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Related Concept Videos

Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
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.
siRNA - Small Interfering RNAs02:30

siRNA - Small Interfering RNAs

Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional level in some cases. siRNAs are important for protecting cells against viral infections and silencing transposable genetic elements.
In the cytoplasm, siRNA is processed from a double-stranded RNA, which comes from either endogenous DNA transcription or exogenous sources like a virus. This double-stranded RNA is then cleaved by the ATP-dependent...
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Inhibition of CDK Activity02:34

Inhibition of CDK Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...

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Related Experiment Video

Updated: May 17, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Structural basis for sirtuin activity and inhibition.

Hua Yuan1, Ronen Marmorstein

  • 1Program in Gene Expression and Regulation, The Wistar Institute, University of Pennsylvania,Philadelphia, Pennsylvania 19104, USA.

The Journal of Biological Chemistry
|October 23, 2012
PubMed
Summary
This summary is machine-generated.

Sir2 proteins, or sirtuins, are enzymes with catalytic activities including deacetylation. Over 40 crystal structures reveal molecular details crucial for understanding sirtuin function and regulation.

Related Experiment Videos

Last Updated: May 17, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Sirtuins (Sir2 proteins) are a class of enzymes involved in crucial cellular processes.
  • They exhibit NAD(+)-dependent deacetylation and other enzymatic activities like ribosyltransferase, demalonylase, and desuccinylase.
  • Understanding their molecular mechanisms is vital for biological research.

Purpose of the Study:

  • To summarize the known structural features of sirtuins.
  • To discuss the implications of these structural details for understanding sirtuin function.
  • To provide a foundation for future research on sirtuin mechanisms.

Main Methods:

  • Review of over 40 determined crystal structures of sirtuins.
  • Analysis of structures in various liganded forms.
  • Synthesis of existing structural data.

Main Results:

  • Detailed high-resolution architectural information of sirtuins is available.
  • Structural data provides insights into catalysis, regulation, substrate specificity, and inhibition.
  • Multiple liganded forms offer diverse perspectives on enzyme-substrate interactions.

Conclusions:

  • The wealth of sirtuin crystal structures is foundational for mechanistic understanding.
  • Structural insights are key to deciphering sirtuin's diverse biological roles.
  • Further research can leverage these structural features to explore sirtuin function and inhibition.