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Related Concept Videos

Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
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.
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...
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...
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...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...

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Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
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Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O

Published on: August 9, 2024

Kinase regulation by sulfur and selenium containing compounds.

Carmen Sanmartín1, Daniel Plano, María Font

  • 1Department of Organic and Pharmaceutical Chemistry, University of Navarra, Irunlarrea 1, E-31008, Pamplona, Spain. sanmartin@unav.es

Current Cancer Drug Targets
|March 15, 2011
PubMed
Summary

Sulfur and selenium compounds modulate kinases, offering potential anticancer therapies. Selenium derivatives show enhanced chemopreventive activity compared to sulfur analogs, targeting key cancer pathways.

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Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Oncology

Background:

  • Kinases are crucial enzymes regulating cellular processes; aberrant activity is linked to diseases like cancer.
  • Over 518 human kinases present therapeutic targets, driving drug development for cancer therapy.
  • Sulfur and selenium are recognized for their chemopreventive properties, particularly against various cancers.

Purpose of the Study:

  • To review the development of novel sulfur and selenium-containing compounds for cancer therapy.
  • To explore the kinase modulation mechanisms of sulfur and selenium derivatives in cancer prevention.
  • To discuss the implications of kinase modulation for antitumoral effects.

Main Methods:

  • Literature review of studies on sulfur, selenium, and kinase modulation in cancer.
  • Analysis of signaling pathways targeted by these elements, including MAP, ERK, JNK, Akt, Cdc2, Cyclin B1, and Cdc25c.
  • Comparison of the biochemical differences and anticancer activities between sulfur and selenium compounds.

Main Results:

  • Sulfur and selenium derivatives modulate various kinases involved in cell signaling pathways.
  • Selenium analogs often exhibit superior chemopreventive and anticancer efficacy compared to their sulfur counterparts.
  • Kinase modulation by these elements is a key mechanism underlying their antitumoral effects.

Conclusions:

  • Targeting kinase modulation pathways with novel sulfur and selenium structures holds promise for cancer treatment.
  • Understanding the distinct properties of sulfur and selenium is crucial for designing effective chemopreventive agents.
  • Further research into these elements and their kinase interactions can lead to advanced cancer therapies.