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Related Concept Videos

Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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...
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
Antimicrobial Proteins01:23

Antimicrobial Proteins

Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
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

Eukaryotic cells can degrade proteins through several pathways. One of the most important among 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. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Updated: May 20, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

Published on: July 18, 2017

Structure, function and control of complement C5 and its proteolytic fragments.

N S Laursen1, F Magnani, R H Gottfredsen

  • 1Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark.

Current Molecular Medicine
|July 21, 2012
PubMed
Summary
This summary is machine-generated.

The complement system

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Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
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Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

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Last Updated: May 20, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
08:26

Measuring the 50% Haemolytic Complement (CH50) Activity of Serum

Published on: March 29, 2010

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

Area of Science:

  • Immunology
  • Molecular Biology
  • Structural Biology

Background:

  • The complement system is a key part of innate immunity, identifying pathogens and altered self cells.
  • Complement activation leads to C5 protein cleavage into C5a and C5b fragments, initiating immune responses.
  • C5a triggers inflammation, while C5b forms the membrane attack complex for pathogen lysis.

Purpose of the Study:

  • To review the functional and structural aspects of complement C5 and its fragments.
  • To discuss pathological conditions linked to C5a and C5b.
  • To explore pathogen evasion strategies and their therapeutic implications.

Main Methods:

  • Review of recent crystal structures of C5 and its fragments.
  • Analysis of functional data on C5a and C5b.
  • Examination of pathogen-complement interactions.

Main Results:

  • Recent structural data provide insights into C5 architecture, function, and pathogen interference.
  • C5a contributes to inflammatory diseases like sepsis and arthritis.
  • Inhibition of membrane attack complex is an established therapy for specific disorders.

Conclusions:

  • Understanding C5 structure and pathogen evasion strategies is crucial for developing new C5 inhibitors.
  • Targeting C5 offers therapeutic potential for inflammatory and autoimmune diseases.
  • Novel selective C5 inhibitors could advance treatment options.