.
  • PARPs add ADP-ribose units to proteins, altering their function.
  • Non-covalent binding to poly(ADP-ribose) (pADPr) regulates intracellular pathways.

Purpose of the Study:

  • To describe the basis of non-covalent binding to pADPr.
  • To introduce the concept of pADPr-responsive signaling pathways.
  • To emphasize structural elements and modular strategies in pADPr-binding proteins.

Main Methods:

  • Literature review of poly(ADP-ribosyl)ation and pADPr-binding proteins.
  • Analysis of structural elements and modular strategies.
  • Highlighting characterized and newly discovered pADPr-binding modules.

Main Results:

  • Non-covalent binding to pADPr is a key regulatory mechanism.
  • pADPr-binding proteins utilize modular strategies for pathway control.
  • Four specialized pADPr-binding modules accommodate different pADPr structures.

Conclusions:

  • pADPr-binding modules fine-tune protein functions in diverse pathways.
  • Understanding these modules is crucial for comprehending cellular regulation.
  • This mechanism plays a role in DNA damage response, protein stability, and cell death.