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Inclusion Body Measurement

Known as: INCLBOD, Inclusion Bodies 
A measurement of the protein, lipid or small molecule aggregates located within the cytoplasm.
National Institutes of Health

Papers overview

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Review
2019
Review
2019
TAR DNA binding protein 43 (TDP-43) is a versatile RNA/DNA binding protein involved in RNA-related metabolism. Hyper… Expand
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Review
2008
Review
2008
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) represents a cellular stress induced by multiple stimuli… Expand
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Highly Cited
2006
Highly Cited
2006
Protein quality-control, especially the removal of proteins with aberrant structures, has an important role in maintaining the… Expand
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Review
2005
Review
2005
Inclusion bodies produced in Escherichia coli are composed of densely packed denatured protein molecules in the form of particles… Expand
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Highly Cited
2004
Highly Cited
2004
Huntington's disease is caused by an abnormal polyglutamine expansion within the protein huntingtin and is characterized by… Expand
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Highly Cited
2001
Highly Cited
2001
The huntingtin exon 1 proteins with a polyglutamine repeat in the pathological range (51 or 83 glutamines), but not with a… Expand
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Review
2000
Review
2000
  • R. Kopito
  • Trends in cell biology
  • 2000
  • Corpus ID: 24294639
Intracellular and extracellular accumulation of aggregated protein are linked to many diseases, including ageing-related… Expand
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Highly Cited
2000
Highly Cited
2000
Deposition of aggregated protein into neurofilament-rich cytoplasmic inclusion bodies is a common cytopathological feature of… Expand
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Review
2000
Review
2000
  • A. Minton
  • Current opinion in structural biology
  • 2000
  • Corpus ID: 21614204
Recent studies have led to increased appreciation of the influence of excluded volume in solutions of high total macromolecular… Expand
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Review
1998
Review
1998
  • A. Fink
  • Folding & design
  • 1998
  • Corpus ID: 44892759
Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the… Expand
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