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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

Tracking protein aggregate interactions.

Christina J Sigurdson1, Jason C Bartz, K Peter R Nilsson

  • 1Department of Pathology, University of California San Diego, La Jolla, CA, USA. red b-sheets aligne

Prion
|May 21, 2011
PubMed
Summary
This summary is machine-generated.

Amyloid fibrils can template new protein misfolding. This study investigates how different amyloid structures interact within the central nervous system, impacting prion disease.

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Last Updated: Jun 1, 2026

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Amyloid fibrils feature ordered β-sheets that recruit monomers for fibril extension.
  • Distinct amyloid structures, or strains, are linked to varied prion disease phenotypes.
  • Interactions between co-occurring amyloid proteins in the central nervous system are not well understood.

Purpose of the Study:

  • To explore the interactions between distinct amyloid fibrils or prion strains in the central nervous system.
  • To clarify whether co-existing protein aggregates influence each other's assembly.

Main Methods:

  • Literature review of reported interactions between amyloids and prion strains in vivo.
  • Analysis of studies focusing on co-pathologies in the central nervous system.

Main Results:

  • Amyloid structures can influence the assembly of other proteins.
  • Prion strains exhibit distinct structural properties that affect disease presentation.
  • Interactions between different amyloid aggregates can lead to complex pathological outcomes.

Conclusions:

  • Understanding cross-seeding and strain interactions is crucial for deciphering amyloid and prion diseases.
  • Further research is needed to elucidate the mechanisms governing these interactions and their clinical implications.