Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

18.5K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.5K
The Unfolded Protein Response01:37

The Unfolded Protein Response

5.2K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
5.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.6K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.6K
Stringent Response in E. coli01:23

Stringent Response in E. coli

71
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
71
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

5.2K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
5.2K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.7K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Clade 2.3.4.4b H5N1 HPAIV from Migratory Birds in Beidaihe Wetland, North China.

Viruses·2026
Same author

Structural characterization, rheological properties, and skin bioactivities of a glucomannan from Bletilla striata.

Natural products and bioprospecting·2026
Same author

Glycodeoxycholic acid synergizes with L-malic acid to upregulate the malolactic enzyme pathway to alleviate self-toxicity in <i>Lacticaseibacillus paracasei</i> L9.

Applied and environmental microbiology·2026
Same author

Common, Intermediate and Well-Documented HLA Alleles in the Chinese Population: CIWD Version 2025.

HLA·2026
Same author

Selection and application of aptamers targeting the Brucella BP26 protein.

Analytical biochemistry·2026
Same author

Integrating aptamer-transduced signal amplification and superwettable droplet microarrays for single-cell detection of cell surface vimentin.

Talanta·2026

Related Experiment Video

Updated: Oct 5, 2025

Loop-mediated Isothermal Amplification LAMP Assays for the Species-specific Detection of Eimeria that Infect Chickens
06:57

Loop-mediated Isothermal Amplification LAMP Assays for the Species-specific Detection of Eimeria that Infect Chickens

Published on: February 20, 2015

27.1K

Eimeria proteins: order amidst disorder.

Joshua Seun Olajide1,2,3, Zigang Qu1,2, Shunli Yang1,2

  • 1State Key Laboratory of Veterinary Etiological Biology, Key Laboratory of Veterinary Parasitology of Gansu, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, 730046, China.

Parasites & Vectors
|January 25, 2022
PubMed
Summary
This summary is machine-generated.

This review overviews constitutively expressed Eimeria proteins, crucial for understanding these apicomplexan parasites. It details their functions across developmental stages and cellular components, aiding future research.

Keywords:
AntigenApicomplexaCoccidiosisEimeriaParasiteProteinSecretion

More Related Videos

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
12:48

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

12.2K
Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites
08:26

Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites

Published on: February 14, 2020

7.1K

Related Experiment Videos

Last Updated: Oct 5, 2025

Loop-mediated Isothermal Amplification LAMP Assays for the Species-specific Detection of Eimeria that Infect Chickens
06:57

Loop-mediated Isothermal Amplification LAMP Assays for the Species-specific Detection of Eimeria that Infect Chickens

Published on: February 20, 2015

27.1K
The Multifaceted Benefits of Protein Co-expression in Escherichia coli
12:48

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

12.2K
Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites
08:26

Nucleofection and In Vivo Propagation of Chicken Eimeria Parasites

Published on: February 14, 2020

7.1K

Area of Science:

  • Parasitology
  • Molecular Biology
  • Veterinary Medicine

Background:

  • Apicomplexans are significant pathogens in humans and animals.
  • Protein modulation is key in parasite development, physiology, and pathogenesis.
  • Eimeria species cause substantial economic losses in livestock, necessitating protein characterization.

Purpose of the Study:

  • To provide a comprehensive overview of constitutively expressed Eimeria proteins.
  • To discuss these proteins across different developmental stages and cellular locations.
  • To offer insights and suggestions for future Eimeria protein research.

Main Methods:

  • Literature review of existing studies on Eimeria proteins.
  • Analysis of protein functions in relation to parasite biology.
  • Synthesis of information on protein localization and roles.

Main Results:

  • Identification and discussion of key constitutively expressed Eimeria proteins.
  • Elucidation of protein functions during various life cycle stages.
  • Mapping of proteins to specific organelles and sub-cellular compartments.

Conclusions:

  • Constitutively expressed proteins are vital for Eimeria survival and pathogenesis.
  • Further characterization of these proteins can reveal new therapeutic targets.
  • This review establishes a baseline for future Eimeria protein studies.