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Related Concept Videos

Prodrugs01:30

Prodrugs

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Prodrugs are a class of pharmaceutical compounds that undergo a biotransformation process within the body to be converted into a pharmacologically active drug. Prodrugs are designed to improve the therapeutic properties of the parent drug, such as enhancing bioavailability, increasing stability, or reducing toxicity. The concept of prodrugs revolves around modifying the chemical structure of the original drug to make it more effective or convenient for administration.
Prodrugs help overcome...
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Upstream Processing01:27

Upstream Processing

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Upstream processing represents a critical phase in biomanufacturing, wherein biological systems such as microorganisms, mammalian cells, or insect cells are cultivated to produce therapeutic proteins, vaccines, enzymes, or other biologically derived products. This phase encompasses all steps from the selection and genetic manipulation of the production organism to the cultivation of cells in bioreactors under tightly controlled environmental conditions.Host Selection and Genetic OptimizationThe...
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Pore Transport and Ion-Pair Transport01:17

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Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Ribozymes02:47

Ribozymes

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The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
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Updated: Apr 3, 2026

PRP as a New Approach to Prevent Infection: Preparation and In vitro Antimicrobial Properties of PRP
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Prions: what are they good for?

Kausik Si1

  • 1Stowers Institute for Medical Research, Kansas City, Missouri 64110;

Annual Review of Cell and Developmental Biology
|September 26, 2015
PubMed
Summary

Prions, or self-templating proteins, can cause disease but may also offer benefits. This review explores how prion-like protein states can create lasting physiological changes from temporary triggers.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Cell Biology

Background:

  • Prions are misfolded proteins that can induce normal proteins to misfold, leading to neurodegenerative diseases.
  • The aggregation of proteins into prionogenic and amyloid forms was traditionally viewed as detrimental.

Purpose of the Study:

  • To challenge the notion that all prion-like protein aggregation is harmful.
  • To explore the potential beneficial roles of prion-like protein states.
  • To discuss the mechanisms by which transient stimuli can induce sustained physiological changes via prion-based conformational switches.

Main Methods:

  • Literature review of prion biology and protein aggregation.
  • Analysis of studies identifying non-pathogenic prion-like proteins.
Keywords:
amyloidsfunctional prionsprions

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  • Conceptual framework for prion-based conformational switching.

    • Main Results:

    • Emerging evidence suggests some prion-like protein states are non-pathogenic and potentially beneficial.
    • Prion-based conformational changes can be harnessed for physiological adaptation.

    Conclusions:

    • Protein aggregation is not exclusively harmful; prion-like mechanisms can serve physiological functions.
    • Understanding prion-based conformational switches offers insights into cellular adaptation and potential therapeutic strategies.