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Related Concept Videos

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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. 
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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Related Experiment Video

Updated: Oct 2, 2025

Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis
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Genetic Analysis of Hereditary Transthyretin Ala97Ser Related Amyloidosis

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Transthyretin: Its function and amyloid formation.

Mitsuharu Ueda1

  • 1Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto, 860-0811, Japan.

Neurochemistry International
|February 26, 2022
PubMed
Summary
This summary is machine-generated.

Transthyretin amyloidosis (ATTR) involves amyloid deposits in organs. This review covers ATTR clinical features and new therapies like TTR stabilizers and gene silencing.

Keywords:
AmyloidosisGene silencing therapyHereditary ATTR amyloidosisTTR stabilizerTransthyretinWild-type ATTR amyloidosis

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Area of Science:

  • Biochemistry
  • Genetics
  • Medicine

Background:

  • Transthyretin (TTR) is a major amyloidogenic protein causing systemic amyloidosis.
  • ATTR amyloidosis presents in hereditary (ATTRv) and wild-type (ATTRwt) forms, affecting organs like nerves and the heart.
  • Over 150 TTR gene mutations are linked to amyloidosis, often destabilizing TTR tetramers.

Purpose of the Study:

  • To review the clinical phenotypes of transthyretin amyloidosis (ATTR).
  • To discuss the biochemical features of TTR relevant to amyloid formation.
  • To summarize recent advancements in disease-modifying therapies for ATTR.

Main Methods:

  • Literature review of clinical studies on ATTR phenotypes.
  • Analysis of TTR protein structure and mutation data.
  • Review of recent therapeutic strategies for ATTR.

Main Results:

  • ATTR involves extracellular amyloid deposits in multiple organs.
  • TTR tetramer destabilization is a key step in amyloid formation.
  • Emerging therapies include TTR tetramer stabilizers and gene silencing.

Conclusions:

  • ATTR amyloidosis has diverse clinical presentations.
  • Understanding TTR's role is crucial for developing effective treatments.
  • Promising therapies offer new hope for managing ATTR.