Related Experiment Video

Updated: Aug 29, 2026

Forward Genetic Approaches in Chlamydia trachomatis
09:03

Forward Genetic Approaches in Chlamydia trachomatis

Published on: October 23, 2013

Chlorate: a reversible inhibitor of proteoglycan sulphation in Chlamydia trachomatis-infected cells

Sanaa Fadel1, Adrian Eley1

  • 1Division of Genomic Medicine, Medical School, University of Sheffield, Sheffield, S10 2RX, UK.

Journal of Medical Microbiology
|January 20, 2004
PubMed

More Related Videos

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis10:35

Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis

Published on: January 30, 2020

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis10:32

Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

Published on: June 10, 2020

Related Concept Videos

Bacterial Phylum Chlamydiae01:29

Bacterial Phylum Chlamydiae

The phylum Chlamydiae or Chlamydiota is composed of a single order, Chlamydiales. This phylum consists entirely of obligate intracellular parasites that infect eukaryotic hosts. While human pathogens within this group have been studied extensively, the phylum encompasses many species capable of interacting with various eukaryotic organisms. Members of Chlamydiae are typically small cocci, approximately 0.5 μm in diameter, and exhibit a distinctive developmental cycle. As is characteristic of...
Trichomoniasis01:18

Trichomoniasis

Trichomonas vaginalis is a flagellated protozoan parasite and the causative agent of trichomoniasis, one of the most prevalent non-viral sexually transmitted infections in the United States. This extracellular parasite primarily colonizes the lower genitourinary tract in women—particularly the vagina—and in men, the urethra and prostate. Its structural and functional adaptations enable its survival, motility, and pathogenicity within the host environment.Structural Features and Host EntryT.
Antiprotozoal Agents01:21

Antiprotozoal Agents

Leishmaniasis is a widespread parasitic disease caused by several Leishmania species. It affects millions of people each year and remains a major public health problem in endemic regions. First-line treatment relies on pentavalent antimonials, including meglumine antimoniate and sodium stibogluconate. Even so, how these drugs work has not been fully clear, especially their interaction with parasite-specific biochemical pathways. One key target is trypanothione reductase (TR), an enzyme that...
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:29

Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

Indirect-acting cholinergic agonists are agents that interact with the acetylcholinesterase enzyme in the synaptic cleft, preventing the breakdown of acetylcholine into choline and acetate. Consequently, the concentration of acetylcholine in the synaptic cleft increases. These agonists can be classified into reversible and irreversible inhibitors based on their duration of action.
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Carboxylic Acids to Acid Chlorides01:18

Carboxylic Acids to Acid Chlorides

Carboxylic acids react with SOCl2 or PCl5 to form acid chlorides. Amongst the carboxylic acid derivatives, acid chlorides are the most reactive and synthetically important derivatives. They are useful reagents for Friedel–Crafts acylation of some aromatic compounds.
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...