Related Experiment Video

Updated: Sep 27, 2026

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis
13:31

Novel Atomic Force Microscopy Based Biopanning for Isolation of Morphology Specific Reagents against TDP-43 Variants in Amyotrophic Lateral Sclerosis

Published on: February 12, 2015

Pathological study of alpha-chain disease, with special emphasis on evolution

A Galian, M J Lecestre, J Scotto

    Cancer
    |May 1, 1977
    PubMed

    More Related Videos

    Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein12:01

    Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

    Published on: May 30, 2015

    Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains09:27

    Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

    Published on: January 5, 2016

    Related Concept Videos

    Protein and Protein Structure02:39

    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...
    Conservation of Protein Domains Over Different Proteins02:26

    Conservation of Protein Domains Over Different Proteins

    Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
    A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...