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Related Concept Videos

Globular Proteins01:27

Globular Proteins

7.5K
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
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Transcytosis of IgG01:15

Transcytosis of IgG

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Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
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Cytoplasm01:24

Cytoplasm

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The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The cytosol is a rich broth of water, ions, salts, and various organic molecules.
Protein Folding and Misfolding
The cytoplasm is the location for several cellular processes, including protein synthesis and folding. The aqueous nature of the cytosol promotes protein folding such that the hydrophobic amino acid side chains are buried in the protein...
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Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

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There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
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Hemoglobin01:24

Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Related Experiment Video

Updated: Jul 16, 2025

Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity
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Encapsulating Cytochrome c in Silica Aerogel Nanoarchitectures without Metal Nanoparticles while Retaining Gas-phase Bioactivity

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Insights into the function of cytoglobin.

Brandon J Reeder1

  • 1School of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex, U.K.

Biochemical Society Transactions
|September 18, 2023
PubMed
Summary

Cytoglobin (Cygb), a hemoglobin family member, has unclear functions despite extensive research. This review synthesizes two decades of studies on Cygb

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Cytoglobin (Cygb), a member of the hemoglobin family, was discovered in 2001, but its physiological and pathological functions remain largely elusive.
  • Over 200 publications have investigated Cygb's structure, redox chemistry, and involvement in cell signaling pathways, indicating significant research interest.
  • Despite diverse research, common themes regarding Cygb's roles are emerging, necessitating a comprehensive review.

Approach:

  • This review synthesizes structural, biochemical, and in vivo data on cytoglobin published over the past two decades.
  • It examines key areas including radical scavenging, nitric oxide homeostasis, and lipid binding/oxidation.
  • The review also investigates the influence of an intramolecular disulfide bond on Cygb's redox chemistry and its roles in cancer progression and liver fibrosis.
Keywords:
cytoglobindisulphide bondsprotein structureredox chemistry

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Key Points:

  • Cytoglobin's structure and redox properties are influenced by an intramolecular disulfide bond.
  • Cygb plays potential roles in radical scavenging, nitric oxide homeostasis, and lipid metabolism.
  • Emerging evidence links Cygb to cancer progression and liver fibrosis.

Conclusions:

  • The multifaceted nature of cytoglobin suggests diverse physiological and pathological roles.
  • Further research is needed to fully elucidate cytoglobin's mechanisms in cellular processes and disease.
  • Synthesizing current knowledge provides a foundation for future investigations into cytoglobin's functions.