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Related Concept Videos

Complement System01:27

Complement System

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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...
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Antibody Actions01:26

Antibody Actions

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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
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T Cell Activation and Clonal Selection01:22

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T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...
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Activation of Integrins01:15

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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Antimicrobial Proteins01:23

Antimicrobial Proteins

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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.
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Updated: Apr 5, 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

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Structural insights on complement activation.

Martín Alcorlo1, Andrés López-Perrote1, Sandra Delgado2

  • 1Centro de Investigaciones Biológicas (CIB), Consejo Superior de Investigaciones Científicas, Madrid, Spain.

The FEBS Journal
|August 8, 2015
PubMed
Summary
This summary is machine-generated.

The complement system

Keywords:
C3bcomplementelectron microscopyiC3bthio-ester-containing domain

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

  • Immunology and biochemistry.
  • Structural biology and protein dynamics.

Background:

  • Complement activation is crucial for innate immunity, with C3 cleavage to C3b being central.
  • C3b covalently binds surfaces, initiating complement cascades and immune responses.

Purpose of the Study:

  • To review current knowledge on C3b structural flexibility.
  • To propose a model for C3b conformational heterogeneity and its regulatory implications.

Main Methods:

  • Comparative structural analysis of C3 and C3b.
  • Review of recent evidence on C3b solution structure and dynamics.

Main Results:

  • C3 to C3b transition involves significant conformational changes and exposure of a reactive thioester group.
  • C3b structural flexibility allows diverse conformations, impacting regulator interactions.
  • The thioester-containing domain (TED) exhibits dynamic positioning relative to the macroglobulin (MG) ring.

Conclusions:

  • C3b exhibits substantial structural flexibility, challenging previous static models.
  • This conformational heterogeneity is critical for effective complement regulation by various factors.
  • Understanding C3b dynamics is key to deciphering complement system function and dysregulation.