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Related Concept Videos

Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
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Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Septins01:19

Septins

Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
Aromatic Hydrocarbon Cations: Structural Overview01:18

Aromatic Hydrocarbon Cations: Structural Overview

Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
Removing one hydrogen from the intervening CH2 group with both...

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Related Experiment Video

Updated: May 10, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &beta;2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Specific structure and unique function define the hemicentin.

Xuehong Xu1, Mengmeng Xu, Xin Zhou

  • 1School of Life Sciences, Shaanxi Normal University, Xi'an, Shaanxi 710062, China. xhx0708@gmail.com.

Cell & Bioscience
|June 28, 2013
PubMed
Summary
This summary is machine-generated.

Hemicentin protein maintains tissue integrity and plays a key role in cell division. Further research is needed to fully understand this evolutionarily conserved protein and its functions.

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Related Experiment Videos

Last Updated: May 10, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &beta;2-Microglobulin
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Published on: March 10, 2021

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Developmental Biology

Background:

  • Hemicentin, initially identified in C. elegans as him-4, is an evolutionarily conserved protein.
  • It is crucial for maintaining the architectural integrity of vertebrate tissues and organs.
  • Hemicentin is found on the cell surface of various cell types, including epithelial and endothelial cells.

Purpose of the Study:

  • To highlight the established and newly discovered functions of hemicentin.
  • To emphasize the protein's role in maintaining tissue architecture and mitotic cytokinesis.
  • To underscore the need for further investigation into hemicentin's functions.

Main Methods:

  • Literature review of hemicentin research.
  • Analysis of conserved hemicentin sequences across species.
  • Examination of hemicentin distribution in mouse tissues.

Main Results:

  • Hemicentin is vital for vertebrate tissue and organ integrity.
  • The protein is widely distributed on cell surfaces in various mouse tissues.
  • Hemicentin plays a critical role in the maturation of the cleavage furrow during mitotic cytokinesis.

Conclusions:

  • Hemicentin is an important extracellular matrix protein with conserved functions.
  • Its roles extend from maintaining tissue structure to facilitating cell division.
  • Despite recent advances, significant aspects of hemicentin's biology remain to be elucidated.