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Related Concept Videos

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...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

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The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Targeted Cancer Therapies02:57

Targeted Cancer Therapies

The targeted cancer therapies, also known as “molecular targeted therapies,” take advantage of the molecular and genetic differences between the cancer cells and the normal cells. It needs a thorough understanding of the cancer cells to develop drugs that can target specific molecular aspects that drive the growth, progression, and spread of cancer cells without affecting the growth and survival of other normal cells in the body.
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
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Targeting the purinome.

Jeremy M Murray1, Dirksen E Bussiere

  • 1Department of Protein Engineering, Genentech, Inc., South San Francisco, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 4, 2009
PubMed
Summary
This summary is machine-generated.

Purine-binding proteins, or the purinome, are crucial for life and represent significant drug targets. Understanding protein:purine recognition and druggability aids in developing new therapeutics.

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Area of Science:

  • Biochemistry
  • Drug Discovery
  • Structural Biology

Background:

  • Purines are essential cofactors in biological processes.
  • The human purinome comprises over 3,000 proteins utilizing purine cofactors.
  • Many purinome proteins, like kinases and G-proteins, are validated drug targets.

Purpose of the Study:

  • To review forces mediating protein:purine recognition.
  • To discuss factors determining protein target druggability.
  • To explore structure-based drug design for purine-binding proteins.

Main Methods:

  • Review of literature on protein:purine interactions.
  • Analysis of druggability factors for purinome members.
  • Examination of structure-based drug design principles.

Main Results:

  • Protein:purine recognition is mediated by specific binding forces.
  • Druggability of purinome targets varies, influenced by protein structure and function.
  • Structure-based design is a key strategy for developing purinome-targeted drugs.

Conclusions:

  • The human purinome offers vast potential for therapeutic intervention.
  • Understanding molecular recognition and druggability is vital for successful drug discovery.
  • Structure-based approaches are critical for targeting purine-binding proteins effectively.