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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2010-6-16
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pubmed:abstractText |
Protein aggregation is a hallmark of several neurodegenerative diseases including Huntington's disease. We describe the use of the recently developed number and brightness method (N&B) that uses confocal images to monitor aggregation of Huntingtin exon 1 protein (Httex1p) directly in living cells. N&B measures the molecular brightness of protein aggregates in the entire cell noninvasively based on intensity fluctuations at each pixel in an image. N&B applied to mutant Httex1p in living cells showed a two-step pathway leading to inclusion formation that is polyQ length dependent and involves four phases. An initial phase of monomer accumulation is followed by formation of small oligomers (5-15 proteins); as protein concentration increases, an inclusion is seeded and forms in the cytoplasm; the growing inclusion recruits most of the Httex1p and depletes the cell leaving only a low concentration of monomers. The behavior of Httex1p in COS-7 and ST14A cells is compared.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-10078548,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-17937391,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-19487684,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-9302293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-9413985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-9671979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-9765898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20550921-9778247
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1542-0086
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
16
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pubmed:volume |
98
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3078-85
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:20550921-Humans,
pubmed-meshheading:20550921-Animals,
pubmed-meshheading:20550921-Rats,
pubmed-meshheading:20550921-Peptides,
pubmed-meshheading:20550921-Peptide Fragments,
pubmed-meshheading:20550921-Calibration,
pubmed-meshheading:20550921-Protein Structure, Quaternary,
pubmed-meshheading:20550921-Nerve Tissue Proteins,
pubmed-meshheading:20550921-Nuclear Proteins,
pubmed-meshheading:20550921-Cercopithecus aethiops,
pubmed-meshheading:20550921-Protein Multimerization,
pubmed-meshheading:20550921-COS Cells,
pubmed-meshheading:20550921-Microscopy, Confocal,
pubmed-meshheading:20550921-Green Fluorescent Proteins,
pubmed-meshheading:20550921-Molecular Imaging
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