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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Fibrous Proteins00:55

Fibrous Proteins

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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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Classification of Skeletal Muscle Fibers01:48

Classification of Skeletal Muscle Fibers

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Skeletal muscles continuously produce ATP to provide the energy that enables muscle contractions. Skeletal muscle fibers can be categorized into three types based on differences in their contraction speed and how they produce ATP, as well as physical differences related to these factors. Most human muscles contain all three muscle fiber types, albeit in varying proportions.
Slow-Twitch Muscle Fibers
Slow oxidative, muscle fibers appear red due to large numbers of capillaries and high levels of...
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Related Experiment Video

Updated: Aug 19, 2025

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
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Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers

Published on: April 26, 2018

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ENTAIL: yEt aNoTher amyloid fIbrils cLassifier.

Alessia Auriemma Citarella1, Luigi Di Biasi2, Fabiola De Marco2

  • 1Department of Computer Science, University of Salerno, Fisciano, Italy. aauriemmacitarella@unisa.it.

BMC Bioinformatics
|December 1, 2022
PubMed
Summary
This summary is machine-generated.

A new classifier, ENTAIL, aids in identifying amyloid fibril precursors. This tool, using over 4000 molecular descriptors, achieved 81.80% accuracy on a balanced dataset for improved amyloidosis research.

Keywords:
AmyloidosesFibrils machine learningProtein classification

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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Related Experiment Videos

Last Updated: Aug 19, 2025

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers
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Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers

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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Medical Research

Background:

  • Amyloidoses are protein misfolding disorders impacting protein function and structure.
  • Fibrillar deposits characterize diseases like Alzheimer's, Creutzfeldt-Jakob disease, and type II diabetes.
  • Identifying novel amyloid protein precursors is crucial for understanding disease pathology.

Purpose of the Study:

  • To develop a computational tool for identifying novel protein precursors of amyloid fibril deposits.
  • To enhance the understanding of the pathological processes underlying amyloidoses.

Main Methods:

  • Development of a novel classifier named ENTAIL.
  • Utilized over 4000 molecular descriptors for feature extraction.
  • Employed a Naive Bayes Classifier with Unbounded Support and Gaussian Kernel Type.

Main Results:

  • The ENTAIL classifier demonstrated high performance on a balanced dataset.
  • Achieved an accuracy of 81.80% on the test set.
  • Reported a sensitivity (SN) of 100%, specificity (SP) of 63.63%, and Matthews Correlation Coefficient (MCC) of 0.683.

Conclusions:

  • The developed ENTAIL classifier shows significant potential in identifying amyloid precursors.
  • Performance metrics indicate robust predictive capabilities, particularly on balanced datasets.
  • This advancement contributes to a deeper understanding of amyloidosis pathogenesis.