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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2010-5-3
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pubmed:abstractText |
Protein-protein interactions and protein complex/aggregate formation play an essential role in almost all biological functions and activities. Through a nanoparticle aggregation immunoassay, we discovered that some proteins are substantially more complexed/aggregated in cancer tissues than normal tissues. This study examined four biomarkers proteins, CA125, CEA (carcinoembryonic antigen), CA19-9 and PAP (prostatic acid phosphatase) in ovarian, colon and prostate tissue lysates. The most exciting results were observed from the PAP assay of prostate tissues: prostate cancer can be clearly distinguished from normal prostate and prostate with benign conditions such as BPH (benign prostate hyperplasia) based on the complex/aggregation level of PAP in prostate tissue lysates. The complex/aggregate level of a protein can be potential biomarkers for cancer detection and diagnosis.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/CA-125 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/CA-19-9 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Carcinoembryonic Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Gold,
http://linkedlifedata.com/resource/pubmed/chemical/MUC16 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological,
http://linkedlifedata.com/resource/pubmed/chemical/prostatic acid phosphatase
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1873-4367
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pubmed:author |
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pubmed:copyrightInfo |
2010 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-65
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pubmed:meshHeading |
pubmed-meshheading:20392611-Adult,
pubmed-meshheading:20392611-Aged,
pubmed-meshheading:20392611-Aged, 80 and over,
pubmed-meshheading:20392611-Antibodies,
pubmed-meshheading:20392611-CA-125 Antigen,
pubmed-meshheading:20392611-CA-19-9 Antigen,
pubmed-meshheading:20392611-Carcinoembryonic Antigen,
pubmed-meshheading:20392611-Colonic Neoplasms,
pubmed-meshheading:20392611-Diagnosis, Differential,
pubmed-meshheading:20392611-Female,
pubmed-meshheading:20392611-Gold,
pubmed-meshheading:20392611-Humans,
pubmed-meshheading:20392611-Immunoassay,
pubmed-meshheading:20392611-Male,
pubmed-meshheading:20392611-Membrane Proteins,
pubmed-meshheading:20392611-Metal Nanoparticles,
pubmed-meshheading:20392611-Middle Aged,
pubmed-meshheading:20392611-Neoplasms,
pubmed-meshheading:20392611-Ovarian Neoplasms,
pubmed-meshheading:20392611-Prostatic Hyperplasia,
pubmed-meshheading:20392611-Prostatic Neoplasms,
pubmed-meshheading:20392611-Protein Binding,
pubmed-meshheading:20392611-Protein Conformation,
pubmed-meshheading:20392611-Protein Tyrosine Phosphatases,
pubmed-meshheading:20392611-Proteins,
pubmed-meshheading:20392611-Sensitivity and Specificity,
pubmed-meshheading:20392611-Tumor Markers, Biological
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pubmed:year |
2010
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pubmed:articleTitle |
Protein complexes/aggregates as potential cancer biomarkers revealed by a nanoparticle aggregation immunoassay.
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pubmed:affiliation |
NanoScience Technology Center, University of Central Florida, 12424 Research Parkway Suite 400, Orlando, FL 32826, USA. qhuo@mail.ucf.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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